NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|896156623|ref|WP_049173074|]
View 

MULTISPECIES: 3-oxoacyl-ACP reductase [Corynebacterium]

Protein Classification

3-oxoacyl-ACP reductase( domain architecture ID 11483198)

3-oxoacyl-ACP reductase such as Mycobacterium tuberculosis FabG4, a high-molecular-weight FabG containing an N-terminal flavodoxin type domain and a C-terminal catalytically active oxoreductase domain that utilizes NADH to reduce beta-oxoacyl-CoA to beta-hydroxyacyl-CoA

CATH:  3.40.50.720
EC:  1.1.1.212
Gene Ontology:  GO:0016491
PubMed:  20423462|19011750
SCOP:  4000029

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-452 0e+00

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


:

Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 589.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623   2 TDKYQELVNGGPLTGLAKAAGLPQPPFLRRHKPGGPLLNNDkVLVTGEGADADAVAAQLAEWGLQVRRGN--------AA 73
Cdd:PRK08261   1 SDRYLQFVNSGLGKFLAKKLGLPQPVPLRRYRPGQPLLDGP-VLVGGAGRLAEALAALLAGLGYDVVANNdggltwaaGW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  74 DDKIGAIVLVATEAKRPAELQGPVLAAAKHMRKLDKGGRIVTVSRAKDAhhnatPAEIAENAVAGGIEGLIRSLGHEVRG 153
Cdd:PRK08261  80 GDRFGALVFDATGITDPADLKALYEFFHPVLRSLAPCGRVVVLGRPPEA-----AADPAAAAAQRALEGFTRSLGKELRR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 154 GSTANGILVAPGvsvTAPSVISSLHFFLSGRSAFIDGQFLRVTSDAGEIPSDWDKPLAGKVAAVTGSARGIGAAIARQLK 233
Cdd:PRK08261 155 GATAQLVYVAPG---AEAGLESTLRFFLSPRSAYVSGQVVRVGAADAAPPADWDRPLAGKVALVTGAARGIGAAIAEVLA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 234 ADGAEVIVIDVPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDIVIHNAGITRDKMFANMDDAKWGSV 313
Cdd:PRK08261 232 RDGAHVVCLDVPAAGEALAAVANRVGGTALALDITAPDAPARIAEHLAERHGGLDIVVHNAGITRDKTLANMDEARWDSV 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 314 IAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIET 393
Cdd:PRK08261 312 LAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIET 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 896156623 394 DMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCGQNIVGA 452
Cdd:PRK08261 392 QMTAAIPFATREAGRRMNSLQQGGLPVDVAETIAWLASPASGGVTGNVVRVCGQSLLGA 450
 
Name Accession Description Interval E-value
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-452 0e+00

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 589.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623   2 TDKYQELVNGGPLTGLAKAAGLPQPPFLRRHKPGGPLLNNDkVLVTGEGADADAVAAQLAEWGLQVRRGN--------AA 73
Cdd:PRK08261   1 SDRYLQFVNSGLGKFLAKKLGLPQPVPLRRYRPGQPLLDGP-VLVGGAGRLAEALAALLAGLGYDVVANNdggltwaaGW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  74 DDKIGAIVLVATEAKRPAELQGPVLAAAKHMRKLDKGGRIVTVSRAKDAhhnatPAEIAENAVAGGIEGLIRSLGHEVRG 153
Cdd:PRK08261  80 GDRFGALVFDATGITDPADLKALYEFFHPVLRSLAPCGRVVVLGRPPEA-----AADPAAAAAQRALEGFTRSLGKELRR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 154 GSTANGILVAPGvsvTAPSVISSLHFFLSGRSAFIDGQFLRVTSDAGEIPSDWDKPLAGKVAAVTGSARGIGAAIARQLK 233
Cdd:PRK08261 155 GATAQLVYVAPG---AEAGLESTLRFFLSPRSAYVSGQVVRVGAADAAPPADWDRPLAGKVALVTGAARGIGAAIAEVLA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 234 ADGAEVIVIDVPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDIVIHNAGITRDKMFANMDDAKWGSV 313
Cdd:PRK08261 232 RDGAHVVCLDVPAAGEALAAVANRVGGTALALDITAPDAPARIAEHLAERHGGLDIVVHNAGITRDKTLANMDEARWDSV 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 314 IAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIET 393
Cdd:PRK08261 312 LAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIET 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 896156623 394 DMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCGQNIVGA 452
Cdd:PRK08261 392 QMTAAIPFATREAGRRMNSLQQGGLPVDVAETIAWLASPASGGVTGNVVRVCGQSLLGA 450
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 213-446 4.29e-67

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 214.33  E-value: 4.29e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEA-LSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAeTVEEIKALGGnaAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMV 369
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896156623 370 EAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:cd05333  161 KSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNG 237
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 208-446 1.98e-64

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 207.72  E-value: 1.98e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARY 284
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRdAEALEAAAAELRAAGGraLAVAADVTDEAAVEALVAAAVAAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:COG1028   82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNS--LQQGGQPGDVAQAIAFLVSDRALGVNGHVL 442
Cdd:COG1028  162 VVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARipLGRLGTPEEVAAAVLFLASDAASYITGQVL 241


                 ....
gi 896156623 443 RVCG 446
Cdd:COG1028  242 AVDG 245
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 215-446 5.60e-60

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 195.89  E-value: 5.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  215 AAVTGSARGIGAAIARQLKADGAEVIVIDV--PQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDIV 290
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRssEEGAEEVVEELKALGVkaLGVVLDVSDREDVKAVVEEIEEELGTIDIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  291 IHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVE 370
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156623  371 AYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:TIGR01830 161 SLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDG 236
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 220-446 1.35e-48

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 166.07  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  220 SARGIGAAIARQLKADGAEVIVIDVPQAG-EALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDIVIHNAGITR 298
Cdd:pfam13561   4 NESGIGWAIARALAEEGAEVVLTDLNEALaKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFAP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  299 DKM--FANMDDAKWGSVIAVNIESQLKMNEQLLnhKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAYAEEF 376
Cdd:pfam13561  84 KLKgpFLDTSREDFDRALDVNLYSLFLLAKAAL--PLMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVEL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896156623  377 AKRGGNINAVAPGFIETDMTAAIPFVN--RQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:pfam13561 162 GPRGIRVNAISPGPIKTLAASGIPGFDelLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDG 233
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
 213-446 4.15e-20

mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR family oxidoreductase regularly found encoded next to genes for mycofactocin biosynthesis proteins, and never found in genomes lacking mycofactocin. Members of this family are likely to represent a family of proteins that share a specific function.


Pssm-ID: 468513 [Multi-domain]  Cd Length: 256  Bit Score: 89.35  E-value: 4.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDV--------PQAGEA-LSKVANELGG--LALQQDITADDAGNAIADAAV 281
Cdd:NF040491   1 RVALVTGAARGIGAATVRRLAARGYAVVAVDAcagdpapyPLGTEAdLDALVASSPGrvETVVADVRDRAALAAAVALAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYGRLDIVIHNAG-ITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNH---KAFEKAPRIATMASTSGIAGNRGQTN 357
Cdd:NF040491  81 DRWGRLDAAVAAAAvIAGGRPLWETPPEELDALWDVDVRGVWNLAAAAVPAllaGPDPRGCRFVAVASAAGHRGLFHLAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDM---TAAI-------PFVNRQVARRVNslqqggQPGDVAQAIA 427
Cdd:NF040491 161 YCAAKHAVVGLVRGLAADLAGTGVTACAVSPGSTDTPMlaaTAALyglddvtELAAHQLVRRLL------DPDEVAAVVA 234

                        250
                 ....*....|....*....
gi 896156623 428 FLVSDRALGVNGHVLRVCG 446
Cdd:NF040491 235 FACSPGGAAVNGSVVHADG 253
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 217-392 1.77e-15

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 74.06  E-value: 1.77e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623   217 VTGSARGIGAAIARQLKADGAEVIVI-----DVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:smart00822   5 ITGGLGGLGRALARWLAERGARRLVLlsrsgPDAPGAAALLAELEAAGArvTVVACDVADRDALAAVLAAIPAVEGPLTG 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623   290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESqlkmneqLLN-HKAFEKAP--RIATMASTSGIAGNRGQTNYATSkagvI 366
Cdd:smart00822  85 VIHAAGVLDDGVLASLTPERFAAVLAPKAAG-------AWNlHELTADLPldFFVLFSSIAGVLGSPGQANYAAA----N 153

                          170       180
                   ....*....|....*....|....*.
gi 896156623   367 AMVEAYAEEFAKRGGNINAVAPGFIE 392
Cdd:smart00822 154 AFLDALAEYRRARGLPALSIAWGAWA 179
 
Name Accession Description Interval E-value
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-452 0e+00

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 589.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623   2 TDKYQELVNGGPLTGLAKAAGLPQPPFLRRHKPGGPLLNNDkVLVTGEGADADAVAAQLAEWGLQVRRGN--------AA 73
Cdd:PRK08261   1 SDRYLQFVNSGLGKFLAKKLGLPQPVPLRRYRPGQPLLDGP-VLVGGAGRLAEALAALLAGLGYDVVANNdggltwaaGW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  74 DDKIGAIVLVATEAKRPAELQGPVLAAAKHMRKLDKGGRIVTVSRAKDAhhnatPAEIAENAVAGGIEGLIRSLGHEVRG 153
Cdd:PRK08261  80 GDRFGALVFDATGITDPADLKALYEFFHPVLRSLAPCGRVVVLGRPPEA-----AADPAAAAAQRALEGFTRSLGKELRR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 154 GSTANGILVAPGvsvTAPSVISSLHFFLSGRSAFIDGQFLRVTSDAGEIPSDWDKPLAGKVAAVTGSARGIGAAIARQLK 233
Cdd:PRK08261 155 GATAQLVYVAPG---AEAGLESTLRFFLSPRSAYVSGQVVRVGAADAAPPADWDRPLAGKVALVTGAARGIGAAIAEVLA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 234 ADGAEVIVIDVPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDIVIHNAGITRDKMFANMDDAKWGSV 313
Cdd:PRK08261 232 RDGAHVVCLDVPAAGEALAAVANRVGGTALALDITAPDAPARIAEHLAERHGGLDIVVHNAGITRDKTLANMDEARWDSV 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 314 IAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIET 393
Cdd:PRK08261 312 LAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIET 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 896156623 394 DMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCGQNIVGA 452
Cdd:PRK08261 392 QMTAAIPFATREAGRRMNSLQQGGLPVDVAETIAWLASPASGGVTGNVVRVCGQSLLGA 450
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 213-446 4.29e-67

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 214.33  E-value: 4.29e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEA-LSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAeTVEEIKALGGnaAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMV 369
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896156623 370 EAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:cd05333  161 KSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNG 237
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
210-446 1.50e-65

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 210.79  E-value: 1.50e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGR 286
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSnEEAAEALAAELRAAGGeaRVLVFDVSDEAAVRALIEAAVEAFGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:PRK05653  83 LDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK05653 163 GFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVNG 242
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 208-446 1.98e-64

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 207.72  E-value: 1.98e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARY 284
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRdAEALEAAAAELRAAGGraLAVAADVTDEAAVEALVAAAVAAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:COG1028   82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNS--LQQGGQPGDVAQAIAFLVSDRALGVNGHVL 442
Cdd:COG1028  162 VVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARipLGRLGTPEEVAAAVLFLASDAASYITGQVL 241


                 ....
gi 896156623 443 RVCG 446
Cdd:COG1028  242 AVDG 245
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 210-446 1.25e-60

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 198.11  E-value: 1.25e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAG--EALSKVANELGG--LALQQDITADDAGNAIADAAVARYG 285
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAgaEALVAEIGALGGkaLAVQGDVSDAESVERAVDEAKAEFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:PRK05557  83 GVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVC 445
Cdd:PRK05557 163 IGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHVN 242


                 .
gi 896156623 446 G 446
Cdd:PRK05557 243 G 243
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 215-446 5.60e-60

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 195.89  E-value: 5.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  215 AAVTGSARGIGAAIARQLKADGAEVIVIDV--PQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDIV 290
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRssEEGAEEVVEELKALGVkaLGVVLDVSDREDVKAVVEEIEEELGTIDIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  291 IHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVE 370
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156623  371 AYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:TIGR01830 161 SLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDG 236
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 215-444 3.30e-54

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 180.94  E-value: 3.30e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 215 AAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDIVIH 292
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALGGnaVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 293 NAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAY 372
Cdd:cd05233   81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156623 373 AEEFAKRGGNINAVAPGFIETDMTAA-IPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRV 444
Cdd:cd05233  161 ALELAPYGIRVNAVAPGLVDTPMLAKlGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPV 233
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 209-446 1.17e-52

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 177.37  E-value: 1.17e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAEVIVI---DVPQAGEALSKVANELG-GLALQQDITADDAGNAIADAAVARY 284
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHyrsDEEAAEELVEAVEALGRrAQAVQADVTDKAALEAAVAAAVERF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK12825  83 GRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRV 444
Cdd:PRK12825 163 LVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQVIEV 242


                 ..
gi 896156623 445 CG 446
Cdd:PRK12825 243 TG 244
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 220-446 1.35e-48

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 166.07  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  220 SARGIGAAIARQLKADGAEVIVIDVPQAG-EALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDIVIHNAGITR 298
Cdd:pfam13561   4 NESGIGWAIARALAEEGAEVVLTDLNEALaKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFAP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  299 DKM--FANMDDAKWGSVIAVNIESQLKMNEQLLnhKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAYAEEF 376
Cdd:pfam13561  84 KLKgpFLDTSREDFDRALDVNLYSLFLLAKAAL--PLMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVEL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896156623  377 AKRGGNINAVAPGFIETDMTAAIPFVN--RQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:pfam13561 162 GPRGIRVNAISPGPIKTLAASGIPGFDelLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDG 233
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
 213-446 1.85e-48

acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.


Pssm-ID: 273823 [Multi-domain]  Cd Length: 242  Bit Score: 166.07  E-value: 1.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAgEALSKVANELGGL-----ALQQDITADDAGNAIADAAVARYGRL 287
Cdd:TIGR01829   1 RIALVTGGMGGIGTAICQRLAKDGYRVAANCGPNE-ERAEAWLQEQGALgfdfrVVEGDVSSFESCKAAVAKVEAELGPV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:TIGR01829  80 DVLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTNYSAAKAGMIG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896156623  368 MVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:TIGR01829 160 FTKALAQEGATKGVTVNTISPGYIATDMVMAMREDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYITGATLSING 238
PRK12826 PRK12826
SDR family oxidoreductase;
208-446 3.00e-46

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 160.47  E-value: 3.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV--PQAGEALSKVANELGGL-ALQQDITADDAGNAIADAAVARY 284
Cdd:PRK12826   2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDIcgDDAAATAELVEAAGGKArARQVDVRDRAALKAAVAAGVEDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhKAFEKA--PRIATMASTSGIA-GNRGQTNYATS 361
Cdd:PRK12826  82 GRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAAL--PALIRAggGRIVLTSSVAGPRvGYPGLAHYAAS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPF--VNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRALGVNG 439
Cdd:PRK12826 160 KAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDaqWAEAIAAAI-PLGRLGEPEDIAAAVLFLASDEARYITG 238


                 ....*..
gi 896156623 440 HVLRVCG 446
Cdd:PRK12826 239 QTLPVDG 245
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
213-446 1.07e-45

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 158.78  E-value: 1.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALsKVANELGGLALQQDITADDAGNAIADAA-----VARYGRL 287
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAK-DWFEEYGFTEDQVRLKELDVTDTEECAEalaeiEEEEGPV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:PRK12824  82 DILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 368 MVEAYAEEFAKRGGNINAVAPGFIETDMTAAI-PFVNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK12824 162 FTKALASEGARYGITVNCIAPGYIATPMVEQMgPEVLQSIVNQI-PMKRLGTPEEIAAAVAFLVSEAAGFITGETISING 240
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 210-446 2.64e-45

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 157.70  E-value: 2.64e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI-DVPQagEALSKVANELG-----GLALQQDITADDAGNAIADAAVAR 283
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINE--EAAQELLEEIKeeggdAIAVKADVSSEEDVENLVEQIVEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKA 363
Cdd:PRK05565  81 FGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLR 443
Cdd:PRK05565 161 AVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIIT 240


                 ...
gi 896156623 444 VCG 446
Cdd:PRK05565 241 VDG 243
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 209-446 1.98e-44

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 155.65  E-value: 1.98e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEALSKVANEL----GG--LALQQDITADDAGNAIADAAV 281
Cdd:PRK12827   3 SLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIhPMRGRAEADAVAAGieaaGGkaLGLAFDVRDFAATRAALDAGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHK-AFEKAPRIATMASTSGIAGNRGQTNYAT 360
Cdd:PRK12827  83 EEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMiRARRGGRIVNIASVAGVRGNRGQVNYAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMtAAIPFVNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRALGVNGH 440
Cdd:PRK12827 163 SKAGLIGLTKTLANELAPRGITVNAVAPGAINTPM-ADNAAPTEHLLNPV-PVQRLGEPDEVAALVAFLVSDAASYVTGQ 240


                 ....*.
gi 896156623 441 VLRVCG 446
Cdd:PRK12827 241 VIPVDG 246
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 213-400 1.28e-43

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 151.61  E-value: 1.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANELGGL-----ALQQDITADDAGNAIADAAVARYGRL 287
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDR--SEEKLEAVAKELGALggkalFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:pfam00106  79 DILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIG 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 896156623  368 MVEAYAEEFAKRGGNINAVAPGFIETDMTAAIP 400
Cdd:pfam00106 159 FTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 210-446 1.41e-43

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 153.24  E-value: 1.41e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEViVIDVPQAGEALSKVANELGG-----LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKV-VINYNSSKEAAENLVNELGKeghdvYAVQADVSKVEDANRLVEEAVNHF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK12935  83 GKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPF-VNRQVARRVNSlQQGGQPGDVAQAIAFLVSDRALgVNGHVLR 443
Cdd:PRK12935 163 MLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEeVRQKIVAKIPK-KRFGQADEIAKGVVYLCRDGAY-ITGQQLN 240


                 ...
gi 896156623 444 VCG 446
Cdd:PRK12935 241 ING 243
FabG-like PRK07231
SDR family oxidoreductase;
210-446 1.36e-42

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 150.75  E-value: 1.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGG----LALQQDITADDAGNAIADAAVARYG 285
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNE--EAAERVAAEILAggraIAVAADVSDEADVEAAVAAALERFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGIT-RDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK07231  81 SVDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFV----NRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGH 440
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEptpeNRAKFLATIPLGRLGTPEDIANAALFLASDEASWITGV 240


                 ....*.
gi 896156623 441 VLRVCG 446
Cdd:PRK07231 241 TLVVDG 246
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 210-446 2.63e-42

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 150.12  E-value: 2.63e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQA-GEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGR 286
Cdd:PRK12939   5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAeARELAAALEAAGGraHAIAADLADPASVQRFFDAAAAALGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:PRK12939  85 LDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAVI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNR-QVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVC 445
Cdd:PRK12939 165 GMTRSLARELGGRGITVNAIAPGLTATEATAYVPADERhAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLLPVN 244


                 .
gi 896156623 446 G 446
Cdd:PRK12939 245 G 245
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 211-434 9.45e-41

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 145.71  E-value: 9.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 211 AGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRA--ERLEALAAELGGraLAVPLDVTDEAAVEAAVAAAVAEFGRLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAM 368
Cdd:COG4221   82 VLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156623 369 VEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRA 434
Cdd:COG4221  162 SESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQPA 227
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 210-446 4.38e-39

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 141.34  E-value: 4.38e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV--PQAGEALSKVANE-LGGLALQQDITADDAGNAIADAAVARYGR 286
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRneEKAEEAQQLIEKEgVEATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:cd05347   83 IDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFVNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLR 443
Cdd:cd05347  163 GLTKALATEWARHGIQVNAIAPGYFATEMTEAVvadPEFNDDILKRI-PAGRWGQPEDLVGAAVFLASDASDYVNGQIIF 241


                 ...
gi 896156623 444 VCG 446
Cdd:cd05347  242 VDG 244
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 208-446 7.58e-39

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 141.35  E-value: 7.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAgeALSKVANELGGL---ALQQDITADDAGNAIADAAVARY 284
Cdd:PRK12829   7 KPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEA--ALAATAARLPGAkvtATVADVADPAQVERVFDTAVERF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGIT-RDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNH-KAFEKAPRIATMASTSGIAGNRGQTNYATSK 362
Cdd:PRK12829  85 GGLDVLVNNAGIAgPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLlKASGHGGVIIALSSVAGRLGYPGRTPYAASK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGFIETD-MTAAIPFVNRQVARRVN----------SLQQGGQPGDVAQAIAFLVS 431
Cdd:PRK12829 165 WAVVGLVKSLAIELGPLGIRVNAILPGIVRGPrMRRVIEARAQQLGIGLDemeqeylekiSLGRMVEPEDIAATALFLAS 244

                        250
                 ....*....|....*
gi 896156623 432 DRALGVNGHVLRVCG 446
Cdd:PRK12829 245 PAARYITGQAISVDG 259
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 210-446 7.80e-39

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 140.82  E-value: 7.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAevIVIDVPQAGEALSKVANELGGLA--LQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGA--IVGLHGTRVEKLEALAAELGERVkiFPANLSDRDEVKALGQKAEADLEGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:PRK12936  82 DILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIG 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896156623 368 MVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK12936 162 FSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTIHVNG 240
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
210-437 8.95e-38

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 138.08  E-value: 8.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGG-----LALQQDITADDAGNAIADAAVARY 284
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDA--ERLEALAAELRAagarvEVVALDVTDPDAVAALAEAVLARF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:COG0300   81 GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAaipfvnrqvARRVNSLQQGGQPGDVAQAIAFLVSDRALGV 437
Cdd:COG0300  161 LEGFSESLRAELAPTGVRVTAVCPGPVDTPFTA---------RAGAPAGRPLLSPEEVARAILRALERGRAEV 224
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 210-446 1.96e-37

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 136.64  E-value: 1.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEViVIDVPQAGEALSKVANEL-----GGLALQQDITADDAGNAIADAAVARY 284
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASV-VVNYASSKAAAEEVVAEIeaaggKAIAVQADVSDPSQVARLFDAAEKAF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHkaFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:cd05362   80 GGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKR--LRDGGRIINISSSLTAAYTPNYGAYAGSKAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFVNRQVARrvNSLQQGGQPGDVAQAIAFLVSDRALGVNGHV 441
Cdd:cd05362  158 VEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGkteEAVEGYAKM--SPLGRLGEPEDIAPVVAFLASPDGRWVNGQV 235


                 ....*
gi 896156623 442 LRVCG 446
Cdd:cd05362  236 IRANG 240
fabG_rel TIGR01831
3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well ...
 217-446 4.39e-37

3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well conserved family of proteins closely related to the FabG family, TIGR01830, and possibly equal in function. In all completed genomes with a member of this family, a FabG in TIGR01830 is also found. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273825 [Multi-domain]  Cd Length: 239  Bit Score: 135.80  E-value: 4.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  217 VTGSARGIGAAIARQLKADGAEVIV---IDVPQAGEALSK-VANELGGLALQQDITADDAGNAIADAAVARYGRLDIVIH 292
Cdd:TIGR01831   3 VTGASRGIGRAIANQLAADGFNIGVhyhSDAAGAQETLNAiVANGGNGRLLSFDVADRVACREVLEADIAQHGAYYGVVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  293 NAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQL-LNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEA 371
Cdd:TIGR01831  83 NAGIARDAAFPALSEDDWDAVIHTNLDGFYNVIHPCiMPMIGARQGGRIITLASVSGVMGNRGQVNYSAAKAGLIGATKA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156623  372 YAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:TIGR01831 163 LAIELAKRKITVNCIAPGLIDTGMIAMEESALKEALSMV-PMKRMGQPEEVAGLASFLMSDIAGYVTRQVISVNG 236
PRK06138 PRK06138
SDR family oxidoreductase;
210-446 3.13e-35

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 131.04  E-value: 3.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANELG----GLALQQDITADDAGNAIADAAVARYG 285
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADR--DAEAAERVAAAIAaggrAFARQGDVGSAEAVEALVDFVAARWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI------PFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNG 439
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIfarhadPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFATG 240


                 ....*..
gi 896156623 440 HVLRVCG 446
Cdd:PRK06138 241 TTLVVDG 247
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 210-446 3.67e-35

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 130.85  E-value: 3.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGGLALQQ-----DITADDAGNAIADAAVARY 284
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQ--EKLEEAVAECGALGTEVrgyaaNVTDEEDVEATFAQIAEDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRD---------KMFANMDDAKWGSVIAVNI--------ESQLKMNEQllnhkafEKAPRIATMASTS 347
Cdd:PRK08217  81 GQLNGLINNAGILRDgllvkakdgKVTSKMSLEQFQSVIDVNLtgvflcgrEAAAKMIES-------GSKGVIINISSIA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 348 gIAGNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIA 427
Cdd:PRK08217 154 -RAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEALERLEKMIPVGRLGEPEEIAHTVR 232

                        250
                 ....*....|....*....
gi 896156623 428 FLVSDRAlgVNGHVLRVCG 446
Cdd:PRK08217 233 FIIENDY--VTGRVLEIDG 249
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 210-446 4.61e-35

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 130.58  E-value: 4.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV--PQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYG 285
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRskEDAAEEVVEEIKAVGGkaIAVQADVSKEEDVVALFQSAIKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAP-RIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:cd05358   81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIKgKIINMSSVHEKIPWPGHVNYAASKGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQG--GQPGDVAQAIAFLVSDRALGVNGHVL 442
Cdd:cd05358  161 VKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSLIPMGriGEPEEIAAAAAWLASDEASYVTGTTL 240


                 ....
gi 896156623 443 RVCG 446
Cdd:cd05358  241 FVDG 244
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 212-400 5.88e-35

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 130.52  E-value: 5.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-------PQAGEALSKVANEL---GGLALQQDITADDaGNAIADAAV 281
Cdd:cd05353    5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggdrkgsGKSSSAADKVVDEIkaaGGKAVANYDSVED-GEKIVKTAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATS 361
Cdd:cd05353   84 DAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYSAA 163

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGfIETDMTAAIP 400
Cdd:cd05353  164 KLGLLGLSNTLAIEGAKYNITCNTIAPA-AGSRMTETVM 201
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 205-446 6.18e-34

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 127.85  E-value: 6.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 205 DWDKPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqaGEALSKVANELGG---LALQQDITADDAGNAIADAAV 281
Cdd:PRK06841   8 DLAFDLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDR---SEDVAEVAAQLLGgnaKGLVCDVSDSQSVEAAVAAVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATS 361
Cdd:PRK06841  85 SAFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCAS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGFIET-------------DMTAAIPfvnrqvARRVnslqqgGQPGDVAQAIAF 428
Cdd:PRK06841 165 KAGVVGMTKVLALEWGPYGITVNAISPTVVLTelgkkawagekgeRAKKLIP------AGRF------AYPEEIAAAALF 232

                        250
                 ....*....|....*...
gi 896156623 429 LVSDRALGVNGHVLRVCG 446
Cdd:PRK06841 233 LASDAAAMITGENLVIDG 250
PRK06172 PRK06172
SDR family oxidoreductase;
208-446 1.98e-33

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 126.40  E-value: 1.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEALSKVANELGGLAL--QQDITADDAGNAIADAAVARY 284
Cdd:PRK06172   3 MTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRdAAGGEETVALIREAGGEALfvACDVTRDAEVKALVEQTIAAY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDK-MFANMDDAKWGSVIAVNIESQ-LKMNEQLLNHKAfEKAPRIATMASTSGIAGNRGQTNYATSK 362
Cdd:PRK06172  83 GRLDYAFNNAGIEIEQgRLAEGSEAEFDAIMGVNVKGVwLCMKYQIPLMLA-QGGGAIVNTASVAGLGAAPKMSIYAASK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGFIETDM----TAAIPFVnRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVN 438
Cdd:PRK06172 162 HAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMfrraYEADPRK-AEFAAAMHPVGRIGKVEEVASAVLYLCSDGASFTT 240


                 ....*...
gi 896156623 439 GHVLRVCG 446
Cdd:PRK06172 241 GHALMVDG 248
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 210-446 2.10e-33

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 125.97  E-value: 2.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:cd05345    3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGIT-RDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAM 368
Cdd:cd05345   83 LVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVTA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 369 VEAYAEEFAKRGGNINAVAP-----GFIETDMTAAIPfVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLR 443
Cdd:cd05345  163 TKAMAVELAPRNIRVNCLCPvagetPLLSMFMGEDTP-ENRAKFRATIPLGRLSTPDDIANAALYLASDEASFITGVALE 241


                 ...
gi 896156623 444 VCG 446
Cdd:cd05345  242 VDG 244
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
210-446 3.85e-33

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 125.62  E-value: 3.85e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDETRRLIEKEGRkvTFVQVDLTKPESAEKVVKEALEEFGKI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:PRK06935  93 DILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTASKHGVAG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 368 MVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFVNRQVARRVNSlQQGGQPGDVAQAIAFLVSDRALGVNGHVLRV 444
Cdd:PRK06935 173 LTKAFANELAAYNIQVNAIAPGYIKTANTAPIradKNRNDEILKRIPA-GRWGEPDDLMGAAVFLASRASDYVNGHILAV 251


                 ..
gi 896156623 445 CG 446
Cdd:PRK06935 252 DG 253
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
208-449 1.23e-32

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 130.74  E-value: 1.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANELGG----LALQQDITADDAGNAIADAAVAR 283
Cdd:PRK08324 418 KPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADL--DEEAAEAAAAELGGpdraLGVACDVTDEAAVQAAFEEAALA 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLlnHKAFEKAP---RIATMASTSGIAGNRGQTNYAT 360
Cdd:PRK08324 496 FGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREA--VRIMKAQGlggSIVFIASKNAVNPGPNFGAYGA 573

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAP------------GFIETDMTA---AIPFVNRQVARRvNSLQQGGQPGDVAQA 425
Cdd:PRK08324 574 AKAAELHLVRQLALELGPDGIRVNGVNPdavvrgsgiwtgEWIEARAAAyglSEEELEEFYRAR-NLLKREVTPEDVAEA 652

                        250       260
                 ....*....|....*....|....
gi 896156623 426 IAFLVSDRALGVNGHVLRVCGQNI 449
Cdd:PRK08324 653 VVFLASGLLSKTTGAIITVDGGNA 676
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 210-446 3.03e-32

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 123.21  E-value: 3.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV--PQAGEALSKVANELG--GLALQQDITADDAGNAIADAAVARYG 285
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNsaPRAEEKAEELAKKYGvkTKAYKCDVSSQESVEKTFKQIQKDFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNH-KAFEKAPRIATmASTSGIAGNRGQTN--YATSK 362
Cdd:cd05352   86 KIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIfKKQGKGSLIIT-ASMSGTIVNRPQPQaaYNASK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVL 442
Cdd:cd05352  165 AAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYTTGSDL 244


                 ....
gi 896156623 443 RVCG 446
Cdd:cd05352  245 IIDG 248
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 210-449 3.33e-32

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 122.97  E-value: 3.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIdvPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVL--YNSAENEAKELREKGVFTIKCDVGNRDQVKKSKEVVEKEFGRVDV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIA-GNRGQTNYATSKAGVIAM 368
Cdd:PRK06463  83 LVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGtAAEGTTFYAITKAGIIIL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 369 VEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVN-----RQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLR 443
Cdd:PRK06463 163 TRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEeaeklRELFRNKTVLKTTGKPEDIANIVLFLASDDARYITGQVIV 242


                 ....*.
gi 896156623 444 VCGQNI 449
Cdd:PRK06463 243 ADGGRI 248
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 210-446 3.41e-32

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 122.88  E-value: 3.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGGLA--LQQDITADDAGNAIADAAVARYGRL 287
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILD--EEGQAAAAELGDAArfFHLDVTDEDGWTAVVDTAREAFGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhKAFEKAPR--IATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:cd05341   81 DVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVI--PPMKEAGGgsIINMSSIEGLVGDPALAAYNASKGAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNI--NAVAPGFIETDMTAAIPfvNRQVARRV---NSLQQGGQPGDVAQAIAFLVSDRALGVNGH 440
Cdd:cd05341  159 RGLTKSAALECATQGYGIrvNSVHPGYIYTPMTDELL--IAQGEMGNypnTPMGRAGEPDEIAYAVVYLASDESSFVTGS 236


                 ....*.
gi 896156623 441 VLRVCG 446
Cdd:cd05341  237 ELVVDG 242
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
210-434 3.77e-32

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 122.81  E-value: 3.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIV---IDVPQAGEALSKvANELGG--LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgPNSPRRVKWLED-QKALGFdfIASEGNVGDWDSTKAAFDKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK12938  80 GEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAG 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI-PFVNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRA 434
Cdd:PRK12938 160 IHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIrPDVLEKIVATI-PVRRLGSPDEIGSIVAWLASEES 229
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 212-446 1.01e-31

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 121.61  E-value: 1.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDvpQAGEALSKVANEL-----GGLALQQDITADDAGNAIADAAVARYGR 286
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICA--RNRENLERAASELraggaGVLAVVADLTDPEDIDRLVEKAGDAFGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:cd05344   79 VDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETD--------MTAAIPFVNRQVARRVNS---LQQGGQPGDVAQAIAFLVSDRAL 435
Cdd:cd05344  159 GLVKTLSRELAPDGVTVNSVLPGYIDTErvrrlleaRAEKEGISVEEAEKEVASqipLGRVGKPEELAALIAFLASEKAS 238

                        250
                 ....*....|.
gi 896156623 436 GVNGHVLRVCG 446
Cdd:cd05344  239 YITGQAILVDG 249
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 210-452 1.21e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 121.38  E-value: 1.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEAlskVANELGGLALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIdPEAGKA---AADEVGGLFVPTDVTDEDAVNALFDTAAETYGSVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGIT--RDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGN-RGQTNYATSKAGV 365
Cdd:PRK06057  82 IAFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSaTSQISYTASKGGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIET----DMTAAIPfvnRQVARRVNSLQQG--GQPGDVAQAIAFLVSDRALGVNG 439
Cdd:PRK06057 162 LAMSRELGVQFARQGIRVNALCPGPVNTpllqELFAKDP---ERAARRLVHVPMGrfAEPEEIAAAVAFLASDDASFITA 238

                        250
                 ....*....|...
gi 896156623 440 HVLRVCGqNIVGA 452
Cdd:PRK06057 239 STFLVDG-GISGA 250
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 209-446 3.01e-31

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 120.23  E-value: 3.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVAN--ELGG--LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK12937   2 TLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEieAAGGraIAVQADVADAAAVTRLFDAAETAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHkaFEKAPRIATMaSTSGIA-GNRGQTNYATSKA 363
Cdd:PRK12937  82 GRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARH--LGQGGRIINL-STSVIAlPLPGYGPYAASKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAiPFVNRQVAR--RVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHV 441
Cdd:PRK12937 159 AVEGLVHVLANELRGRGITVNAVAPGPVATELFFN-GKSAEQIDQlaGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQV 237


                 ....*
gi 896156623 442 LRVCG 446
Cdd:PRK12937 238 LRVNG 242
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 210-446 3.78e-31

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 119.90  E-value: 3.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADI--DGGAAQAVVAQIAGgaLALRVDVTDEQQVAALFERAVEEFGGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITR-DKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:cd08944   79 DLLVNNAGAMHlTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMT---------AAIPFVNRQVarRVNSLQQGGQPGDVAQAIAFLVSDRALGV 437
Cdd:cd08944  159 NLTRTLAAELRHAGIRCNALAPGLIDTPLLlaklagfegALGPGGFHLL--IHQLQGRLGRPEDVAAAVVFLLSDDASFI 236


                 ....*....
gi 896156623 438 NGHVLRVCG 446
Cdd:cd08944  237 TGQVLCVDG 245
PRK06124 PRK06124
SDR family oxidoreductase;
210-446 6.18e-31

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 119.82  E-value: 6.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI--DVPQAGEALSKV-ANELGGLALQQDITADDAGNAIADAAVARYGR 286
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNgrNAATLEAAVAALrAAGGAAEALAFDIADEEAVAAAFARIDAEHGR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:PRK06124  89 LDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLT 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFVNRQVARRvNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLR 443
Cdd:PRK06124 169 GLMRALAAEFGPHGITSNAIAPGYFATETNAAMaadPAVGPWLAQR-TPLGRWGRPEEIAGAAVFLASPAASYVNGHVLA 247


                 ...
gi 896156623 444 VCG 446
Cdd:PRK06124 248 VDG 250
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 210-449 1.02e-30

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 119.78  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-------PQAGEALSKVANEL---GGLALQQ--DITADDAGNAIA 277
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIgvgldgsASGGSAAQAVVDEIvaaGGEAVANgdDIADWDGAANLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 278 DAAVARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNiesqLKMNEQLLNH-----KAFEKA-----PRIATMASTS 347
Cdd:PRK07791  84 DAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVH----LKGHFATLRHaaaywRAESKAgravdARIINTSSGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 348 GIAGNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGfIETDMTAAIpfvnrqVARRVNSLQQGG----QPGDVA 423
Cdd:PRK07791 160 GLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA-ARTRMTETV------FAEMMAKPEEGEfdamAPENVS 232

                        250       260
                 ....*....|....*....|....*.
gi 896156623 424 QAIAFLVSDRALGVNGHVLRVCGQNI 449
Cdd:PRK07791 233 PLVVWLGSAESRDVTGKVFEVEGGKI 258
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 203-446 1.22e-30

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 120.27  E-value: 1.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 203 PSDWDKPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEAlSKVANELGGLALQQDITADDAGN-AIADAAV 281
Cdd:PRK07792   3 RTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDA-SDVLDEIRAAGAKAVAVAGDISQrATADELV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 AR---YGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNH-KAFEKAP------RIATMASTSGIAG 351
Cdd:PRK07792  82 ATavgLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYwRAKAKAAggpvygRIVNTSSEAGLVG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 352 NRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGfIETDMTAAIpFVNRQ--VARRVNSLqqggQPGDVAQAIAFL 429
Cdd:PRK07792 162 PVGQANYGAAKAGITALTLSAARALGRYGVRANAICPR-ARTAMTADV-FGDAPdvEAGGIDPL----SPEHVVPLVQFL 235

                        250
                 ....*....|....*..
gi 896156623 430 VSDRALGVNGHVLRVCG 446
Cdd:PRK07792 236 ASPAAAEVNGQVFIVYG 252
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 215-446 1.60e-30

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 118.22  E-value: 1.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 215 AAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVA--NELGG--LALQQDITADDAGNAIADAAVARYGRLDIV 290
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVAAeiEELGGkaVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 291 IHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVE 370
Cdd:cd05359   81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 371 AYAEEFAKRGGNINAVAPGFIETDMTAAIPFV--------NRQVARRVnslqqgGQPGDVAQAIAFLVSDRALGVNGHVL 442
Cdd:cd05359  161 YLAVELGPRGIRVNAVSPGVIDTDALAHFPNRedlleaaaANTPAGRV------GTPQDVADAVGFLCSDAARMITGQTL 234


                 ....
gi 896156623 443 RVCG 446
Cdd:cd05359  235 VVDG 238
PRK07063 PRK07063
SDR family oxidoreductase;
210-446 3.23e-30

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 117.84  E-value: 3.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIV--IDVPQAGEALSKVANELGG---LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALadLDAALAERAAAAIARDVAGarvLAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITrdkMFAN---MDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATS 361
Cdd:PRK07063  85 GPLDVLVNNAGIN---VFADplaMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI------PFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRAL 435
Cdd:PRK07063 162 KHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWwnaqpdPAAARAETLALQPMKRIGRPEEVAMTAVFLASDEAP 241

                        250
                 ....*....|.
gi 896156623 436 GVNGHVLRVCG 446
Cdd:PRK07063 242 FINATCITIDG 252
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 213-446 4.21e-30

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 117.25  E-value: 4.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLALQQDITADDAGN-----AIADAAVARYGRL 287
Cdd:cd08945    4 EVALVTGATSGIGLAIARRLGKEGLRVFV--CARGEEGLATTVKELREAGVEADGRTCDVRSvpeieALVAAAVARYGPI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAP--RIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:cd08945   82 DVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAGGMLERGtgRIINIASTGGKQGVVHAAPYSASKHGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI--------PFVNRQVARRVNS---LQQGGQPGDVAQAIAFLVSDRA 434
Cdd:cd08945  162 VGFTKALGLELARTGITVNAVCPGFVETPMAASVrehyadiwEVSTEEAFDRITArvpLGRYVTPEEVAGMVAYLIGDGA 241

                        250
                 ....*....|..
gi 896156623 435 LGVNGHVLRVCG 446
Cdd:cd08945  242 AAVTAQALNVCG 253
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 210-446 2.41e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 115.43  E-value: 2.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANEL-----GGLALQQDITADDAGNAIADAAVARY 284
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVL--SARKAEELEEAAAHLealgiDALWIAADVADEADIERLAEETLERF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFE-KAPRIATMASTSGIAGN-RGQTN---YA 359
Cdd:PRK08213  88 GHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPrGYGRIINVASVAGLGGNpPEVMDtiaYN 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 360 TSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAA-IPFVNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRALGVN 438
Cdd:PRK08213 168 TSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGtLERLGEDLLAHT-PLGRLGDDEDLKGAALLLASDASKHIT 246


                 ....*...
gi 896156623 439 GHVLRVCG 446
Cdd:PRK08213 247 GQILAVDG 254
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 210-446 4.57e-29

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 114.48  E-value: 4.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANELG---GLALQQDITADDAGNAIADAAVARYGR 286
Cdd:cd05326    2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADI--DDDAGQAVAAELGdpdISFVHCDVTVEADVRAAVDTAVARFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFA--NMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:cd05326   80 LDIMFNNAGVLGAPCYSilETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPF-----VNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNG 439
Cdd:cd05326  160 VLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGvedeaIEEAVRGAANLKGTALRPEDIAAAVLYLASDDSRYVSG 239


                 ....*..
gi 896156623 440 HVLRVCG 446
Cdd:cd05326  240 QNLVVDG 246
PRK07831 PRK07831
SDR family oxidoreductase;
210-447 9.84e-29

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 113.59  E-value: 9.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSA-RGIGAAIARQLKADGAEVIVIDVPQA--GEALSKVANELGGLALQQ---DITADDAGNAIADAAVAR 283
Cdd:PRK07831  15 LAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERrlGETADELAAELGLGRVEAvvcDVTSEAQVDALIDAAVER 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNH-KAFEKAPRIATMASTSGIAGNRGQTNYATSK 362
Cdd:PRK07831  95 LGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYmRARGHGGVIVNNASVLGWRAQHGQAHYAAAK 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGFietdmtAAIPFVNR--------QVARRvNSLQQGGQPGDVAQAIAFLVSDRA 434
Cdd:PRK07831 175 AGVMALTRCSALEAAEYGVRINAVAPSI------AMHPFLAKvtsaelldELAAR-EAFGRAAEPWEVANVIAFLASDYS 247

                        250
                 ....*....|...
gi 896156623 435 LGVNGHVLRVCGQ 447
Cdd:PRK07831 248 SYLTGEVVSVSSQ 260
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 213-442 1.34e-28

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 112.46  E-value: 1.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANElGGLALQQDITADDAGNAIADAAVARYGRLDIVIH 292
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGG-DVEAVPYDARDPEDARALVDALRDRFGRIDVLVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 293 NAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAY 372
Cdd:cd08932   80 NAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHAL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 373 AEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNslqqggQPGDVAQAIAFLVSDRALGVNGHVL 442
Cdd:cd08932  160 RQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAFPPEEMI------QPKDIANLVRMVIELPENITSVAVL 223
PRK09242 PRK09242
SDR family oxidoreductase;
210-446 1.69e-28

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 112.92  E-value: 1.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI-----DVPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARY 284
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVardadALAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDHW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK09242  87 DGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKAA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI--------PFVNRQVARRVnslqqgGQPGDVAQAIAFLVSDRALG 436
Cdd:PRK09242 167 LLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPlsdpdyyeQVIERTPMRRV------GEPEEVAAAVAFLCMPAASY 240

                        250
                 ....*....|
gi 896156623 437 VNGHVLRVCG 446
Cdd:PRK09242 241 ITGQCIAVDG 250
PRK06484 PRK06484
short chain dehydrogenase; Validated
 212-446 1.79e-28

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 117.64  E-value: 1.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPqaGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRN--VERARERADSLGPdhHALAMDVSDEAQIREGFEQLHREFGRIDV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDA--KWGSVIAVNIESQLKMNEQLLNHKAFEK-APRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:PRK06484  83 LVNNAGVTDPTMTATLDTTleEFARLQAINLTGAYLVAREALRLMIEQGhGAAIVNVASGAGLVALPKRTAYSASKAAVI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIP---FVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLR 443
Cdd:PRK06484 163 SLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELEragKLDPSAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGSTLV 242


                 ...
gi 896156623 444 VCG 446
Cdd:PRK06484 243 VDG 245
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 212-446 1.79e-28

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 112.85  E-value: 1.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQ--AGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLeeAAKSTIQEISEAGYnaVAVGADVTDKDDVEALIDQAVEKFGSF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQL-KMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:cd05366   82 DVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLfGIQAAARQFKKLGHGGKIINASSIAGVQGFPNLGAYSASKFAVR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIpfvNRQVARRVNSLQQGG--------------QPGDVAQAIAFLVSD 432
Cdd:cd05366  162 GLTQTAAQELAPKGITVNAYAPGIVKTEMWDYI---DEEVGEIAGKPEGEGfaefsssiplgrlsEPEDVAGLVSFLASE 238

                        250
                 ....*....|....
gi 896156623 433 RALGVNGHVLRVCG 446
Cdd:cd05366  239 DSDYITGQTILVDG 252
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
210-439 2.38e-28

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 112.59  E-value: 2.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqaGEALSKVANELGG-----LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDI---SPEIEKLADELCGrghrcTAVVADVRDPASVAAAIKRAKEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSG-IAGNRGQTNYATSKA 363
Cdd:PRK08226  81 GRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYALTKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPF---------VNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRA 434
Cdd:PRK08226 161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARqsnpedpesVLTEMAKAI-PLRRLADPLEVGELAAFLASDES 239


                 ....*
gi 896156623 435 LGVNG 439
Cdd:PRK08226 240 SYLTG 244
PRK07774 PRK07774
SDR family oxidoreductase;
210-450 6.16e-28

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 111.37  E-value: 6.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEALSKVANELGGLAL--QQDITADDAGNAIADAAVARYGR 286
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADInAEGAERVAKQIVADGGTAIavQVDVSDPDSAKAMADATVSAFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRD---KMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTsgiAGNRGQTNYATSKA 363
Cdd:PRK07774  84 IDYLVNNAAIYGGmklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSST---AAWLYSNFYGLAKV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFVNRQVARRVnsLQQGGQPGDVAQAIAFLVSDRALGVNGH 440
Cdd:PRK07774 161 GLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVtpkEFVADMVKGIP--LSRMGTPEDLVGMCLFLLSDEASWITGQ 238

                        250
                 ....*....|
gi 896156623 441 VLRVCGQNIV 450
Cdd:PRK07774 239 IFNVDGGQII 248
PRK06398 PRK06398
aldose dehydrogenase; Validated
 210-446 7.44e-28

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 111.08  E-value: 7.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVanelgglaLQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDY--------FKVDVSNKEQVIKGIDYVISKYGRIDI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMV 369
Cdd:PRK06398  76 LVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVLGLT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 370 EAYAEEFAKRgGNINAVAPGFIETDMT--AAIPFVNR---QVARRVNS------LQQGGQPGDVAQAIAFLVSDRALGVN 438
Cdd:PRK06398 156 RSIAVDYAPT-IRCVAVCPGSIRTPLLewAAELEVGKdpeHVERKIREwgemhpMKRVGKPEEVAYVVAFLASDLASFIT 234


                 ....*...
gi 896156623 439 GHVLRVCG 446
Cdd:PRK06398 235 GECVTVDG 242
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 210-446 7.48e-28

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 110.66  E-value: 7.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEA-----LSKVANELGGLalqqDITADDAGNAIADAAVARY 284
Cdd:PRK12828   5 LQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSqtlpgVPADALRIGGI----DLVDPQAARRAVDEVNRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK12828  81 GRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAA-IPfvNRQVARRVnslqqggQPGDVAQAIAFLVSDRALGVNGHVLR 443
Cdd:PRK12828 161 VARLTEALAAELLDRGITVNAVLPSIIDTPPNRAdMP--DADFSRWV-------TPEQIAAVIAFLLSDEAQAITGASIP 231


                 ...
gi 896156623 444 VCG 446
Cdd:PRK12828 232 VDG 234
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 208-439 2.82e-27

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 109.71  E-value: 2.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEAlskVANELGGLAL--QQDITADDAGNAIADAAVARY 284
Cdd:PRK08265   2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIdADNGAA---VAASLGERARfiATDITDDAAIERAVATVVARF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANmDDAKWGSVIAVNIESQLkmneqLLNHKAFEKAPR----IATMASTSGIAGNRGQTNYAT 360
Cdd:PRK08265  79 GRVDILVNLACTYLDDGLAS-SRADWLAALDVNLVSAA-----MLAQAAHPHLARgggaIVNFTSISAKFAQTGRWLYPA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNS----LQQGGQPGDVAQAIAFLVSDRALG 436
Cdd:PRK08265 153 SKAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSGGDRAKADRVAApfhlLGRVGDPEEVAQVVAFLCSDAASF 232


                 ...
gi 896156623 437 VNG 439
Cdd:PRK08265 233 VTG 235
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 213-396 3.50e-27

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 108.48  E-value: 3.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVI---DVPQAGEALSKVANE-LGGLALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGTVILtarDVERGQAAVEKLRAEgLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRDKM-FANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIagnrGQTNYATSKAGVIA 367
Cdd:cd05324   81 ILVNNAGIAFKGFdDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGS----LTSAYGVSKAALNA 156

                        170       180
                 ....*....|....*....|....*....
gi 896156623 368 MVEAYAEEFAKRGGNINAVAPGFIETDMT 396
Cdd:cd05324  157 LTRILAKELKETGIKVNACCPGWVKTDMG 185
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 212-446 3.59e-27

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 109.30  E-value: 3.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQA-GEALSKVanELGGLALQQDITADDAGNAIADAAVARYGRLDIV 290
Cdd:cd05371    2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSpGETVAKL--GDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 291 IHNAGIT-------RDKMFANMDDaKWGSVIAVNI----------ESQLKMNEQLLNhkaFEKAPRIATmASTSGIAGNR 353
Cdd:cd05371   80 VNCAGIAvaaktynKKGQQPHSLE-LFQRVINVNLigtfnvirlaAGAMGKNEPDQG---GERGVIINT-ASVAAFEGQI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 354 GQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIP-FVNRQVARRVNSLQQGGQPGDVAQAIAFLVSD 432
Cdd:cd05371  155 GQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPeKVRDFLAKQVPFPSRLGDPAEYAHLVQHIIEN 234

                        250
                 ....*....|....
gi 896156623 433 RALgvNGHVLRVCG 446
Cdd:cd05371  235 PYL--NGEVIRLDG 246
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 210-439 7.51e-27

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 108.44  E-value: 7.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-----PQAGEALSKVANELGGLALqqDITADDAGNAIADAAVARY 284
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLndeaaAAAAEALQKAGGKAIGVAM--DVTDEEAINAGIDYAVETF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK12429  80 GGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETdmtaaiPFVNRQVARRVNSLQ------------------QGGQPGDVAQAI 426
Cdd:PRK12429 160 LIGLTKVVALEGATHGVTVNAICPGYVDT------PLVRKQIPDLAKERGiseeevledvllplvpqkRFTTVEEIADYA 233

                        250
                 ....*....|...
gi 896156623 427 AFLVSDRALGVNG 439
Cdd:PRK12429 234 LFLASFAAKGVTG 246
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 211-439 1.72e-26

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 107.17  E-value: 1.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 211 AGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANELGGLALQQDITADDAgnaiADAAVARYGRLDIV 290
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDI--NEEKLKELERGPGITTRVLDVTDKEQ----VAALAKEEGRIDVL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 291 IHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMAS-TSGIAGNRGQTNYATSKAGVIAMV 369
Cdd:cd05368   75 FNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSvASSIKGVPNRFVYSTTKAAVIGLT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 370 EAYAEEFAKRGGNINAVAPGFIETDM------------TAAIPFVNRQVARRVnslqqgGQPGDVAQAIAFLVSDRALGV 437
Cdd:cd05368  155 KSVAADFAQQGIRCNAICPGTVDTPSleeriqaqpdpeEALKAFAARQPLGRL------ATPEEVAALAVYLASDESAYV 228


                 ..
gi 896156623 438 NG 439
Cdd:cd05368  229 TG 230
PRK06484 PRK06484
short chain dehydrogenase; Validated
 180-446 2.62e-26

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 111.48  E-value: 2.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 180 FLSGRSAFIDGQFLRVTSDAGEIPSDWDKPLA--GKVAAVTGSARGIGAAIARQLKADGAEVIVIDvpQAGEALSKVANE 257
Cdd:PRK06484 235 YITGSTLVVDGGWTVYGGSGPASTAQAPSPLAesPRVVAITGGARGIGRAVADRFAAAGDRLLIID--RDAEGAKKLAEA 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 258 LGG--LALQQDITADDAGNAIADAAVARYGRLDIVIHNAGITrDKMFANMDDA--KWGSVIAVNIESQLKMNEQLLNhkA 333
Cdd:PRK06484 313 LGDehLSVQADITDEAAVESAFAQIQARWGRLDVLVNNAGIA-EVFKPSLEQSaeDFTRVYDVNLSGAFACARAAAR--L 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 334 FEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNR----QVARR 409
Cdd:PRK06484 390 MSQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLALKASGRadfdSIRRR 469

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 896156623 410 VnSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK06484 470 I-PLGRLGDPEEVAEAIAFLASPAASYVNGATLTVDG 505
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 210-446 4.03e-26

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 106.47  E-value: 4.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQ-AGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGR 286
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINAdAANHVVDEIQQLGGqaFACRCDITSEQELSALADFALSKLGK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMF-ANMDDAKWGsvIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:PRK06113  89 VDILVNNAGGGGPKPFdMPMADFRRA--YELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI--PFVNRQVARRvNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLR 443
Cdd:PRK06113 167 SHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVitPEIEQKMLQH-TPIRRLGQPQDIANAALFLCSPAASWVSGQILT 245


                 ...
gi 896156623 444 VCG 446
Cdd:PRK06113 246 VSG 248
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
210-446 4.23e-26

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 106.11  E-value: 4.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKV-ANELGGLALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPTETIEQVtALGRRFLSLTADLRKIDGIPALLERAVAEFGHID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNH-KAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:PRK08993  88 ILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHfIAQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 368 MVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQG--GQPGDVAQAIAFLVSDRALGVNGHVLRVC 445
Cdd:PRK08993 168 VTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEILDRIPAGrwGLPSDLMGPVVFLASSASDYINGYTIAVD 247


                 .
gi 896156623 446 G 446
Cdd:PRK08993 248 G 248
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 213-449 4.25e-26

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 105.85  E-value: 4.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDV---PQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRnenPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDK--MFANMDDAKWGSVIAVNIES-----QLKMneQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSK 362
Cdd:cd05323   81 LINNAGILDEKsyLFAGKLPPPWEKTIDVNLTGvinttYLAL--HYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYA-EEFAKRGGNINAVAPGFIETDMTAAIPF--VNRQVARRVNSlqqggqPGDVAQAIAFLVSDRALgvNG 439
Cdd:cd05323  159 HGVVGFTRSLAdLLEYKTGVRVNAICPGFTNTPLLPDLVAkeAEMLPSAPTQS------PEVVAKAIVYLIEDDEK--NG 230

                        250
                 ....*....|
gi 896156623 440 HVLRVCGQNI 449
Cdd:cd05323  231 AIWIVDGGKL 240
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 209-399 6.53e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 106.59  E-value: 6.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAgeALSKVANELGG----LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEA--ELAALAAELGGddrvLTVVADVTDLAAMQAAAEEAVERF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHkAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK05872  84 GGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPA-LIERRGYVLQVSSLAAFAAAPGMAAYCASKAG 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI 399
Cdd:PRK05872 163 VEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDA 197
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 212-446 6.75e-26

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 105.99  E-value: 6.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGG-----LALQQDITADDAGNAIADAAVARYGR 286
Cdd:cd08940    2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKhgvkvLYHGADLSKPAAIEDMVAYAQRQFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:cd08940   82 VDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDM----------TAAIPF--VNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRA 434
Cdd:cd08940  162 GLTKVVALETAGTGVTCNAICPGWVLTPLvekqisalaqKNGVPQeqAARELLLEKQPSKQFVTPEQLGDTAVFLASDAA 241

                        250
                 ....*....|..
gi 896156623 435 LGVNGHVLRVCG 446
Cdd:cd08940  242 SQITGTAVSVDG 253
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 210-446 1.39e-25

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 104.84  E-value: 1.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELG--GL---ALQQDITADDAGNAIADAAVARY 284
Cdd:cd05329    4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYT--CARNQKELDECLTEWRekGFkveGSVCDVSSRSERQELMDTVASHF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 -GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEqlLNH---KAFEKApRIATMASTSGIAGNRGQTNYAT 360
Cdd:cd05329   82 gGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSR--LAHpllKASGNG-NIVFISSVAGVIAVPSGAPYGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI--------PFVNRQVARRVnslqqgGQPGDVAQAIAFLVSD 432
Cdd:cd05329  159 TKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPViqqkenldKVIERTPLKRF------GEPEEVAALVAFLCMP 232

                        250
                 ....*....|....
gi 896156623 433 RALGVNGHVLRVCG 446
Cdd:cd05329  233 AASYITGQIIAVDG 246
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 204-446 1.42e-25

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 105.09  E-value: 1.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 204 SDWDKpLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVanelggLALQQDITADDAGNAIADAAVAR 283
Cdd:PRK06171   2 QDWLN-LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQHENY------QFVPTDVSSAEEVNHTVAEIIEK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITRDKMFAN---------MDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRG 354
Cdd:PRK06171  75 FGRIDGLVNNAGINIPRLLVDekdpagkyeLNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 355 QTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIE-TDM-----TAAIPFVNRQVARRVNS---------LQQGGQP 419
Cdd:PRK06171 155 QSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEaTGLrtpeyEEALAYTRGITVEQLRAgytktstipLGRSGKL 234

                        250       260
                 ....*....|....*....|....*..
gi 896156623 420 GDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK06171 235 SEVADLVCYLLSDRASYITGVTTNIAG 261
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 210-431 1.71e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 104.42  E-value: 1.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIV---IDVPQAGEALSKVANELG-GLALQQDITADDAGNAIADAAVARYG 285
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVnakKRAEEMNETLKMVKENGGeGIGVLADVSTREGCETLAKATIDRYG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLlnHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:PRK06077  84 VADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQEL--AKEMREGGAIVNIASVAGIRPAYGLSIYGAMKAAV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRgGNINAVAPGFIETDMTAAIPFV----NRQVARRVNSLQQGGQPGDVAQAIAFLVS 431
Cdd:PRK06077 162 INLTKYLALELAPK-IRVNAIAPGFVKTKLGESLFKVlgmsEKEFAEKFTLMGKILDPEEVAEFVAAILK 230
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 210-439 1.73e-25

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 104.98  E-value: 1.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAG-EALSKVANELGGLA--LQQDITADDAGNAIADAAVARYGR 286
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGaNAVADEINKAGGKAigVAMDVTNEDAVNAGIDKVAERFGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEK-APRIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:PRK13394  85 VDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrGGVVIYMGSVHSHEASPLKSAYVTAKHGL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETdmtaaiPFVNRQV---ARR--------VNSLQQGGQPG-------DVAQAIA 427
Cdd:PRK13394 165 LGLARVLAKEGAKHNVRSHVVCPGFVRT------PLVDKQIpeqAKElgiseeevVKKVMLGKTVDgvfttveDVAQTVL 238

                        250
                 ....*....|..
gi 896156623 428 FLVSDRALGVNG 439
Cdd:PRK13394 239 FLSSFPSAALTG 250
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 213-446 2.84e-25

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 104.14  E-value: 2.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAG-----EALSKVANELGGLALQQDITADDAGNAIADAAVARYGRL 287
Cdd:cd05330    4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGleaakAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFGRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGIT-RDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:cd05330   84 DGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMTA-AIPFVN----RQVARR---VNSLQQGGQPGDVAQAIAFLVSDRALGVN 438
Cdd:cd05330  164 GLTRNSAVEYGQYGIRINAIAPGAILTPMVEgSLKQLGpenpEEAGEEfvsVNPMKRFGEPEEVAAVVAFLLSDDAGYVN 243


                 ....*...
gi 896156623 439 GHVLRVCG 446
Cdd:cd05330  244 AAVVPIDG 251
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
210-448 3.72e-25

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 103.57  E-value: 3.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANELG--GLALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADI--KPARARLAALEIGpaAIAVSLDVTRQDSIDRIVAAAVERFGGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHK-AFEKAPRIATMASTsgiAGNRGQ---TNYATSKA 363
Cdd:PRK07067  82 DILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMvEQGRGGKIINMASQ---AGRRGEalvSHYCATKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAipfVNRQVARRVNsLQQG---------------GQPGDVAQAIAF 428
Cdd:PRK07067 159 AVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQ---VDALFARYEN-RPPGekkrlvgeavplgrmGVPDDLTGMALF 234

                        250       260
                 ....*....|....*....|
gi 896156623 429 LVSDRALGVNGHVLRVCGQN 448
Cdd:PRK07067 235 LASADADYIVAQTYNVDGGN 254
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 210-446 3.83e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 103.50  E-value: 3.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGG-----LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVL--AARTAERLDEVAAEIDDlgrraLAVPTDITDEDQCANLVALALERF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNA-GITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAfEKAPRIATMASTSGIAGNRGQTNYATSKA 363
Cdd:PRK07890  81 GRVDALVNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALA-ESGGSIVMINSMVLRHSQPKYGAYKMAKG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAipFVNRQVARRVNSLQQGGQ-------------PGDVAQAIAFLV 430
Cdd:PRK07890 160 ALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKG--YFRHQAGKYGVTVEQIYAetaansdlkrlptDDEVASAVLFLA 237

                        250
                 ....*....|....*..
gi 896156623 431 SDRALGVNGHVLRV-CG 446
Cdd:PRK07890 238 SDLARAITGQTLDVnCG 254
PRK06114 PRK06114
SDR family oxidoreductase;
210-446 5.36e-25

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 103.32  E-value: 5.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGeALSKVAN---ELGGLALQqdITADDAGNAIADAAVAR--- 283
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDD-GLAETAEhieAAGRRAIQ--IAADVTSKADLRAAVARtea 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 -YGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIES-----QLKMNEQLLNHKAfekapRIATMASTSGIAGNRG--Q 355
Cdd:PRK06114  83 eLGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGvflscQAEARAMLENGGG-----SIVNIASMSGIIVNRGllQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 356 TNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAiPFVNRQVA--RRVNSLQQGGQPGDVAQAIAFLVSDR 433
Cdd:PRK06114 158 AHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTR-PEMVHQTKlfEEQTPMQRMAKVDEMVGPAVFLLSDA 236

                        250
                 ....*....|...
gi 896156623 434 ALGVNGHVLRVCG 446
Cdd:PRK06114 237 ASFCTGVDLLVDG 249
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 210-446 6.06e-25

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 102.87  E-value: 6.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI--------DVPQAGEALSKVANELggLALQQDITADDAGNAIADAAV 281
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTgrdaerleETRQSCLQAGVSEKKI--LLVVADLTEEEGQDRIISTTL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKApRIATMASTSGIAGNRGQTNYATS 361
Cdd:cd05364   79 AKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKG-EIVNVSSVAGGRSFPGVLYYCIS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQG------GQPGDVAQAIAFLVSDRAL 435
Cdd:cd05364  158 KAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMPEEQYIKFLSRAKEThplgrpGTVDEVAEAIAFLASDASS 237

                        250
                 ....*....|.
gi 896156623 436 GVNGHVLRVCG 446
Cdd:cd05364  238 FITGQLLPVDG 248
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 213-446 6.41e-25

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 102.92  E-value: 6.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIViDVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDIV 290
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVV-NYYRSTESAEAVAAEAGEraIAIQADVRDRDQVQAMIEEAKNHFGPVDTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 291 IHNAgiTRDKMFANM-----DDAKW---GSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSK 362
Cdd:cd05349   80 VNNA--LIDFPFDPDqrktfDTIDWedyQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGFI-ETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHV 441
Cdd:cd05349  158 AALLGFTRNMAKELGPYGITVNMVSGGLLkVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQN 237


                 ....*
gi 896156623 442 LRVCG 446
Cdd:cd05349  238 LVVDG 242
PRK07035 PRK07035
SDR family oxidoreductase;
210-446 7.60e-25

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 102.79  E-value: 7.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANEL---GGLA--LQQDITADDAGNAIADAAVARY 284
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIV--SSRKLDGCQAVADAIvaaGGKAeaLACHIGEMEQIDALFAHIRERH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGItrDKMFANM---DDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATS 361
Cdd:PRK07035  84 GRLDILVNNAAA--NPYFGHIldtDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSIT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIpFVNRQVARRVNS---LQQGGQPGDVAQAIAFLVSDRALGVN 438
Cdd:PRK07035 162 KAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASAL-FKNDAILKQALAhipLRRHAEPSEMAGAVLYLASDASSYTT 240


                 ....*...
gi 896156623 439 GHVLRVCG 446
Cdd:PRK07035 241 GECLNVDG 248
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 212-446 7.72e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 102.35  E-value: 7.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqagEALSKVANELGglALQQDITADdagnaiADAAVARYGRLDIVI 291
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDK----QDKPDLSGNFH--FLQLDLSDD------LEPLFDWVPSVDILC 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 292 HNAGITRD-KMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVE 370
Cdd:PRK06550  73 NTAGILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGFTK 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896156623 371 AYAEEFAKRGGNINAVAPGFIETDMTAAiPFVNRQVARRVNSLQQGG---QPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK06550 153 QLALDYAKDGIQVFGIAPGAVKTPMTAA-DFEPGGLADWVARETPIKrwaEPEEVAELTLFLASGKADYMQGTIVPIDG 230
PRK07074 PRK07074
SDR family oxidoreductase;
213-446 7.83e-25

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 102.93  E-value: 7.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPqaGEALSKVANELGG---LALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDID--AAALAAFADALGDarfVPVACDLTDAASLAAALANAAAERGPVDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGnRGQTNYATSKAGVIAMV 369
Cdd:PRK07074  81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAA-LGHPAYSAAKAGLIHYT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 370 EAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQV---ARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRV-C 445
Cdd:PRK07074 160 KLLAVEYGRFGIRANAVAPGTVKTQAWEARVAANPQVfeeLKKWYPLQDFATPDDVANAVLFLASPAARAITGVCLPVdG 239


                 .
gi 896156623 446 G 446
Cdd:PRK07074 240 G 240
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 214-446 9.06e-25

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 102.54  E-value: 9.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 214 VAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAgEALSKVANEL-----GGLALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDD-DQATEVVAEVlaagrRAIYFQADIGELSDHEALLDQAWEDFGRLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGIT----RDKMFANMDDakWGSVIAVNIE-----SQ---LKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQt 356
Cdd:cd05337   82 CLVNNAGIAvrprGDLLDLTEDS--FDRLIAINLRgpfflTQavaRRMVEQPDRFDGPHRSIIFVTSINAYLVSPNRGE- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 357 nYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTA-AIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRAL 435
Cdd:cd05337  159 -YCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTApVKEKYDELIAAGLVPIRRWGQPEDIAKAVRTLASGLLP 237

                        250
                 ....*....|.
gi 896156623 436 GVNGHVLRVCG 446
Cdd:cd05337  238 YSTGQPINIDG 248
PRK07069 PRK07069
short chain dehydrogenase; Validated
 215-446 1.19e-24

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 102.10  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 215 AAVTGSARGIGAAIARQLKADGAEVIVIDVpQAGEALSKVANELGG-------LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDI-NDAAGLDAFAAEINAahgegvaFAAVQDVTDEAQWQALLAQAADAMGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:PRK07069  81 SVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 368 MVEAYAEEFAKRGGNI--NAVAPGFIETDMTAAI------PFVNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRALGVNG 439
Cdd:PRK07069 161 LTKSIALDCARRGLDVrcNSIHPTFIRTGIVDPIfqrlgeEEATRKLARGV-PLGRLGEPDDVAHAVLYLASDESRFVTG 239


                 ....*..
gi 896156623 440 HVLRVCG 446
Cdd:PRK07069 240 AELVIDG 246
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 211-446 1.57e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 101.72  E-value: 1.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 211 AGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAgeALSKVANELGGLALQQDITADDAgnaiADAAVARYGRLDIV 290
Cdd:PRK07060   8 SGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAA--ALDRLAGETGCEPLRLDVGDDAA----IRAALAAAGAFDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 291 IHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhKAFEKAPRIATMASTSGIAGNRGQTN---YATSKAGVIA 367
Cdd:PRK07060  82 VNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVA--RAMIAAGRGGSIVNVSSQAALVGLPDhlaYCASKAALDA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 368 MVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PfVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRV 444
Cdd:PRK07060 160 ITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAwsdP-QKSGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLPV 238


                 ..
gi 896156623 445 CG 446
Cdd:PRK07060 239 DG 240
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 207-446 1.78e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 101.90  E-value: 1.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 207 DKPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIdvpqageALSKVANELGGLA-LQQDITADDAGNAIADAAVARYG 285
Cdd:PRK06523   4 FLELAGKRALVTGGTKGIGAATVARLLEAGARVVTT-------ARSRPDDLPEGVEfVAADLTTAEGCAAVARAVLERLG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKM--FANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSG-IAGNRGQTNYATSK 362
Cdd:PRK06523  77 GVDILVHVLGGSSAPAggFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRrLPLPESTTAYAAAK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGFIETdmTAAIPFVNR---------QVARRVNSLQQGG-------QPGDVAQAI 426
Cdd:PRK06523 157 AALSTYSKSLSKEVAPKGVRVNTVSPGWIET--EAAVALAERlaeaagtdyEGAKQIIMDSLGGiplgrpaEPEEVAELI 234

                        250       260
                 ....*....|....*....|
gi 896156623 427 AFLVSDRALGVNGHVLRVCG 446
Cdd:PRK06523 235 AFLASDRAASITGTEYVIDG 254
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 210-431 1.90e-24

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 101.46  E-value: 1.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANEL---GG--LALQQDITADDAGNAIADAAVARY 284
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAI--AARRVDRLEALADELeaeGGkaLVLELDVTDEQQVDAAVERTVEAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:cd08934   79 GRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFG 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVA--RRVNSLQQgGQPGDVAQAIAFLVS 431
Cdd:cd08934  159 VNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAyeERISTIRK-LQAEDIAAAVRYAVT 226
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 214-446 2.07e-24

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 101.11  E-value: 2.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 214 VAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANE---LGG--LALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADL--KSEGAEAVAAAiqqAGGqaIGLECNVTSEQDLEAVVKATVSQFGGIT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRDKMFA-NMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:cd05365   79 ILVNNAGGGGPKPFDmPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 368 MVEAYAEEFAKRGGNINAVAPGFIETDM--TAAIPFVNRQVARRvNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVC 445
Cdd:cd05365  159 MTRNLAFDLGPKGIRVNAVAPGAVKTDAlaSVLTPEIERAMLKH-TPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVS 237


                 .
gi 896156623 446 G 446
Cdd:cd05365  238 G 238
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
209-446 2.19e-24

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 101.33  E-value: 2.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAEvIVIDVPQAGEALSKVANELGGL-----ALQQDITADDAGNAIADAAVAR 283
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYD-IAVNYARSRKAAEETAEEIEALgrkalAVKANVGDVEKIKEMFAQIDEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNA--GITRDKMfaNMDDAKWGSVIAVNIESqlkmneqlLNHKAFEKAPRI-----ATMASTSGIAGNRGQT 356
Cdd:PRK08063  80 FGRLDVFVNNAasGVLRPAM--ELEESHWDWTMNINAKA--------LLFCAQEAAKLMekvggGKIISLSSLGSIRYLE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 357 NYAT---SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDmtAAIPFVNRQ----VARRVNSLQQGGQPGDVAQAIAFL 429
Cdd:PRK08063 150 NYTTvgvSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTD--ALKHFPNREelleDARAKTPAGRMVEPEDVANAVLFL 227

                        250
                 ....*....|....*..
gi 896156623 430 VSDRALGVNGHVLRVCG 446
Cdd:PRK08063 228 CSPEADMIRGQTIIVDG 244
PRK07577 PRK07577
SDR family oxidoreductase;
213-446 2.27e-24

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 100.96  E-value: 2.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIdvpqAGEALSKVANELgglaLQQDItADDAGNAIADAAVARYGRLDIVIH 292
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGI----ARSAIDDFPGEL----FACDL-ADIEQTAATLAQINEIHPVDAIVN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 293 NAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSgIAGNRGQTNYATSKAGVIAMVEAY 372
Cdd:PRK07577  75 NVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-IFGALDRTSYSAAKSALVGCTRTW 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896156623 373 AEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNS---LQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK07577 154 ALELAEYGITVNAVAPGPIETELFRQTRPVGSEEEKRVLAsipMRRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDG 230
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 210-446 5.46e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 100.39  E-value: 5.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANEL---GG--LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVV--GARRQAELDQLVAEIraeGGeaVALAGDVRDEAYAKALVALAVERF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRD-KMFANMDDAKWGSVIAVNIESqlkmneqllnhkAFEKAP-RIATMASTSG------------IA 350
Cdd:PRK07478  82 GGLDIAFNNAGTLGEmGPVAEMSLEGWRETLATNLTS------------AFLGAKhQIPAMLARGGgsliftstfvghTA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 351 GNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMT---AAIPFVnRQVARRVNSLQQGGQPGDVAQAIA 427
Cdd:PRK07478 150 GFPGMAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGramGDTPEA-LAFVAGLHALKRMAQPEEIAQAAL 228

                        250
                 ....*....|....*....
gi 896156623 428 FLVSDRALGVNGHVLRVCG 446
Cdd:PRK07478 229 FLASDAASFVTGTALLVDG 247
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 208-446 6.63e-24

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 100.19  E-value: 6.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIV---IDVPQAGEALSKVANELG-GLALQQDITADDAGNAIADAAVAR 283
Cdd:PRK08936   3 SDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVInyrSDEEEANDVAEEIKKAGGeAIAVKGDVTVESDVVNLIQTAVKE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQ-LKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSK 362
Cdd:PRK08936  83 FGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAfLGSREAIKYFVEHDIKGNIINMSSVHEQIPWPLFVHYAASK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQG--GQPGDVAQAIAFLVSDRALGVNGH 440
Cdd:PRK08936 163 GGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRADVESMIPMGyiGKPEEIAAVAAWLASSEASYVTGI 242


                 ....*.
gi 896156623 441 VLRVCG 446
Cdd:PRK08936 243 TLFADG 248
PRK06500 PRK06500
SDR family oxidoreductase;
210-434 6.76e-24

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 100.03  E-value: 6.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAgeALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPA--SLEAARAELGEsaLVIRADAGDVAAQKALAQALAEAFGRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:PRK06500  82 DAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALL--PLLANPASIVLNGSINAHIGMPNSSVYAASKAALLS 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156623 368 MVEAYAEEFAKRGGNINAVAPGFIETDM-------TAAIPFVNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRA 434
Cdd:PRK06500 160 LAKTLSGELLPRGIRVNAVSPGPVQTPLygklglpEATLDAVAAQIQALV-PLGRFGTPEEIAKAVLYLASDES 232
PRK09135 PRK09135
pteridine reductase; Provisional
 208-446 8.74e-24

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 99.62  E-value: 8.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEViVIDVPQAGEALSKVANELGGL------ALQQDITADDAGNAIADAAV 281
Cdd:PRK09135   2 MTDSAKVALITGGARRIGAAIARTLHAAGYRV-AIHYHRSAAEADALAAELNALrpgsaaALQADLLDPDALPELVAACV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIesqlkmneqllnhkafeKAPRIATMASTSGIAGNRG------- 354
Cdd:PRK09135  81 AAFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNL-----------------KAPFFLSQAAAPQLRKQRGaivnitd 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 355 ---------QTNYATSKAGVIAMVEAYAEEFAKRgGNINAVAPGFIE-TDMTAAIPFVNRQvaRRVNS--LQQGGQPGDV 422
Cdd:PRK09135 144 ihaerplkgYPVYCAAKAALEMLTRSLALELAPE-VRVNAVAPGAILwPEDGNSFDEEARQ--AILARtpLKRIGTPEDI 220

                        250       260
                 ....*....|....*....|....
gi 896156623 423 AQAIAFLVSDrALGVNGHVLRVCG 446
Cdd:PRK09135 221 AEAVRFLLAD-ASFITGQILAVDG 243
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 210-446 1.05e-23

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 99.58  E-value: 1.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI--DVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYG 285
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAgrKPEVLEAAAEEISSATGGraHPIQCDVRDPEAVEAAVDETLKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNH-KAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:cd05369   81 KIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRlIEAKHGGSILNISATYAYTGSPFQVHSAAAKAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETD--MTAAIP-FVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHV 441
Cdd:cd05369  161 VDALTRSLAVEWGPYGIRVNAIAPGPIPTTegMERLAPsGKSEKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTT 240


                 ....*
gi 896156623 442 LRVCG 446
Cdd:cd05369  241 LVVDG 245
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 213-441 2.47e-23

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 98.46  E-value: 2.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVI-----VIDVPQAGEALSkvaneLGGLALQQDITADDAGNAIADAAVARYGRL 287
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIatarnPDKLESLGELLN-----DNLEVLELDVTDEESIKAAVKEVIERFGRI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:cd05374   76 DVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 368 MVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQV--------------ARRVNSLQQGGQPGDVAQAIAFLVSDR 433
Cdd:cd05374  156 LSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDpeispyaperkeikENAAGVGSNPGDPEKVADVIVKALTSE 235


                 ....*...
gi 896156623 434 ALGVNGHV 441
Cdd:cd05374  236 SPPLRYFL 243
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 208-442 3.41e-23

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 98.22  E-value: 3.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSAR--GIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGGLALQQ--------------DITADD 271
Cdd:PRK12748   1 LPLMKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPWGMHDKEPVLLKEeiesygvrcehmeiDLSQPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 272 AGNAIADAAVARYGRLDIVIHNAGITRDKMFANMD----DAKWgsviAVNIESQLKMNEQLLNHKAFEKAPRIATMASTS 347
Cdd:PRK12748  81 APNRVFYAVSERLGDPSILINNAAYSTHTRLEELTaeqlDKHY----AVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 348 GIAGNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGfiETDMTAAIPFVNRQVARRvnsLQQG--GQPGDVAQA 425
Cdd:PRK12748 157 SLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG--PTDTGWITEELKHHLVPK---FPQGrvGEPVDAARL 231

                        250
                 ....*....|....*..
gi 896156623 426 IAFLVSDRALGVNGHVL 442
Cdd:PRK12748 232 IAFLVSEEAKWITGQVI 248
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 217-452 4.49e-23

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 97.54  E-value: 4.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELgglaLQQDITADDAGNAIADAAVARYGRLDIVIHNAGI 296
Cdd:cd05331    3 VTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRL----TPLDVADAAAVREVCSRLLAEHGPIDALVNCAGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 297 TRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAYAEEF 376
Cdd:cd05331   79 LRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLEL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 377 AKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNS----------LQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:cd05331  159 APYGVRCNVVSPGSTDTAMQRTLWHDEDGAAQVIAGvpeqfrlgipLGKIAQPADIANAVLFLASDQAGHITMHDLVVDG 238


                 ....*.
gi 896156623 447 QNIVGA 452
Cdd:cd05331  239 GATLGA 244
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
210-446 8.14e-23

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 96.90  E-value: 8.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVaNELGG--LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQV-EALGRkfHFITADLIQQKDIDSIVSQAVEVMGHI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQL----KMNEQLLNHKAFEKAPRIATMASTSGiaGNRgQTNYATSKA 363
Cdd:PRK12481  85 DILINNAGIIRRQDLLEFGNKDWDDVININQKTVFflsqAVAKQFVKQGNGGKIINIASMLSFQG--GIR-VPSYTASKS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFVNRQVARRVNSlQQGGQPGDVAQAIAFLVSDRALGVNGH 440
Cdd:PRK12481 162 AVMGLTRALATELSQYNINVNAIAPGYMATDNTAALradTARNEAILERIPA-SRWGTPDDLAGPAIFLSSSASDYVTGY 240


                 ....*.
gi 896156623 441 VLRVCG 446
Cdd:PRK12481 241 TLAVDG 246
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 210-446 9.69e-23

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 96.75  E-value: 9.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGGLALQQ-----DITADDAGNAIADAAVARY 284
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITA--ERAELAVAKLRQEGIKAhaapfNVTHKQEVEAAIEHIEKDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK08085  85 GPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIpfVNRQ-----VARRVNSlQQGGQPGDVAQAIAFLVSDRALGVNG 439
Cdd:PRK08085 165 VKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKAL--VEDEaftawLCKRTPA-ARWGDPQELIGAAVFLSSKASDFVNG 241


                 ....*..
gi 896156623 440 HVLRVCG 446
Cdd:PRK08085 242 HLLFVDG 248
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 213-446 1.33e-22

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 96.57  E-value: 1.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAgEALSKVANELGGL-----ALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDD-EELAATQQELRALgveviFFPADVADLSAHEAMLDAAQAAWGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGI---TRDKMFANMDDAkWGSVIAVNIESQLKMNEQLLNHKAFEKAPR------IATMASTSGIAG--NRGQt 356
Cdd:PRK12745  82 DCLVNNAGVgvkVRGDLLDLTPES-FDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIVFVSSVNAIMVspNRGE- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 357 nYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTA-AIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRAL 435
Cdd:PRK12745 160 -YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTApVTAKYDALIAKGLVPMPRWGEPEDVARAVAALASGDLP 238

                        250
                 ....*....|.
gi 896156623 436 GVNGHVLRVCG 446
Cdd:PRK12745 239 YSTGQAIHVDG 249
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 210-389 1.48e-22

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 96.31  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI-------------DVPQAGEALSKVANELGG--LALQQDITADDAGN 274
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAaktasegdngsakSLPGTIEETAEEIEAAGGqaLPIVVDVRDEDQVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 275 AIADAAVARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRG 354
Cdd:cd05338   81 ALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARG 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 896156623 355 QTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPG 389
Cdd:cd05338  161 DVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPS 195
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 212-448 1.52e-22

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 96.31  E-value: 1.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPraLGVQCDVTSEAQVQSAFEQAVLEFGGLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDAKWGSVIAVNIES-QLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAM 368
Cdd:cd08943   81 VVSNAGIATSSPIAETSLEDWNRSMDINLTGhFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 369 VEAYAEEFAKRGGNINAVAP-----GFIETDMTAAipfVNRQVARRV--------NSLQQGGQPGDVAQAIAFLVSDRAL 435
Cdd:cd08943  161 ARCLALEGGEDGIRVNTVNPdavfrGSKIWEGVWR---AARAKAYGLleeeyrtrNLLKREVLPEDVAEAVVAMASEDFG 237

                        250
                 ....*....|...
gi 896156623 436 GVNGHVLRVCGQN 448
Cdd:cd08943  238 KTTGAIVTVDGGN 250
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
212-446 2.08e-22

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 95.95  E-value: 2.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYnEETAQAAADKLSKDGGkaIAVKADVSDRDQVFAAVRQVVDTFGDLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNH-KAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:PRK08643  82 VVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAfKKLGHGGKIINATSQAGVVGNPELAVYSSTKFAVRG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 368 MVEAYAEEFAKRGGNINAVAPGFIETDMTAAIpfvNRQVARRVN--------------SLQQGGQPGDVAQAIAFLVSDR 433
Cdd:PRK08643 162 LTQTAARDLASEGITVNAYAPGIVKTPMMFDI---AHQVGENAGkpdewgmeqfakdiTLGRLSEPEDVANCVSFLAGPD 238

                        250
                 ....*....|...
gi 896156623 434 ALGVNGHVLRVCG 446
Cdd:PRK08643 239 SDYITGQTIIVDG 251
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 210-395 2.12e-22

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 95.53  E-value: 2.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGeaLSKVANELGGLALQQDI-TADDAGNAIADAAVAR----Y 284
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEEN--LKAVAEEVEAYGVKVVIaTADVSDYEEVTAAIEQlkneL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK07666  83 GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFG 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDM 395
Cdd:PRK07666 163 VLGLTESLMQEVRKHNIRVTALTPSTVATDM 193
PRK08589 PRK08589
SDR family oxidoreductase;
208-446 4.30e-22

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 95.62  E-value: 4.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGGLA--LQQDITADDAGNAIADAAVARYG 285
Cdd:PRK08589   2 KRLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIKSNGGKAkaYHVDISDEQQVKDFASEIKEQFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGItrDKMFANMDDAK---WGSVIAVNIESQLKMNEQLLNhKAFEKAPRIATMASTSGIAGNRGQTNYATSK 362
Cdd:PRK08589  82 RVDVLFNNAGV--DNAAGRIHEYPvdvFDKIMAVDMRGTFLMTKMLLP-LMMEQGGSIINTSSFSGQAADLYRSGYNAAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGFIET----------DMTAAIPFvnRQVARRVNSLQQGGQPGDVAQAIAFLVSD 432
Cdd:PRK08589 159 GAVINFTKSIAIEYGRDGIRANAIAPGTIETplvdkltgtsEDEAGKTF--RENQKWMTPLGRLGKPEEVAKLVVFLASD 236

                        250
                 ....*....|....
gi 896156623 433 RALGVNGHVLRVCG 446
Cdd:PRK08589 237 DSSFITGETIRIDG 250
PRK05650 PRK05650
SDR family oxidoreductase;
216-408 9.20e-22

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 94.34  E-value: 9.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 216 AVTGSARGIGAAIARQLKADGAEVIVIDVPQA-GEALSKVANELGGLALQQ--DITADDAGNAIADAAVARYGRLDIVIH 292
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEgGEETLKLLREAGGDGFYQrcDVRDYSQLTALAQACEEKWGGIDVIVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 293 NAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAY 372
Cdd:PRK05650  84 NAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETL 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 896156623 373 AEEFAKRGGNINAVAPGFIETD----MTAAIPFVNRQVAR 408
Cdd:PRK05650 164 LVELADDEIGVHVVCPSFFQTNlldsFRGPNPAMKAQVGK 203
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 210-442 9.57e-22

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 93.80  E-value: 9.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDvpQAGEALSKVANELGGLALQQDI---------TADDAgNAIADAA 280
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLG--RNEEKLRQVADHINEEGGRQPQwfildlltcTSENC-QQLAQRI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 281 VARYGRLDIVIHNAGITRDKM-FANMDDAKWGSVIAVNIESQLKMNEQLLnhkAFEKAPRIATMASTSGIAGNRGQTN-- 357
Cdd:cd05340   79 AVNYPRLDGVLHNAGLLGDVCpLSEQNPQVWQDV*QVNVNATFMLTQALL---PLLLKSDAGSLVFTSSSVGRQGRANwg 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 -YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDM-TAAIPFVNRQVARRvnslqqggqPGDVAQAIAFLVSDRAL 435
Cdd:cd05340  156 aYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMrASAFPTEDPQKLKT---------PADIMPLYLWLMGDDSR 226


                 ....*..
gi 896156623 436 GVNGHVL 442
Cdd:cd05340  227 RKTGMTF 233
PRK09730 PRK09730
SDR family oxidoreductase;
213-446 1.11e-21

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 93.76  E-value: 1.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIViDVPQAGEALSKVANEL---GG--LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAV-NYQQNLHAAQEVVNLItqaGGkaFVLQADISDENQVVAMFTAIDQHDEPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGIT-RDKMFANMDDAKWGSVIAVNIESQL---KMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQ-TNYATSK 362
Cdd:PRK09730  81 AALVNNAGILfTQCTVENLTAERINRVLSTNVTGYFlccREAVKRMALKHGGSGGAIVNVSSAASRLGAPGEyVDYAASK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRqvARRVNS---LQQGGQPGDVAQAIAFLVSDRALGVNG 439
Cdd:PRK09730 161 GAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGR--VDRVKSnipMQRGGQPEEVAQAIVWLLSDKASYVTG 238


                 ....*..
gi 896156623 440 HVLRVCG 446
Cdd:PRK09730 239 SFIDLAG 245
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 208-442 1.34e-21

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 93.70  E-value: 1.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSAR--GIGAAIARQLKADGAEV---------------IVIDVP-QAGEALSKVANELGGLALqqDITA 269
Cdd:PRK12859   2 NQLKNKVAVVTGVSRldGIGAAICKELAEAGADIfftywtaydkempwgVDQDEQiQLQEELLKNGVKVSSMEL--DLTQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 270 DDAGNAIADAAVARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGI 349
Cdd:PRK12859  80 NDAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 350 AGNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETD-MTAAIpfvnRQVARRVNSLQQGGQPGDVAQAIAF 428
Cdd:PRK12859 160 GPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGwMTEEI----KQGLLPMFPFGRIGEPKDAARLIKF 235

                        250
                 ....*....|....
gi 896156623 429 LVSDRALGVNGHVL 442
Cdd:PRK12859 236 LASEEAEWITGQII 249
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 210-446 2.63e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 93.20  E-value: 2.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGGLALQQ-----DITADDAGNAIADAAVARY 284
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQ--ELVDKGLAAYRELGIEAhgyvcDVTDEDGVQAMVSQIEKEV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK07097  86 GVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI----------PF----VNRQVARRvnslqqGGQPGDVAQAIAFLV 430
Cdd:PRK07097 166 LKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLrelqadgsrhPFdqfiIAKTPAAR------WGDPEDLAGPAVFLA 239

                        250
                 ....*....|....*.
gi 896156623 431 SDRALGVNGHVLRVCG 446
Cdd:PRK07097 240 SDASNFVNGHILYVDG 255
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 210-446 3.07e-21

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 92.54  E-value: 3.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGL----ALQQDITADDAGNAIADAAVARYG 285
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVII--SARKAEACADAAEELSAYgeciAIPADLSSEEGIEALVARVAERSD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLN----HKAFEKAPRIATMASTSGIAGNRGQT-NYAT 360
Cdd:cd08942   82 RLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPllraAATAENPARVINIGSIAGIVVSGLENySYGA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFVNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRALGV 437
Cdd:cd08942  162 SKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLlndPAALEAEEKSI-PLGRWGRPEDMAGLAIMLASRAGAYL 240


                 ....*....
gi 896156623 438 NGHVLRVCG 446
Cdd:cd08942  241 TGAVIPVDG 249
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 210-451 3.69e-21

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 92.74  E-value: 3.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANEL-----GGLALQQDITADDAGNAIADAAVARY 284
Cdd:cd05355   24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAEETKKLIeeegrKCLLIPGDLGDESFCRDLVKEVVKEF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKM-FANMDDAKWGSVIAVNIESQLKMNEQLLNHkaFEKAPRIATMASTSGIAGNRGQTNYATSKA 363
Cdd:cd05355  104 GKLDILVNNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPH--LKKGSSIINTTSVTAYKGSPHLLDYAATKG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDM-TAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVL 442
Cdd:cd05355  182 AIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLiPSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQDSSYVTGQVL 261


                 ....*....
gi 896156623 443 RVCGQNIVG 451
Cdd:cd05355  262 HVNGGEIIN 270
PRK06123 PRK06123
SDR family oxidoreductase;
213-446 4.80e-21

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 91.76  E-value: 4.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIV--IDVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLnyLRNRDAAEAVVQAIRRQGGeaLAVAADVADEADVLRLFEAVDRELGRLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRDKM-FANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTN----YATSKA 363
Cdd:PRK06123  83 ALVNNAGILEAQMrLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRGGAIVNVSSMAARLGSPGeyidYAASKG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRqvARRVNS---LQQGGQPGDVAQAIAFLVSDRALGVNGH 440
Cdd:PRK06123 163 AIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGR--VDRVKAgipMGRGGTAEEVARAILWLLSDEASYTTGT 240


                 ....*.
gi 896156623 441 VLRVCG 446
Cdd:PRK06123 241 FIDVSG 246
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 209-446 4.83e-21

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 92.21  E-value: 4.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGR 286
Cdd:cd08937    1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEILAAGDaaHVHTADLETYAGAQGVVRAAVERFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGIT-RDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRgqTNYATSKAGV 365
Cdd:cd08937   81 VDVLINNVGGTiWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGIYR--IPYSAAKGGV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIET----------DMTAAIP-----FVNRQVARRVnsLQQGGQPGDVAQAIAFLV 430
Cdd:cd08937  159 NALTASLAFEHARDGIRVNAVAPGGTEApprkiprnaaPMSEQEKvwyqrIVDQTLDSSL--MGRYGTIDEQVRAILFLA 236

                        250
                 ....*....|....*.
gi 896156623 431 SDRALGVNGHVLRVCG 446
Cdd:cd08937  237 SDEASYITGTVLPVGG 252
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 212-450 7.42e-21

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 91.24  E-value: 7.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAG-EALSKVANELGG---LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:cd08930    2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPAlEQLKEELTNLYKnrvIALELDITSKESIKELIESYLEKFGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGIT---RDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAG----NRGQTN--- 357
Cdd:cd08930   82 DILINNAYPSpkvWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIApdfrIYENTQmys 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 ---YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAipFVNRQvaRRVNSLQQGGQPGDVAQAIAFLVSDRA 434
Cdd:cd08930  162 pveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSE--FLEKY--TKKCPLKRMLNPEDLRGAIIFLLSDAS 237

                        250
                 ....*....|....*.
gi 896156623 435 LGVNghvlrvcGQNIV 450
Cdd:cd08930  238 SYVT-------GQNLV 246
PRK08267 PRK08267
SDR family oxidoreductase;
217-426 7.76e-21

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 91.54  E-value: 7.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVIDVPQAGeaLSKVANELGGLAL---QQDITADDA-GNAIADAAVARYGRLDIVIH 292
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAG--LAALAAELGAGNAwtgALDVTDRAAwDAALADFAAATGGRLDVLFN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 293 NAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAY 372
Cdd:PRK08267  84 NAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEAL 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 896156623 373 AEEFAKRGGNINAVAPGFIETDMTAAIPFVNrqvarRVNSLQQGG---QPGDVAQAI 426
Cdd:PRK08267 164 DLEWRRHGIRVADVMPLFVDTAMLDGTSNEV-----DAGSTKRLGvrlTPEDVAEAV 215
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 209-434 9.05e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 91.54  E-value: 9.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPqaGEALSKVANELGG-LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLD--EALAKETAAELGLvVGGPLDVTDPASFAAFLDAVEADLGPI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIE-----SQL---KMNEQLLNHkafekaprIATMASTSGIAGNRGQTNYA 359
Cdd:PRK07825  80 DVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYgvilgSKLaapRMVPRGRGH--------VVNVASLAGKIPVPGMATYC 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156623 360 TSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVnrQVARRVnslqqggQPGDVAQAIAFLVSDRA 434
Cdd:PRK07825 152 ASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGGA--KGFKNV-------EPEDVAAAIVGTVAKPR 217
PRK07856 PRK07856
SDR family oxidoreductase;
210-446 1.04e-20

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 91.15  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANelgglALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRPAE-----FHAADVRDPDQVAALVDAIVERHGRLDV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLlnHKAFEKAPR---IATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:PRK07856  79 LVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAA--NAVMQQQPGggsIVNIGSVSGRRPSPGTAAYGAAKAGLL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRgGNINAVAPGFIETDMT-------AAIPFVNRQVArrvnsLQQGGQPGDVAQAIAFLVSDRALGVNG 439
Cdd:PRK07856 157 NLTRSLAVEWAPK-VRVNAVVVGLVRTEQSelhygdaEGIAAVAATVP-----LGRLATPADIAWACLFLASDLASYVSG 230


                 ....*..
gi 896156623 440 HVLRVCG 446
Cdd:PRK07856 231 ANLEVHG 237
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 208-446 1.26e-20

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 91.06  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGGLALQQDITADDAGNA-----IADAAVA 282
Cdd:cd08936    6 DPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQ--QNVDRAVATLQGEGLSVTGTVCHVGKAedrerLVATAVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 283 RYGRLDIVIHNAGItrDKMFANMDDAK---WGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYA 359
Cdd:cd08936   84 LHGGVDILVSNAAV--NPFFGNILDSTeevWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 360 TSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIpFVNRQVARRVN---SLQQGGQPGDVAQAIAFLVSDRALG 436
Cdd:cd08936  162 VSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSAL-WMDKAVEESMKetlRIRRLGQPEDCAGIVSFLCSEDASY 240

                        250
                 ....*....|
gi 896156623 437 VNGHVLRVCG 446
Cdd:cd08936  241 ITGETVVVGG 250
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 210-426 1.28e-20

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 90.72  E-value: 1.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLA------LQQDITADDAGNAIADAAVAR 283
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVL--SARREERLEEVKSECLELGapsphvVPLDMSDLEDAEQVVEEALKL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITRDKMF--ANMDDAKWgsVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATS 361
Cdd:cd05332   79 FGGLDILINNAGISMRSLFhdTSIDVDRK--IMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAAS 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTA-AIPFVNRQVARRVNSLQQGGQPGDVAQAI 426
Cdd:cd05332  157 KHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMnALSGDGSMSAKMDDTTANGMSPEECALEI 222
PLN02253 PLN02253
xanthoxin dehydrogenase
 210-446 2.38e-20

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 90.65  E-value: 2.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGG----LALQQDITA-DDAGNAIaDAAVARY 284
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQD--DLGQNVCDSLGGepnvCFFHCDVTVeDDVSRAV-DFTVDKF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKM--FANMDDAKWGSVIAVNIESQ-LKMneqllNHKAF----EKAPRIATMASTSGIAGNRGQTN 357
Cdd:PLN02253  93 GTLDIMVNNAGLTGPPCpdIRNVELSEFEKVFDVNVKGVfLGM-----KHAARimipLKKGSIVSLCSVASAIGGLGPHA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAA-IPFVNRQ----------VARRVNSLQQGGQPGDVAQAI 426
Cdd:PLN02253 168 YTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAhLPEDERTedalagfrafAGKNANLKGVELTVDDVANAV 247

                        250       260
                 ....*....|....*....|
gi 896156623 427 AFLVSDRALGVNGHVLRVCG 446
Cdd:PLN02253 248 LFLASDEARYISGLNLMIDG 267
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 214-429 2.70e-20

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 89.61  E-value: 2.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 214 VAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEALSKVANELGGLA--LQQDITADDAGNAIADAAVARYGRLDIV 290
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDInEKGAEETANNVRKAGGKVhyYKCDVSKREEVYEAAKKIKKEVGDVTIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 291 IHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVE 370
Cdd:cd05339   81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896156623 371 AYAEEFaKRGG--NINA--VAPGFIETDMTA--AIPFVN-------RQVARR-VNSLQQGGQ----PGDVAQAIAFL 429
Cdd:cd05339  161 SLRLEL-KAYGkpGIKTtlVCPYFINTGMFQgvKTPRPLlapilepEYVAEKiVRAILTNQQmlylPFYAYFLPILK 236
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
 213-446 4.15e-20

mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR family oxidoreductase regularly found encoded next to genes for mycofactocin biosynthesis proteins, and never found in genomes lacking mycofactocin. Members of this family are likely to represent a family of proteins that share a specific function.


Pssm-ID: 468513 [Multi-domain]  Cd Length: 256  Bit Score: 89.35  E-value: 4.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDV--------PQAGEA-LSKVANELGG--LALQQDITADDAGNAIADAAV 281
Cdd:NF040491   1 RVALVTGAARGIGAATVRRLAARGYAVVAVDAcagdpapyPLGTEAdLDALVASSPGrvETVVADVRDRAALAAAVALAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYGRLDIVIHNAG-ITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNH---KAFEKAPRIATMASTSGIAGNRGQTN 357
Cdd:NF040491  81 DRWGRLDAAVAAAAvIAGGRPLWETPPEELDALWDVDVRGVWNLAAAAVPAllaGPDPRGCRFVAVASAAGHRGLFHLAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDM---TAAI-------PFVNRQVARRVNslqqggQPGDVAQAIA 427
Cdd:NF040491 161 YCAAKHAVVGLVRGLAADLAGTGVTACAVSPGSTDTPMlaaTAALyglddvtELAAHQLVRRLL------DPDEVAAVVA 234

                        250
                 ....*....|....*....
gi 896156623 428 FLVSDRALGVNGHVLRVCG 446
Cdd:NF040491 235 FACSPGGAAVNGSVVHADG 253
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 210-446 4.28e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 89.44  E-value: 4.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDvpQAGEALSKVANELGGL-----ALQQDITADDAGNAIADAAVARY 284
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNG--RDPAKLAAAAESLKGQglsahALAFDVTDHDAVRAAIDAFEAEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK07523  86 GPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFVNRQVARRVNSlqqgGQPGDVAQ---AIAFLVSDRALGVN 438
Cdd:PRK07523 166 VGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALvadPEFSAWLEKRTPA----GRWGKVEElvgACVFLASDASSFVN 241


                 ....*...
gi 896156623 439 GHVLRVCG 446
Cdd:PRK07523 242 GHVLYVDG 249
PRK12742 PRK12742
SDR family oxidoreductase;
209-439 5.99e-20

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 88.66  E-value: 5.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAEViVIDVPQAGEALSKVANELGGLALQQDITADDAgnaiADAAVARYGRLD 288
Cdd:PRK12742   3 AFTGKKVLVLGGSRGIGAAIVRRFVTDGANV-RFTYAGSKDAAERLAQETGATAVQTDSADRDA----VIDVVRKSGALD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITR--DKMFANMDDakwgsviavnIESQLKMNEQLLNHKAFEKAP------RIATMASTSGiagNR----GQT 356
Cdd:PRK12742  78 ILVVNAGIAVfgDALELDADD----------IDRLFKINIHAPYHASVEAARqmpeggRIIIIGSVNG---DRmpvaGMA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 357 NYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVaRRVNSLQQGGQPGDVAQAIAFLVSDRALG 436
Cdd:PRK12742 145 AYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDANPANGPMKDMM-HSFMAIKRHGRPEEVAGMVAWLAGPEASF 223


                 ...
gi 896156623 437 VNG 439
Cdd:PRK12742 224 VTG 226
PRK12744 PRK12744
SDR family oxidoreductase;
207-432 1.09e-19

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 88.26  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 207 DKPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVI------DVPQAGEALSKV-ANELGGLALQQDITADDAGNAIADA 279
Cdd:PRK12744   3 DHSLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIhynsaaSKADAEETVAAVkAAGAKAVAFQADLTTAAAVEKLFDD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 280 AVARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQ---LKMNEQLLNHKAfekapRIATMASTSGIAGNRGQT 356
Cdd:PRK12744  83 AKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAfffIKEAGRHLNDNG-----KIVTLVTSLLGAFTPFYS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 357 NYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIET------DMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLV 430
Cdd:PRK12744 158 AYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTpffypqEGAEAVAYHKTAAALSPFSKTGLTDIEDIVPFIRFLV 237


                 ..
gi 896156623 431 SD 432
Cdd:PRK12744 238 TD 239
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 210-452 1.23e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 88.14  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI--DVPQAGEALSKVANELGGLAL--QQDITADDAGNAIADAAVARYG 285
Cdd:PRK06198   4 LDGKVALVTGGTQGLGAAIARAFAERGAAGLVIcgRNAEKGEAQAAELEALGAKAVfvQADLSDVEDCRRVVAAADEAFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAP-RIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK06198  84 RLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEgTIVNIGSMSAHGGQPFLAAYCASKGA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVE--AYAEEFAKRggNINAVAPGFIETDMTAAIP---------FVNRQVARRvnSLQQGGQPGDVAQAIAFLVSDR 433
Cdd:PRK06198 164 LATLTRnaAYALLRNRI--RVNGLNIGWMATEGEDRIQrefhgapddWLEKAAATQ--PFGRLLDPDEVARAVAFLLSDE 239

                        250
                 ....*....|....*....
gi 896156623 434 ALGVNGHVLRVcGQNIVGA 452
Cdd:PRK06198 240 SGLMTGSVIDF-DQSVWGA 257
PRK05855 PRK05855
SDR family oxidoreductase;
208-426 2.61e-19

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 90.43  E-value: 2.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEALSKVANELGGLAL--QQDITADDAGNAIADAAVARY 284
Cdd:PRK05855 311 GPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIdEAAAERTAELIRAAGAVAHayRVDVSDADAMEAFAEWVRAEH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQL--------KMNEQllnhkafEKAPRIATMASTSGIAGNRGQT 356
Cdd:PRK05855 391 GVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIhgcrlfgrQMVER-------GTGGHIVNVASAAAYAPSRSLP 463

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896156623 357 NYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVN---RQVARRVNSLQQGGQ-----PGDVAQAI 426
Cdd:PRK05855 464 AYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVATTRFAGadaEDEARRRGRADKLYQrrgygPEKVAKAI 541
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 217-443 3.19e-19

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 86.57  E-value: 3.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANEL-GGLALQQ---DITADDAGNAIADAAVARYGRLDIVIH 292
Cdd:cd05367    4 LTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEELrPGLRVTTvkaDLSDAAGVEQLLEAIRKLDGERDLLIN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 293 NAGITRD-KMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPR-IATMASTSGIAGNRGQTNYATSKAGVIAMVE 370
Cdd:cd05367   84 NAGSLGPvSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKKtVVNVSSGAAVNPFKGWGLYCSSKAARDMFFR 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896156623 371 AYAEEfaKRGGNINAVAPGFIETDMTAAIPFVNRQ--VARRVNSLQQGGQ---PGDVAQAIAFLVsDRALGVNGHVLR 443
Cdd:cd05367  164 VLAAE--EPDVRVLSYAPGVVDTDMQREIRETSADpeTRSRFRSLKEKGElldPEQSAEKLANLL-EKDKFESGAHVD 238
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 210-448 3.98e-19

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 86.52  E-value: 3.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV-PQAGEALskvANELG--GLALQQDITADDAGNAIADAAVARYGR 286
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADInLEAARAT---AAEIGpaACAISLDVTDQASIDRCVAALVDRWGS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFE-KAPRIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:cd05363   78 IDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCATKAAV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFV------------NRQVARRVnSLQQGGQPGDVAQAIAFLVSDR 433
Cdd:cd05363  158 ISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKfaryenrprgekKRLVGEAV-PFGRMGRAEDLTGMAIFLASTD 236

                        250
                 ....*....|....*
gi 896156623 434 ALGVNGHVLRVCGQN 448
Cdd:cd05363  237 ADYIVAQTYNVDGGN 251
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 210-446 6.24e-19

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 86.36  E-value: 6.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQ-AGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGR 286
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQeKGDKVAKEITALGGraIALAADVLDRASLERAREEIVAQFGT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAG--------------ITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGN 352
Cdd:cd08935   83 VDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 353 RGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFV-NRQVARRVNSLQQG------GQPGDVAQA 425
Cdd:cd08935  163 TKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINpDGSYTDRSNKILGRtpmgrfGKPEELLGA 242

                        250       260
                 ....*....|....*....|..
gi 896156623 426 IAFLVSDRALG-VNGHVLRVCG 446
Cdd:cd08935  243 LLFLASEKASSfVTGVVIPVDG 264
PRK05867 PRK05867
SDR family oxidoreductase;
210-431 6.65e-19

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 85.86  E-value: 6.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGG-----LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAI--AARHLDALEKLADEIGTsggkvVPVCCDVSQHQQVTSMLDQVTAEL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLkmneqlLNHKAFEKA-------PRIATMASTSGIAGNRGQ-- 355
Cdd:PRK05867  85 GGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVF------LTAQAAAKAmvkqgqgGVIINTASMSGHIINVPQqv 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156623 356 TNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVnSLQQGGQPGDVAQAIAFLVS 431
Cdd:PRK05867 159 SHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQPLWEPKI-PLGRLGRPEELAGLYLYLAS 233
PRK06947 PRK06947
SDR family oxidoreductase;
213-446 6.86e-19

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 85.63  E-value: 6.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIV--IDVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGInyARDAAAAEETADAVRAAGGraCVVAGDVANEADVIAMFDAVQSAFGRLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRDKM-FANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTN----YATSKA 363
Cdd:PRK06947  83 ALVNNAGIVAPSMpLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRGGAIVNVSSIASRLGSPNeyvdYAGSKG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRqvARRVNS---LQQGGQPGDVAQAIAFLVSDRALGVNGH 440
Cdd:PRK06947 163 AVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGR--AARLGAqtpLGRAGEADEVAETIVWLLSDAASYVTGA 240


                 ....*.
gi 896156623 441 VLRVCG 446
Cdd:PRK06947 241 LLDVGG 246
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 210-446 9.12e-19

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 85.32  E-value: 9.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDV---PQAGEALSkvanelgglALQQDITADDAGNAIADAAVARYGR 286
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQaflTQEDYPFA---------TFVLDVSDAAAVAQVCQRLLAETGP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:PRK08220  77 LDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNS----------LQQGGQPGDVAQAIAFLVSDRALG 436
Cdd:PRK08220 157 SLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLWVDEDGEQQVIAGfpeqfklgipLGKIARPQEIANAVLFLASDLASH 236

                        250
                 ....*....|
gi 896156623 437 VNGHVLRVCG 446
Cdd:PRK08220 237 ITLQDIVVDG 246
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 211-446 4.04e-18

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 83.84  E-value: 4.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 211 AGKVAAVTGSARGIGAAIARQLKADGAEVIVIDvpqAGEALSKVANEL-----GGLALQQDITADDAGNAIADAAVARYG 285
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVD---RSELVHEVAAELraaggEALALTADLETYAGAQAAMAAAVEAFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGIT-RDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMAS--TSGIagNRgqTNYATSK 362
Cdd:PRK12823  84 RIDVLINNVGGTiWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSiaTRGI--NR--VPYSAAK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGfietdMTAAIPfvnRQVARrvNSLQQG-----------------------GQP 419
Cdd:PRK12823 160 GGVNALTASLAFEYAEHGIRVNAVAPG-----GTEAPP---RRVPR--NAAPQSeqekawyqqivdqtldsslmkryGTI 229

                        250       260
                 ....*....|....*....|....*..
gi 896156623 420 GDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK12823 230 DEQVAAILFLASDEASYITGTVLPVGG 256
PRK12746 PRK12746
SDR family oxidoreductase;
208-446 4.08e-18

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 83.54  E-value: 4.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIV---IDVPQAGEALSKV-ANELGGLALQQDITADDAGNAIADAAVAR 283
Cdd:PRK12746   2 KNLDGKVALVTGASRGIGRAIAMRLANDGALVAIhygRNKQAADETIREIeSNGGKAFLIEADLNSIDGVKKLVEQLKNE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 Y------GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhKAFEKAPRIATMASTSGIAGNRGQTN 357
Cdd:PRK12746  82 LqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTL--PLLRAEGRVINISSAEVRLGFTGSIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFVnRQVARRVNSLQQGGQPGDVAQAIAFLVSDRA 434
Cdd:PRK12746 160 YGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLlddPEI-RNFATNSSVFGRIGQVEDIADAVAFLASSDS 238

                        250
                 ....*....|..
gi 896156623 435 LGVNGHVLRVCG 446
Cdd:PRK12746 239 RWVTGQIIDVSG 250
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 210-452 4.51e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 84.31  E-value: 4.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEA-LSKVANELGG---LALQQDITADDAGNAIADAAVARYG 285
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDAnETKQRVEKEGvkcLLIPGDVSDEAFCKDAVEETVRELG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKM-FANMDDAKWGSVIAVNIESQLKMNEQLLNHkaFEKAPRIATMASTSGIAGNRGQTNYATSKAG 364
Cdd:PRK06701 124 RLDILVNNAAFQYPQQsLEDITAEQLDKTFKTNIYSYFHMTKAALPH--LKQGSAIINTGSITGYEGNETLIDYSATKGA 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAiPFVNRQVAR--RVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVL 442
Cdd:PRK06701 202 IHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPS-DFDEEKVSQfgSNTPMQRPGQPEELAPAYVFLASPDSSYITGQML 280

                        250
                 ....*....|
gi 896156623 443 RVCGQNIVGA 452
Cdd:PRK06701 281 HVNGGVIVNG 290
PRK07814 PRK07814
SDR family oxidoreductase;
210-446 5.88e-18

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 83.29  E-value: 5.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLALQQ-----DITADDAGNAIADAAVARY 284
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLI--AARTESQLDEVAEQIRAAGRRAhvvaaDLAHPEATAGLAGQAVEAF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNE----QLLNHKAfekAPRIATMASTSGIAGNRGQTNYAT 360
Cdd:PRK07814  86 GRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVaavpLMLEHSG---GGSVINISSTMGRLAGRGFAAYGT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRgGNINAVAPGFIetdMTAAIPFVN-----RQVARRVNSLQQGGQPGDVAQAIAFLVSDRAL 435
Cdd:PRK07814 163 AKAALAHYTRLAALDLCPR-IRVNAIAPGSI---LTSALEVVAandelRAPMEKATPLRRLGDPEDIAAAAVYLASPAGS 238

                        250
                 ....*....|.
gi 896156623 436 GVNGHVLRVCG 446
Cdd:PRK07814 239 YLTGKTLEVDG 249
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 209-446 6.05e-18

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 83.22  E-value: 6.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAEViVIDVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGR 286
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARV-VVNYHQSEDAAEALADELGDraIALQADVTDREQVQAMFATATEHFGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 -LDIVIHNA-------GITRDKmfanMDDAKWGSVIAvNIESQLKmnEQLLNHKAFEKAPRIATMASTSGIAGNRGQT-- 356
Cdd:PRK08642  81 pITTVVNNAladfsfdGDARKK----ADDITWEDFQQ-QLEGSVK--GALNTIQAALPGMREQGFGRIINIGTNLFQNpv 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 357 ----NYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFI-ETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVS 431
Cdd:PRK08642 154 vpyhDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLrTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAVLFFAS 233

                        250
                 ....*....|....*
gi 896156623 432 DRALGVNGHVLRVCG 446
Cdd:PRK08642 234 PWARAVTGQNLVVDG 248
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 217-395 1.04e-17

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 81.73  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVIDVPQAGeaLSKVANELGG---LALQQDITADDA-GNAIADAAVARYGRLDIVIH 292
Cdd:cd08931    5 ITGAASGIGRETALLFARNGWFVGLYDIDEDG--LAALAAELGAenvVAGALDVTDRAAwAAALADFAAATGGRLDALFN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 293 NAGITRDKMFANMDDAKWGSVIAVNIESqlkmneqLLN--HKAF---EKAP--RIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:cd08931   83 NAGVGRGGPFEDVPLAAHDRMVDINVKG-------VLNgaYAALpylKATPgaRVINTASSSAIYGQPDLAVYSATKFAV 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETDM 395
Cdd:cd08931  156 RGLTEALDVEWARHGIRVADVWPWFVDTPI 185
PRK06181 PRK06181
SDR family oxidoreductase;
212-394 1.32e-17

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 82.33  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANEL---GG--LALQQDITADDAGNAIADAAVARYGR 286
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNE--TRLASLAQELadhGGeaLVVPTDVSDAEACERLIEAAVARFGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGS-VIAVNIESQLKMNEQLLNHKAFEKApRIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:PRK06181  79 IDILVNNAGITMWSRFDELTDLSVFErVMRVNYLGAVYCTHAALPHLKASRG-QIVVVSSLAGLTGVPTRSGYAASKHAL 157

                        170       180
                 ....*....|....*....|....*....
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETD 394
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVATD 186
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 216-446 1.71e-17

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 81.77  E-value: 1.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 216 AVTGSARGIGAAIARQLKADGAEVIVIDVPQAgealsKVANELGglalqqdiTADDAGNAIADAAVARYGRLDIVIHNAG 295
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHTVIGIDLREA-----DVIADLS--------TPEGRAAAIADVLARCSGVLDGLVNCAG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 296 ITrdkmfanmDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGI-------------------------- 349
Cdd:cd05328   70 VG--------GTTVAGLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAgwaqdklelakalaagtearavalae 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 350 -AGNRGQTNYATSKAGVIAMVEAYAEE-FAKRGGNINAVAPGFIETDMTAAIPFVNR---QVARRVNSLQQGGQPGDVAQ 424
Cdd:cd05328  142 hAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRggeSVDAFVTPMGRRAEPDEIAP 221

                        250       260
                 ....*....|....*....|..
gi 896156623 425 AIAFLVSDRALGVNGHVLRVCG 446
Cdd:cd05328  222 VIAFLASDAASWINGANLFVDG 243
PRK07062 PRK07062
SDR family oxidoreductase;
207-446 2.42e-17

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 81.63  E-value: 2.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 207 DKPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVI--DVPQAGEALSKVANELGG---LALQQDITADDAGNAIADAAV 281
Cdd:PRK07062   3 QIQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICgrDEERLASAEARLREKFPGarlLAARCDVLDEADVAAFAAAVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYGRLDIVIHNAGITRDKMFANMDDAKWGSviavniESQLKMNEQLLNHKAF----EKAPRIATMASTSGIAGNRGQTN 357
Cdd:PRK07062  83 ARFGGVDMLVNNAGQGRVSTFADTTDDAWRD------ELELKYFSVINPTRAFlpllRASAAASIVCVNSLLALQPEPHM 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 YATS--KAGVIAMVEAYAEEFAKRGGNINAVAPGFIET------------------DMTAAIpfvnrqvARRVN-SLQQG 416
Cdd:PRK07062 157 VATSaaRAGLLNLVKSLATELAPKGVRVNSILLGLVESgqwrrryearadpgqsweAWTAAL-------ARKKGiPLGRL 229

                        250       260       270
                 ....*....|....*....|....*....|
gi 896156623 417 GQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK07062 230 GRPDEAARALFFLASPLSSYTTGSHIDVSG 259
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 213-446 2.99e-17

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 80.78  E-value: 2.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVA--NELGG--LALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDelNALRNsaVLVQADLSDFAACADLVAAAFRAFGRCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRD-KMFANMDDAkWGSVIAVNIESQLkmneqLLNHKAfekAPRIATMASTSGI--------AGNRGQTNYA 359
Cdd:cd05357   81 VLVNNASAFYPtPLGQGSEDA-WAELFGINLKAPY-----LLIQAF---ARRLAGSRNGSIIniidamtdRPLTGYFAYC 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 360 TSKAGVIAMVEAYAEEFAKRgGNINAVAPGFIETDMTAaiPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRAlgVNG 439
Cdd:cd05357  152 MSKAALEGLTRSAALELAPN-IRVNGIAPGLILLPEDM--DAEYRENALRKVPLKRRPSAEEIADAVIFLLDSNY--ITG 226


                 ....*..
gi 896156623 440 HVLRVCG 446
Cdd:cd05357  227 QIIKVDG 233
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 212-446 3.00e-17

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 81.23  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANELGG-------LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADI--NSEKAANVAQEINAeygegmaYGFGADATSEQSVLALSRGVDEIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNiesqlkMNEQLLNHKAFEK-------APRIATMASTSGIAGNRGQTN 357
Cdd:PRK12384  80 GRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVN------LVGYFLCAREFSRlmirdgiQGRIIQINSKSGKVGSKHNSG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 YATSKAGVIAMVEAYAEEFAKRGGNINAVAPG-FIETDM-TAAIPfvnrQVARRVN--------------SLQQGGQPGD 421
Cdd:PRK12384 154 YSAAKFGGVGLTQSLALDLAEYGITVHSLMLGnLLKSPMfQSLLP----QYAKKLGikpdeveqyyidkvPLKRGCDYQD 229

                        250       260
                 ....*....|....*....|....*
gi 896156623 422 VAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK12384 230 VLNMLLFYASPKASYCTGQSINVTG 254
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 210-433 5.44e-17

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 80.38  E-value: 5.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEAlsKVANELGG--LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLA--SLRQRFGDhvLVVEGDVTSYADNQRAVDQTVDAFGKL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITrdKMFANMDDAKWGS-------VIAVNIESQLKMNEQLLNHKAFEKAPRIATmASTSGIAGNRGQTNYAT 360
Cdd:PRK06200  82 DCFVGNAGIW--DYNTSLVDIPAETldtafdeIFNVNVKGYLLGAKAALPALKASGGSMIFT-LSNSSFYPGGGGPLYTA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRgGNINAVAPGFIETDM------------TAAIPFVNRQVARRVnSLQQGGQPGDVAQAIAF 428
Cdd:PRK06200 159 SKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLrgpaslgqgetsISDSPGLADMIAAIT-PLQFAPQPEDHTGPYVL 236


                 ....*
gi 896156623 429 LVSDR 433
Cdd:PRK06200 237 LASRR 241
PRK08628 PRK08628
SDR family oxidoreductase;
210-446 5.83e-17

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 80.39  E-value: 5.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGGLA--LQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEELRALQPRAefVQVDLTDDAQCRDAVEQTVAKFGRI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSvIAVNIESQLKMNEQLLNHKafeKAPR--IATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:PRK08628  85 DGLVNNAGVNDGVGLEAGREAFVAS-LERNLIHYYVMAHYCLPHL---KASRgaIVNISSKTALTGQGGTSGYAAAKGAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPG---------FIET---------DMTAAIPFVNRQVarrvnslqqggQPGDVAQAIA 427
Cdd:PRK08628 161 LALTREWAVALAKDGVRVNAVIPAevmtplyenWIATfddpeaklaAITAKIPLGHRMT-----------TAEEIADTAV 229

                        250
                 ....*....|....*....
gi 896156623 428 FLVSDRALGVNGHVLRVCG 446
Cdd:PRK08628 230 FLLSERSSHTTGQWLFVDG 248
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 210-452 6.63e-17

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 80.07  E-value: 6.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSA--RGIGAAIARQLKADGAEVIVIDVP-QAGEALSKVANELGG-LALQQDITADDAGNAIADAAVARYG 285
Cdd:COG0623    3 LKGKRGLITGVAndRSIAWGIAKALHEEGAELAFTYQGeALKKRVEPLAEELGSaLVLPCDVTDDEQIDALFDEIKEKWG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGitrdkmFANMDDaKWGSVIAVNIESQLK-MN-------------EQLLNHKAfekapRIATMastSGIAG 351
Cdd:COG0623   83 KLDFLVHSIA------FAPKEE-LGGRFLDTSREGFLLaMDisayslvalakaaEPLMNEGG-----SIVTL---TYLGA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 352 NRGQTNY---ATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETdmTAA--IPFVNR--QVARRVNSLQQGGQPGDVAQ 424
Cdd:COG0623  148 ERVVPNYnvmGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKT--LAAsgIPGFDKllDYAEERAPLGRNVTIEEVGN 225

                        250       260
                 ....*....|....*....|....*....
gi 896156623 425 AIAFLVSDRALGVNGHVLRV-CGQNIVGA 452
Cdd:COG0623  226 AAAFLLSDLASGITGEIIYVdGGYHIMGM 254
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 217-429 7.68e-17

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 78.33  E-value: 7.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGA-EVIVIDvpqagealskvanelgglalqqditaddagnaiadaavarygRLDIVIHNAG 295
Cdd:cd02266    3 VTGGSGGIGGAIARWLASRGSpKVLVVS------------------------------------------RRDVVVHNAA 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 296 ITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAYAEE 375
Cdd:cd02266   41 ILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASE 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 896156623 376 FAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFL 429
Cdd:cd02266  121 GWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARALLNA 174
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 210-446 7.72e-17

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 80.12  E-value: 7.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIV---IDVPQAGEALSKVANELG-----GLALQQDITADDAGNAIADAAV 281
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIhygNRKEEAEETVYEIQSNGGsafsiGANLESLHGVEALYSSLDNELQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYG--RLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHkaFEKAPRIATMASTSGIAGNRGQTNYA 359
Cdd:PRK12747  82 NRTGstKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSR--LRDNSRIINISSAATRISLPDFIAYS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 360 TSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFVnRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALG 436
Cdd:PRK12747 160 MTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELlsdPMM-KQYATTISAFNRLGEVEDIADTAAFLASPDSRW 238

                        250
                 ....*....|
gi 896156623 437 VNGHVLRVCG 446
Cdd:PRK12747 239 VTGQLIDVSG 248
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 212-439 8.63e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 79.72  E-value: 8.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGG-----LALQQDITADDAGNAIADAAVARYGR 286
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVI--TGRTKEKLEEAKLEIEQfpgqvLTVQMDVRNPEDVQKMVEQIDEKFGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAG----ITRDKMFANmddaKWGSVIAVNIESQLKMNEQLLNH-KAFEKAPRIATMASTSGIAGNRGQTNYATS 361
Cdd:PRK07677  79 IDALINNAAgnfiCPAEDLSVN----GWNSVIDIVLNGTFYCSQAVGKYwIEKGIKGNIINMVATYAWDAGPGVIHSAAA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 362 KAGVIAMVEAYAEEFAKR-GGNINAVAPGFIETDMTAAIPFVNRQVARRV-NSLQQG--GQPGDVAQAIAFLVSDRALGV 437
Cdd:PRK07677 155 KAGVLAMTRTLAVEWGRKyGIRVNAIAPGPIERTGGADKLWESEEAAKRTiQSVPLGrlGTPEEIAGLAYFLLSDEAAYI 234


                 ..
gi 896156623 438 NG 439
Cdd:PRK07677 235 NG 236
PRK12743 PRK12743
SDR family oxidoreductase;
213-446 1.42e-16

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 79.31  E-value: 1.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVI--DVPQAGEALSKVANELGGLA--LQQDITADDAGNAIADAAVARYGRLD 288
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITwhSDEEGAKETAEEVRSHGVRAeiRQLDLSDLPEGAQALDKLIQRLGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRDKMFANMDDAKWGSVIAVNIE-----SQL---KMNEQllnhkafEKAPRIATMASTSGIAGNRGQTNYAT 360
Cdd:PRK12743  83 VLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDgaflcSQIaarHMVKQ-------GQGGRIINITSVHEHTPLPGASAYTA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGH 440
Cdd:PRK12743 156 AKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQ 235


                 ....*.
gi 896156623 441 VLRVCG 446
Cdd:PRK12743 236 SLIVDG 241
PRK09072 PRK09072
SDR family oxidoreductase;
210-427 1.65e-16

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 79.22  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLALQQDITAD---DAGNAIADAAVARYGR 286
Cdd:PRK09072   3 LKDKRVLLTGASGGIGQALAEALAAAGARLLL--VGRNAEKLEALAARLPYPGRHRWVVADltsEAGREAVLARAREMGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHkaFEKAPRIATMA--STSGIAGNRGQTNYATSKAG 364
Cdd:PRK09072  81 INVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPL--LRAQPSAMVVNvgSTFGSIGYPGYASYCASKFA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIETDM-TAAIPFVNRQVARRVNSlqqggqPGDVAQAIA 427
Cdd:PRK09072 159 LRGFSEALRRELADTGVRVLYLAPRATRTAMnSEAVQALNRALGNAMDD------PEDVAAAVL 216
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 210-446 1.98e-16

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 78.67  E-value: 1.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLalqQDITADDAGNAIADAAVARYGRLDI 289
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVA--VSRTQADLDSLVRECPGI---EPVCVDLSDWDATEEALGSVGPVDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLL-NHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAM 368
Cdd:cd05351   80 LVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVArGMIARGVPGSIVNVSSQASQRALTNHTVYCSTKAALDML 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 369 VEAYAEEFAKRGGNINAVAPGFIETDMTA--------AIPFVNRQVARRVNSLQqggqpgDVAQAIAFLVSDRALGVNGH 440
Cdd:cd05351  160 TKVMALELGPHKIRVNSVNPTVVMTDMGRdnwsdpekAKKMLNRIPLGKFAEVE------DVVNAILFLLSDKSSMTTGS 233


                 ....*.
gi 896156623 441 VLRVCG 446
Cdd:cd05351  234 TLPVDG 239
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 210-350 2.05e-16

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 78.67  E-value: 2.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidvpqAG---EALSKVANELGGL-ALQQDITADDAGNAIADAAVARYG 285
Cdd:COG3967    3 LTGNTILITGGTSGIGLALAKRLHARGNTVII-----TGrreEKLEEAAAANPGLhTIVLDVADPASIAALAEQVTAEFP 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896156623 286 RLDIVIHNAGITRDKMFAN--MDDAKWGSVIAVNIESQLKMNEQLLNHkaFEKAPRIATMASTSGIA 350
Cdd:COG3967   78 DLNVLINNAGIMRAEDLLDeaEDLADAEREITTNLLGPIRLTAAFLPH--LKAQPEAAIVNVSSGLA 142
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 211-432 2.89e-16

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 78.35  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 211 AGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQ-AGEALSKVANELG---GLALQQDITADDAGNAIADAAVARYGR 286
Cdd:cd08933    8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEaAGQALESELNRAGpgsCKFVPCDVTKEEDIKTLISVTVERFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGI-----TRDKMFANmddaKWGSVIAVNIESQLKMNEQLLNHKAfEKAPRIATMASTSGIAGNRGQTNYATS 361
Cdd:cd08933   88 IDCLVNNAGWhpphqTTDETSAQ----EFRDLLNLNLISYFLASKYALPHLR-KSQGNIINLSSLVGSIGQKQAAPYVAT 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDM----TAAIPFVNRQVARRVNS--LQQGGQPGDVAQAIAFLVSD 432
Cdd:cd08933  163 KGAITAMTKALAVDESRYGVRVNCISPGNIWTPLweelAAQTPDTLATIKEGELAqlLGRMGTEAESGLAALFLAAE 239
PRK08219 PRK08219
SDR family oxidoreductase;
213-430 3.09e-16

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 77.67  E-value: 3.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLkADGAEVIVIDVPQagEALSKVANELGGL-ALQQDITADDAgnaiADAAVARYGRLDIVI 291
Cdd:PRK08219   4 PTALITGASRGIGAAIAREL-APTHTLLLGGRPA--ERLDELAAELPGAtPFPVDLTDPEA----IAAAVEQLGRLDVLV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 292 HNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhkafeKAPRIA-----TMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:PRK08219  77 HNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLL------PALRAAhghvvFINSGAGLRANPGWGSYAASKFALR 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156623 367 AMVEAYAEEFAkrgGNI--NAVAPGFIETDMTAAIpfvnrqVArrvnslQQGG--------QPGDVAQAIAFLV 430
Cdd:PRK08219 151 ALADALREEEP---GNVrvTSVHPGRTDTDMQRGL------VA------QEGGeydperylRPETVAKAVRFAV 209
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 210-398 3.78e-16

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 77.35  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidvpqAG---EALSKVANELGGLALQQDITADDAG-NAIADAAVARYG 285
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVII-----TGrreERLAEAKKELPNIHTIVLDVGDAESvEALAEALLSEYP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKMFANMDD--AKWGSVIAVNIESQLKMNEQLLNHkaFEKAPRIATMASTSGIAGN--RGQTNYATS 361
Cdd:cd05370   78 NLDILINNAGIQRPIDLRDPASdlDKADTEIDTNLIGPIRLIKAFLPH--LKKQPEATIVNVSSGLAFVpmAANPVYCAT 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAA 398
Cdd:cd05370  156 KAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEE 192
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 212-446 6.79e-16

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 76.85  E-value: 6.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDIVI 291
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 292 HNAGITRDKMFANMDDAKWGSVIAVNIESQLKMN----EQLLNHKAfekapRIATMASTSGIAGNRGQTNYATSKAGVIA 367
Cdd:cd09761   81 NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSrycrDELIKNKG-----RIINIASTRAFQSEPDSEAYAASKGGLVA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 368 MVEAYAEEFAkRGGNINAVAPGFIETDMTAAIPFVN-RQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:cd09761  156 LTHALAMSLG-PDIRVNCISPGWINTTEQQEFTAAPlTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIVDG 234
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 212-395 9.35e-16

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 76.52  E-value: 9.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLALQQ---------DIT-ADDAGNAIAdAAV 281
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVII--VARSESKLEEAVEEIEAEANASgqkvsyisaDLSdYEEVEQAFA-QAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATS 361
Cdd:cd08939   78 EKGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPS 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDM 395
Cdd:cd08939  158 KFALRGLAESLRQELKPYNIRVSVVYPPDTDTPG 191
PRK07326 PRK07326
SDR family oxidoreductase;
210-431 1.40e-15

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 75.82  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI--DVPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITarDQKELEEAAAELNNKGNVLGLAADVRDEADVQRAVDAIVAAFGGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMneqllNHKAFEKAPR----IATMASTSGIAGNRGQTNYATSKA 363
Cdd:PRK07326  84 DVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYT-----IKAAVPALKRgggyIINISSLAGTNFFAGGAAYNASKF 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPfvNRQVARRVnslqqggQPGDVAQAIAFLVS 431
Cdd:PRK07326 159 GLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTP--SEKDAWKI-------QPEDIAQLVLDLLK 217
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 217-392 1.77e-15

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 74.06  E-value: 1.77e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623   217 VTGSARGIGAAIARQLKADGAEVIVI-----DVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:smart00822   5 ITGGLGGLGRALARWLAERGARRLVLlsrsgPDAPGAAALLAELEAAGArvTVVACDVADRDALAAVLAAIPAVEGPLTG 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623   290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESqlkmneqLLN-HKAFEKAP--RIATMASTSGIAGNRGQTNYATSkagvI 366
Cdd:smart00822  85 VIHAAGVLDDGVLASLTPERFAAVLAPKAAG-------AWNlHELTADLPldFFVLFSSIAGVLGSPGQANYAAA----N 153

                          170       180
                   ....*....|....*....|....*.
gi 896156623   367 AMVEAYAEEFAKRGGNINAVAPGFIE 392
Cdd:smart00822 154 AFLDALAEYRRARGLPALSIAWGAWA 179
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 42-387 2.35e-15

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 77.79  E-value: 2.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  42 DKVLVTGEGADADAVAAQLAEWGLQVRRGNAADDKIGAIVLVATEAkRPAELQGPVLAAAKHMRKLdKGGRIVTVSRAKD 121
Cdd:cd08953   37 QPVWAPAALASAFLALAYEAALLGLAAAEAALLDALSALDPAAALQ-LLESLQRLLKAGLLAARAS-GRALLQVVTGLPG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 122 AHhnatpAEIAENAVAGGIEGLIRSLGHEVRGGSTANGILVAPGVSVTAPS--VISSLHFFLSGRSAFIDGQ-----FLR 194
Cdd:cd08953  115 AL-----GLDALDPAGAGLAGLLRTLAQEYPGLTCRLIDLDAGEASAEALAreLAAELAAPGAAEVRYRDGLryvqtLEP 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 195 VTSDAGEIPSDwdKPLAGKVAAVTGSARGIGAAIARQL-KADGAEVIVI---DVPQAGEALSKVANELGGLALQQDITAD 270
Cdd:cd08953  190 LPLPAGAAASA--PLKPGGVYLVTGGAGGIGRALARALaRRYGARLVLLgrsPLPPEEEWKAQTLAALEALGARVLYISA 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 271 DAGNAIA-----DAAVARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESqlkmneqLLN-HKAFEKAP--RIAT 342
Cdd:cd08953  268 DVTDAAAvrrllEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDG-------LLNlAQALADEPldFFVL 340

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 896156623 343 MASTSGIAGNRGQTNYATSKagviAMVEAYAEEFAKRGGNINAVA 387
Cdd:cd08953  341 FSSVSAFFGGAGQADYAAAN----AFLDAFAAYLRQRGPQGRVLS 381
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 210-397 2.47e-15

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 75.76  E-value: 2.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGeaLSKVANELGGLALQQ-----DITADDAGNAIADAAVARY 284
Cdd:PRK05876   4 FPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPG--LRQAVNHLRAEGFDVhgvmcDVRHREEVTHLADEAFRLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNhKAFEKAP--RIATMASTSGIAGNRGQTNYATSK 362
Cdd:PRK05876  82 GHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLP-RLLEQGTggHVVFTASFAGLVPNAGLGAYGVAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 896156623 363 AGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTA 397
Cdd:PRK05876 161 YGVVGLAETLAREVTADGIGVSVLCPMVVETNLVA 195
PRK05717 PRK05717
SDR family oxidoreductase;
212-446 2.70e-15

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 75.31  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGGLALQqdITADDAGNAIADAAVA----RYGRL 287
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDR--ERGSKVAKALGENAWF--IAMDVADEAQVAAGVAevlgQFGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGIT--RDKMFANMDDAKWGSVIAVNIESQLkmneQLLNHKA-FEKAPR--IATMASTSGIAGNRGQTNYATSK 362
Cdd:PRK05717  86 DALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPM----LLAKHCApYLRAHNgaIVNLASTRARQSEPDTEAYAASK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIAMVEAYAEEFAKRgGNINAVAPGFIETDMTA---AIPFVNRQVAR----RVNSLQqggqpgDVAQAIAFLVSDRAL 435
Cdd:PRK05717 162 GGLLALTHALAISLGPE-IRVNAVSPGWIDARDPSqrrAEPLSEADHAQhpagRVGTVE------DVAAMVAWLLSRQAG 234

                        250
                 ....*....|.
gi 896156623 436 GVNGHVLRVCG 446
Cdd:PRK05717 235 FVTGQEFVVDG 245
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 208-389 2.83e-15

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 78.04  E-value: 2.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANELGGLALQQDITADDAGNAIADAAVAR---- 283
Cdd:COG3347  421 KPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADL--DGEAAEAAAAELGGGYGADAVDATDVDVTAEAAVAAAfgfa 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 ---YGRLDIVIHNAGI--------TRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhkafekAPRIATMASTSGIAGN 352
Cdd:COG3347  499 gldIGGSDIGVANAGIassspeeeTRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGL-------GGSSVFAVSKNAAAAA 571

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 896156623 353 RGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPG 389
Cdd:COG3347  572 YGAAAAATAKAAAQHLLRALAAEGGANGINANRVNPD 608
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 210-446 3.29e-15

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 75.71  E-value: 3.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANEL---GG--LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQ--EKAEAVVAEIkaaGGeaLAVKADVLDKESLEQARQQILEDF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAG---------------ITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSG- 348
Cdd:PRK08277  86 GPCDILINGAGgnhpkattdnefhelIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAf 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 349 -----IAGnrgqtnYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPF-------------VNRQVARRV 410
Cdd:PRK08277 166 tpltkVPA------YSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALLFnedgslterankiLAHTPMGRF 239

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 896156623 411 nslqqgGQPGDVAQAIAFLVSDRALG-VNGHVLRVCG 446
Cdd:PRK08277 240 ------GKPEELLGTLLWLADEKASSfVTGVVLPVDG 270
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 215-396 3.45e-15

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 74.64  E-value: 3.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 215 AAVTGSARGIGAAIARQLKADGAEVIVIDV--PQAGEALSKVANELGGL-ALQQDITadDAGNAIADAAVARYG--RLDI 289
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNTVIATCrdPSAATELAALGASHSRLhILELDVT--DEIAESAEAVAERLGdaGLDV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGI-TRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSG-IAGNR--GQTNYATSKAGV 365
Cdd:cd05325   79 LINNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsIGDNTsgGWYSYRASKAAL 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETDMT 396
Cdd:cd05325  159 NMLTKSLAVELKRDGITVVSLHPGWVRTDMG 189
PRK07832 PRK07832
SDR family oxidoreductase;
213-408 4.05e-15

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 75.08  E-value: 4.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAG-EALSKVANELGG---LALQQDITADDAGNAIADAAVARYGRLD 288
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGlAQTVADARALGGtvpEHRALDISDYDAVAAFAADIHAAHGSMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhKAFEKAPR---IATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:PRK07832  81 VVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFV--PPMVAAGRgghLVNVSSAAGLVALPWHAAYSASKFGL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETDM--TAAIPFVNRQVAR 408
Cdd:PRK07832 159 RGLSEVLRFDLARHGIGVSVVVPGAVKTPLvnTVEIAGVDREDPR 203
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 210-431 5.59e-15

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 74.70  E-value: 5.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEAlsKVANELGG--LALQQDITADDAGNAIADAAVARYGRL 287
Cdd:cd05348    2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVA--ELRADFGDavVGVEGDVRSLADNERAVARCVERFGKL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITrDKMFANMD------DAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATmASTSGIAGNRGQTNYATS 361
Cdd:cd05348   80 DCFIGNAGIW-DYSTSLVDipeeklDEAFDELFHINVKGYILGAKAALPALYATEGSVIFT-VSNAGFYPGGGGPLYTAS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 362 KAGVIAMVEAYAEEFAKRgGNINAVAPGFIETDMT--AAIPFVNRQVA--------RRVNSLQQGGQPGDVAQAIAFLVS 431
Cdd:cd05348  158 KHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLRgpASLGQGETSIStpplddmlKSILPLGFAPEPEDYTGAYVFLAS 236
PRK06128 PRK06128
SDR family oxidoreductase;
210-448 6.42e-15

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 75.28  E-value: 6.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQ----AGEALSKVANE-LGGLALQQDITADDAGNAIADAAVARY 284
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNYLPEeeqdAAEVVQLIQAEgRKAVALPGDLKDEAFCRQLVERAVKEL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGI-TRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHkafekAPRIATMASTSGIAG---NRGQTNYAT 360
Cdd:PRK06128 133 GGLDILVNIAGKqTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPH-----LPPGASIINTGSIQSyqpSPTLLDYAS 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAA-------IPFVNRQvarrvNSLQQGGQPGDVAQAIAFLVSDR 433
Cdd:PRK06128 208 TKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSggqppekIPDFGSE-----TPMKRPGQPVEMAPLYVLLASQE 282

                        250
                 ....*....|....*
gi 896156623 434 ALGVNGHVLRVCGQN 448
Cdd:PRK06128 283 SSYVTGEVFGVTGGL 297
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 210-446 9.60e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 74.07  E-value: 9.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLALQ-------QDITADDAGNAIADAAVA 282
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMI--VGRNPDKLAAAAEEIEALKGAgavryepADVTDEDQVARAVDAATA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 283 RYGRLDIVIHNAG-------ITRdkmfanMDDAKWGSVIAVNIESQLkmneQLLNHKAFE----KAPRIATMASTSGIAG 351
Cdd:PRK05875  83 WHGRLHGVVHCAGgsetigpITQ------IDSDAWRRTVDLNVNGTM----YVLKHAARElvrgGGGSFVGISSIAASNT 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 352 NRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVA--RRVNSLQQGGQPGDVAQAIAFL 429
Cdd:PRK05875 153 HRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSAdyRACTPLPRVGEVEDVANLAMFL 232

                        250
                 ....*....|....*..
gi 896156623 430 VSDRALGVNGHVLRVCG 446
Cdd:PRK05875 233 LSDAASWITGQVINVDG 249
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 212-396 1.56e-14

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 73.02  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANEL------GGLALQQDITA-DDAGNAIADAAVAry 284
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQ--EKLDAVAKEIeekygvETKTIAADFSAgDDIYERIEKELEG-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 grLDI--VIHNAGITRD--KMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYAT 360
Cdd:cd05356   77 --LDIgiLVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSA 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMT 396
Cdd:cd05356  155 SKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMS 190
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 215-410 1.67e-14

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 72.75  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 215 AAVTGSARGIGAAIARQLKADGAEVIVidvpqAG---EALSKVANELGGLALQQ-----DITADDAGNAIADAAVARYGR 286
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVAL-----AArrtDRLDELKAELLNPNPSVeveilDVTDEERNQLVIAELEAELGG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:cd05350   76 LDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI---PFV--NRQVARRV 410
Cdd:cd05350  156 SLAESLRYDVKKRGIRVTVINPGFIDTPLTANMftmPFLmsVEQAAKRI 204
PRK07024 PRK07024
SDR family oxidoreductase;
217-401 5.44e-14

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 71.50  E-value: 5.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLALQQDITAD----DAGNAIADAAVARYGRLDIVIH 292
Cdd:PRK07024   7 ITGASSGIGQALAREYARQGATLGL--VARRTDALQAFAARLPKAARVSVYAADvrdaDALAAAAADFIAAHGLPDVVIA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 293 NAGITRDKMFANMDDAK-WGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEA 371
Cdd:PRK07024  85 NAGISVGTLTEEREDLAvFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLES 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 896156623 372 YAEEFAKRGGNINAVAPGFIETDMTA----AIPF 401
Cdd:PRK07024 165 LRVELRPAGVRVVTIAPGYIRTPMTAhnpyPMPF 198
PRK07985 PRK07985
SDR family oxidoreductase;
193-451 6.14e-14

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 71.95  E-value: 6.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 193 LRVTSDAGEIPSDWDKPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVP---QAGEALSKVANELGGLA--LQQDI 267
Cdd:PRK07985  30 MTPVPDCGEKTYVGSGRLKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPveeEDAQDVKKIIEECGRKAvlLPGDL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 268 TADDAGNAIADAAVARYGRLDIVIHNAGI-TRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHkafekAPRIATMAST 346
Cdd:PRK07985 110 SDEKFARSLVHEAHKALGGLDIMALVAGKqVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPL-----LPKGASIITT 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 347 SGIAGNRGQTN---YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAA-------IPFVNRQvarrvNSLQQG 416
Cdd:PRK07985 185 SSIQAYQPSPHlldYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISggqtqdkIPQFGQQ-----TPMKRA 259

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 896156623 417 GQPGDVAQAIAFLVSDRALGVNGHVLRVCGQNIVG 451
Cdd:PRK07985 260 GQPAELAPVYVYLASQESSYVTAEVHGVCGGEHLG 294
PRK06949 PRK06949
SDR family oxidoreductase;
210-442 8.03e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 71.33  E-value: 8.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANEL---GGLA--LQQDITADDAGNAIADAAVARY 284
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVL--ASRRVERLKELRAEIeaeGGAAhvVSLDVTDYQSIKAAVAHAETEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGI-TRDKM-------FANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQT 356
Cdd:PRK06949  85 GTIDILVNNSGVsTTQKLvdvtpadFDFVFDTNTRGAFFVAQEVAKRMIARAKGAGNTKPGGRIINIASVAGLRVLPQIG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 357 NYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIpFVNRQVARRVNSL--QQGGQPGDVAQAIAFLVSDRA 434
Cdd:PRK06949 165 LYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHH-WETEQGQKLVSMLprKRVGKPEDLDGLLLLLAADES 243


                 ....*...
gi 896156623 435 LGVNGHVL 442
Cdd:PRK06949 244 QFINGAII 251
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 210-431 1.21e-13

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 70.62  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGaeVIVIDVPQAGEALSKVANELGG------LALQQDITADDAGNAIADAAVAR 283
Cdd:cd05343    4 WRGRVALVTGASVGIGAAVARALVQHG--MKVVGCARRVDKIEALAAECQSagyptlFPYQCDLSNEEQILSMFSAIRTQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPR--IATMASTSG---IAGNRGQTnY 358
Cdd:cd05343   82 HQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDghIININSMSGhrvPPVSVFHF-Y 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156623 359 ATSKAGVIAMVEAYAEE--FAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVS 431
Cdd:cd05343  161 AATKHAVTALTEGLRQElrEAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANAVLYVLS 235
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 212-451 1.54e-13

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 70.30  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSA--RGIGAAIARQLKADGAEVIVIDVPQAGEA-LSKVANELGG--LALQQDITADDAGNAIADAAVARYGR 286
Cdd:cd05372    1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTYQPEALRKrVEKLAERLGEsaLVLPCDVSNDEEIKELFAEVKKDWGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGitrdkmFANMDDAKwGSVIAVNIESQLKMNE-------QLLNHkAFEKAPRIATMASTSGIAGNRGQTNY- 358
Cdd:cd05372   81 LDGLVHSIA------FAPKVQLK-GPFLDTSRKGFLKALDisayslvSLAKA-ALPIMNPGGSIVTLSYLGSERVVPGYn 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 359 --ATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQV--ARRVNSLQQGGQPGDVAQAIAFLVSDRA 434
Cdd:cd05372  153 vmGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAASGITGFDKMLeySEQRAPLGRNVTAEEVGNTAAFLLSDLS 232

                        250
                 ....*....|....*...
gi 896156623 435 LGVNGHVLRV-CGQNIVG 451
Cdd:cd05372  233 SGITGEIIYVdGGYHIMG 250
PRK09186 PRK09186
flagellin modification protein A; Provisional
 210-450 3.21e-13

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 69.25  E-value: 3.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIV--IDVPQAGEALSKVANELGG--LALQQ-DITADDAGNAIADAAVARY 284
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAadIDKEALNELLESLGKEFKSkkLSLVElDITDQESLEEFLSKSAEKY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAgITRDKMFAN-MDDAKWGSVIAvNIESQLK----MNEQLLNHKAFEKAPRIATMASTSGIAGNRGQT--- 356
Cdd:PRK09186  82 GKIDGAVNCA-YPRNKDYGKkFFDVSLDDFNE-NLSLHLGssflFSQQFAKYFKKQGGGNLVNISSIYGVVAPKFEIyeg 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 357 -------NYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAipFVNrqvARRVNSLQQGG-QPGDVAQAIAF 428
Cdd:PRK09186 160 tsmtspvEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQPEA--FLN---AYKKCCNGKGMlDPDDICGTLVF 234

                        250       260
                 ....*....|....*....|..
gi 896156623 429 LVSDRALGVNghvlrvcGQNIV 450
Cdd:PRK09186 235 LLSDQSKYIT-------GQNII 249
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 212-447 3.22e-13

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 69.56  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVI--DVPQAGEALSKVANELGG---------LALQQDItaddagNAIADAA 280
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIAcrNEEKGEEAAAEIKKETGNakveviqldLSSLASV------RQFAEEF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 281 VARYGRLDIVIHNAGItrdkMfanmddAKWGSVIAVNIESQLKMN---EQLLNHK---AFEKA--PRIATMASTSGIAGN 352
Cdd:cd05327   75 LARFPRLDILINNAGI----M------APPRRLTKDGFELQFAVNylgHFLLTNLllpVLKASapSRIVNVSSIAHRAGP 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 353 RGQTN--------------YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMT--AAIPFVNRQVARR--VNSLQ 414
Cdd:cd05327  145 IDFNDldlennkeyspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLrrNGSFFLLYKLLRPflKKSPE 224

                        250       260       270
                 ....*....|....*....|....*....|...
gi 896156623 415 QGGQPgdVAQAIAflvSDRALGVNGHVLRVCGQ 447
Cdd:cd05327  225 QGAQT--ALYAAT---SPELEGVSGKYFSDCKI 252
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 212-430 6.54e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 68.91  E-value: 6.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVA--TARDTATLADLAEKYGDrlLPLALDVTDRAAVFAAVETAVEHFGRLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMV 369
Cdd:PRK08263  81 VVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896156623 370 EAYAEEFAKRGGNINAVAPGFIETD-----MTAAIPF-----VNRQVARRVNSLQQGGQPGDVAQAIAFLV 430
Cdd:PRK08263 161 EALAQEVAEFGIKVTLVEPGGYSTDwagtsAKRATPLdaydtLREELAEQWSERSVDGDPEAAAEALLKLV 231
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 212-446 7.90e-13

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 68.26  E-value: 7.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVpqAGEALSKVANELGG------LALQQDITADDAGNAIADAAVARYG 285
Cdd:cd05322    2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADI--NSENAEKVADEINAeygekaYGFGADATNEQSVIALSKGVDEIFK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGITRDKMFANMDDAKWGSVIAVNiesqlkMNEQLLNHKAFEK-------APRIATMASTSGIAGNRGQTNY 358
Cdd:cd05322   80 RVDLLVYSAGIAKSAKITDFELGDFDRSLQVN------LVGYFLCAREFSKlmirdgiQGRIIQINSKSGKVGSKHNSGY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 359 ATSKAGVIAMVEAYAEEFAKRGGNINAVAPG-FIETDM-TAAIPfvnrQVARRVN--------------SLQQGGQPGDV 422
Cdd:cd05322  154 SAAKFGGVGLTQSLALDLAEHGITVNSLMLGnLLKSPMfQSLLP----QYAKKLGikeseveqyyidkvPLKRGCDYQDV 229

                        250       260
                 ....*....|....*....|....
gi 896156623 423 AQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:cd05322  230 LNMLLFYASPKASYCTGQSINITG 253
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 214-429 1.03e-12

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 67.41  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 214 VAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAG-EALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDIV 290
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEAlHELAREVRELGGeaIAVVADVADAAQVERAADTAVERFGRIDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 291 IHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVE 370
Cdd:cd05360   82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTE 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156623 371 AYAEEFAKRGGNIN--AVAPGFIETdmtaaiPFVNrQVARRVNSLQQGG----QPGDVAQAIAFL 429
Cdd:cd05360  162 SLRAELAHDGAPISvtLVQPTAMNT------PFFG-HARSYMGKKPKPPppiyQPERVAEAIVRA 219
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 210-445 1.72e-12

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 67.47  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI--DVPQAGEALSKVANELGG--LALQQDITADDAGNA-IADAAVARY 284
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITgrTILPQLPGTAEEIEARGGkcIPVRCDHSDDDEVEAlFERVAREQQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNA-------GITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAgNRGQTN 357
Cdd:cd09763   81 GRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLE-YLFNVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIP--FVNRQVARRVNSLQQGGQPGDVAQAIAFLVSD-RA 434
Cdd:cd09763  160 YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPedDEGSWHAKERDAFLNGETTEYSGRCVVALAADpDL 239

                        250
                 ....*....|.
gi 896156623 435 LGVNGHVLRVC 445
Cdd:cd09763  240 MELSGRVLITG 250
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 210-446 1.81e-12

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 66.71  E-value: 1.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIdvPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCIN--SRNENKLKRMKKTLSKYGNIHYVVGDVSSTESARNVIEKAAKVLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRdkmfanmddakwGSVIAVNIESQLKMNEQLLNH--------KAF----EKAPRIATMASTSGI-AGNRGQT 356
Cdd:PRK05786  81 AIDGLVVTV------------GGYVEDTVEEFSGLEEMLTNHikiplyavNASlrflKEGSSIVLVSSMSGIyKASPDQL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 357 NYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMtaaIPFVNRQVARRVNSLQqgGQPGDVAQAIAFLVSDRALG 436
Cdd:PRK05786 149 SYAVAKAGLAKAVEILASELLGRGIRVNGIAPTTISGDF---EPERNWKKLRKLGDDM--APPEDFAKVIIWLLTDEADW 223

                        250
                 ....*....|
gi 896156623 437 VNGHVLRVCG 446
Cdd:PRK05786 224 VDGVVIPVDG 233
PRK07806 PRK07806
SDR family oxidoreductase;
210-294 2.39e-12

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 66.67  E-value: 2.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEAlSKVANEL---GG--LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK07806   4 LPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRA-NKVVAEIeaaGGraSAVGADLTDEESVAALMDTAREEF 82

                         90
                 ....*....|
gi 896156623 285 GRLDIVIHNA 294
Cdd:PRK07806  83 GGLDALVLNA 92
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 210-442 3.74e-12

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 66.05  E-value: 3.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIdvpqaGEALSK---VANELGGLALQQ------DITADDAGN--AIAD 278
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILL-----GRTEEKleaVYDEIEAAGGPQpaiiplDLLTATPQNyqQLAD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 279 AAVARYGRLDIVIHNAGITRDKM-FANMDDAKWGSVIAVNIESQLKMNEQLLnhKAFEKAPRiATMASTSGIAGNRGQTN 357
Cdd:PRK08945  85 TIEEQFGRLDGVLHNAGLLGELGpMEQQDPEVWQDVMQVNVNATFMLTQALL--PLLLKSPA-ASLVFTSSSVGRQGRAN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 ---YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTA-AIPFVNRQvarrvnSLQqggQPGDVAQAIAFLVSDR 433
Cdd:PRK08945 162 wgaYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMRAsAFPGEDPQ------KLK---TPEDIMPLYLYLMGDD 232


                 ....*....
gi 896156623 434 ALGVNGHVL 442
Cdd:PRK08945 233 SRRKNGQSF 241
PRK06194 PRK06194
hypothetical protein; Provisional
 208-393 4.70e-12

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 66.19  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGG-----LALQQDITADDAGNAIADAAVA 282
Cdd:PRK06194   2 KDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQ--DALDRAVAELRAqgaevLGVRTDVSDAAQVEALADAALE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 283 RYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQL--------KMNEQLLNHKAFEKapRIATMASTSGIAGNRG 354
Cdd:PRK06194  80 RFGAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIhgvraftpLMLAAAEKDPAYEG--HIVNTASMAGLLAPPA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 896156623 355 QTNYATSKAGVIAMVEAYAEEFAKRGGNINA--VAPGFIET 393
Cdd:PRK06194 158 MGIYNVSKHAVVSLTETLYQDLSLVTDQVGAsvLCPYFVPT 198
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 217-359 7.31e-12

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 63.74  E-value: 7.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  217 VTGSARGIGAAIARQLKADGAEVIVI-----DVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:pfam08659   5 ITGGLGGLGRELARWLAERGARHLVLlsrsaAPRPDAQALIAELEARGVevVVVACDVSDPDAVAALLAEIKAEGPPIRG 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896156623  290 VIHNAGITRDKMFANMDDAKWGSVIAVniesqlKMNEQLLNHKAFEKAP--RIATMASTSGIAGNRGQTNYA 359
Cdd:pfam08659  85 VIHAAGVLRDALLENMTDEDWRRVLAP------KVTGTWNLHEATPDEPldFFVLFSSIAGLLGSPGQANYA 150
PRK08278 PRK08278
SDR family oxidoreductase;
207-295 9.37e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 65.31  E-value: 9.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 207 DKPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVI--------DVPQAGEALSKVANELGG--LALQQDITADDAGNAI 276
Cdd:PRK08278   1 MMSLSGKTLFITGASRGIGLAIALRAARDGANIVIAaktaephpKLPGTIHTAAEEIEAAGGqaLPLVGDVRDEDQVAAA 80

                         90
                 ....*....|....*....
gi 896156623 277 ADAAVARYGRLDIVIHNAG 295
Cdd:PRK08278  81 VAKAVERFGGIDICVNNAS 99
PRK08264 PRK08264
SDR family oxidoreductase;
210-401 1.30e-11

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 64.14  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEviviDVPQAGEALSKVANELGG-LALQQDITADDAGNAIADAAvaryGRLD 288
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLLARGAA----KVYAAARDPESVTDLGPRvVPLQLDVTDPASVAAAAEAA----SDVT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 289 IVIHNAGITRDKMF---ANMDDAKwgSVIAVNIESQLKMNeqllnhKAFekAPRIA--------TMASTSGIAGNRGQTN 357
Cdd:PRK08264  76 ILVNNAGIFRTGSLlleGDEDALR--AEMETNYFGPLAMA------RAF--APVLAangggaivNVLSVLSWVNFPNLGT 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 896156623 358 YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPF 401
Cdd:PRK08264 146 YSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGLDA 189
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 213-431 1.79e-11

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 63.68  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGeaLSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDIV 290
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEAR--LAAAAAQELEgvLGLAGDVRDEADVRRAVDAMEEAFGGLDAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 291 IHNAGITRDKMFANMDDAKWGSVIAVNIESQLkmneqLLNHKAFEKAPR-----IATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:cd08929   79 VNNAGVGVMKPVEELTPEEWRLVLDTNLTGAF-----YCIHKAAPALLRrgggtIVNVGSLAGKNAFKGGAAYNASKFGL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156623 366 IAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVarrvnslqqggQPGDVAQAIAFLVS 431
Cdd:cd08929  154 LGLSEAAMLDLREANIRVVNVMPGSVDTGFAGSPEGQAWKL-----------APEDVAQAVLFALE 208
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 214-446 1.12e-10

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 61.87  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  214 VAAVTGSARGIGAAIARQLKADGAEViVIDVPQAGEALSKVANELG------GLALQQDITAD----DAGNAIADAAVAR 283
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRV-VLHYHRSAAAASTLAAELNarrpnsAVTCQADLSNSatlfSRCEAIIDACFRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  284 YGRLDIVIHNAGITRDKMFANMDDAKwGSVIAVNIESQLKmneQLLNHKAFekAPRIATMASTSGIAGNRGQ-------- 355
Cdd:TIGR02685  82 FGRCDVLVNNASAFYPTPLLRGDAGE-GVGDKKSLEVQVA---ELFGSNAI--APYFLIKAFAQRQAGTRAEqrstnlsi 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  356 ---------------TNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFieTDMTAAIPFVNRQVARRVNSL-QQGGQP 419
Cdd:TIGR02685 156 vnlcdamtdqpllgfTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL--SLLPDAMPFEVQEDYRRKVPLgQREASA 233

                         250       260
                  ....*....|....*....|....*..
gi 896156623  420 GDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:TIGR02685 234 EQIADVVIFLVSPKAKYITGTCIKVDG 260
PRK07041 PRK07041
SDR family oxidoreductase;
217-446 1.20e-10

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 61.21  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDIVIHNAGi 296
Cdd:PRK07041   2 VVGGSSGIGLALARAFAAEGARVTI--ASRSRDRLAAAARALGGGAPVRTAALDITDEAAVDAFFAEAGPFDHVVITAA- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 297 trdkmfanmdDAKWGSVIAVNIES-QLKMNEQLLNHKAFEKAPRIATMAS---TSGIAGNR---GQTNYATSKAGVIAMV 369
Cdd:PRK07041  79 ----------DTPGGPVRALPLAAaQAAMDSKFWGAYRVARAARIAPGGSltfVSGFAAVRpsaSGVLQGAINAALEALA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 370 EAYAEEFAKRggNINAVAPGFIETDMTAAIPFVNRQV----------ARRVnslqqgGQPGDVAQAIAFLVSDRAlgVNG 439
Cdd:PRK07041 149 RGLALELAPV--RVNTVSPGLVDTPLWSKLAGDAREAmfaaaaerlpARRV------GQPEDVANAILFLAANGF--TTG 218


                 ....*..
gi 896156623 440 HVLRVCG 446
Cdd:PRK07041 219 STVLVDG 225
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 210-452 1.22e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 61.89  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI-----DVPQAGEALSKVANELGGLALqqDITADDAGNAIADAAVARY 284
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVAsrsqeKVDAAVAQLQQAGPEGLGVSA--DVRDYAAVEAAFAQIADEF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAG----ITRDKMFANmddaKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAgNRGQTNYAT 360
Cdd:PRK07576  85 GPIDVLVSGAAgnfpAPAAGMSAN----GFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVP-MPMQAHVCA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIE----TDMTAAIPFVNRQVARRVnSLQQGGQPGDVAQAIAFLVSDRALG 436
Cdd:PRK07576 160 AKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAgtegMARLAPSPELQAAVAQSV-PLKRNGTKQDIANAALFLASDMASY 238

                        250
                 ....*....|....*..
gi 896156623 437 VNGHVLRV-CGQNIVGA 452
Cdd:PRK07576 239 ITGVVLPVdGGWSLGGA 255
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 214-446 1.50e-10

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 61.05  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 214 VAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEA-LSKVANELGGLalqQDITADDAGNAIaDAAVARYGRLDIVIH 292
Cdd:cd05361    3 IALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAeRQAFESENPGT---KALSEQKPEELV-DAVLQAGGAIDVLVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 293 NAGITRdkMFANMDDAK----WGSVIAVNIESQLKMNEQLLNHKAfEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAM 368
Cdd:cd05361   79 NDYIPR--PMNPIDGTSeadiRQAFEALSIFPFALLQAAIAQMKK-AGGGSIIFITSAVPKKPLAYNSLYGPARAAAVAL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 369 VEAYAEEFAKRGGNINAVAPGFIET-DMTAAIPFVN----RQVARRVNSLQQGGQPGDVAQAIAFLVSDRALGVNGHVLR 443
Cdd:cd05361  156 AESLAKELSRDNILVYAIGPNFFNSpTYFPTSDWENnpelRERVKRDVPLGRLGRPDEMGALVAFLASRRADPITGQFFA 235


                 ...
gi 896156623 444 VCG 446
Cdd:cd05361  236 FAG 238
PRK06720 PRK06720
hypothetical protein; Provisional
 210-303 1.87e-10

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 59.60  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQ-AGEALSKVANELGGLALQQDITADDAGN--AIADAAVARYGR 286
Cdd:PRK06720  14 LAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQeSGQATVEEITNLGGEALFVSYDMEKQGDwqRVISITLNAFSR 93

                         90
                 ....*....|....*...
gi 896156623 287 LDIVIHNAGITR-DKMFA 303
Cdd:PRK06720  94 IDMLFQNAGLYKiDSIFS 111
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 98-445 2.21e-10

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 62.02  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  98 LAAAKHMRKLDKGGRIVTVSRakdaHHNATPAEIAENAVAGGIEGLIRSLGHE---VRGGStangILVAPGVSVTAPSVI 174
Cdd:cd05274   36 LVAALLAAYASTGPPLWLVTR----GAEAVSADDVAALAQAALWGLLRVLALEhpeLWGGL----VDLDAADAADEAAAL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 175 SSL--HFFLSGRSAFIDGQFL-----RVTSDAGEIPSDwDKPLAGKVAaVTGSARGIGAAIARQLKADGAEVIVI---DV 244
Cdd:cd05274  108 AALlaGAPGEDELALRGGQRLvprlvRAPAAALELAAA-PGGLDGTYL-ITGGLGGLGLLVARWLAARGARHLVLlsrRG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 245 PQAGEALSKVANELGG---LALQQDITaDDAGNAIADAAVARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVniesq 321
Cdd:cd05274  186 PAPRAAARAALLRAGGarvSVVRCDVT-DPAALAALLAELAAGGPLAGVIHAAGVLRDALLAELTPAAFAAVLAA----- 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 322 lKMNEQLLNHKAFEKAP--RIATMASTSGIAGNRGQTNYatskAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI 399
Cdd:cd05274  260 -KVAGALNLHELTPDLPldFFVLFSSVAALLGGAGQAAY----AAANAFLDALAAQRRRRGLPATSVQWGAWAGGGMAAA 334

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 896156623 400 PFVNRQVARRvnslqqGGQPGDVAQAIAFLvsDRALGVNGHVLRVC 445
Cdd:cd05274  335 AALRARLARS------GLGPLAPAEALEAL--EALLASDAPQAVVA 372
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 208-307 2.56e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 61.48  E-value: 2.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIdvPQAGEALSKVANEL---GGLALqqDITAD----DAGNAIADAA 280
Cdd:PRK07109   4 KPIGRQVVVITGASAGVGRATARAFARRGAKVVLL--ARGEEGLEALAAEIraaGGEAL--AVVADvadaEAVQAAADRA 79

                         90       100
                 ....*....|....*....|....*..
gi 896156623 281 VARYGRLDIVIHNAGITrdkMFANMDD 307
Cdd:PRK07109  80 EEELGPIDTWVNNAMVT---VFGPFED 103
PRK07102 PRK07102
SDR family oxidoreductase;
224-426 6.12e-10

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 59.55  E-value: 6.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 224 IGAAIARQLKADGAEVIVidVPQAGEALSKVANEL---GGLA---LQQDITADDAGNAIADAAVARygrLDIVIHNAGIT 297
Cdd:PRK07102  13 IARACARRYAAAGARLYL--AARDVERLERLADDLrarGAVAvstHELDILDTASHAAFLDSLPAL---PDIVLIAVGTL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 298 RDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHkaFEkAPRIATMASTSGIAGNRG-QTNY--ATSKAGVIAMVEAYAE 374
Cdd:PRK07102  88 GDQAACEADPALALREFRTNFEGPIALLTLLANR--FE-ARGSGTIVGISSVAGDRGrASNYvyGSAKAALTAFLSGLRN 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896156623 375 EFAKRGGNINAVAPGFIETDMTAAIPFVNRQVArrvnslqqggQPGDVAQAI 426
Cdd:PRK07102 165 RLFKSGVHVLTVKPGFVRTPMTAGLKLPGPLTA----------QPEEVAKDI 206
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 212-426 8.82e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 59.54  E-value: 8.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIV-IDVPQAGEALSKVANELGgLALQQDITADDAGNAIADAAVARYGRLDIV 290
Cdd:PRK06180   4 MKTWLITGVSSGFGRALAQAALAAGHRVVGtVRSEAARADFEALHPDRA-LARLLDVTDFDAIDAVVADAEATFGPIDVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 291 IHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVE 370
Cdd:PRK06180  83 VNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISE 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896156623 371 AYAEEFAKRGGNINAVAPGFIETD-----MTAA---IP-----FVNRQVARRVNSLQQGGQPGDVAQAI 426
Cdd:PRK06180 163 SLAKEVAPFGIHVTAVEPGSFRTDwagrsMVRTprsIAdydalFGPIRQAREAKSGKQPGDPAKAAQAI 231
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 215-419 9.16e-10

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 58.30  E-value: 9.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 215 AAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLALQQDITADDAGNAIADAAvaryGRLDIVIHNA 294
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLL--SGRDAGALAGLAAEVGALARPADVAAELEVWALAQEL----GPLDLLVYAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 295 GITRDKMFANMDDAKWGSVIAVNIESQLKMneqlLNHKAFEKAP--RIATMASTSGIAGNRGQTNYATSKAGVIAMVEAY 372
Cdd:cd11730   75 GAILGKPLARTKPAAWRRILDANLTGAALV----LKHALALLAAgaRLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVA 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 896156623 373 AEEFakRGGNINAVAPGFIETDMTAAIPFVNR------QVARRV-NSLQQGGQP 419
Cdd:cd11730  151 RKEV--RGLRLTLVRPPAVDTGLWAPPGRLPKgalspeDVAAAIlEAHQGEPQG 202
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 210-388 2.09e-09

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 57.84  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI--------DVPQAGEALSKVANELGG--LALQQDITADDAGNAIADA 279
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAaktaephpKLPGTIYTAAEEIEAAGGkaLPCIVDIRDEDQVRAAVEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 280 AVARYGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGN--RGQTN 357
Cdd:cd09762   81 AVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKwfKNHTA 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 896156623 358 YATSKAGVIAMVEAYAEEFAKRGGNINAVAP 388
Cdd:cd09762  161 YTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK08416 PRK08416
enoyl-ACP reductase;
340-446 2.29e-09

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 57.86  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 340 IATMASTsgiaGNRGQT-NYA---TSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPF---VNRQVARRvNS 412
Cdd:PRK08416 147 IISLSST----GNLVYIeNYAghgTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNyeeVKAKTEEL-SP 221

                         90       100       110
                 ....*....|....*....|....*....|....
gi 896156623 413 LQQGGQPGDVAQAIAFLVSDRALGVNGHVLRVCG 446
Cdd:PRK08416 222 LNRMGQPEDLAGACLFLCSEKASWLTGQTIVVDG 255
PRK07201 PRK07201
SDR family oxidoreductase;
209-295 2.36e-09

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 59.58  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAevIVIDVPQAGEALSKVANEL---GG--LALQQDITADDAGNAIADAAVAR 283
Cdd:PRK07201 368 PLVGKVVLITGASSGIGRATAIKVAEAGA--TVFLVARNGEALDELVAEIrakGGtaHAYTCDLTDSAAVDHTVKDILAE 445

                         90
                 ....*....|..
gi 896156623 284 YGRLDIVIHNAG 295
Cdd:PRK07201 446 HGHVDYLVNNAG 457
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 198-296 2.52e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 58.11  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 198 DAGEIPSDwdkplAGKVAAVTGSARGIGAAIARQLKADGAEVI--VIDVPQAGEALSKV--ANELGGLALQQ-DITADDA 272
Cdd:PRK06197   7 TAADIPDQ-----SGRVAVVTGANTGLGYETAAALAAKGAHVVlaVRNLDKGKAAAARItaATPGADVTLQElDLTSLAS 81

                         90       100
                 ....*....|....*....|....
gi 896156623 273 GNAIADAAVARYGRLDIVIHNAGI 296
Cdd:PRK06197  82 VRAAADALRAAYPRIDLLINNAGV 105
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 208-395 2.58e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 58.09  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIV-----------IDVPQAGEALSKVANELGG--LALQQDITADDAGN 274
Cdd:PRK08303   4 KPLRGKVALVAGATRGAGRGIAVELGAAGATVYVtgrstrarrseYDRPETIEETAELVTAAGGrgIAVQVDHLVPEQVR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 275 AIADAAVARYGRLDIVIHNagITRDKMFANMDDAKWGSviavNIESQLKMNEQ------LLNHKAFE---KAPRIATMAS 345
Cdd:PRK08303  84 ALVERIDREQGRLDILVND--IWGGEKLFEWGKPVWEH----SLDKGLRMLRLaidthlITSHFALPlliRRPGGLVVEI 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 896156623 346 TSGIA-----GNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDM 395
Cdd:PRK08303 158 TDGTAeynatHYRLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEM 212
PRK07023 PRK07023
SDR family oxidoreductase;
215-432 2.69e-09

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 57.33  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 215 AAVTGSARGIGAAIARQLKADGAEVIVID-------VPQAGEALSKVANELGGLALQQDITADDAGNAIADAAvarygRL 287
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVArsrhpslAAAAGERLAEVELDLSDAAAAAAWLAGDLLAAFVDGA-----SR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRD-KMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVI 366
Cdd:PRK07023  79 VLLINNAGTVEPiGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAALD 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156623 367 AMVEAYAEEfAKRGGNINAVAPGFIETDMTAAI------PFVNRQVARRVNSLQQGGQPGDVA-QAIAFLVSD 432
Cdd:PRK07023 159 HHARAVALD-ANRALRIVSLAPGVVDTGMQATIratdeeRFPMRERFRELKASGALSTPEDAArRLIAYLLSD 230
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
213-444 2.80e-09

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 57.39  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDvPQAGEALSKVANELGG------LALQQDITADDAGNAI-----ADAAV 281
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISIS-RTENKELTKLAEQYNSnltfhsLDLQDVHELETNFNEIlssiqEDNVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 282 ARYgrldiVIHNAGitrdkMFANMDDAKWGSV------IAVNIESQLKMNEQLLNH-KAFEKAPRIATMasTSGIAGN-- 352
Cdd:PRK06924  81 SIH-----LINNAG-----MVAPIKPIEKAESeelitnVHLNLLAPMILTSTFMKHtKDWKVDKRVINI--SSGAAKNpy 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 353 RGQTNYATSKAGVIAMVEAYAEEFAKR--GGNINAVAPGFIETDMTAAIPFVNRQVARRVN---SLQQGGQ---PGDVAQ 424
Cdd:PRK06924 149 FGWSAYCSSKAGLDMFTQTVATEQEEEeyPVKIVAFSPGVMDTNMQAQIRSSSKEDFTNLDrfiTLKEEGKllsPEYVAK 228

                        250       260
                 ....*....|....*....|
gi 896156623 425 AIAFLVSDRALGvNGHVLRV 444
Cdd:PRK06924 229 ALRNLLETEDFP-NGEVIDI 247
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
217-430 3.03e-09

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 58.07  E-value: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVIDVPQAGEAlsKVANELGGLALQQDITADDAgnaiADAAVARYgrlDIVIHNAGI 296
Cdd:COG0451    4 VTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAA--NLAALPGVEFVRGDLRDPEA----LAAALAGV---DAVVHLAAP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 297 TRDKMfanmddAKWGSVIAVNIESQLKMNEQLLNHkafeKAPRIaTMASTSGIAGN-----------RGQTNYATSKagv 365
Cdd:COG0451   75 AGVGE------EDPDETLEVNVEGTLNLLEAARAA----GVKRF-VYASSSSVYGDgegpidedtplRPVSPYGASK--- 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156623 366 iAMVEAYAEEFAKRGGnINAVA---PGFIETDMTAAIPFVNRQVARR--VNSLQQGGQP------GDVAQAIAFLV 430
Cdd:COG0451  141 -LAAELLARAYARRYG-LPVTIlrpGNVYGPGDRGVLPRLIRRALAGepVPVFGDGDQRrdfihvDDVARAIVLAL 214
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 212-401 4.24e-09

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 56.65  E-value: 4.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGGL-ALQQDITadDAGNAIADAAVARygRLDIV 290
Cdd:cd05354    3 DKTVLVTGANRGIGKAFVESLLAHGAKKVYAAVRDPGSAAHLVAKYGDKVvPLRLDVT--DPESIKAAAAQAK--DVDVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 291 IHNAGITRDK-MFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMV 369
Cdd:cd05354   79 INNAGVLKPAtLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSLT 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 896156623 370 EAYAEEFAKRGGNINAVAPGFIETDMTAAIPF 401
Cdd:cd05354  159 QGLRAELAAQGTLVLSVHPGPIDTRMAAGAGG 190
PRK05866 PRK05866
SDR family oxidoreductase;
209-295 1.02e-08

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 56.29  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANEL---GG--LALQQDITADDAGNAIADAAVAR 283
Cdd:PRK05866  37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVA--VARREDLLDAVADRItraGGdaMAVPCDLSDLDAVDALVADVEKR 114

                         90
                 ....*....|..
gi 896156623 284 YGRLDIVIHNAG 295
Cdd:PRK05866 115 IGGVDILINNAG 126
PRK06196 PRK06196
oxidoreductase; Provisional
 195-296 1.37e-08

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 56.23  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 195 VTSDAGEIPSDWDkpLAGKVAAVTGSARGIGAAIARQLKADGAEVIVI--DVPQAGEALSKVAN-ELGGLalqqDITADD 271
Cdd:PRK06196  11 AASTAEEVLAGHD--LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVParRPDVAREALAGIDGvEVVML----DLADLE 84

                         90       100
                 ....*....|....*....|....*
gi 896156623 272 AGNAIADAAVARYGRLDIVIHNAGI 296
Cdd:PRK06196  85 SVRAFAERFLDSGRRIDILINNAGV 109
PRK08251 PRK08251
SDR family oxidoreductase;
217-397 1.54e-08

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 55.33  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGA------------EVIVIDVPQAGEALSKVANELgglalqqDITADDAGNAIADAAVARY 284
Cdd:PRK08251   7 ITGASSGLGAGMAREFAAKGRdlalcarrtdrlEELKAELLARYPGIKVAVAAL-------DVNDHDQVFEVFAEFRDEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRD------KMFANMDDAKWGSVIA-VNIESQLKM-NEQLLNHkafekaprIATMASTSGIAGNRG-Q 355
Cdd:PRK08251  80 GGLDRVIVNAGIGKGarlgtgKFWANKATAETNFVAAlAQCEAAMEIfREQGSGH--------LVLISSVSAVRGLPGvK 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 896156623 356 TNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTA 397
Cdd:PRK08251 152 AAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNA 193
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
210-451 1.60e-08

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 55.49  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSA--RGIGAAIARQLKADGAEVIVIDVP-QAGEALSKVANELGGLA--------LQQDITADDAGNAIAD 278
Cdd:PRK07370   4 LTGKKALVTGIAnnRSIAWGIAQQLHAAGAELGITYLPdEKGRFEKKVRELTEPLNpslflpcdVQDDAQIEETFETIKQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 279 aavaRYGRLDIVIHNAGitrdkmFANMDD--------AKWGSVIAVNIESQLKMNeqlLNHKAFEKAPRIATMASTSGIA 350
Cdd:PRK07370  84 ----KWGKLDILVHCLA------FAGKEEligdfsatSREGFARALEISAYSLAP---LCKAAKPLMSEGGSIVTLTYLG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 351 GNRGQTNY---ATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQV--ARRVNSLQQGGQPGDVAQA 425
Cdd:PRK07370 151 GVRAIPNYnvmGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLASSAVGGILDMIhhVEEKAPLRRTVTQTEVGNT 230

                        250       260
                 ....*....|....*....|....*..
gi 896156623 426 IAFLVSDRALGVNGHVLRV-CGQNIVG 451
Cdd:PRK07370 231 AAFLLSDLASGITGQTIYVdAGYCIMG 257
PRK09134 PRK09134
SDR family oxidoreductase;
208-435 1.62e-08

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 55.32  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIV--IDVPQAGEALSKVANELGG--LALQQDITADDAGNAIADAAVAR 283
Cdd:PRK09134   5 SMAAPRAALVTGAARRIGRAIALDLAAHGFDVAVhyNRSRDEAEALAAEIRALGRraVALQADLADEAEVRALVARASAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLlnHKAFEKAPR--IATMASTSGIAGNRGQTNYATS 361
Cdd:PRK09134  85 LGPITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAF--ARALPADARglVVNMIDQRVWNLNPDFLSYTLS 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156623 362 KAGVIAMVEAYAEEFAKRgGNINAVAPG--FIETDMTAAipfvNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRAL 435
Cdd:PRK09134 163 KAALWTATRTLAQALAPR-IRVNAIGPGptLPSGRQSPE----DFARQHAATPLGRGSTPEEIAAAVRYLLDAPSV 233
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
210-451 1.94e-08

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 55.12  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSA--RGIGAAIARQLKADGAEVIVIdvpQAGEALSKVANELGG-------LALQQDITADDAgnaiADAA 280
Cdd:PRK08594   5 LEGKTYVVMGVAnkRSIAWGIARSLHNAGAKLVFT---YAGERLEKEVRELADtlegqesLLLPCDVTSDEE----ITAC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 281 VARYGRLDIVIHnaGITRDKMFANMDD--------AKWGSVIAVNIESqlkMNEQLLNHKAFEKAPRIATMASTSGIAGN 352
Cdd:PRK08594  78 FETIKEEVGVIH--GVAHCIAFANKEDlrgefletSRDGFLLAQNISA---YSLTAVAREAKKLMTEGGSIVTLTYLGGE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 353 RGQTNY---ATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVN---RQVARRVnSLQQGGQPGDVAQAI 426
Cdd:PRK08594 153 RVVQNYnvmGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTLSAKGVGGFNsilKEIEERA-PLRRTTTQEEVGDTA 231

                        250       260
                 ....*....|....*....|....*.
gi 896156623 427 AFLVSDRALGVNGHVLRV-CGQNIVG 451
Cdd:PRK08594 232 AFLFSDLSRGVTGENIHVdSGYHIIG 257
PRK06482 PRK06482
SDR family oxidoreductase;
217-399 2.28e-08

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 55.12  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVI-VIDVPQAGEAL-SKVANELGGLALqqDITADDAGNAIADAAVARYGRLDIVIHNA 294
Cdd:PRK06482   7 ITGASSGFGRGMTERLLARGDRVAaTVRRPDALDDLkARYGDRLWVLQL--DVTDSAAVRAVVDRAFAALGRIDVVVSNA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 295 GITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEAYAE 374
Cdd:PRK06482  85 GYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAVAQ 164

                        170       180
                 ....*....|....*....|....*
gi 896156623 375 EFAKRGGNINAVAPGFIETDMTAAI 399
Cdd:PRK06482 165 EVAPFGIEFTIVEPGPARTNFGAGL 189
PRK07454 PRK07454
SDR family oxidoreductase;
213-393 3.80e-08

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 54.20  E-value: 3.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANEL---GGLA--LQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLAL--VARSQDALEALAAELrstGVKAaaYSIDLSNPEAIAPGIAELLEQFGCP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKafeKAPRIATMASTSGIAGNR---GQTNYATSKAG 364
Cdd:PRK07454  85 DVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGM---RARGGGLIINVSSIAARNafpQWGAYCVSKAA 161

                        170       180
                 ....*....|....*....|....*....
gi 896156623 365 VIAMVEAYAEEFAKRGGNINAVAPGFIET 393
Cdd:PRK07454 162 LAAFTKCLAEEERSHGIRVCTITLGAVNT 190
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 217-436 4.19e-08

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 53.35  E-value: 4.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVIDvPQAGEalskvanelgglaLQQDITADDAgnaiADAAVARYGRLDIVIHNAGI 296
Cdd:cd11731    3 VIGATGTIGLAVAQLLSAHGHEVITAG-RSSGD-------------YQVDITDEAS----IKALFEKVGHFDAIVSTAGD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 297 TRDKMFANMDDAKWGSVIAVNIESQLKMneqllnhkAFEKAPRIATMAS---TSGIAGNR---GQTNYATSKAGVIAMVE 370
Cdd:cd11731   65 AEFAPLAELTDADFQRGLNSKLLGQINL--------VRHGLPYLNDGGSitlTSGILAQRpipGGAAAATVNGALEGFVR 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896156623 371 AYAEEFAkRGGNINAVAPGFIETDMTAAIPFVnrqvarrvnslqQGGQPG---DVAQAIAFLVSDRALG 436
Cdd:cd11731  137 AAAIELP-RGIRINAVSPGVVEESLEAYGDFF------------PGFEPVpaeDVAKAYVRSVEGAFTG 192
PRK06182 PRK06182
short chain dehydrogenase; Validated
 213-295 6.52e-08

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 53.81  E-value: 6.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVidvpqAGEALSKVAN--ELGGLALQQDITADDAGNAIADAAVARYGRLDIV 290
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYG-----AARRVDKMEDlaSLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDVL 78


                 ....*
gi 896156623 291 IHNAG 295
Cdd:PRK06182  79 VNNAG 83
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 213-434 7.22e-08

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 53.44  E-value: 7.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVidvpqAG---EALSKVANELG------GLALQQDITADDAGNAIADAAVAR 283
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLIL-----TGrraERLQELADELGakfpvkVLPLQLDVSDRESIEAALENLPEE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITR--DKMF-ANMDDakWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYAT 360
Cdd:cd05346   76 FRDIDILVNNAGLALglDPAQeADLED--WETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNSLQQGGQPGDVAQAIAFLVSDRA 434
Cdd:cd05346  154 TKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLVRFHGDKEKADKVYEGVEPLTPEDIAETILWVASRPA 227
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 217-398 7.59e-08

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 53.27  E-value: 7.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGGLALQQDITADDAGNAIADAAVArYGRLDIVIHNAGI 296
Cdd:cd08951   12 ITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNA-IGRFDAVIHNAGI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 297 TRDKmFANMDDAKWGSVIAVNIESQLKMNEQLLNHKafekapRIATM---------ASTSGI-AGNRGQTN---YATSKA 363
Cdd:cd08951   91 LSGP-NRKTPDTGIPAMVAVNVLAPYVLTALIRRPK------RLIYLssgmhrggnASLDDIdWFNRGENDspaYSDSKL 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 896156623 364 GVIAMVEAYAEEFAKRggNINAVAPGFIETDMTAA 398
Cdd:cd08951  164 HVLTLAAAVARRWKDV--SSNAVHPGWVPTKMGGA 196
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 217-439 7.72e-08

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 53.01  E-value: 7.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVI---DVPQAgEALskvaNELGGLALQQDITADDAGNAIADAAVARYGRLDIVIHN 293
Cdd:PRK06483   7 ITGAGQRIGLALAWHLLAQGQPVIVSyrtHYPAI-DGL----RQAGAQCIQADFSTNAGIMAFIDELKQHTDGLRAIIHN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 294 A--------GITRDKMFANMddakwgsvIAVNIESQLKMN---EQLLNHKAFEKAPRI------ATMASTSGIAgnrgqt 356
Cdd:PRK06483  82 AsdwlaekpGAPLADVLARM--------MQIHVNAPYLLNlalEDLLRGHGHAASDIIhitdyvVEKGSDKHIA------ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 357 nYATSKAGVIAMVEAYAEEFAKRgGNINAVAPGFI---ETDMTAAipfvnRQVARRVNSLQQGGQPGDVAQAIAFL---- 429
Cdd:PRK06483 148 -YAASKAALDNMTLSFAAKLAPE-VKVNSIAPALIlfnEGDDAAY-----RQKALAKSLLKIEPGEEEIIDLVDYLltsc 220

                        250
                 ....*....|.
gi 896156623 430 -VSDRALGVNG 439
Cdd:PRK06483 221 yVTGRSLPVDG 231
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
210-452 8.98e-08

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 53.29  E-value: 8.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTG--SARGIGAAIARQLKADGAEVIVIDV-PQAGEALSKVANELGG-LALQQDITADDAGNAIADAAVARYG 285
Cdd:PRK06997   4 LAGKRILITGllSNRSIAYGIAKACKREGAELAFTYVgDRFKDRITEFAAEFGSdLVFPCDVASDEQIDALFASLGQHWD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGIT-RDKMFANMDDA--KWGSVIAVNIESqlkMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYAT-- 360
Cdd:PRK06997  84 GLDGLVHSIGFApREAIAGDFLDGlsRENFRIAHDISA---YSFPALAKAALPMLSDDASLLTLSYLGAERVVPNYNTmg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 -SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIET-------DMTAAIPFVNRQVARRVNSLQQggqpgDVAQAIAFLVSD 432
Cdd:PRK06997 161 lAKASLEASVRYLAVSLGPKGIRANGISAGPIKTlaasgikDFGKILDFVESNAPLRRNVTIE-----EVGNVAAFLLSD 235

                        250       260
                 ....*....|....*....|.
gi 896156623 433 RALGVNGHVLRV-CGQNIVGA 452
Cdd:PRK06997 236 LASGVTGEITHVdSGFNAVVG 256
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 212-446 1.05e-07

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 52.33  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGGLALQQDITADdagnaiaDAAVARYGRLDIVI 291
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEADASIIVLDSDSFTEQAKQVV-------ASVARLSGKVDALI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 292 HNAGitrdkMFAnMDDAKWGSVIAvNIESQLKMN------EQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:cd05334   74 CVAG-----GWA-GGSAKSKSFVK-NWDLMWKQNlwtsfiASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYGAAKAAV 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 366 IAMVEAYAEEFAKRGGNI--NAVAPGFIETDMT-AAIPFVNRQvarRVNSLQQggqpgdVAQAIAFLVSDRALGVNGHVL 442
Cdd:cd05334  147 HQLTQSLAAENSGLPAGStaNAILPVTLDTPANrKAMPDADFS---SWTPLEF------IAELILFWASGAARPKSGSLI 217


                 ....
gi 896156623 443 RVCG 446
Cdd:cd05334  218 PVVT 221
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 207-446 1.14e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 52.74  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 207 DKPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGlALQQDITA---DDAGNAIADAAVAR 283
Cdd:PRK06125   2 DLHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHL--VARDADALEALAADLRA-AHGVDVAVhalDLSSPEAREQLAAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhkAFEKAPRIATMASTSGIAGNRGQTNY---AT 360
Cdd:PRK06125  79 AGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAY---PRMKARGSGVIVNVIGAAGENPDADYicgSA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQ----VARRVNSLQQG------GQPGDVAQAIAFLV 430
Cdd:PRK06125 156 GNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLLKGRARaelgDESRWQELLAGlplgrpATPEEVADLVAFLA 235

                        250
                 ....*....|....*.
gi 896156623 431 SDRALGVNGHVLRVCG 446
Cdd:PRK06125 236 SPRSGYTSGTVVTVDG 251
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 214-431 1.28e-07

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 52.38  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 214 VAAVTGSARGIGAAIARQLKADGAEVIVI-DVPQAGEALSKVANELGG---LALQQDITADDAGNAIADAAVARYGRLDI 289
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAaRREAKLEALLVDIIRDAGgsaKAVPTDARDEDEVIALFDLIEEEIGPLEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMV 369
Cdd:cd05373   81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156623 370 EAYAEEFAKRGGNI-NAVAPGFIETDmtaaipFVNRQVARRVNSLQQGG--QPGDVAQAIAFLVS 431
Cdd:cd05373  161 QSMARELGPKGIHVaHVIIDGGIDTD------FIRERFPKRDERKEEDGilDPDAIAEAYWQLHT 219
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 210-446 1.77e-07

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 52.16  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIVI-----DVPQAGEALSKVANeLGGLALQQDITA-DDAGNAIADaaVAR 283
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLsrneeNLKKAREKIKSESN-VDVSYIVADLTKrEDLERTVKE--LKN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhKAFEKApRIATMASTSGIAGNRGQTNYATSKA 363
Cdd:PRK08339  83 IGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALV--PAMERK-GFGRIIYSTSVAIKEPIPNIALSNV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAM---VEAYAEEFAKRGGNINAVAPGFIETDMTaaIPFVNRQVARRVNSLQQG-------------GQPGDVAQAIA 427
Cdd:PRK08339 160 VRISMaglVRTLAKELGPKGITVNGIMPGIIRTDRV--IQLAQDRAKREGKSVEEAlqeyakpiplgrlGEPEEIGYLVA 237

                        250
                 ....*....|....*....
gi 896156623 428 FLVSDRALGVNGHVLRVCG 446
Cdd:PRK08339 238 FLASDLGSYINGAMIPVDG 256
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
210-451 1.98e-07

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 52.06  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSA--RGIGAAIARQLKADGAEvivIDVPQAGEALSK----VANELGG-LALQQDITADDAGNAIADAAVA 282
Cdd:PRK08159   8 MAGKRGLILGVAnnRSIAWGIAKACRAAGAE---LAFTYQGDALKKrvepLAAELGAfVAGHCDVTDEASIDAVFETLEK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 283 RYGRLDIVIHNAG-------------ITRDKMFANMDDAKWgSVIAVNIESQLKMNE-----QLLNHKAFEKAPRIATMa 344
Cdd:PRK08159  85 KWGKLDFVVHAIGfsdkdeltgryvdTSRDNFTMTMDISVY-SFTAVAQRAEKLMTDggsilTLTYYGAEKVMPHYNVM- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 345 stsGIAgnrgqtnyatsKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAI-PFvnRQVAR--RVNS-LQQGGQPG 420
Cdd:PRK08159 163 ---GVA-----------KAALEASVKYLAVDLGPKNIRVNAISAGPIKTLAASGIgDF--RYILKwnEYNApLRRTVTIE 226

                        250       260       270
                 ....*....|....*....|....*....|..
gi 896156623 421 DVAQAIAFLVSDRALGVNGHVLRV-CGQNIVG 451
Cdd:PRK08159 227 EVGDSALYLLSDLSRGVTGEVHHVdSGYHVVG 258
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
209-451 7.68e-07

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 50.32  E-value: 7.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 209 PLAGKVAAVTGSA--RGIGAAIARQLKADGAEVIVIDVPQAGEA-LSKVANELGG-LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK07533   7 PLAGKRGLVVGIAneQSIAWGCARAFRALGAELAVTYLNDKARPyVEPLAEELDApIFLPLDVREPGQLEAVFARIAEEW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGitrdkmFANMDDAKwGSVIAVNIES-QLKMNeqlLNHKAFEKAPRIA--------TMASTSGIAGNRGQ 355
Cdd:PRK07533  87 GRLDFLLHSIA------FAPKEDLH-GRVVDCSREGfALAMD---VSCHSFIRMARLAeplmtnggSLLTMSYYGAEKVV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 356 TNY---ATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQV--ARRVNSLQQGGQPGDVAQAIAFLV 430
Cdd:PRK07533 157 ENYnlmGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKTRAASGIDDFDALLedAAERAPLRRLVDIDDVGAVAAFLA 236

                        250       260
                 ....*....|....*....|..
gi 896156623 431 SDRALGVNGHVLRV-CGQNIVG 451
Cdd:PRK07533 237 SDAARRLTGNTLYIdGGYHIVG 258
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
210-444 1.03e-06

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 49.72  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSA--RGIGAAIARQLKADGAEVIVIdvpQAGEALSKVANELGG---LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK06079   5 LSGKKIVVMGVAnkRSIAWGCAQAIKDQGATVIYT---YQNDRMKKSLQKLVDeedLLVECDVASDESIERAFATIKERV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITRDKMFAN--MDDAKWGSVIAVNIESQ-----LKMNEQLLNHKAfekapRIATMastSGIAGNRGQTN 357
Cdd:PRK06079  82 GKIDGIVHAIAYAKKEELGGnvTDTSRDGYALAQDISAYsliavAKYARPLLNPGA-----SIVTL---TYFGSERAIPN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 YAT---SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPfVNRQVARRVNSLQQGGQP---GDVAQAIAFLVS 431
Cdd:PRK06079 154 YNVmgiAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAVTGIK-GHKDLLKESDSRTVDGVGvtiEEVGNTAAFLLS 232

                        250
                 ....*....|...
gi 896156623 432 DRALGVNGHVLRV 444
Cdd:PRK06079 233 DLSTGVTGDIIYV 245
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 212-395 1.10e-06

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 49.77  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVI--DVPQAGEALSKVANELGG---LALQQDITADDAGNAIADAAVARYGR 286
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVIMAcrDMAKCEEAAAEIRRDTLNhevIVRHLDLASLKSIRAFAAEFLAEEDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 LDIVIHNAGITRDKMFANMDdakwgsviavNIESQLKMNE-------QLLNHKAFEKAP-RIATMASTSGIAGN------ 352
Cdd:cd09807   81 LDVLINNAGVMRCPYSKTED----------GFEMQFGVNHlghflltNLLLDLLKKSAPsRIVNVSSLAHKAGKinfddl 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 896156623 353 RGQTNYATSKA---GVIAMVeAYAEEFAKR----GGNINAVAPGFIETDM 395
Cdd:cd09807  151 NSEKSYNTGFAycqSKLANV-LFTRELARRlqgtGVTVNALHPGVVRTEL 199
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 213-297 1.87e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 49.13  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIvidvpQAGEALSKVANELGGLALQQDITADDAGNAIADAAVARYGRLDIVIH 292
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVF-----GTSRNPARAAPIPGVELLELDVTDDASVQAAVDEVIARAGRIDVLVN 79


                 ....*
gi 896156623 293 NAGIT 297
Cdd:PRK06179  80 NAGVG 84
PRK05693 PRK05693
SDR family oxidoreductase;
213-393 2.13e-06

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 49.02  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVI-----DVPQAGEAlskvanelGGLALQQDITADDAGNAIADAAVARYGRL 287
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATarkaeDVEALAAA--------GFTAVQLDVNDGAALARLAEELEAEHGGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 288 DIVIHNAGitrdkmFANMDDAKWGSVIAV------NIESQLKMNEQLLNHKAfEKAPRIATMASTSGIAGNRGQTNYATS 361
Cdd:PRK05693  74 DVLINNAG------YGAMGPLLDGGVEAMrrqfetNVFAVVGVTRALFPLLR-RSRGLVVNIGSVSGVLVTPFAGAYCAS 146

                        170       180       190
                 ....*....|....*....|....*....|..
gi 896156623 362 KAGVIAMVEAYAEEFAKRGGNINAVAPGFIET 393
Cdd:PRK05693 147 KAAVHALSDALRLELAPFGVQVMEVQPGAIAS 178
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
212-450 2.44e-06

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 48.97  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSA--RGIGAAIARQLKADGAEvivIDVPQAGEALSK----VANELGG-LALQQDITADDAGNAIADAAVARY 284
Cdd:PRK06505   7 GKRGLIMGVAndHSIAWGIAKQLAAQGAE---LAFTYQGEALGKrvkpLAESLGSdFVLPCDVEDIASVDAVFEALEKKW 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 GRLDIVIHNAGITrDK-----MFANMDDAKWGSVIAVnieSQLKMNEqlLNHKAFEKAPRIATMASTSGIAGNRGQTNY- 358
Cdd:PRK06505  84 GKLDFVVHAIGFS-DKnelkgRYADTTRENFSRTMVI---SCFSFTE--IAKRAAKLMPDGGSMLTLTYGGSTRVMPNYn 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 359 --ATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIpfvnrQVARRVNSLQQGGQP-------GDVAQAIAFL 429
Cdd:PRK06505 158 vmGVAKAALEASVRYLAADYGPQGIRVNAISAGPVRTLAGAGI-----GDARAIFSYQQRNSPlrrtvtiDEVGGSALYL 232

                        250       260
                 ....*....|....*....|..
gi 896156623 430 VSDRALGVNGHVLRV-CGQNIV 450
Cdd:PRK06505 233 LSDLSSGVTGEIHFVdSGYNIV 254
PRK08177 PRK08177
SDR family oxidoreductase;
213-440 2.47e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 48.49  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVI-VIDVPQAGEALskvaNELGGLALQQdITADDAGNAIADAAVARYGRLDIVI 291
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTaTVRGPQQDTAL----QALPGVHIEK-LDMNDPASLDQLLQRLQGQRFDLLF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 292 HNAGIT--RDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAfEKAPRIATMASTSG-IAGNRGQTN--YATSKAGVI 366
Cdd:PRK08177  77 VNAGISgpAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVR-PGQGVLAFMSSQLGsVELPDGGEMplYKASKAALN 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896156623 367 AMVEAYAEEFAKRGGNINAVAPGFIETDMtaaipfvnrqvarrvnslqqGGQ--PGDVAQAIAFLVS--DRALGVNGH 440
Cdd:PRK08177 156 SMTRSFVAELGEPTLTVLSMHPGWVKTDM--------------------GGDnaPLDVETSVKGLVEqiEAASGKGGH 213
PRK06139 PRK06139
SDR family oxidoreductase;
208-296 3.35e-06

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 48.95  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANE---LGG--LALQQDITADDAGNAIADAAVA 282
Cdd:PRK06139   3 GPLHGAVVVITGASSGIGQATAEAFARRGARLVL--AARDEEALQAVAEEcraLGAevLVVPTDVTDADQVKALATQAAS 80

                         90
                 ....*....|....
gi 896156623 283 RYGRLDIVIHNAGI 296
Cdd:PRK06139  81 FGGRIDVWVNNVGV 94
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
229-446 4.16e-06

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 47.69  E-value: 4.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 229 ARQLKADGAEVIVIDVPQAGealskvanelggLALQQDITADDAGNAIADAAVARY-GRLDIVIHNAGITrdkmfanmDD 307
Cdd:PRK12428   2 ARLLRFLGARVIGVDRREPG------------MTLDGFIQADLGDPASIDAAVAALpGRIDALFNIAGVP--------GT 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 308 AKWGSVIAVNIESQLKMNEQLLNHKA----------------FEKAPRIATMASTSGIAGNRG---------QTNYATSK 362
Cdd:PRK12428  62 APVELVARVNFLGLRHLTEALLPRMApggaivnvaslagaewPQRLELHKALAATASFDEGAAwlaahpvalATGYQLSK 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 363 AGVIA--MVEAYaEEFAKRGGNINAVAPGFIETDMTAAipFVNRQVARRVNS----LQQGGQPGDVAQAIAFLVSDRALG 436
Cdd:PRK12428 142 EALILwtMRQAQ-PWFGARGIRVNCVAPGPVFTPILGD--FRSMLGQERVDSdakrMGRPATADEQAAVLVFLCSDAARW 218

                        250
                 ....*....|
gi 896156623 437 VNGHVLRVCG 446
Cdd:PRK12428 219 INGVNLPVDG 228
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 214-396 6.67e-06

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 47.60  E-value: 6.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  214 VAAVTGSARGIGAAIARQL----KADGAEVIVIDVPQagEALSKVANELGGL--ALQQDITADDAGNA----------IA 277
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELakclKSPGSVLVLSARND--EALRQLKAEIGAErsGLRVVRVSLDLGAEagleqllkalRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  278 DAAVARYGRLdIVIHNAGITRD--KMFANMDDAKW-GSVIAVNIESQLKMNEQLLnhKAFEKAP----RIATMASTSGIA 350
Cdd:TIGR01500  80 LPRPKGLQRL-LLINNAGTLGDvsKGFVDLSDSTQvQNYWALNLTSMLCLTSSVL--KAFKDSPglnrTVVNISSLCAIQ 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 896156623  351 GNRGQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMT 396
Cdd:TIGR01500 157 PFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQ 202
PRK06914 PRK06914
SDR family oxidoreductase;
211-394 1.54e-05

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 46.56  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 211 AGKVAAVTGSARGIGAAIARQLKADGAEVIV-IDVPQAGEALSKVANELG---GLALQQ-DITADDAGNAIaDAAVARYG 285
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIAtMRNPEKQENLLSQATQLNlqqNIKVQQlDVTDQNSIHNF-QLVLKEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGitrdkmFAN--------MDDakWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTN 357
Cdd:PRK06914  81 RIDLLVNNAG------YANggfveeipVEE--YRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSP 152

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 896156623 358 YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETD 394
Cdd:PRK06914 153 YVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNTN 189
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
210-452 3.16e-05

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 45.38  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSAR--GIGAAIARQLKADGAEVIVIDVPQAGEALSK-VANELG-GLALQQDITADDAGNAIADAAVARYG 285
Cdd:PRK06603   6 LQGKKGLITGIANnmSISWAIAQLAKKHGAELWFTYQSEVLEKRVKpLAEEIGcNFVSELDVTNPKSISNLFDDIKEKWG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGitrdkmFANMDDAKwGSVIAVNIES-------------QLKMNEQLLNHKAfekapriATMASTSGIAGN 352
Cdd:PRK06603  86 SFDFLLHGMA------FADKNELK-GRYVDTSLENfhnslhiscysllELSRSAEALMHDG-------GSIVTLTYYGAE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 353 RGQTNY---ATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVARRVNS--LQQGGQPGDVAQAIA 427
Cdd:PRK06603 152 KVIPNYnvmGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAIGDFSTMLKSHAATapLKRNTTQEDVGGAAV 231

                        250       260
                 ....*....|....*....|....*.
gi 896156623 428 FLVSDRALGVNGHVLRV-CGQNIVGA 452
Cdd:PRK06603 232 YLFSELSKGVTGEIHYVdCGYNIMGS 257
PRK05599 PRK05599
SDR family oxidoreductase;
217-426 6.17e-05

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 44.49  E-value: 6.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGGLA---LQQDITADDAGNAIADAAVARYGRLDIVIHN 293
Cdd:PRK05599   5 ILGGTSDIAGEIATLLCHGEDVVLAARRPEAAQGLASDLRQRGATSvhvLSFDAQDLDTHRELVKQTQELAGEISLAVVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 294 AGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPriATMASTSGIAGNRG-QTN--YATSKAGVIAMVE 370
Cdd:PRK05599  85 FGILGDQERAETDEAHAVEIATVDYTAQVSMLTVLADELRAQTAP--AAIVAFSSIAGWRArRANyvYGSTKAGLDAFCQ 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 896156623 371 AYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVArrvnslqqggqPGDVAQAI 426
Cdd:PRK05599 163 GLADSLHGSHVRLIIARPGFVIGSMTTGMKPAPMSVY-----------PRDVAAAV 207
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 217-429 6.73e-05

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 44.21  E-value: 6.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  217 VTGSARGIGAAIARQLKADGAEVIVIDVPQAGEALskvaNELGGLALQQ-DITADDAGNAIADAAvarygRLDIVIHNAG 295
Cdd:pfam01370   3 VTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNT----ARLADLRFVEgDLTDRDALEKLLADV-----RPDAVIHLAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  296 ITRDKmfANMDDAkwGSVIAVNIEsqlkMNEQLLNHkAFEKAPRIATMASTSGIAGNRGQTN---------------YAT 360
Cdd:pfam01370  74 VGGVG--ASIEDP--EDFIEANVL----GTLNLLEA-ARKAGVKRFLFASSSEVYGDGAEIPqeettltgplapnspYAA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623  361 SKAGVIAMVEAYAEEFAKRGGNI---NAVAPGFIETDMTAAIPFVNRQVARRVNSLQQG-GQP-------GDVAQAIAFL 429
Cdd:pfam01370 145 AKLAGEWLVLAYAAAYGLRAVILrlfNVYGPGDNEGFVSRVIPALIRRILEGKPILLWGdGTQrrdflyvDDVARAILLA 224
PRK08703 PRK08703
SDR family oxidoreductase;
208-295 7.92e-05

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 44.15  E-value: 7.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 208 KPLAGKVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGeaLSKVANEL---GG---LALQQDI--TADDAGNAIAdA 279
Cdd:PRK08703   2 ATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKK--LEKVYDAIveaGHpepFAIRFDLmsAEEKEFEQFA-A 78

                         90
                 ....*....|....*...
gi 896156623 280 AVAR--YGRLDIVIHNAG 295
Cdd:PRK08703  79 TIAEatQGKLDGIVHCAG 96
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
210-444 1.83e-04

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 43.03  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTG--SARGIGAAIARQLKADGAEV-IVIDVPQAGEALSKVANELGG-LALQQDITADDAGNAIADAAVARYG 285
Cdd:PRK08690   4 LQGKKILITGmiSERSIAYGIAKACREQGAELaFTYVVDKLEERVRKMAAELDSeLVFRCDVASDDEINQVFADLGKHWD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 286 RLDIVIHNAGIT-RDKMFANMDDAKwgSVIAVNIESQLKMneqlLNHKAFEKAPRI------ATMASTSGIAGNRGQTNY 358
Cdd:PRK08690  84 GLDGLVHSIGFApKEALSGDFLDSI--SREAFNTAHEISA----YSLPALAKAARPmmrgrnSAIVALSYLGAVRAIPNY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 359 ---ATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNR--QVARRVNSLQQGGQPGDVAQAIAFLVSDR 433
Cdd:PRK08690 158 nvmGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIADFGKllGHVAAHNPLRRNVTIEEVGNTAAFLLSDL 237

                        250
                 ....*....|.
gi 896156623 434 ALGVNGHVLRV 444
Cdd:PRK08690 238 SSGITGEITYV 248
PRK07775 PRK07775
SDR family oxidoreductase;
215-431 1.93e-04

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 43.20  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 215 AAVTGSARGIGAAIARQLKADGAEVIV--IDVPQAGEALSKVANELG-GLALQQDITADDAGNAIADAAVARYGRLDIVI 291
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALgaRRVEKCEELVDKIRADGGeAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 292 HNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGVIAMVEA 371
Cdd:PRK07775  93 SGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTN 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896156623 372 YAEEFAKRGGNINAVAPGFIETDMTAAIPfvNRQVARRVNSLQQGGQ--------PGDVAQAIAFLVS 431
Cdd:PRK07775 173 LQMELEGTGVRASIVHPGPTLTGMGWSLP--AEVIGPMLEDWAKWGQarhdyflrASDLARAITFVAE 238
PRK06953 PRK06953
SDR family oxidoreductase;
213-398 3.30e-04

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 41.98  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVIVIDVPQAGEAlskVANELGGLALQQDITADDAGNAIA---DAAvarygRLDI 289
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALA---ALQALGAEALALDVADPASVAGLAwklDGE-----ALDA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGI--TRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLnhkAFEKAPR------IATMASTSGIAGNRGQTnYATS 361
Cdd:PRK06953  74 AVYVAGVygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILL---PLVEAAGgvlavlSSRMGSIGDATGTTGWL-YRAS 149

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 896156623 362 KAGVIAMVEAYAeeFAKRGGNINAVAPGFIETDMTAA 398
Cdd:PRK06953 150 KAALNDALRAAS--LQARHATCIALHPGWVRTDMGGA 184
PRK07984 PRK07984
enoyl-ACP reductase FabI;
210-446 3.43e-04

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 42.20  E-value: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTG--SARGIGAAIARQLKADGAEVIVidVPQAGEALSKV---ANELGG-LALQQDITADDAGNAIADAAVAR 283
Cdd:PRK07984   4 LSGKRILVTGvaSKLSIAYGIAQAMHREGAELAF--TYQNDKLKGRVeefAAQLGSdIVLPCDVAEDASIDAMFAELGKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGRLDIVIHNAGitrdkmFANMDDAKWGSVIAVNIES-QLKMNEQLLNHKAFEKAPRI-----ATMASTSGIAGNRGQTN 357
Cdd:PRK07984  82 WPKFDGFVHSIG------FAPGDQLDGDYVNAVTREGfKIAHDISSYSFVAMAKACRSmlnpgSALLTLSYLGAERAIPN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 358 Y---ATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTAAIPFVNRQVA--RRVNSLQQGGQPGDVAQAIAFLVSD 432
Cdd:PRK07984 156 YnvmGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAhcEAVTPIRRTVTIEDVGNSAAFLCSD 235

                        250
                 ....*....|....
gi 896156623 433 RALGVNGHVLRVCG 446
Cdd:PRK07984 236 LSAGISGEVVHVDG 249
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 217-365 3.97e-04

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 42.05  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVIDVPQagEALSKVANELGG--LALQQDITADDAGNAIADAAVARYGRLDIVIHNA 294
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQ--ERLQELKDELGDnlYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156623 295 GIT---RDKMFANMDDakWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKAGV 365
Cdd:PRK10538  83 GLAlglEPAHKASVED--WETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFV 154
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 213-426 6.69e-04

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 41.29  E-value: 6.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAE----VIVIDVPQAGEALSKVANELGGLAL---QQDITADDagnAIAdAAVARY- 284
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASDPSKrfkvYATMRDLKKKGRLWEAAGALAGGTLetlQLDVCDSK---SVA-AAVERVt 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 285 -GRLDIVIHNAGITRDKMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYATSKA 363
Cdd:cd09806   77 eRHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 364 GVIAMVEAYAEEFAKRGGNINAVAPGFIET-------------DMTAAIP-----FVNRQVARRVNSLQQGGQ-PGDVAQ 424
Cdd:cd09806  157 ALEGLCESLAVQLLPFNVHLSLIECGPVHTafmekvlgspeevLDRTADDittfhFFYQYLAHSKQVFREAAQnPEEVAE 236


                 ..
gi 896156623 425 AI 426
Cdd:cd09806  237 VF 238
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 213-396 6.77e-04

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 41.49  E-value: 6.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSARGIGAAIARQLKADGAEVI--VIDVPQAG-EALSKVANELGGLaLQQDITadDAGNaIADAA------VAR 283
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLagCLTKNGPGaKELRRVCSDRLRT-LQLDVT--KPEQ-IKRAAqwvkehVGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 284 YGrLDIVIHNAGIT---RDKMFANMDDAKwgSVIAVNIESQLKMNEQLLnhkafekaP-------RIATMASTSGIAGNR 353
Cdd:cd09805   77 KG-LWGLVNNAGILgfgGDEELLPMDDYR--KCMEVNLFGTVEVTKAFL--------PllrrakgRVVNVSSMGGRVPFP 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 896156623 354 GQTNYATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMT 396
Cdd:cd09805  146 AGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGIT 188
PRK05854 PRK05854
SDR family oxidoreductase;
210-296 6.98e-04

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 41.59  E-value: 6.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTGSARGIGAAIARQLKADGAEVIV-IDVPQAGE-ALSKVANELGGLAL---QQDITADDAGNAIADAAVARY 284
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILpVRNRAKGEaAVAAIRTAVPDAKLslrALDLSSLASVAALGEQLRAEG 91

                         90
                 ....*....|..
gi 896156623 285 GRLDIVIHNAGI 296
Cdd:PRK05854  92 RPIHLLINNAGV 103
PRK05993 PRK05993
SDR family oxidoreductase;
217-406 1.12e-03

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 40.78  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIV-IDVPQAGEALskvanELGGL-ALQQDITADDAGNAIADAAVARY-GRLDIVIHN 293
Cdd:PRK05993   9 ITGCSSGIGAYCARALQSDGWRVFAtCRKEEDVAAL-----EAEGLeAFQLDYAEPESIAALVAQVLELSgGRLDALFNN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 294 -----AGITRDKmfanmddakwgSVIAvnIESQLKMN--------EQLLNHKAFEKAPRIATMASTSGIAGNRGQTNYAT 360
Cdd:PRK05993  84 gaygqPGAVEDL-----------PTEA--LRAQFEANffgwhdltRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 896156623 361 SKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTA-AIPFVNRQV 406
Cdd:PRK05993 151 SKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRFRAnALAAFKRWI 197
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
 216-380 2.38e-03

Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 39.67  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 216 AVTGSARGIGAAIARQLKADGA--EVIVIDV--PQAGEALSKVanelgglalqQDITADDAGNAIADAAVAryGRLDIVI 291
Cdd:cd05238    4 LITGASGFVGQRLAERLLSDVPneRLILIDVvsPKAPSGAPRV----------TQIAGDLAVPALIEALAN--GRPDVVF 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 292 HNAGITRDKMFANMDDAkwgsvIAVNIESQLKMNEQLlnhkafEKAPRIATMASTSGIAGNRG--------------QTN 357
Cdd:cd05238   72 HLAAIVSGGAEADFDLG-----YRVNVDGTRNLLEAL------RKNGPKPRFVFTSSLAVYGLplpnpvtdhtaldpASS 140

                        170       180
                 ....*....|....*....|...
gi 896156623 358 YATSKagviAMVEAYAEEFAKRG 380
Cdd:cd05238  141 YGAQK----AMCELLLNDYSRRG 159
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 212-397 2.40e-03

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 39.85  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 212 GKVAAVTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGLALQQDITA---DDAGNaiADAAVARYGR-- 286
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVL--VARNPDKLKDVSDSIQSKYSKTQIKTvvvDFSGD--IDEGVKRIKEti 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 287 --LD--IVIHNAGITRD--KMFANMDDAKWGSVIAVNIESQLKMNEQLLNHKAFEKAPRIATMASTSG--IAGNRGQTNY 358
Cdd:PLN02780 129 egLDvgVLINNVGVSYPyaRFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAivIPSDPLYAVY 208

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 896156623 359 ATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMTA 397
Cdd:PLN02780 209 AATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMAS 247
KR_fFAS_SDR_c_like cd08950
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like ...
 209-241 2.58e-03

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like SDRs; KR domain of fungal-type fatty acid synthase (FAS), type I. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member, is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the Classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187653 [Multi-domain]  Cd Length: 259  Bit Score: 39.48  E-value: 2.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 896156623 209 PLAGKVAAVTGSARG-IGAAIARQLKADGAEVIV 241
Cdd:cd08950    4 SFAGKVALVTGAGPGsIGAEVVAGLLAGGATVIV 37
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
210-313 2.80e-03

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 39.54  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 210 LAGKVAAVTG--SARGIGAAIARQLKADGAEVIVIDVPQAGEALSKVANELGGLA--LQQDITADDAGNAIADAAVARYG 285
Cdd:PRK07889   5 LEGKRILVTGviTDSSIAFHVARVAQEQGAEVVLTGFGRALRLTERIAKRLPEPApvLELDVTNEEHLASLADRVREHVD 84

                         90       100
                 ....*....|....*....|....*....
gi 896156623 286 RLDIVIHNAGIT-RDKMFANMDDAKWGSV 313
Cdd:PRK07889  85 GLDGVVHSIGFApQSALGGNFLDAPWEDV 113
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
 217-376 4.24e-03

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 38.44  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVIDvpqagealskvanelgglalqqditaddagnaiadaavarygRLDIVIHNAGI 296
Cdd:cd08946    3 VTGGAGFIGSHLVRRLLERGHEVVVID------------------------------------------RLDVVVHLAAL 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 297 TrdkmfanMDDAKWGS---VIAVNIESQLKMneqllnHKAFEKA--PRIaTMASTSGIAGN------------RGQTNYA 359
Cdd:cd08946   41 V-------GVPASWDNpdeDFETNVVGTLNL------LEAARKAgvKRF-VYASSASVYGSpeglpeeeetppRPLSPYG 106

                        170
                 ....*....|....*..
gi 896156623 360 TSKAGVIAMVEAYAEEF 376
Cdd:cd08946  107 VSKLAAEHLLRSYGESY 123
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 213-439 5.85e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 38.46  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 213 KVAAVTGSArGIGAAIARQLKAdGAEVIVIDV-PQAGEALSKVANELGG--LALQQDITADDAGNAIADAAvARYGRLDI 289
Cdd:PRK06940   3 EVVVVIGAG-GIGQAIARRVGA-GKKVLLADYnEENLEAAAKTLREAGFdvSTQEVDVSSRESVKALAATA-QTLGPVTG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 290 VIHNAGITRDKmfANMDD-------------AKWGSVIA-----VNIESqlkMNEQLLNHKAFEKAPRIATMASTSGIAG 351
Cdd:PRK06940  80 LVHTAGVSPSQ--ASPEAilkvdlygtalvlEEFGKVIApggagVVIAS---QSGHRLPALTAEQERALATTPTEELLSL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 352 NRGQTN--------YATSKAGVIAMVEAYAEEFAKRGGNINAVAPGFIETDMtAAIPFVNRQVARRVNSLQ-----QGGQ 418
Cdd:PRK06940 155 PFLQPDaiedslhaYQIAKRANALRVMAEAVKWGERGARINSISPGIISTPL-AQDELNGPRGDGYRNMFAkspagRPGT 233

                        250       260
                 ....*....|....*....|.
gi 896156623 419 PGDVAQAIAFLVSDRALGVNG 439
Cdd:PRK06940 234 PDEIAALAEFLMGPRGSFITG 254
PRK12743 PRK12743
SDR family oxidoreductase;
92-165 7.44e-03

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 38.09  E-value: 7.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896156623  92 ELQGPVLA---AAKHMRKLDKGGRIVTVSRAKDahHNATPAEIAENAVAGGIEGLIRSLGHE-VRGGSTANGilVAPG 165
Cdd:PRK12743 111 DVDGAFLCsqiAARHMVKQGQGGRIINITSVHE--HTPLPGASAYTAAKHALGGLTKAMALElVEHGILVNA--VAPG 184
PRK08340 PRK08340
SDR family oxidoreductase;
217-295 9.84e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 37.86  E-value: 9.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156623 217 VTGSARGIGAAIARQLKADGAEVIVidVPQAGEALSKVANELGGL----ALQQDITA-DDAGNAIADAAVArYGRLDIVI 291
Cdd:PRK08340   5 VTASSRGIGFNVARELLKKGARVVI--SSRNEENLEKALKELKEYgevyAVKADLSDkDDLKNLVKEAWEL-LGGIDALV 81


                 ....
gi 896156623 292 HNAG 295
Cdd:PRK08340  82 WNAG 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH