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Conserved domains on  [gi|15599980|ref|NP_253474|]
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3-ketoacyl-ACP reductase [Pseudomonas aeruginosa PAO1]

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

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List of domain hits

 Name Accession Description Interval E-value
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-451 0e+00

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


:

Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 690.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980    2 TDRYIAFANSPVGRRLVGAVGLPSPLRLERWQAGRVrPVDGPLVIGGSGALAEAVLPFAGKLTDAVFAAVDGQfelPRWT 81
Cdd:PRK08261   1 SDRYLQFVNSGLGKFLAKKLGLPQPVPLRRYRPGQP-LLDGPVLVGGAGRLAEALAALLAGLGYDVVANNDGG---LTWA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   82 AEHSPRAKAVLFDASGLTRFEQLVALRDFFQPVLKGLDKCPKVVVLGRPPESLKDPVTASVQRSLEGFTRSLGKEIRRGG 161
Cdd:PRK08261  77 AGWGDRFGALVFDATGITDPADLKALYEFFHPVLRSLAPCGRVVVLGRPPEAAADPAAAAAQRALEGFTRSLGKELRRGA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  162 NVQLLYVGKGAEDQLEGALRFFLSPKSAYVSGQVIRL-AANSAQVHDWSKPLAGQRALVTGAARGIGAAIAETLARDGAE 240
Cdd:PRK08261 157 TAQLVYVAPGAEAGLESTLRFFLSPRSAYVSGQVVRVgAADAAPPADWDRPLAGKVALVTGAARGIGAAIAEVLARDGAH 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  241 VVLLDVPPAREALEGLAARLGGRAVALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNL 317
Cdd:PRK08261 237 VVCLDVPAAGEALAAVANRVGGTALALDITAPDAPARIAEHLAErhgGLDIVVHNAGITRDKTLANMDEARWDSVLAVNL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  318 NAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAA 397
Cdd:PRK08261 317 LAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMTAA 396

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15599980  398 IPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCGQSLLGA 451
Cdd:PRK08261 397 IPFATREAGRRMNSLQQGGLPVDVAETIAWLASPASGGVTGNVVRVCGQSLLGA 450
 
Name Accession Description Interval E-value
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-451 0e+00

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 690.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980    2 TDRYIAFANSPVGRRLVGAVGLPSPLRLERWQAGRVrPVDGPLVIGGSGALAEAVLPFAGKLTDAVFAAVDGQfelPRWT 81
Cdd:PRK08261   1 SDRYLQFVNSGLGKFLAKKLGLPQPVPLRRYRPGQP-LLDGPVLVGGAGRLAEALAALLAGLGYDVVANNDGG---LTWA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   82 AEHSPRAKAVLFDASGLTRFEQLVALRDFFQPVLKGLDKCPKVVVLGRPPESLKDPVTASVQRSLEGFTRSLGKEIRRGG 161
Cdd:PRK08261  77 AGWGDRFGALVFDATGITDPADLKALYEFFHPVLRSLAPCGRVVVLGRPPEAAADPAAAAAQRALEGFTRSLGKELRRGA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  162 NVQLLYVGKGAEDQLEGALRFFLSPKSAYVSGQVIRL-AANSAQVHDWSKPLAGQRALVTGAARGIGAAIAETLARDGAE 240
Cdd:PRK08261 157 TAQLVYVAPGAEAGLESTLRFFLSPRSAYVSGQVVRVgAADAAPPADWDRPLAGKVALVTGAARGIGAAIAEVLARDGAH 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  241 VVLLDVPPAREALEGLAARLGGRAVALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNL 317
Cdd:PRK08261 237 VVCLDVPAAGEALAAVANRVGGTALALDITAPDAPARIAEHLAErhgGLDIVVHNAGITRDKTLANMDEARWDSVLAVNL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  318 NAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAA 397
Cdd:PRK08261 317 LAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMTAA 396

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15599980  398 IPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCGQSLLGA 451
Cdd:PRK08261 397 IPFATREAGRRMNSLQQGGLPVDVAETIAWLASPASGGVTGNVVRVCGQSLLGA 450
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 234-445 1.18e-61

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: 200.47  E-value: 1.18e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 234 LARDGAEVVLLDVPPAREALEGLAARLGG---RAVALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSSD 307
Cdd:cd05333  20 LAAEGAKVAVTDRSEEAAAETVEEIKALGgnaAALEADVSDREAVEALVEKVEAefgPVDILVNNAGITRDNLLMRMSEE 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 308 FWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAP 387
Cdd:cd05333 100 DWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAVAP 179

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599980 388 GFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:cd05333 180 GFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNG 237
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 232-445 1.54e-59

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: 195.00  E-value: 1.54e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 232 ETLARDGAEVVLLDVppAREALEGLAARL---GGRA--VALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAK 303
Cdd:COG1028  24 RALAAEGARVVITDR--DAEALEAAAAELraaGGRAlaVAADVTDEAAVEALVAAAVAafgRLDILVNNAGITPPGPLEE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 304 MSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITIN 383
Cdd:COG1028 102 LTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVN 181

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599980 384 AVAPGFIETQMTAAIPLT--IREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:COG1028 182 AVAPGPIDTPMTRALLGAeeVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDG 245
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 217-445 5.08e-55

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: 183.18  E-value: 5.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPArEALEGLAARL---GGRA--VALDICAADAGQQLVEALPE---GVDI 288
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSE-EGAEEVVEELkalGVKAlgVVLDVSDREDVKAVVEEIEEelgTIDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   289 VVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLA 368
Cdd:TIGR01830  80 LVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   369 QAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAgrrMNS---MSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:TIGR01830 160 KSLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKK---ILSqipLGRFGQPEEVANAVAFLASDEASYITGQVIHVDG 236
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 232-445 1.21e-47

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: 163.76  E-value: 1.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   232 ETLARDGAEVVLLDVPPA-REALEGLAARLGGRAVALDICAADAGQQLVEALPE---GVDIVVHNAGITR--DKTLAKMS 305
Cdd:pfam13561  14 RALAEEGAEVVLTDLNEAlAKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVEkfgRLDILVNNAGFAPklKGPFLDTS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   306 SDFWNSVINVNLNAPQVLTQALLDggKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAV 385
Cdd:pfam13561  94 REDFDRALDVNLYSLFLLAKAALP--LMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAI 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599980   386 APGFIETQMTAAIPLT--IREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:pfam13561 172 SPGPIKTLAASGIPGFdeLLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDG 233
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 234-383 8.74e-14

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: 69.43  E-value: 8.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980    234 LARDGAE-VVLL-----DVPPAREALEGLAARLGG-RAVALDICAADAGQQLVEALPEG---VDIVVHNAGITRDKTLAK 303
Cdd:smart00822  20 LAERGARrLVLLsrsgpDAPGAAALLAELEAAGARvTVVACDVADRDALAAVLAAIPAVegpLTGVIHAAGVLDDGVLAS 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980    304 MSSDFWNSVINVNLNAPQVLTQALLDggklHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWApALGKRGITIN 383
Cdd:smart00822 100 LTPERFAAVLAPKAAGAWNLHELTAD----LPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRR-ARGLPALSIA 174
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
 217-445 6.44e-12

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: 65.47  E-value: 6.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVVLLDV--------PPAREA-LEGLAARLGGRAVAL-----DICAADAGQQLVEAL 282
Cdd:NF040491   3 ALVTGAARGIGAATVRRLAARGYAVVAVDAcagdpapyPLGTEAdLDALVASSPGRVETVvadvrDRAALAAAVALALDR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  283 PEGVDIVVHNAG-ITRDKTLAKMSSDFWNSVINVNL----NAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSNY 357
Cdd:NF040491  83 WGRLDAAVAAAAvIAGGRPLWETPPEELDALWDVDVrgvwNLAAAAVPALLAGPD-PRGCRFVAVASAAGHRGLFHLAAY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  358 AVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQM---TAAI-------PLTIREAGRRMNSmsqgglPQDVAETVAW 427
Cdd:NF040491 162 CAAKHAVVGLVRGLAADLAGTGVTACAVSPGSTDTPMlaaTAALyglddvtELAAHQLVRRLLD------PDEVAAVVAF 235

                        250
                 ....*....|....*...
gi 15599980  428 FAQPSSGAVSGQVLRVCG 445
Cdd:NF040491 236 ACSPGGAAVNGSVVHADG 253
 
Name Accession Description Interval E-value
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-451 0e+00

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 690.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980    2 TDRYIAFANSPVGRRLVGAVGLPSPLRLERWQAGRVrPVDGPLVIGGSGALAEAVLPFAGKLTDAVFAAVDGQfelPRWT 81
Cdd:PRK08261   1 SDRYLQFVNSGLGKFLAKKLGLPQPVPLRRYRPGQP-LLDGPVLVGGAGRLAEALAALLAGLGYDVVANNDGG---LTWA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   82 AEHSPRAKAVLFDASGLTRFEQLVALRDFFQPVLKGLDKCPKVVVLGRPPESLKDPVTASVQRSLEGFTRSLGKEIRRGG 161
Cdd:PRK08261  77 AGWGDRFGALVFDATGITDPADLKALYEFFHPVLRSLAPCGRVVVLGRPPEAAADPAAAAAQRALEGFTRSLGKELRRGA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  162 NVQLLYVGKGAEDQLEGALRFFLSPKSAYVSGQVIRL-AANSAQVHDWSKPLAGQRALVTGAARGIGAAIAETLARDGAE 240
Cdd:PRK08261 157 TAQLVYVAPGAEAGLESTLRFFLSPRSAYVSGQVVRVgAADAAPPADWDRPLAGKVALVTGAARGIGAAIAEVLARDGAH 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  241 VVLLDVPPAREALEGLAARLGGRAVALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNL 317
Cdd:PRK08261 237 VVCLDVPAAGEALAAVANRVGGTALALDITAPDAPARIAEHLAErhgGLDIVVHNAGITRDKTLANMDEARWDSVLAVNL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  318 NAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAA 397
Cdd:PRK08261 317 LAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMTAA 396

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15599980  398 IPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCGQSLLGA 451
Cdd:PRK08261 397 IPFATREAGRRMNSLQQGGLPVDVAETIAWLASPASGGVTGNVVRVCGQSLLGA 450
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
212-445 6.75e-63

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 203.85  E-value: 6.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARL---GGRAVAL--DICAADAGQQLVEALPE-- 284
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDS--NEEAAEALAAELraaGGEARVLvfDVSDEAAVRALIEAAVEaf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 -GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:PRK05653  81 gALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  364 LIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRV 443
Cdd:PRK05653 161 VIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPV 240


                 ..
gi 15599980  444 CG 445
Cdd:PRK05653 241 NG 242
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 234-445 1.18e-61

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: 200.47  E-value: 1.18e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 234 LARDGAEVVLLDVPPAREALEGLAARLGG---RAVALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSSD 307
Cdd:cd05333  20 LAAEGAKVAVTDRSEEAAAETVEEIKALGgnaAALEADVSDREAVEALVEKVEAefgPVDILVNNAGITRDNLLMRMSEE 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 308 FWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAP 387
Cdd:cd05333 100 DWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAVAP 179

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599980 388 GFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:cd05333 180 GFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNG 237
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 232-445 1.54e-59

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: 195.00  E-value: 1.54e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 232 ETLARDGAEVVLLDVppAREALEGLAARL---GGRA--VALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAK 303
Cdd:COG1028  24 RALAAEGARVVITDR--DAEALEAAAAELraaGGRAlaVAADVTDEAAVEALVAAAVAafgRLDILVNNAGITPPGPLEE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 304 MSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITIN 383
Cdd:COG1028 102 LTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVN 181

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599980 384 AVAPGFIETQMTAAIPLT--IREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:COG1028 182 AVAPGPIDTPMTRALLGAeeVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDG 245
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 209-445 6.51e-57

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 188.15  E-value: 6.51e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  209 SKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLlDVPPAREALEGLAA---RLGGRAVAL--DICAADAGQQLVEALP 283
Cdd:PRK12825   1 MGSLMGRVALVTGAARGLGRAIALRLARAGADVVV-HYRSDEEAAEELVEaveALGRRAQAVqaDVTDKAALEAAVAAAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  284 E---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVS 360
Cdd:PRK12825  80 ErfgRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQV 440
Cdd:PRK12825 160 KAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQV 239


                 ....*
gi 15599980  441 LRVCG 445
Cdd:PRK12825 240 IEVTG 244
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 212-445 7.57e-57

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 188.09  E-value: 7.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAAR--LGGRAVAL--DICAADAGQQLVEALPE--- 284
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIgaLGGKALAVqgDVSDAESVERAVDEAKAefg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK05557  83 GVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVC 444
Cdd:PRK05557 163 IGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHVN 242


                 .
gi 15599980  445 G 445
Cdd:PRK05557 243 G 243
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 217-445 5.08e-55

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: 183.18  E-value: 5.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPArEALEGLAARL---GGRA--VALDICAADAGQQLVEALPE---GVDI 288
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSE-EGAEEVVEELkalGVKAlgVVLDVSDREDVKAVVEEIEEelgTIDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   289 VVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLA 368
Cdd:TIGR01830  80 LVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   369 QAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAgrrMNS---MSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:TIGR01830 160 KSLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKK---ILSqipLGRFGQPEEVANAVAFLASDEASYITGQVIHVDG 236
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 232-443 3.10e-50

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: 170.54  E-value: 3.10e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 232 ETLARDGAEVVLLDVPPAREALEGLAARLGGRAVAL--DICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSS 306
Cdd:cd05233  16 RRLAREGAKVVLADRNEEALAELAAIEALGGNAVAVqaDVSDEEDVEALVEEALEefgRLDILVNNAGIARPGPLEELTD 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 307 DFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVA 386
Cdd:cd05233  96 EDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVA 175

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599980 387 PGFIETQMTAAIPLTIREAG-RRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRV 443
Cdd:cd05233 176 PGLVDTPMLAKLGPEEAEKElAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPV 233
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 232-445 1.21e-47

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: 163.76  E-value: 1.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   232 ETLARDGAEVVLLDVPPA-REALEGLAARLGGRAVALDICAADAGQQLVEALPE---GVDIVVHNAGITR--DKTLAKMS 305
Cdd:pfam13561  14 RALAEEGAEVVLTDLNEAlAKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVEkfgRLDILVNNAGFAPklKGPFLDTS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   306 SDFWNSVINVNLNAPQVLTQALLDggKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAV 385
Cdd:pfam13561  94 REDFDRALDVNLYSLFLLAKAALP--LMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAI 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599980   386 APGFIETQMTAAIPLT--IREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:pfam13561 172 SPGPIKTLAASGIPGFdeLLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDG 233
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
217-445 3.59e-47

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 162.63  E-value: 3.59e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGL----AARLGGRAVALDICAADAGQQLVEALPE---GVDIV 289
Cdd:PRK12824   5 ALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFeeygFTEDQVRLKELDVTDTEECAEALAEIEEeegPVDIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  290 VHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQ 369
Cdd:PRK12824  85 VNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGFTK 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599980  370 AWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PRK12824 165 ALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFITGETISING 240
PRK12826 PRK12826
SDR family oxidoreductase;
209-449 3.80e-45

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 157.39  E-value: 3.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  209 SKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAR--EALEGLAARlGGRAVAL--DICAADAGQQLVEALPE 284
Cdd:PRK12826   1 TRDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDaaATAELVEAA-GGKARARqvDVRDRAALKAAVAAGVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 ---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIA-GNLGQSNYAVS 360
Cdd:PRK12826  80 dfgRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvGYPGLAHYAAS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAiPLTIREAGRRMNSMSQGGL--PQDVAETVAWFAQPSSGAVSG 438
Cdd:PRK12826 160 KAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGN-LGDAQWAEAIAAAIPLGRLgePEDIAAAVLFLASDEARYITG 238

                        250
                 ....*....|.
gi 15599980  439 QVLRVCGQSLL 449
Cdd:PRK12826 239 QTLPVDGGATL 249
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
 217-445 6.25e-42

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: 148.74  E-value: 6.25e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   217 ALVTGAARGIGAAIAETLARDGAEVVLLDVP--PAREALEGLAARLGG--RAVALDICAADAGQQLVEALPEG---VDIV 289
Cdd:TIGR01829   3 ALVTGGMGGIGTAICQRLAKDGYRVAANCGPneERAEAWLQEQGALGFdfRVVEGDVSSFESCKAAVAKVEAElgpVDVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   290 VHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQ 369
Cdd:TIGR01829  83 VNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTNYSAAKAGMIGFTK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599980   370 AWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:TIGR01829 163 ALAQEGATKGVTVNTISPGYIATDMVMAMREDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYITGATLSING 238
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 212-445 1.28e-40

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 145.44  E-value: 1.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARLGGRAVALDICAAD-----AGQQLVEALPEGV 286
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGT--RVEKLEALAAELGERVKIFPANLSDrdevkALGQKAEADLEGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIG 366
Cdd:PRK12936  82 DILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIG 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980  367 LAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PRK12936 162 FSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTIHVNG 240
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 209-445 3.79e-39

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 141.40  E-value: 3.79e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  209 SKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPP--AREALEGLAARL---GGRA--VALDICAADAGQQLVEA 281
Cdd:PRK12827   1 MASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPmrGRAEADAVAAGIeaaGGKAlgLAFDVRDFAATRAALDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  282 LPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGG-KLHDNGRVVLLASISGIAGNLGQSNY 357
Cdd:PRK12827  81 GVEefgRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMiRARRGGRIVNIASVAGVRGNRGQVNY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  358 AVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTirEAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVS 437
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPT--EHLLNPVPVQRLGEPDEVAALVAFLVSDAASYVT 238


                 ....*...
gi 15599980  438 GQVLRVCG 445
Cdd:PRK12827 239 GQVIPVDG 246
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 212-445 3.85e-38

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 138.95  E-value: 3.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDV--PPAREALEGLAARlGGRAVA--LDICAADAGQQLVEALPE--- 284
Cdd:PRK12939   5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGlaAEARELAAALEAA-GGRAHAiaADLADPASVQRFFDAAAAalg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK12939  84 GLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAG-RRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRV 443
Cdd:PRK12939 164 IGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADERHAYyLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLLPV 243


                 ..
gi 15599980  444 CG 445
Cdd:PRK12939 244 NG 245
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 212-445 8.58e-38

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 137.83  E-value: 8.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLlDVPPAREALEGLAARLGGR-----AVALDICAADAGQQLVEALPEG- 285
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVI-NYNSSKEAAENLVNELGKEghdvyAVQADVSKVEDANRLVEEAVNHf 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 --VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:PRK12935  83 gkVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  364 LIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQpsSGA-VSGQVLR 442
Cdd:PRK12935 163 MLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCR--DGAyITGQQLN 240


                 ...
gi 15599980  443 VCG 445
Cdd:PRK12935 241 ING 243
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 232-442 1.37e-36

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: 134.54  E-value: 1.37e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 232 ETLARDGAEVVLLDVPParEALEGLAARLGGRA--VALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSS 306
Cdd:COG4221  23 RALAAAGARVVLAARRA--ERLEALAAELGGRAlaVPLDVTDEAAVEAAVAAAVAefgRLDVLVNNAGVALLGPLEELDP 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 307 DFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVA 386
Cdd:COG4221 101 EDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIE 180

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15599980 387 PGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFA-QPSSGAVSGQVLR 442
Cdd:COG4221 181 PGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALtQPAHVNVNELVLR 237
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 232-402 9.82e-36

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 130.81  E-value: 9.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   232 ETLARDGAEVVLLD--VPPAREALEGLAArLGGRAVAL--DICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKM 304
Cdd:pfam00106  18 KRLAKEGAKVVLVDrsEEKLEAVAKELGA-LGGKALFIqgDVTDRAQVKALVEQAVErlgRLDILVNNAGITGLGPFSEL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   305 SSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINA 384
Cdd:pfam00106  97 SDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNA 176

                         170
                  ....*....|....*...
gi 15599980   385 VAPGFIETQMTAAIPLTI 402
Cdd:pfam00106 177 VAPGGVDTDMTKELREDE 194
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 210-445 2.45e-35

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 131.72  E-value: 2.45e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  210 KPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARLGGRAVALDIC-AADAGQqlVEALPE---- 284
Cdd:PRK12829   7 KPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDV--SEAALAATAARLPGAKVTATVAdVADPAQ--VERVFDtave 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 ---GVDIVVHNAGIT-RDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVL-LASISGIAGNLGQSNYAV 359
Cdd:PRK12829  83 rfgGLDVLVNNAGIAgPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIaLSSVAGRLGYPGRTPYAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  360 SKAGLIGLAQAWAPALGKRGITINAVAPGFIET-QMTAAIPLTIREAGR--------RMNSMSQGGL--PQDVAETVAWF 428
Cdd:PRK12829 163 SKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGpRMRRVIEARAQQLGIgldemeqeYLEKISLGRMvePEDIAATALFL 242

                        250
                 ....*....|....*..
gi 15599980  429 AQPSSGAVSGQVLRVCG 445
Cdd:PRK12829 243 ASPAARYITGQAISVDG 259
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
234-425 1.48e-33

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 126.52  E-value: 1.48e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 234 LARDGAEVVLLDVPPAReaLEGLAARLGGR-----AVALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMS 305
Cdd:COG0300  25 LAARGARVVLVARDAER--LEALAAELRAAgarveVVALDVTDPDAVAALAEAVLArfgPIDVLVNNAGVGGGGPFEELD 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 306 SDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAV 385
Cdd:COG0300 103 LEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRVTAV 182

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15599980 386 APGFIETQMTAAiplTIREAGRRMNSmsqgglPQDVAETV 425
Cdd:COG0300 183 CPGPVDTPFTAR---AGAPAGRPLLS------PEEVARAI 213
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 212-445 2.08e-33

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: 125.85  E-value: 2.08e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLlDVPPAREALEGLAARL---GGRAVAL--DICAADAGQQLVEALPE-- 284
Cdd:cd05362   1 LAGKVALVTGASRGIGRAIAKRLARDGASVVV-NYASSKAAAEEVVAEIeaaGGKAIAVqaDVSDPSQVARLFDAAEKaf 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 285 -GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDggKLHDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:cd05362  80 gGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAK--RLRDGGRIINISSSLTAAYTPNYGAYAGSKAA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 364 LIGLAQAWAPALGKRGITINAVAPGFIETQM-TAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLR 442
Cdd:cd05362 158 VEAFTRVLAKELGGRGITVNAVAPGPVDTDMfYAGKTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQVIR 237


                ...
gi 15599980 443 VCG 445
Cdd:cd05362 238 ANG 240
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 212-445 1.15e-32

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 124.18  E-value: 1.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVL---LDVPPAREALEGLAARLG-GRAVALDICAADAGQQLVEALPE--- 284
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIaydINEEAAQELLEEIKEEGGdAIAVKADVSSEEDVENLVEQIVEkfg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK05565  83 KIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVC 444
Cdd:PRK05565 163 NAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIITVD 242


                 .
gi 15599980  445 G 445
Cdd:PRK05565 243 G 243
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 212-445 1.04e-31

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: 121.31  E-value: 1.04e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDV--PPAREALEGL-AARLGGRAVALDICAADAGQQLVEALPEG--- 285
Cdd:cd05347   3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRneEKAEEAQQLIeKEGVEATAFTCDVSDEEAIKAAVEAIEEDfgk 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:cd05347  83 IDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 366 GLAQAWAPALGKRGITINAVAPGFIETQMTAAI---PLTIREAgRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLR 442
Cdd:cd05347 163 GLTKALATEWARHGIQVNAIAPGYFATEMTEAVvadPEFNDDI-LKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQIIF 241


                ...
gi 15599980 443 VCG 445
Cdd:cd05347 242 VDG 244
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 211-445 1.31e-31

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 122.97  E-value: 1.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLA--ARLGGRAVAL--DICAADAGQQLVEALPE-- 284
Cdd:PRK07792   9 DLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVLDeiRAAGAKAVAVagDISQRATADELVATAVGlg 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLT---------QALLDGGKLHdnGRVVLLASISGIAGNLGQS 355
Cdd:PRK07792  89 GLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTrnaaaywraKAKAAGGPVY--GRIVNTSSEAGLVGPVGQA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  356 NYAVSKAGLIGLAQAWAPALGKRGITINAVAPGfIETQMTAAIPLTIRE-AGRRMNSMSqgglPQDVAETVAWFAQPSSG 434
Cdd:PRK07792 167 NYGAAKAGITALTLSAARALGRYGVRANAICPR-ARTAMTADVFGDAPDvEAGGIDPLS----PEHVVPLVQFLASPAAA 241

                        250
                 ....*....|.
gi 15599980  435 AVSGQVLRVCG 445
Cdd:PRK07792 242 EVNGQVFIVYG 252
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
232-438 2.03e-31

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 120.89  E-value: 2.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  232 ETLARDGAEVVLLDVP--PARE--------------ALEGLAARLGGRAVALDICAADAGQqlvealpegVDIVVHNAGI 295
Cdd:PRK12938  21 QRLHKDGFKVVAGCGPnsPRRVkwledqkalgfdfiASEGNVGDWDSTKAAFDKVKAEVGE---------IDVLVNNAGI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  296 TRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPAL 375
Cdd:PRK12938  92 TRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIHGFTMSLAQEV 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599980  376 GKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSG 438
Cdd:PRK12938 172 ATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTG 234
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 232-445 4.25e-31

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 120.07  E-value: 4.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  232 ETLARDGAEVVLLDVppAREALEGLAARLGGRAVALDICAAD-AGQQLVEALPE-------GVDIVVHNAGITRD----- 298
Cdd:PRK08217  23 EYLAQKGAKLALIDL--NQEKLEEAVAECGALGTEVRGYAANvTDEEDVEATFAqiaedfgQLNGLINNAGILRDgllvk 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  299 ----KTLAKMSSDFWNSVINVNLnapqvlTQALLDG----GKLHDNGRVVLLASISGI--AGNLGQSNYAVSKAGLIGLA 368
Cdd:PRK08217 101 akdgKVTSKMSLEQFQSVIDVNL------TGVFLCGreaaAKMIESGSKGVIINISSIarAGNMGQTNYSASKAGVAAMT 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599980  369 QAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQpsSGAVSGQVLRVCG 445
Cdd:PRK08217 175 VTWAKELARYGIRVAAIAPGVIETEMTAAMKPEALERLEKMIPVGRLGEPEEIAHTVRFIIE--NDYVTGRVLEIDG 249
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 234-445 9.66e-30

(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: 116.27  E-value: 9.66e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 234 LARDGAEVVLLDV--PPAREALEGLAA--------RLGGRAVAlDICAADAGQQLVEALPE---GVDIVVHNAGITRDKT 300
Cdd:cd05353  25 FAERGAKVVVNDLggDRKGSGKSSSAAdkvvdeikAAGGKAVA-NYDSVEDGEKIVKTAIDafgRVDILVNNAGILRDRS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 301 LAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGI 380
Cdd:cd05353 104 FAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNI 183

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980 381 TINAVAPGfIETQMTAAIpltireagrrmnsMSQGGL----PQDVAETVAWFAQPSSgAVSGQVLRVCG 445
Cdd:cd05353 184 TCNTIAPA-AGSRMTETV-------------MPEDLFdalkPEYVAPLVLYLCHESC-EVTGGLFEVGA 237
FabG-like PRK07231
SDR family oxidoreductase;
212-445 7.28e-29

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 113.77  E-value: 7.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPParEALEGLAARLGG----RAVALDICAADAGQQLVEALPE--- 284
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNE--EAAERVAAEILAggraIAVAADVSDEADVEAAVAAALErfg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGIT-RDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:PRK07231  81 SVDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  364 LIGLAQAWAPALGKRGITINAVAPGFIETQMTAA----IPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQ 439
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETGLLEAfmgePTPENRAKFLATIPLGRLGTPEDIANAALFLASDEASWITGV 240


                 ....*.
gi 15599980  440 VLRVCG 445
Cdd:PRK07231 241 TLVVDG 246
PRK07074 PRK07074
SDR family oxidoreductase;
217-445 9.11e-29

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 113.71  E-value: 9.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAreALEGLAARLGGR---AVALDICAADAGQQLVEALPEG---VDIVV 290
Cdd:PRK07074   5 ALVTGAAGGIGQALARRFLAAGDRVLALDIDAA--ALAAFADALGDArfvPVACDLTDAASLAAALANAAAErgpVDVLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  291 HNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGnLGQSNYAVSKAGLIGLAQA 370
Cdd:PRK07074  83 ANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAA-LGHPAYSAAKAGLIHYTKL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  371 WAPALGKRGITINAVAPGFIETQM----TAAIPLTIREAgRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRV-CG 445
Cdd:PRK07074 162 LAVEYGRFGIRANAVAPGTVKTQAwearVAANPQVFEEL-KKWYPLQDFATPDDVANAVLFLASPAARAITGVCLPVdGG 240
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 212-449 1.51e-28

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 112.58  E-value: 1.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDV--PPAREALEGLAARlGGRAVALDICAADAGQQLVEALPE---GV 286
Cdd:PRK12828   5 LQGKVVAITGGFGGLGRATAAWLAARGARVALIGRgaAPLSQTLPGVPAD-ALRIGGIDLVDPQAARRAVDEVNRqfgRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIVVHNAGITRDKTLAKMSSDFWNSVINVN----LNAPQVLTQALLDGGklhdNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:PRK12828  84 DALVNIAGAFVWGTIADGDADTWDRMYGVNvkttLNASKAALPALTASG----GGRIVNIGAGAALKAGPGMGAYAAAKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  363 GLIGLAQAWAPALGKRGITINAVAPGFIET-QMTAAIPltireagrrMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVL 441
Cdd:PRK12828 160 GVARLTEALAAELLDRGITVNAVLPSIIDTpPNRADMP---------DADFSRWVTPEQIAAVIAFLLSDEAQAITGASI 230


                 ....*...
gi 15599980  442 RVCGQSLL 449
Cdd:PRK12828 231 PVDGGVAL 238
PRK06124 PRK06124
SDR family oxidoreductase;
212-445 2.64e-28

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 112.50  E-value: 2.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLL--DVPPAREALEGLAARlGGRA--VALDICAADAGQQLVEALPE--- 284
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNgrNAATLEAAVAALRAA-GGAAeaLAFDIADEEAVAAAFARIDAehg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK06124  88 RLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPL--TIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLR 442
Cdd:PRK06124 168 TGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAAdpAVGPWLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGHVLA 247


                 ...
gi 15599980  443 VCG 445
Cdd:PRK06124 248 VDG 250
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 232-426 7.09e-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: 110.15  E-value: 7.09e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 232 ETLARDGAEVVLLDVPParEALEGLAARLGG-RAVALDICAADAGQQLVEALP---EGVDIVVHNAGITRDKTLAKMSSD 307
Cdd:cd08932  18 RALARDGYRVSLGLRNP--EDLAALSASGGDvEAVPYDARDPEDARALVDALRdrfGRIDVLVHNAGIGRPTTLREGSDA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 308 FWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAP 387
Cdd:cd08932  96 ELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHALRQEGWDHGVRVSAVCP 175

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15599980 388 GFIETQMTAAiplTIREAGRRMNSMSQgglPQDVAETVA 426
Cdd:cd08932 176 GFVDTPMAQG---LTLVGAFPPEEMIQ---PKDIANLVR 208
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 212-445 6.72e-27

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 108.50  E-value: 6.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAARLGGRAVALDICAADAGQ-----QLVEALPE 284
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLS----ARkaEELEEAAAHLEALGIDALWIAADVADeadieRLAEETLE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 ---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQA-----LLDGGKlhdnGRVVLLASISGIAGN----L 352
Cdd:PRK08213  86 rfgHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAvakrsMIPRGY----GRIINVASVAGLGGNppevM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  353 GQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAiplTIREAGRRMNS---MSQGGLPQDVAETVAWFA 429
Cdd:PRK08213 162 DTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRG---TLERLGEDLLAhtpLGRLGDDEDLKGAALLLA 238

                        250
                 ....*....|....*.
gi 15599980  430 QPSSGAVSGQVLRVCG 445
Cdd:PRK08213 239 SDASKHITGQILAVDG 254
PRK07577 PRK07577
SDR family oxidoreductase;
215-445 7.24e-27

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 107.89  E-value: 7.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  215 QRALVTGAARGIGAAIAETLARDGAEVVLLdvppAREALEGLAARLggraVALDIcaADAGQ------QLVEALPegVDI 288
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGI----ARSAIDDFPGEL----FACDL--ADIEQtaatlaQINEIHP--VDA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 VVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISgIAGNLGQSNYAVSKAGLIGLA 368
Cdd:PRK07577  72 IVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-IFGALDRTSYSAAKSALVGCT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  369 QAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNS---MSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PRK07577 151 RTWALELAEYGITVNAVAPGPIETELFRQTRPVGSEEEKRVLAsipMRRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDG 230
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 215-445 1.09e-26

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: 107.54  E-value: 1.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 215 QRALVTGAARGIGAAIAETLARDGAEVVLlDVPPAREALEGLAARLGGRAVAL--DICAADAGQQLVEALPEG---VDIV 289
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVV-NYYRSTESAEAVAAEAGERAIAIqaDVRDRDQVQAMIEEAKNHfgpVDTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 290 VHNAGI------TRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVllasisGIAGNLGQS------NY 357
Cdd:cd05349  80 VNNALIdfpfdpDQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVI------NIGTNLFQNpvvpyhDY 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 358 AVSKAGLIGLAQAWAPALGKRGITINAVAPGFI-ETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAV 436
Cdd:cd05349 154 TTAKAALLGFTRNMAKELGPYGITVNMVSGGLLkVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAV 233


                ....*....
gi 15599980 437 SGQVLRVCG 445
Cdd:cd05349 234 TGQNLVVDG 242
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 212-445 7.61e-26

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: 105.26  E-value: 7.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARLGGRAVALDICAADAgqQLVEALPE------- 284
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADI--DGGAAQAVVAQIAGGALALRVDVTDE--QQVAALFEraveefg 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 285 GVDIVVHNAGITR-DKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:cd08944  77 GLDLLVNNAGAMHlTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 364 LIGLAQAWAPALGKRGITINAVAPGFIETQMTAA---IPLTIREAGRRMNSMSQG----GLPQDVAETVAWFAQPSSGAV 436
Cdd:cd08944 157 IRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAklaGFEGALGPGGFHLLIHQLqgrlGRPEDVAAAVVFLLSDDASFI 236


                ....*....
gi 15599980 437 SGQVLRVCG 445
Cdd:cd08944 237 TGQVLCVDG 245
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 214-445 1.02e-25

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: 105.22  E-value: 1.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREA---LEGLAARLGGRAVAL--DICAADAGQQLVEALPE---G 285
Cdd:cd08940   2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIeavRAGLAAKHGVKVLYHgaDLSKPAAIEDMVAYAQRqfgG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:cd08940  82 VDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 366 GLAQAWAPALGKRGITINAVAPGFIETQM--------TAAIPLTIREAGRRMNSMSQGGL----PQDVAETVAWFAQPSS 433
Cdd:cd08940 162 GLTKVVALETAGTGVTCNAICPGWVLTPLvekqisalAQKNGVPQEQAARELLLEKQPSKqfvtPEQLGDTAVFLASDAA 241

                       250
                ....*....|..
gi 15599980 434 GAVSGQVLRVCG 445
Cdd:cd08940 242 SQITGTAVSVDG 253
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 212-445 1.60e-25

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: 104.77  E-value: 1.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVL---LDVPPAREALEGLAArLGGRAVAL--DICAADAGQQLVEALPE-- 284
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVnyrSKEDAAEEVVEEIKA-VGGKAIAVqaDVSKEEDVVALFQSAIKef 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 285 -GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNApQVLT--QALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSK 361
Cdd:cd05358  80 gTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTG-QFLCarEAIKRFRKSKIKGKIINMSSVHEKIPWPGHVNYAASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 362 AGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLT--IREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQ 439
Cdd:cd05358 159 GGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDpeQRADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGT 238


                ....*.
gi 15599980 440 VLRVCG 445
Cdd:cd05358 239 TLFVDG 244
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
212-445 1.67e-25

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 104.82  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAARLGGRAVA--LDICAADAGQQLVEALPEG---V 286
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDETRRLIEKEGRKVTFvqVDLTKPESAEKVVKEALEEfgkI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALldgGKL---HDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:PRK06935  93 DILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAV---AKVmakQGSGKIINIASMLSFQGGKFVPAYTASKHG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  364 LIGLAQAWAPALGKRGITINAVAPGFIETQMTAAipltIREAGRRMNSM------SQGGLPQDVAETVAWFAQPSSGAVS 437
Cdd:PRK06935 170 VAGLTKAFANELAAYNIQVNAIAPGYIKTANTAP----IRADKNRNDEIlkripaGRWGEPDDLMGAAVFLASRASDYVN 245


                 ....*...
gi 15599980  438 GQVLRVCG 445
Cdd:PRK06935 246 GHILAVDG 253
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 214-445 5.25e-25

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: 103.12  E-value: 5.25e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARL-----GGRAVALDICAADAGQQLVEA---LPEG 285
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICAR--NRENLERAASELraggaGVLAVVADLTDPEDIDRLVEKagdAFGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIA--GNLGQSNyaVSKAG 363
Cdd:cd05344  79 VDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEpePNLVLSN--VARAG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 364 LIGLAQAWAPALGKRGITINAVAPGFIET--------QMTAAIPLTIREAGRRMNS---MSQGGLPQDVAETVAWFAQPS 432
Cdd:cd05344 157 LIGLVKTLSRELAPDGVTVNSVLPGYIDTervrrlleARAEKEGISVEEAEKEVASqipLGRVGKPEELAALIAFLASEK 236

                       250
                ....*....|...
gi 15599980 433 SGAVSGQVLRVCG 445
Cdd:cd05344 237 ASYITGQAILVDG 249
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 234-445 5.88e-25

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 103.98  E-value: 5.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  234 LARDGAEVVLLDV-----------PPAREALEGLAARlGGRAVA--LDICAADAGQQLVEALPE---GVDIVVHNAGITR 297
Cdd:PRK07791  26 FAAEGARVVVNDIgvgldgsasggSAAQAVVDEIVAA-GGEAVAngDDIADWDGAANLVDAAVEtfgGLDVLVNNAGILR 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  298 DKTLAKMSSDFWNSVINVNLNAPQVLT-------QALLDGGKLHDnGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQA 370
Cdd:PRK07791 105 DRMIANMSEEEWDAVIAVHLKGHFATLrhaaaywRAESKAGRAVD-ARIINTSSGAGLQGSVGQGNYSAAKAGIAALTLV 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599980  371 WAPALGKRGITINAVAPGfIETQMTA---AIPLTIREAGrRMNSMSqgglPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PRK07791 184 AAAELGRYGVTVNAIAPA-ARTRMTEtvfAEMMAKPEEG-EFDAMA----PENVSPLVVWLGSAESRDVTGKVFEVEG 255
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 217-445 8.77e-25

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: 102.43  E-value: 8.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLA--ARLGGRAVAL--DICAADAGQQLVEALPE---GVDIV 289
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVAAeiEELGGKAVVVraDVSQPQDVEEMFAAVKErfgRLDVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 290 VHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQ 369
Cdd:cd05359  81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599980 370 AWAPALGKRGITINAVAPGFIETQMTAAIP--LTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:cd05359 161 YLAVELGPRGIRVNAVSPGVIDTDALAHFPnrEDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDG 238
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 234-408 9.30e-25

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: 101.55  E-value: 9.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 234 LARDGAEVVLL---DVPPAREALEGL-AARLGGRAVALDICAADAGQQL---VEALPEGVDIVVHNAGITRDKTLAKMSS 306
Cdd:cd05324  20 LAKSGPGTVILtarDVERGQAAVEKLrAEGLSVRFHQLDVTDDASIEAAadfVEEKYGGLDILVNNAGIAFKGFDDSTPT 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 307 -DFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIagnlGQSNYAVSKAGLIGLAQAWAPALGKRGITINAV 385
Cdd:cd05324 100 rEQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGS----LTSAYGVSKAALNALTRILAKELKETGIKVNAC 175

                       170       180
                ....*....|....*....|....
gi 15599980 386 APGFIETQMTAAI-PLTIREAGRR 408
Cdd:cd05324 176 CPGWVKTDMGGGKaPKTPEEGAET 199
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 211-445 2.48e-24

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 100.97  E-value: 2.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREAlEGLAARL---GGRAVALDICAADAG--QQLVEALPE- 284
Cdd:PRK12937   2 TLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAA-DELVAEIeaaGGRAIAVQADVADAAavTRLFDAAETa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 --GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAP-QVLTQALldgGKLHDNGRVVLLaSISGIAGNL-GQSNYAVS 360
Cdd:PRK12937  81 fgRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAfVVLREAA---RHLGQGGRIINL-STSVIALPLpGYGPYAAS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQM-TAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQ 439
Cdd:PRK12937 157 KAAVEGLVHVLANELRGRGITVNAVAPGPVATELfFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQ 236


                 ....*.
gi 15599980  440 VLRVCG 445
Cdd:PRK12937 237 VLRVNG 242
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 211-445 4.65e-24

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 100.55  E-value: 4.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVlLDVPPAREALEGLAARLGGRAVAL--DICAADAGQQLVEALPE---- 284
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARVV-VNYHQSEDAAEALADELGDRAIALqaDVTDREQVQAMFATATEhfgk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNA-------GITRdKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVllasisGIAGNLGQS-- 355
Cdd:PRK08642  81 PITTVVNNAladfsfdGDAR-KKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRII------NIGTNLFQNpv 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  356 ----NYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFI-ETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQ 430
Cdd:PRK08642 154 vpyhDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLrTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAVLFFAS 233

                        250
                 ....*....|....*
gi 15599980  431 PSSGAVSGQVLRVCG 445
Cdd:PRK08642 234 PWARAVTGQNLVVDG 248
PRK06172 PRK06172
SDR family oxidoreductase;
209-445 4.87e-24

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 100.60  E-value: 4.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  209 SKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAR-EALEGLAARLGGRA--VALDICAADAGQQLVEALPEG 285
Cdd:PRK06172   2 SMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGgEETVALIREAGGEAlfVACDVTRDAEVKALVEQTIAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 ---VDIVVHNAGITRDK-TLAKMSSDFWNSVINVNLNA---------PQVLTQalldGGklhdnGRVVLLASISGIAGNL 352
Cdd:PRK06172  82 ygrLDYAFNNAGIEIEQgRLAEGSEAEFDAIMGVNVKGvwlcmkyqiPLMLAQ----GG-----GAIVNTASVAGLGAAP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  353 GQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQM----TAAIPlTIREAGRRMNSMSQGGLPQDVAETVAWF 428
Cdd:PRK06172 153 KMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMfrraYEADP-RKAEFAAAMHPVGRIGKVEEVASAVLYL 231

                        250
                 ....*....|....*..
gi 15599980  429 AQPSSGAVSGQVLRVCG 445
Cdd:PRK06172 232 CSDGASFTTGHALMVDG 248
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 212-438 9.80e-24

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: 99.71  E-value: 9.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDV--PPAREALEGLAARLGGRAVAL--DICAADAGQQLVEALPEG-- 285
Cdd:cd05352   6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNsaPRAEEKAEELAKKYGVKTKAYkcDVSSQESVEKTFKQIQKDfg 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 -VDIVVHNAGITRDKTLAKMSSDFWNSVINVNL----NAPQVLTQALLDGGKlhdnGRVVLLASISGIAGN--LGQSNYA 358
Cdd:cd05352  86 kIDILIANAGITVHKPALDYTYEQWNKVIDVNLngvfNCAQAAAKIFKKQGK----GSLIITASMSGTIVNrpQPQAAYN 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 359 VSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSG 438
Cdd:cd05352 162 ASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYTTG 241
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 215-445 1.03e-23

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: 99.53  E-value: 1.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 215 QRALVTGAARGIGAAIAETLARDGAEVVLLdvppAREAlEGLAARLG-----GRAVALDICAADAGQQlVEALPEG---- 285
Cdd:cd08945   4 EVALVTGATSGIGLAIARRLGKEGLRVFVC----ARGE-EGLATTVKelreaGVEADGRTCDVRSVPE-IEALVAAavar 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 ---VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAP-QVLTQALLDGGKLHDN-GRVVLLASISGIAGNLGQSNYAVS 360
Cdd:cd08945  78 ygpIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVfRVTKEVLKAGGMLERGtGRIINIASTGGKQGVVHAAPYSAS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAI--------PLTIREAGRRMNS---MSQGGLPQDVAETVAWFA 429
Cdd:cd08945 158 KHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVrehyadiwEVSTEEAFDRITArvpLGRYVTPEEVAGMVAYLI 237

                       250
                ....*....|....*.
gi 15599980 430 QPSSGAVSGQVLRVCG 445
Cdd:cd08945 238 GDGAAAVTAQALNVCG 253
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 211-445 1.24e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 99.35  E-value: 1.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppaREALEGLAARLGG---RAVALDICAADAGQQLVEALPE--- 284
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDR---SEDVAEVAAQLLGgnaKGLVCDVSDSQSVEAAVAAVISafg 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK06841  89 RIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIET-------------QMTAAIPltireAGRRmnsmsqgGLPQDVAETVAWFAQP 431
Cdd:PRK06841 169 VGMTKVLALEWGPYGITVNAISPTVVLTelgkkawagekgeRAKKLIP-----AGRF-------AYPEEIAAAALFLASD 236

                        250
                 ....*....|....
gi 15599980  432 SSGAVSGQVLRVCG 445
Cdd:PRK06841 237 AAAMITGENLVIDG 250
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
210-443 1.75e-23

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 103.39  E-value: 1.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  210 KPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPParEALEGLAARLGGR----AVALDICAADAGQQLVEALPE- 284
Cdd:PRK08324 418 KPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDE--EAAEAAAAELGGPdralGVACDVTDEAAVQAAFEEAALa 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 --GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQA----LLDGGKlhdNGRVVLLASISGIAGNLGQSNYA 358
Cdd:PRK08324 496 fgGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREavriMKAQGL---GGSIVFIASKNAVNPGPNFGAYG 572

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  359 VSKAGLIGLAQAWAPALGKRGITINAVAP------------GFIETQMtAAIPLTIREAG---RRMNSMSQGGLPQDVAE 423
Cdd:PRK08324 573 AAKAAELHLVRQLALELGPDGIRVNGVNPdavvrgsgiwtgEWIEARA-AAYGLSEEELEefyRARNLLKREVTPEDVAE 651

                        250       260
                 ....*....|....*....|
gi 15599980  424 TVAWFAQPSSGAVSGQVLRV 443
Cdd:PRK08324 652 AVVFLASGLLSKTTGAIITV 671
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 217-445 1.76e-23

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: 98.99  E-value: 1.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAR--EALEGLAARLGGRAVA--LDICAADAGQQLVEALPE---GVDIV 289
Cdd:cd05366   5 AIITGAAQGIGRAIAERLAADGFNIVLADLNLEEaaKSTIQEISEAGYNAVAvgADVTDKDDVEALIDQAVEkfgSFDVM 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 290 VHNAGITRDKTLAKMSSDFWNSVINVN----LNAPQVLTQALLdggKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:cd05366  85 VNNAGIAPITPLLTITEEDLKKVYAVNvfgvLFGIQAAARQFK---KLGHGGKIINASSIAGVQGFPNLGAYSASKFAVR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 366 GLAQAWAPALGKRGITINAVAPGFIETQMTAAI-----PLTIREAGRRMN------SMSQGGLPQDVAETVAWFAQPSSG 434
Cdd:cd05366 162 GLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIdeevgEIAGKPEGEGFAefsssiPLGRLSEPEDVAGLVSFLASEDSD 241

                       250
                ....*....|.
gi 15599980 435 AVSGQVLRVCG 445
Cdd:cd05366 242 YITGQTILVDG 252
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 212-441 3.29e-23

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 98.32  E-value: 3.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEglAARLGGRAVALDICAAD----AGQQLVEALPEgVD 287
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKE--LREKGVFTIKCDVGNRDqvkkSKEVVEKEFGR-VD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  288 IVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIA-GNLGQSNYAVSKAGLIG 366
Cdd:PRK06463  82 VLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGtAAEGTTFYAITKAGIII 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  367 LAQAWAPALGKRGITINAVAPGFIETQMTAAIPLT-----IREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVL 441
Cdd:PRK06463 162 LTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQeeaekLRELFRNKTVLKTTGKPEDIANIVLFLASDDARYITGQVI 241
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 212-445 4.79e-23

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 98.04  E-value: 4.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDV--PPAREALEGLAARlGGRA--VALDICAADAGQQLVEALPE--- 284
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLnqDGANAVADEINKA-GGKAigVAMDVTNEDAVNAGIDKVAErfg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDN-GRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:PRK13394  84 SVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRgGVVIYMGSVHSHEASPLKSAYVTAKHG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  364 LIGLAQAWAPALGKRGITINAVAPGFIETQMTAA-IPLTIREAG--------RRMNSMSQGGL---PQDVAETVAWFAQP 431
Cdd:PRK13394 164 LLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKqIPEQAKELGiseeevvkKVMLGKTVDGVfttVEDVAQTVLFLSSF 243

                        250
                 ....*....|....
gi 15599980  432 SSGAVSGQVLRVCG 445
Cdd:PRK13394 244 PSAALTGQSFVVSH 257
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 212-445 7.74e-23

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 97.26  E-value: 7.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDV-PPAREALEGLAARLGGRAVAL-----DICAADAGQQLVEALPEG 285
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLnDEAAAAAAEALQKAGGKAIGVamdvtDEEAINAGIDYAVETFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:PRK12429  82 VDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  366 GLAQAWAPALGKRGITINAVAPGFIET-----QMTA-AIPLTIREAGRRMNSMS----QGGL--PQDVAETVAWFAQPSS 433
Cdd:PRK12429 162 GLTKVVALEGATHGVTVNAICPGYVDTplvrkQIPDlAKERGISEEEVLEDVLLplvpQKRFttVEEIADYALFLASFAA 241

                        250
                 ....*....|..
gi 15599980  434 GAVSGQVLRVCG 445
Cdd:PRK12429 242 KGVTGQAWVVDG 253
PRK06138 PRK06138
SDR family oxidoreductase;
212-450 8.98e-23

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 96.76  E-value: 8.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARL--GGRAVAL--DICAADAGQQLVEALP---E 284
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADR--DAEAAERVAAAIaaGGRAFARqgDVGSAEAVEALVDFVAarwG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIETQMTAAI------PLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSG 438
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIfarhadPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFATG 240

                        250
                 ....*....|..
gi 15599980  439 QVLRVCGQSLLG 450
Cdd:PRK06138 241 TTLVVDGGWLAA 252
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 208-445 1.05e-22

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: 96.75  E-value: 1.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 208 WSkpLAGQRALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAARLGGR-----AVALDICAADAGQQLVE 280
Cdd:cd05329   2 WN--LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTC----ARnqKELDECLTEWREKgfkveGSVCDVSSRSERQELMD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 281 ALP----EGVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQ---ALLdggKLHDNGRVVLLASISGIAGNLG 353
Cdd:cd05329  76 TVAshfgGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRlahPLL---KASGNGNIVFISSVAGVIAVPS 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 354 QSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAI--------PLTIREAGRRMnsmsqgGLPQDVAETV 425
Cdd:cd05329 153 GAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPViqqkenldKVIERTPLKRF------GEPEEVAALV 226

                       250       260
                ....*....|....*....|
gi 15599980 426 AWFAQPSSGAVSGQVLRVCG 445
Cdd:cd05329 227 AFLCMPAASYITGQIIAVDG 246
PRK09242 PRK09242
SDR family oxidoreductase;
206-445 1.18e-22

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 96.74  E-value: 1.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  206 HDWSkpLAGQRALVTGAARGIGAAIAETLARDGAEVVLL-----DVPPAREALEGLAARLGGRAVALDICAADAGQQLVE 280
Cdd:PRK09242   3 HRWR--LDGQTALITGASKGIGLAIAREFLGLGADVLIVardadALAQARDELAEEFPEREVHGLAADVSDDEDRRAILD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  281 ALPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNY 357
Cdd:PRK09242  81 WVEDhwdGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  358 AVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAI---PLTIREAGRRmNSMSQGGLPQDVAETVAWFAQPSSG 434
Cdd:PRK09242 161 GMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPlsdPDYYEQVIER-TPMRRVGEPEEVAAAVAFLCMPAAS 239

                        250
                 ....*....|.
gi 15599980  435 AVSGQVLRVCG 445
Cdd:PRK09242 240 YITGQCIAVDG 250
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 214-445 5.23e-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: 94.77  E-value: 5.23e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAARLGGRAVAL--DICAADAGQQLVEALPE---GVDI 288
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRALGVqcDVTSEAQVQSAFEQAVLefgGLDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 289 VVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQ-VLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGL 367
Cdd:cd08943  81 VVSNAGIATSSPIAETSLEDWNRSMDINLTGHFlVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 368 AQAWAPALGKRGITINAVAPGFIETqmTAAIPLTIREAGRRM------------NSMSQGGLPQDVAETVAWFAQPSSGA 435
Cdd:cd08943 161 ARCLALEGGEDGIRVNTVNPDAVFR--GSKIWEGVWRAARAKayglleeeyrtrNLLKREVLPEDVAEAVVAMASEDFGK 238

                       250
                ....*....|
gi 15599980 436 VSGQVLRVCG 445
Cdd:cd08943 239 TTGAIVTVDG 248
PRK06500 PRK06500
SDR family oxidoreductase;
212-445 8.62e-22

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 93.87  E-value: 8.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAreALEGLAARLGGRAVALDICAADAGQQ--LVEALPE---GV 286
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPA--SLEAARAELGESALVIRADAGDVAAQkaLAQALAEafgRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLdggKLHDNG-RVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:PRK06500  82 DAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALL---PLLANPaSIVLNGSINAHIGMPNSSVYAASKAALL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  366 GLAQAWAPALGKRGITINAVAPGFIET--------------QMTAAIPLTIrEAGRRmnsmsqgGLPQDVAETVAWFAQP 431
Cdd:PRK06500 159 SLAKTLSGELLPRGIRVNAVSPGPVQTplygklglpeatldAVAAQIQALV-PLGRF-------GTPEEIAKAVLYLASD 230

                        250
                 ....*....|....
gi 15599980  432 SSGAVSGQVLRVCG 445
Cdd:PRK06500 231 ESAFIVGSEIIVDG 244
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 212-445 1.34e-21

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: 93.60  E-value: 1.34e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARLGGRA--VALDICAADAGQQLVEALPE---GV 286
Cdd:cd05341   3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDI--LDEEGQAAAAELGDAArfFHLDVTDEDGWTAVVDTAREafgRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 287 DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIG 366
Cdd:cd05341  81 DVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 367 LAQAWAPALGKR--GITINAVAPGFIETQMTAAIPLTIREAGRRMNS-MSQGGLPQDVAETVAWFAQPSSGAVSGQVLRV 443
Cdd:cd05341 161 LTKSAALECATQgyGIRVNSVHPGYIYTPMTDELLIAQGEMGNYPNTpMGRAGEPDEIAYAVVYLASDESSFVTGSELVV 240


                ..
gi 15599980 444 CG 445
Cdd:cd05341 241 DG 242
PRK12743 PRK12743
SDR family oxidoreductase;
215-449 2.04e-21

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 93.17  E-value: 2.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  215 QRALVTGAARGIGAAIAETLARDGAEVVLL---DVPPAREALEGLAARlGGRAVA--LDICAADAGQQLVEALPE---GV 286
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITwhsDEEGAKETAEEVRSH-GVRAEIrqLDLSDLPEGAQALDKLIQrlgRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQ----ALLDGGKlhdNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:PRK12743  82 DVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQiaarHMVKQGQ---GGRIINITSVHEHTPLPGASAYTAAKH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  363 GLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLR 442
Cdd:PRK12743 159 ALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSLI 238


                 ....*..
gi 15599980  443 VCGQSLL 449
Cdd:PRK12743 239 VDGGFML 245
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 213-439 3.59e-21

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: 92.15  E-value: 3.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 213 AGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPParEALEGLAARLGGRAVALDICAADAGQQLVEALpEGVDIVVHN 292
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINE--EKLKELERGPGITTRVLDVTDKEQVAALAKEE-GRIDVLFNC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 293 AGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISG-IAGNLGQSNYAVSKAGLIGLAQAW 371
Cdd:cd05368  78 AGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYSTTKAAVIGLTKSV 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599980 372 APALGKRGITINAVAPGFIETQMTAAI------PLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQ 439
Cdd:cd05368 158 AADFAQQGIRCNAICPGTVDTPSLEERiqaqpdPEEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGT 231
PRK07774 PRK07774
SDR family oxidoreductase;
212-445 3.75e-21

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 92.11  E-value: 3.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARL---GGRAVA--LDICAADAGQQLVEALPE-- 284
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADI--NAEGAERVAKQIvadGGTAIAvqVDVSDPDSAKAMADATVSaf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 -GVDIVVHNAGITRD---KTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVllaSISGIAGNLGQSNYAVS 360
Cdd:PRK07774  82 gGIDYLVNNAAIYGGmklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIV---NQSSTAAWLYSNFYGLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQMT-AAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQ 439
Cdd:PRK07774 159 KVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATrTVTPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWITGQ 238


                 ....*.
gi 15599980  440 VLRVCG 445
Cdd:PRK07774 239 IFNVDG 244
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 214-445 9.79e-21

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: 91.20  E-value: 9.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEgLAARLGGRAVALDICAADAGQQLVEALPE---GVDIVV 290
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETV-AKLGDNCRFVPVDVTSEKDVKAALALAKAkfgRLDIVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 291 HNAGIT-RDKTLAK-----MSSDFWNSVINVN---------LNAPQVLTQALLDGGklhDNGRVVLLASISGIAGNLGQS 355
Cdd:cd05371  81 NCAGIAvAAKTYNKkgqqpHSLELFQRVINVNligtfnvirLAAGAMGKNEPDQGG---ERGVIINTASVAAFEGQIGQA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 356 NYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSM-SQGGLPQDVAETVAWFAQPSsg 434
Cdd:cd05371 158 AYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPFpSRLGDPAEYAHLVQHIIENP-- 235

                       250
                ....*....|.
gi 15599980 435 AVSGQVLRVCG 445
Cdd:cd05371 236 YLNGEVIRLDG 246
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 212-445 1.04e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 91.28  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPParEALE-GLAA--RLGGRAVAL--DICAADAGQQLVEALPEGV 286
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQ--ELVDkGLAAyrELGIEAHGYvcDVTDEDGVQAMVSQIEKEV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 ---DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:PRK07097  86 gviDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  364 LIGLAQAWAPALGKRGITINAVAPGFIETQMTAaiPLTIREAGRRMNSMSQ----------GGLPQDVAETVAWFAQPSS 433
Cdd:PRK07097 166 LKMLTKNIASEYGEANIQCNGIGPGYIATPQTA--PLRELQADGSRHPFDQfiiaktpaarWGDPEDLAGPAVFLASDAS 243

                        250
                 ....*....|..
gi 15599980  434 GAVSGQVLRVCG 445
Cdd:PRK07097 244 NFVNGHILYVDG 255
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 209-445 1.09e-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: 1.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 209 SKPLAGQRALVTGAARGIGAAIAETLARDGAEVVL-----LDVPPAREALEGLAARLGGRAVALDIcaADAGQQLVEA-- 281
Cdd:cd08936   5 RDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVssrkqQNVDRAVATLQGEGLSVTGTVCHVGK--AEDRERLVATav 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 282 -LPEGVDIVVHNAGITR-DKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAV 359
Cdd:cd08936  83 nLHGGVDILVSNAAVNPfFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 360 SKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPL--TIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVS 437
Cdd:cd08936 163 SKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMdkAVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASYIT 242


                ....*...
gi 15599980 438 GQVLRVCG 445
Cdd:cd08936 243 GETVVVGG 250
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 235-445 1.26e-20

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 90.79  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  235 ARDGAEVVLldvpPAR--EALEGLAAR---LGGRAVAL--DICAADAGQQLVEALPE---GVDIVVHNA-GITRDKTLAK 303
Cdd:PRK07890  26 ARAGADVVL----AARtaERLDEVAAEiddLGRRALAVptDITDEDQCANLVALALErfgRVDALVNNAfRVPSMKPLAD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  304 MSSDFWNSVINVNLNAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITIN 383
Cdd:PRK07890 102 ADFAHWRAVIELNVLGTLRLTQAFTPALA-ESGGSIVMINSMVLRHSQPKYGAYKMAKGALLAASQSLATELGPQGIRVN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  384 AVAPGFI-------------------ETQMTAAIplTIREAGRRMNSmsqgglPQDVAETVAWFAQPSSGAVSGQVLRV- 443
Cdd:PRK07890 181 SVAPGYIwgdplkgyfrhqagkygvtVEQIYAET--AANSDLKRLPT------DDEVASAVLFLASDLARAITGQTLDVn 252


                 ..
gi 15599980  444 CG 445
Cdd:PRK07890 253 CG 254
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
212-449 1.56e-20

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 90.63  E-value: 1.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPareALEGLAARLGGR-----AVALDICAADAGQQLVEALPEG- 285
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISP---EIEKLADELCGRghrctAVVADVRDPASVAAAIKRAKEKe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 --VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISG-IAGNLGQSNYAVSKA 362
Cdd:PRK08226  81 grIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYALTKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  363 GLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPltiREAG-----RRMNSMSQG------GLPQDVAETVAWFAQP 431
Cdd:PRK08226 161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIA---RQSNpedpeSVLTEMAKAiplrrlADPLEVGELAAFLASD 237

                        250
                 ....*....|....*...
gi 15599980  432 SSGAVSGQVLRVCGQSLL 449
Cdd:PRK08226 238 ESSYLTGTQNVIDGGSTL 255
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 217-445 2.32e-20

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 90.02  E-value: 2.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAA--RLGGRAVAL--DICAADAGQQLVEALPE---GVDIV 289
Cdd:PRK12745   5 ALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQElrALGVEVIFFpaDVADLSAHEAMLDAAQAawgRIDCL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  290 VHNAGIT---RDKTLAkMSSDFWNSVINVNLNAPQVLTQA----LLDGGKLHDN--GRVVLLASISGIAGNLGQSNYAVS 360
Cdd:PRK12745  85 VNNAGVGvkvRGDLLD-LTPESFDRVLAINLRGPFFLTQAvakrMLAQPEPEELphRSIVFVSSVNAIMVSPNRGEYCIS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAaiPLTIR-----EAGrrMNSMSQGGLPQDVAETVAWFAQPSSGA 435
Cdd:PRK12745 164 KAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTA--PVTAKydaliAKG--LVPMPRWGEPEDVARAVAALASGDLPY 239

                        250
                 ....*....|
gi 15599980  436 VSGQVLRVCG 445
Cdd:PRK12745 240 STGQAIHVDG 249
PRK06484 PRK06484
short chain dehydrogenase; Validated
 214-445 2.68e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 93.38  E-value: 2.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAReaLEGLAARLGGR--AVALDICAADAGQQLVEALPE---GVDI 288
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVER--ARERADSLGPDhhALAMDVSDEAQIREGFEQLHRefgRIDV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 VVHNAGITrDKT---LAKMSSDFWNSVINVNLNAP-QVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK06484  83 LVNNAGVT-DPTmtaTLDTTLEEFARLQAINLTGAyLVAREALRLMIEQGHGAAIVNVASGAGLVALPKRTAYSASKAAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIETQMTAAIP---LTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVL 441
Cdd:PRK06484 162 ISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELEragKLDPSAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGSTL 241


                 ....
gi 15599980  442 RVCG 445
Cdd:PRK06484 242 VVDG 245
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 287-425 2.73e-20

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: 87.96  E-value: 2.73e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 287 DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIG 366
Cdd:cd02266  33 DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDG 112

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980 367 LAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETV 425
Cdd:cd02266 113 LAQQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARAL 171
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 212-445 3.09e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 89.60  E-value: 3.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLldvpPAR--EALEGLAA---RLGGRAVAL--DICAADAGQQLVEALPE 284
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVV----GARrqAELDQLVAeirAEGGEAVALagDVRDEAYAKALVALAVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 ---GVDIVVHNAGITRD-KTLAKMSSDFWNSVINVNLN-----APQVLTQALLDGGklhdnGRVVLLASISG-IAGNLGQ 354
Cdd:PRK07478  80 rfgGLDIAFNNAGTLGEmGPVAEMSLEGWRETLATNLTsaflgAKHQIPAMLARGG-----GSLIFTSTFVGhTAGFPGM 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  355 SNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLT--IREAGRRMNSMSQGGLPQDVAETVAWFAQPS 432
Cdd:PRK07478 155 AAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTpeALAFVAGLHALKRMAQPEEIAQAALFLASDA 234

                        250
                 ....*....|...
gi 15599980  433 SGAVSGQVLRVCG 445
Cdd:PRK07478 235 ASFVTGTALLVDG 247
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 218-445 5.24e-20

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: 89.12  E-value: 5.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 218 LVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARL--GGRAVALDICAAD-AGQQLVEALPEG-------VD 287
Cdd:cd05330   7 LITGGGSGLGLATAVRLAKEGAKLSLVDL--NEEGLEAAKAALleIAPDAEVLLIKADvSDEAQVEAYVDAtveqfgrID 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 288 IVVHNAGIT-RDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIG 366
Cdd:cd05330  85 GFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVVG 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 367 LAQAWAPALGKRGITINAVAPGFIETQMTAAI-----PLTIREAGRR---MNSMSQGGLPQDVAETVAWFAQPSSGAVSG 438
Cdd:cd05330 165 LTRNSAVEYGQYGIRINAIAPGAILTPMVEGSlkqlgPENPEEAGEEfvsVNPMKRFGEPEEVAAVVAFLLSDDAGYVNA 244


                ....*..
gi 15599980 439 QVLRVCG 445
Cdd:cd05330 245 AVVPIDG 251
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
212-445 9.47e-20

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 88.42  E-value: 9.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAArLGGR--AVALDICAADAGQQLVEALPE---GV 286
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQVEA-LGRKfhFITADLIQQKDIDSIVSQAVEvmgHI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDG-GKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:PRK12481  85 DILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQfVKQGNGGKIINIASMLSFQGGIRVPSYTASKSAVM 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  366 GLAQAWAPALGKRGITINAVAPGFIETQMTAAipltIREAGRRMNSM------SQGGLPQDVAETVAWFAQPSSGAVSGQ 439
Cdd:PRK12481 165 GLTRALATELSQYNINVNAIAPGYMATDNTAA----LRADTARNEAIleripaSRWGTPDDLAGPAIFLSSSASDYVTGY 240


                 ....*.
gi 15599980  440 VLRVCG 445
Cdd:PRK12481 241 TLAVDG 246
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 212-425 1.41e-19

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 87.44  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAARLGGRAVALDICAAD---------AGQQLVE 280
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLL----ARteENLKAVAEEVEAYGVKVVIATADvsdyeevtaAIEQLKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  281 ALpEGVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVS 360
Cdd:PRK07666  81 EL-GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSAS 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599980  361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNsmsqgglPQDVAETV 425
Cdd:PRK07666 160 KFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDGNPDKVMQ-------PEDLAEFI 217
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 217-445 1.94e-19

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: 87.52  E-value: 1.94e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAA--RLGGRAVA--LDICAADAGQQLVEALPE---GVDIV 289
Cdd:cd05337   4 AIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEvlAAGRRAIYfqADIGELSDHEALLDQAWEdfgRLDCL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 290 VHNAGIT--RDKTLAKMSSDFWNSVINVNLNAPQVLTQA----LLDGGKLHD--NGRVVLLASISGIAGNLGQSNYAVSK 361
Cdd:cd05337  84 VNNAGIAvrPRGDLLDLTEDSFDRLIAINLRGPFFLTQAvarrMVEQPDRFDgpHRSIIFVTSINAYLVSPNRGEYCISK 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 362 AGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREA-GRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQV 440
Cdd:cd05337 164 AGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELiAAGLVPIRRWGQPEDIAKAVRTLASGLLPYSTGQP 243


                ....*
gi 15599980 441 LRVCG 445
Cdd:cd05337 244 INIDG 248
PRK12742 PRK12742
SDR family oxidoreductase;
211-438 2.76e-19

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 86.73  E-value: 2.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPpAREALEGLAARLGGRAVALDICAADAGQQLVEALPEgVDIVV 290
Cdd:PRK12742   3 AFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAG-SKDAAERLAQETGATAVQTDSADRDAVIDVVRKSGA-LDILV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  291 HNAGITRDKTLAKMSSDFWNSVINVNLNAPqvLTQALLDGGKLHDNGRVVLLASISGIAGNL-GQSNYAVSKAGLIGLAQ 369
Cdd:PRK12742  81 VNAGIAVFGDALELDADDIDRLFKINIHAP--YHASVEAARQMPEGGRIIIIGSVNGDRMPVaGMAAYAASKSALQGMAR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  370 AWAPALGKRGITINAVAPGFIETQMTAAI-PLtiREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSG 438
Cdd:PRK12742 159 GLARDFGPRGITINVVQPGPIDTDANPANgPM--KDMMHSFMAIKRHGRPEEVAGMVAWLAGPEASFVTG 226
PRK12746 PRK12746
SDR family oxidoreductase;
210-445 7.00e-19

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 85.86  E-value: 7.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  210 KPLAGQRALVTGAARGIGAAIAETLARDGAEVVL---LDVPPAREALEGLAARlGGRA--VALDICAADAGQQLVEALP- 283
Cdd:PRK12746   2 KNLDGKVALVTGASRGIGRAIAMRLANDGALVAIhygRNKQAADETIREIESN-GGKAflIEADLNSIDGVKKLVEQLKn 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  284 --------EGVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDggKLHDNGRVVLLASISGIAGNLGQS 355
Cdd:PRK12746  81 elqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLP--LLRAEGRVINISSAEVRLGFTGSI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  356 NYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAI--PLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSS 433
Cdd:PRK12746 159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLldDPEIRNFATNSSVFGRIGQVEDIADAVAFLASSDS 238

                        250
                 ....*....|..
gi 15599980  434 GAVSGQVLRVCG 445
Cdd:PRK12746 239 RWVTGQIIDVSG 250
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
217-445 7.47e-19

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 85.93  E-value: 7.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVVLLD--VPPAREALEGLAaRLGGRAVALDICAAD------AGQQLVEALpEGVDI 288
Cdd:PRK08643   5 ALVTGAGQGIGFAIAKRLVEDGFKVAIVDynEETAQAAADKLS-KDGGKAIAVKADVSDrdqvfaAVRQVVDTF-GDLNV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 VVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDG-GKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGL 367
Cdd:PRK08643  83 VVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAfKKLGHGGKIINATSQAGVVGNPELAVYSSTKFAVRGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  368 AQAWAPALGKRGITINAVAPGFIETQMTAAIPLTI-REAGRRMN-SMSQ-------GGL--PQDVAETVAWFAQPSSGAV 436
Cdd:PRK08643 163 TQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVgENAGKPDEwGMEQfakditlGRLsePEDVANCVSFLAGPDSDYI 242


                 ....*....
gi 15599980  437 SGQVLRVCG 445
Cdd:PRK08643 243 TGQTIIVDG 251
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 212-449 1.20e-18

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 85.13  E-value: 1.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAARLGGRAVALDICAADAGQQLVEALPEGV----- 286
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLdnelq 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 --------DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDggKLHDNGRVVLLASISGIAGNLGQSNYA 358
Cdd:PRK12747  82 nrtgstkfDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALS--RLRDNSRIINISSAATRISLPDFIAYS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  359 VSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAI---PLtIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGA 435
Cdd:PRK12747 160 MTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELlsdPM-MKQYATTISAFNRLGEVEDIADTAAFLASPDSRW 238

                        250
                 ....*....|....
gi 15599980  436 VSGQVLRVCGQSLL 449
Cdd:PRK12747 239 VTGQLIDVSGGSCL 252
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 217-445 1.32e-18

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: 84.93  E-value: 1.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAA---RLGGRAVAL--DICAADAGQQLVEALPE---GVDI 288
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADL--KSEGAEAVAAaiqQAGGQAIGLecNVTSEQDLEAVVKATVSqfgGITI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 289 VVHNAGI--TRDKTLAKMSSDFwNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIG 366
Cdd:cd05365  80 LVNNAGGggPKPFDMPMTEEDF-EWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 367 LAQAWAPALGKRGITINAVAPGFIETQMTAAIplTIREAGRRM---NSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRV 443
Cdd:cd05365 159 MTRNLAFDLGPKGIRVNAVAPGAVKTDALASV--LTPEIERAMlkhTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTV 236


                ..
gi 15599980 444 CG 445
Cdd:cd05365 237 SG 238
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 214-445 1.89e-18

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 84.24  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLaarlggRAVALDICaaDAGQQLVEALPEgVDIVVHNA 293
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLSGNF------HFLQLDLS--DDLEPLFDWVPS-VDILCNTA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  294 GITRD-KTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWA 372
Cdd:PRK06550  76 GILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGFTKQLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  373 PALGKRGITINAVAPGFIETQMTAA--------------IPltireAGRRMNsmsqgglPQDVAETVAWFAQPSSGAVSG 438
Cdd:PRK06550 156 LDYAKDGIQVFGIAPGAVKTPMTAAdfepggladwvareTP-----IKRWAE-------PEEVAELTLFLASGKADYMQG 223


                 ....*..
gi 15599980  439 QVLRVCG 445
Cdd:PRK06550 224 TIVPIDG 230
PRK08589 PRK08589
SDR family oxidoreductase;
210-445 1.90e-18

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 84.83  E-value: 1.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  210 KPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppaREALEGLAARL---GGRAVA--LDICAADAGQQLVEALPE 284
Cdd:PRK08589   2 KRLENKVAVITGASTGIGQASAIALAQEGAYVLAVDI---AEAVSETVDKIksnGGKAKAyhVDISDEQQVKDFASEIKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 G---VDIVVHNAGItrDKTLAKMSS---DFWNSVINVNLNAPQVLTQALLDGgKLHDNGRVVLLASISGIAGNLGQSNYA 358
Cdd:PRK08589  79 QfgrVDVLFNNAGV--DNAAGRIHEypvDVFDKIMAVDMRGTFLMTKMLLPL-MMEQGGSIINTSSFSGQAADLYRSGYN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  359 VSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLT--------IREAGRRMNSMSQGGLPQDVAETVAWFAQ 430
Cdd:PRK08589 156 AAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTsedeagktFRENQKWMTPLGRLGKPEEVAKLVVFLAS 235

                        250
                 ....*....|....*
gi 15599980  431 PSSGAVSGQVLRVCG 445
Cdd:PRK08589 236 DDSSFITGETIRIDG 250
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
212-445 3.31e-18

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 83.77  E-value: 3.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAArLGGRAVAL--DICAADAGQQLVE-ALPE--GV 286
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPTETIEQVTA-LGRRFLSLtaDLRKIDGIPALLErAVAEfgHI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNG-RVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:PRK08993  87 DILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGgKIINIASMLSFQGGIRVPSYTASKSGVM 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  366 GLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQG--GLPQDVAETVAWFAQPSSGAVSGQVLRV 443
Cdd:PRK08993 167 GVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEILDRIPAGrwGLPSDLMGPVVFLASSASDYINGYTIAV 246


                 ..
gi 15599980  444 CG 445
Cdd:PRK08993 247 DG 248
PRK06114 PRK06114
SDR family oxidoreductase;
212-394 3.59e-18

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 83.68  E-value: 3.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVP--PAREALEGLAARLGGRAVAL-----DICAADAGQQLVEALPE 284
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRtdDGLAETAEHIEAAGRRAIQIaadvtSKADLRAAVARTEAELG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNL----NAPQVLTQALLDGGKlhdnGRVVLLASISGIAGNLG--QSNYA 358
Cdd:PRK06114  86 ALTLAVNAAGIANANPAEEMEEEQWQTVMDINLtgvfLSCQAEARAMLENGG----GSIVNIASMSGIIVNRGllQAHYN 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15599980  359 VSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQM 394
Cdd:PRK06114 162 ASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPM 197
PRK07856 PRK07856
SDR family oxidoreductase;
212-445 4.62e-18

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 83.44  E-value: 4.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLdvppAREALEGLAARlGGRAVALDICAADAGQQLVEALPE---GVDI 288
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVC----GRRAPETVDGR-PAEFHAADVRDPDQVAALVDAIVErhgRLDV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 VVHNAGITRDKTLAKMSSDFWNSVINVNLNAP-QVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGL 367
Cdd:PRK07856  79 LVNNAGGSPYALAAEASPRFHEKIVELNLLAPlLVAQAANAVMQQQPGGGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  368 AQA----WAPAlgkrgITINAVAPGFIETQ--------------MTAAIPLtireagRRMnsmsqgGLPQDVAETVAWFA 429
Cdd:PRK07856 159 TRSlaveWAPK-----VRVNAVVVGLVRTEqselhygdaegiaaVAATVPL------GRL------ATPADIAWACLFLA 221

                        250
                 ....*....|....*.
gi 15599980  430 QPSSGAVSGQVLRVCG 445
Cdd:PRK07856 222 SDLASYVSGANLEVHG 237
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 217-449 6.66e-18

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: 82.73  E-value: 6.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAARLGG---RAVALDICAADAGQQLVEALPE---GVDIVV 290
Cdd:cd05323   3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINPKvkaTFVQCDVTSWEQLAAAFKKAIEkfgRVDILI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 291 HNAGITRDKTLAKMSSDF--WNSVINVNLNAPQVLTQALLD------GGKlhdNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:cd05323  83 NNAGILDEKSYLFAGKLPppWEKTIDVNLTGVINTTYLALHymdknkGGK---GGVIVNIGSVAGLYPAPQFPVYSASKH 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 363 GLIGLAQAWAPAL-GKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSqgglPQDVAETVAWFAQPSSGAvsGQVL 441
Cdd:cd05323 160 GVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAPTQS----PEVVAKAIVYLIEDDEKN--GAIW 233


                ....*...
gi 15599980 442 RVCGQSLL 449
Cdd:cd05323 234 IVDGGKLI 241
PRK07063 PRK07063
SDR family oxidoreductase;
212-429 7.80e-18

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 82.79  E-value: 7.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVL--LDVPPAREALEGLAARL-GGRAVAL--DICAADAGQQLVEALPE-- 284
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALadLDAALAERAAAAIARDVaGARVLAVpaDVTDAASVAAAVAAAEEaf 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 -GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:PRK07063  85 gPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKHG 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599980  364 LIGLAQAWAPALGKRGITINAVAPGFIETQMT------AAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFA 429
Cdd:PRK07063 165 LLGLTRALGIEYAARNVRVNAIAPGYIETQLTedwwnaQPDPAAARAETLALQPMKRIGRPEEVAMTAVFLA 236
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 217-445 8.29e-18

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: 82.32  E-value: 8.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVL------LDVPPAREALEGlaarLGGRAVAL--DICAADAGQQLVEALPE---G 285
Cdd:cd05357   3 ALVTGAAKRIGRAIAEALAAEGYRVVVhynrseAEAQRLKDELNA----LRNSAVLVqaDLSDFAACADLVAAAFRafgR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:cd05357  79 CDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALE 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 366 GLAQAWAPALGKRgITINAVAPGFIETQMTAaiPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSgaVSGQVLRVCG 445
Cdd:cd05357 159 GLTRSAALELAPN-IRVNGIAPGLILLPEDM--DAEYRENALRKVPLKRRPSAEEIADAVIFLLDSNY--ITGQIIKVDG 233
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 212-445 9.01e-18

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 82.59  E-value: 9.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAAR---LGGRAVAL--DICAADAGQQLVEALPE-- 284
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDI--NADAANHVVDEiqqLGGQAFACrcDITSEQELSALADFALSkl 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 -GVDIVVHNAGITRDKTLAKMSSDF-WnsVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:PRK06113  87 gKVDILVNNAGGGGPKPFDMPMADFrR--AYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  363 GLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIpLT--IREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQV 440
Cdd:PRK06113 165 AASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSV-ITpeIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQI 243


                 ....*
gi 15599980  441 LRVCG 445
Cdd:PRK06113 244 LTVSG 248
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 211-429 9.26e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 83.48  E-value: 9.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAreALEGLAARLGGRAVALDICA--------ADAGQQLVEAL 282
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEA--ELAALAAELGGDDRVLTVVAdvtdlaamQAAAEEAVERF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  283 pEGVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDgGKLHDNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:PRK05872  84 -GGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLP-ALIERRGYVLQVSSLAAFAAAPGMAAYCASKA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980  363 GLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIpLTIREAGRRMNSMSQGGL--PQDVAETVAWFA 429
Cdd:PRK05872 162 GVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDA-DADLPAFRELRARLPWPLrrTTSVEKCAAAFV 229
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 212-445 1.22e-17

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: 82.14  E-value: 1.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLldvpPAR--EALEGLAARLGG----RAVALDICAADAGQQLVEALPE- 284
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVII----SARkaEACADAAEELSAygecIAIPADLSSEEGIEALVARVAEr 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 285 --GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLD----GGKLHDNGRVVLLASISGIAGNLGQS-NY 357
Cdd:cd08942  80 sdRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPllraAATAENPARVINIGSIAGIVVSGLENySY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 358 AVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAI--PLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGA 435
Cdd:cd08942 160 GASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLlnDPAALEAEEKSIPLGRWGRPEDMAGLAIMLASRAGAY 239

                       250
                ....*....|
gi 15599980 436 VSGQVLRVCG 445
Cdd:cd08942 240 LTGAVIPVDG 249
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 212-445 1.42e-17

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: 81.86  E-value: 1.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLL--DVPPAREALEGLAARLGGRA--VALDICAADAGQQLVEALPE--- 284
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAgrKPEVLEAAAEEISSATGGRAhpIQCDVRDPEAVEAAVDETLKefg 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLlaSISGIAGNLG---QSNYAVSK 361
Cdd:cd05369  81 KIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSIL--NISATYAYTGspfQVHSAAAK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 362 AGLIGLAQAWAPALGKRGITINAVAPGFIETQ---------------MTAAIPLtireagRRMnsmsqgGLPQDVAETVA 426
Cdd:cd05369 159 AGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTegmerlapsgksekkMIERVPL------GRL------GTPEEIANLAL 226

                       250
                ....*....|....*....
gi 15599980 427 WFAQPSSGAVSGQVLRVCG 445
Cdd:cd05369 227 FLLSDAASYINGTTLVVDG 245
PRK09072 PRK09072
SDR family oxidoreductase;
232-426 1.55e-17

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 82.30  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  232 ETLARDGAEVVLLdvppAR--EALEGLAARLGG----RAVALDICAADAGQQLVEA--LPEGVDIVVHNAGITRDKTLAK 303
Cdd:PRK09072  23 EALAAAGARLLLV----GRnaEKLEALAARLPYpgrhRWVVADLTSEAGREAVLARarEMGGINVLINNAGVNHFALLED 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  304 MSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITIN 383
Cdd:PRK09072  99 QDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRGFSEALRRELADTGVRVL 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15599980  384 AVAPGFIETQM-TAAIPLTIREAGRRMNSmsqgglPQDVAETVA 426
Cdd:PRK09072 179 YLAPRATRTAMnSEAVQALNRALGNAMDD------PEDVAAAVL 216
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 212-445 2.08e-17

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: 81.28  E-value: 2.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARLGGRAVAL--DICAADAGQQLVEALPE---GV 286
Cdd:cd05345   3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADI--NADGAERVAADIGEAAIAIqaDVTKRADVEAMVEAALSkfgRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 287 DIVVHNAGIT-RDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:cd05345  81 DILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 366 GLAQAWAPALGKRGITINAVAP-----GFIETQMTAAIPlTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQV 440
Cdd:cd05345 161 TATKAMAVELAPRNIRVNCLCPvagetPLLSMFMGEDTP-ENRAKFRATIPLGRLSTPDDIANAALYLASDEASFITGVA 239


                ....*
gi 15599980 441 LRVCG 445
Cdd:cd05345 240 LEVDG 244
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 214-445 2.34e-17

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: 81.09  E-value: 2.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAARLGGRAVALDICAADAGQQLVEALPE---GVDIVV 290
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEklgRIDVLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 291 HNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHdNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQA 370
Cdd:cd09761  81 NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKN-KGRIINIASTRAFQSEPDSEAYAASKGGLVALTHA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599980 371 WAPALGkRGITINAVAPGFIETQMTAAIPLT-IREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:cd09761 160 LAMSLG-PDIRVNCISPGWINTTEQQEFTAApLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIVDG 234
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 209-445 2.61e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 81.49  E-value: 2.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  209 SKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLdvppAREALEGLAArlGGRAVALDICAADAGQQLVEALPE---G 285
Cdd:PRK06523   4 FLELAGKRALVTGGTKGIGAATVARLLEAGARVVTT----ARSRPDDLPE--GVEFVAADLTTAEGCAAVARAVLErlgG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 VDIVVHNAGITRDKT--LAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGiAGNLGQSN--YAVSK 361
Cdd:PRK06523  78 VDILVHVLGGSSAPAggFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQR-RLPLPESTtaYAAAK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  362 AGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTI-------REAGRRMNSMSQGGLP-------QDVAETVAW 427
Cdd:PRK06523 157 AALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAERLaeaagtdYEGAKQIIMDSLGGIPlgrpaepEEVAELIAF 236

                        250
                 ....*....|....*...
gi 15599980  428 FAQPSSGAVSGQVLRVCG 445
Cdd:PRK06523 237 LASDRAASITGTEYVIDG 254
PRK06398 PRK06398
aldose dehydrogenase; Validated
 286-445 2.90e-17

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 81.42  E-value: 2.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:PRK06398  73 IDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVL 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  366 GLAQA----WAPAlgkrgITINAVAPGFIETQMT------------AAIPLTIREAGrRMNSMSQGGLPQDVAETVAWFA 429
Cdd:PRK06398 153 GLTRSiavdYAPT-----IRCVAVCPGSIRTPLLewaaelevgkdpEHVERKIREWG-EMHPMKRVGKPEEVAYVVAFLA 226

                        170
                 ....*....|....*.
gi 15599980  430 QPSSGAVSGQVLRVCG 445
Cdd:PRK06398 227 SDLASFITGECVTVDG 242
PRK07831 PRK07831
SDR family oxidoreductase;
212-446 2.96e-17

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 81.23  E-value: 2.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGI-GAAIAETLARDGAEVVLLDVPPAR--EALEGLAARLGGR---AVALDICAADAGQQLVEALPE- 284
Cdd:PRK07831  15 LAGKVVLVTAAAGTGiGSATARRALEEGARVVISDIHERRlgETADELAAELGLGrveAVVCDVTSEAQVDALIDAAVEr 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 --GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVL-LASISGIAGNLGQSNYAVSK 361
Cdd:PRK07831  95 lgRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIVnNASVLGWRAQHGQAHYAAAK 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  362 AGLIGLAQAWAPALGKRGITINAVAPG-----FIETQMTAAI--PLTIREA-GRrmnsmsqGGLPQDVAETVAWFAQPSS 433
Cdd:PRK07831 175 AGVMALTRCSALEAAEYGVRINAVAPSiamhpFLAKVTSAELldELAAREAfGR-------AAEPWEVANVIAFLASDYS 247

                        250
                 ....*....|...
gi 15599980  434 GAVSGQVLRVCGQ 446
Cdd:PRK07831 248 SYLTGEVVSVSSQ 260
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 212-441 3.35e-17

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: 80.70  E-value: 3.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDvpPAREALEGLA---ARLGGRA---VALDI--CAADAGQQL---VE 280
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLG--RNEEKLRQVAdhiNEEGGRQpqwFILDLltCTSENCQQLaqrIA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 281 ALPEGVDIVVHNAGITRDKT-LAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAV 359
Cdd:cd05340  80 VNYPRLDGVLHNAGLLGDVCpLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 360 SKAGLIGLAQAWAPALGKRGITINAVAPGFIETQM-TAAIPltiREAGRRMNSmsqgglPQDVAETVAWFAQPSSGAVSG 438
Cdd:cd05340 160 SKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMrASAFP---TEDPQKLKT------PADIMPLYLWLMGDDSRRKTG 230


                ...
gi 15599980 439 QVL 441
Cdd:cd05340 231 MTF 233
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 217-399 4.09e-17

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: 80.36  E-value: 4.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLDV-PPAREALEGLAARLGGRAVAL--DICAADAGQQLVEALPE---GVDIVV 290
Cdd:cd05339   2 VLITGGGSGIGRLLALEFAKRGAKVVILDInEKGAEETANNVRKAGGKVHYYkcDVSKREEVYEAAKKIKKevgDVTILI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 291 HNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQA 370
Cdd:cd05339  82 NNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHES 161

                       170       180       190
                ....*....|....*....|....*....|..
gi 15599980 371 WA---PALGKRGITINAVAPGFIETQMTAAIP 399
Cdd:cd05339 162 LRlelKAYGKPGIKTTLVCPYFINTGMFQGVK 193
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 213-445 5.54e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 80.14  E-value: 5.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  213 AGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARLGGRAVALDIcAADAGQQLVEALPEGVDIVVHN 292
Cdd:PRK07060   8 SGKSVLVTGASSGIGRACAVALAQRGARVVAAAR--NAAALDRLAGETGCEPLRLDV-GDDAAIRAALAAAGAFDGLVNC 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  293 AGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQ----ALLDGGKlhdNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLA 368
Cdd:PRK07060  85 AGIASLESALDMTAEGFDRVMAVNARGAALVARhvarAMIAAGR---GGSIVNVSSQAALVGLPDHLAYCASKAALDAIT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  369 QAWAPALGKRGITINAVAPGFIETQMTAAI---PLTiREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PRK07060 162 RVLCVELGPHGIRVNSVNPTVTLTPMAAEAwsdPQK-SGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLPVDG 240
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 210-438 5.94e-17

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 80.44  E-value: 5.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  210 KPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARLGGRA--VALDICAADAGQQLVEALPE--- 284
Cdd:PRK08265   2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDI--DADNGAAVAASLGERArfIATDITDDAAIERAVATVVArfg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDfWNSVINVNLNAPQVLTQA----LLDGGklhdnGRVVLLASISGIAGNLGQSNYAVS 360
Cdd:PRK08265  80 RVDILVNLACTYLDDGLASSRAD-WLAALDVNLVSAAMLAQAahphLARGG-----GAIVNFTSISAKFAQTGRWLYPAS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREA----GRRMNSMSQGGLPQDVAETVAWFAQPSSGAV 436
Cdd:PRK08265 154 KAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSGGDRAKadrvAAPFHLLGRVGDPEEVAQVVAFLCSDAASFV 233


                 ..
gi 15599980  437 SG 438
Cdd:PRK08265 234 TG 235
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 212-445 7.64e-17

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: 79.81  E-value: 7.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARLGGRAVALDICAADAGQQLVEALPEGV----- 286
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADI--DDDAGQAVAAELGDPDISFVHCDVTVEADVRAAVDTAVarfgr 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 287 -DIVVHNAGI--TRDKTLAKMSSDFWNSVINVNLNAPQVLTQ----ALLDGGKlhdnGRVVLLASISGIAGNLGQSNYAV 359
Cdd:cd05326  80 lDIMFNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKhaarVMIPAKK----GSIVSVASVAGVVGGLGPHAYTA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 360 SKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLT----IREAGRRMNSMSQGGL-PQDVAETVAWFAQPSSG 434
Cdd:cd05326 156 SKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVedeaIEEAVRGAANLKGTALrPEDIAAAVLYLASDDSR 235

                       250
                ....*....|.
gi 15599980 435 AVSGQVLRVCG 445
Cdd:cd05326 236 YVSGQNLVVDG 246
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 232-445 1.73e-16

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: 78.92  E-value: 1.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 232 ETLARDGAEVVLLD--VPPAREALEGLAARLGGR--AVALDICAADAGQQLVEALPEG---VDIVVHNAGITRDKTLAK- 303
Cdd:cd08930  20 KALLSAGARLILADinAPALEQLKEELTNLYKNRviALELDITSKESIKELIESYLEKfgrIDILINNAYPSPKVWGSRf 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 304 --MSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAG----NLGQSN------YAVSKAGLIGLAQAW 371
Cdd:cd08930 100 eeFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIApdfrIYENTQmyspveYSVIKAGIIHLTKYL 179

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599980 372 APALGKRGITINAVAPG-FIETQmtaaiPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:cd08930 180 AKYYADTGIRVNAISPGgILNNQ-----PSEFLEKYTKKCPLKRMLNPEDLRGAIIFLLSDASSYVTGQNLVIDG 249
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 212-443 1.73e-16

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 79.23  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDV--PPAREALEGLAAR-LGGRAVALDICAADAGQQLVEA---LPEG 285
Cdd:PRK05876   4 FPGRGAVITGGASGIGLATGTEFARRGARVVLGDVdkPGLRQAVNHLRAEgFDVHGVMCDVRHREEVTHLADEafrLLGH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 VDIVVHNAGITRDKTLAKMSSDFWNSVINVNL----NAPQVLTQALLDGGKlhdNGRVVLLASISGIAGNLGQSNYAVSK 361
Cdd:PRK05876  84 VDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLwgsiHTVEAFLPRLLEQGT---GGHVVFTASFAGLVPNAGLGAYGVAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  362 AGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPlTIREAGRRMNSM--SQGGLP-QDVAETVAWFAQPSSGAVSG 438
Cdd:PRK05876 161 YGVVGLAETLAREVTADGIGVSVLCPMVVETNLVANSE-RIRGAACAQSSTtgSPGPLPlQDDNLGVDDIAQLTADAILA 239


                 ....*
gi 15599980  439 QVLRV 443
Cdd:PRK05876 240 NRLYV 244
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
212-394 2.21e-16

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 78.53  E-value: 2.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAARLGGRAVALDICAADAGQQLVEALPE---GVDI 288
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVErfgGIDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 VVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQA----LLDGGKlhdNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK07067  84 LFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAvarhMVEQGR---GGKIINMASQAGRRGEALVSHYCATKAAV 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIETQM 394
Cdd:PRK07067 161 ISYTQSAALALIRHGINVNAIAPGVVDTPM 190
PRK05717 PRK05717
SDR family oxidoreductase;
214-445 4.28e-16

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 77.62  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREAleGLAARLGGRAVALDICAADAGQ---QLVEALPE--GVDI 288
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGS--KVAKALGENAWFIAMDVADEAQvaaGVAEVLGQfgRLDA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 VVHNAGIT--RDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHdNGRVVLLASISGIAGNLGQSNYAVSKAGLIG 366
Cdd:PRK05717  88 LVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAH-NGAIVNLASTRARQSEPDTEAYAASKGGLLA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  367 LAQAWAPALGKRgITINAVAPGFIETQMTA---AIPLTirEAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRV 443
Cdd:PRK05717 167 LTHALAISLGPE-IRVNAVSPGWIDARDPSqrrAEPLS--EADHAQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFVV 243


                 ..
gi 15599980  444 CG 445
Cdd:PRK05717 244 DG 245
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 209-450 7.62e-16

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: 77.33  E-value: 7.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 209 SKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVP----PAREALEgLAARLGGRAVAL-------DICaADAGQQ 277
Cdd:cd05355  21 SGKLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPeeedDAEETKK-LIEEEGRKCLLIpgdlgdeSFC-RDLVKE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 278 LVEALpEGVDIVVHNAGITRD-KTLAKMSSDFWNSVINVNLNAPQVLTQALLDggKLHDNGRVVLLASISGIAGNLGQSN 356
Cdd:cd05355  99 VVKEF-GKLDILVNNAAYQHPqESIEDITTEQLEKTFRTNIFSMFYLTKAALP--HLKKGSSIINTTSVTAYKGSPHLLD 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 357 YAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMtaaIPLT-----IREAGRRmNSMSQGGLPQDVAETVAWFAQP 431
Cdd:cd05355 176 YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPL---IPSSfpeekVSEFGSQ-VPMGRAGQPAEVAPAYVFLASQ 251

                       250
                ....*....|....*....
gi 15599980 432 SSGAVSGQVLRVCGQSLLG 450
Cdd:cd05355 252 DSSYVTGQVLHVNGGEIIN 270
PRK06128 PRK06128
SDR family oxidoreductase;
212-449 9.34e-16

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 77.59  E-value: 9.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPP----AREALEGLAARlGGRAVAL--DICAADAGQQLVEALPE- 284
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNYLPEeeqdAAEVVQLIQAE-GRKAVALpgDLKDEAFCRQLVERAVKe 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 --GVDIVVHNAGI-TRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDggKLHDNGRVVLLASISGIAGNLGQSNYAVSK 361
Cdd:PRK06128 132 lgGLDILVNIAGKqTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIP--HLPPGASIINTGSIQSYQPSPTLLDYASTK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  362 AGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAA---IPLTIREAGRRmNSMSQGGLPQDVAETVAWFAQPSSGAVSG 438
Cdd:PRK06128 210 AAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSggqPPEKIPDFGSE-TPMKRPGQPVEMAPLYVLLASQESSYVTG 288

                        250
                 ....*....|.
gi 15599980  439 QVLRVCGQSLL 449
Cdd:PRK06128 289 EVFGVTGGLLL 299
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 218-426 9.40e-16

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: 76.56  E-value: 9.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 218 LVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAARLGG----RAVALDICAADAGQQLVEALPEGV---DIVV 290
Cdd:cd05367   3 ILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEELRPglrvTTVKADLSDAAGVEQLLEAIRKLDgerDLLI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 291 HNAGITRD-KTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHD-NGRVVLLASISGIAGNLGQSNYAVSKAGLIGLA 368
Cdd:cd05367  83 NNAGSLGPvSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSSGAAVNPFKGWGLYCSSKAARDMFF 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599980 369 QAWAPALgkRGITINAVAPGFIETQMTAAIPLTIREAG--RRMNSMSQGGL---PQDVAETVA 426
Cdd:cd05367 163 RVLAAEE--PDVRVLSYAPGVVDTDMQREIRETSADPEtrSRFRSLKEKGElldPEQSAEKLA 223
PRK06181 PRK06181
SDR family oxidoreductase;
214-393 1.47e-15

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 76.17  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAReaLEGLAARL---GGRA--VALDICAADAGQQLVEALPE---G 285
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETR--LASLAQELadhGGEAlvVPTDVSDAEACERLIEAAVArfgG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 VDIVVHNAGITRDKTLAKMSSDFW-NSVINVNLNAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK06181  79 IDILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAALPHLK-ASRGQIVVVSSLAGLTGVPTRSGYAASKHAL 157

                        170       180
                 ....*....|....*....|....*....
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIETQ 393
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVATD 186
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 232-451 1.52e-15

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: 75.97  E-value: 1.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 232 ETLARDGAEVVLLDVPPAREALEGLAARLggraVALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSSDF 308
Cdd:cd05331  16 RHLLQAGATVIALDLPFVLLLEYGDPLRL----TPLDVADAAAVREVCSRLLAehgPIDALVNCAGVLRPGATDPLSTED 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 309 WNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPG 388
Cdd:cd05331  92 WEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELAPYGVRCNVVSPG 171

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599980 389 FIETQM--------------TAAIPLTIReAGRRMNSMSQgglPQDVAETVAWFAQPSSGAVSGQVLRVCGQSLLGA 451
Cdd:cd05331 172 STDTAMqrtlwhdedgaaqvIAGVPEQFR-LGIPLGKIAQ---PADIANAVLFLASDQAGHITMHDLVVDGGATLGA 244
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 212-417 2.69e-15

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: 75.12  E-value: 2.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVL------LDVPPAREALEGLAAR-------LGGRAVAL--DICAADAGQ 276
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVaaktasEGDNGSAKSLPGTIEEtaeeieaAGGQALPIvvDVRDEDQVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 277 QLVEALPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLG 353
Cdd:cd05338  81 ALVEATVDqfgRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARG 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599980 354 QSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPG-FIETQ-MTAAIPLTIREAGRRMNSMSQGGL 417
Cdd:cd05338 161 DVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStAIETPaATELSGGSDPARARSPEILSDAVL 226
PRK06484 PRK06484
short chain dehydrogenase; Validated
 171-445 2.93e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 77.97  E-value: 2.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  171 GAEDQLEGALRFFLSPKSAYVSGQVIRL---------AANSAQVHDWSKPL-AGQRALVTGAARGIGAAIAETLARDGAE 240
Cdd:PRK06484 216 GRPEEIAEAVFFLASDQASYITGSTLVVdggwtvyggSGPASTAQAPSPLAeSPRVVAITGGARGIGRAVADRFAAAGDR 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  241 VVLLDVPpaREALEGLAARLGGRAVAldICAADAGQQLVEALPEG-------VDIVVHNAGITRD-KTLAKMSSDFWNSV 312
Cdd:PRK06484 296 LLIIDRD--AEGAKKLAEALGDEHLS--VQADITDEAAVESAFAQiqarwgrLDVLVNNAGIAEVfKPSLEQSAEDFTRV 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  313 INVNLNAPQVLTQALLDggKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIET 392
Cdd:PRK06484 372 YDVNLSGAFACARAAAR--LMSQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980  393 QMTAAIpltIREAGRRMNSMSQG------GLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PRK06484 450 PAVLAL---KASGRADFDSIRRRiplgrlGDPEEVAEAIAFLASPAASYVNGATLTVDG 505
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 212-391 2.99e-15

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 75.43  E-value: 2.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLaarlggRAVALDICAADAGQQLVEALPE---GVDI 288
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQHENY------QFVPTDVSSAEEVNHTVAEIIEkfgRIDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 VVHNAGITRDKTLA---------KMSSDFWNSVINVNLNAPQVLTQA----LLDGGKlhdnGRVVLLASISGIAGNLGQS 355
Cdd:PRK06171  81 LVNNAGINIPRLLVdekdpagkyELNEAAFDKMFNINQKGVFLMSQAvarqMVKQHD----GVIVNMSSEAGLEGSEGQS 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15599980  356 NYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIE 391
Cdd:PRK06171 157 CYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILE 192
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 210-441 4.16e-15

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 74.73  E-value: 4.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  210 KPLAGQRALVTGAARGIG--AAIAETLARDGAEVVLLDVPPAREALEG---------LAARLGGRAVA-----LDICAAD 273
Cdd:PRK12748   1 LPLMKKIALVTGASRLNGigAAVCRRLAAKGIDIFFTYWSPYDKTMPWgmhdkepvlLKEEIESYGVRcehmeIDLSQPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  274 AGQQLVEALPEGV---DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAG 350
Cdd:PRK12748  81 APNRVFYAVSERLgdpSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  351 NLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQ-MTAaiplTIREAGRRMNSMSQGGLPQDVAETVAWFA 429
Cdd:PRK12748 161 MPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGwITE----ELKHHLVPKFPQGRVGEPVDAARLIAFLV 236

                        250
                 ....*....|..
gi 15599980  430 QPSSGAVSGQVL 441
Cdd:PRK12748 237 SEEAKWITGQVI 248
PRK05867 PRK05867
SDR family oxidoreductase;
212-438 4.32e-15

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 74.69  E-value: 4.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLldvpPAR--EALEGLAARL---GGRAVAL--DICAADAGQQLVEALPE 284
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAI----AARhlDALEKLADEIgtsGGKVVPVccDVSQHQQVTSMLDQVTA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 ---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNA----PQVLTQALLDGGKlhdNGRVVLLASISGIAGNLGQ--S 355
Cdd:PRK05867  83 elgGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGvfltAQAAAKAMVKQGQ---GGVIINTASMSGHIINVPQqvS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  356 NYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMnSMSQGGLPQDVAETVAWFAQPSSGA 435
Cdd:PRK05867 160 HYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQPLWEPKI-PLGRLGRPEELAGLYLYLASEASSY 238


                 ...
gi 15599980  436 VSG 438
Cdd:PRK05867 239 MTG 241
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 217-445 6.61e-15

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 74.28  E-value: 6.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   217 ALVTGAARGIGAAIAETLARDGAEVVLLDVP----------PAREALEGLAARLGGRAVAL-----DICAADAGQQLVEA 281
Cdd:TIGR04504   4 ALVTGAARGIGAATVRRLAADGWRVVAVDLCaddpavgyplATRAELDAVAAACPDQVLPViadvrDPAALAAAVALAVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   282 LPEGVDIVVHNAG-ITRDKTLAKMSSDFWNSVINVNL----NAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSN 356
Cdd:TIGR04504  84 RWGRLDAAVAAAGvIAGGRPLWETTDAELDLLLDVNLrgvwNLARAAVPAMLARPD-PRGGRFVAVASAAATRGLPHLAA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   357 YAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQM---TAAIpLTIREAGRRMNSMSQGGL--PQDVAETVAWFAQP 431
Cdd:TIGR04504 163 YCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMlaaTARL-YGLTDVEEFAGHQLLGRLlePEEVAAAVAWLCSP 241

                         250
                  ....*....|....
gi 15599980   432 SSGAVSGQVLRVCG 445
Cdd:TIGR04504 242 ASSAVTGSVVHADG 255
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 212-451 8.09e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 74.27  E-value: 8.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAE-VVLLDVPPAR-EALEGLAARLGGRA--VALDICAADAGQQLVEALPE--- 284
Cdd:PRK06198   4 LDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKgEAQAAELEALGAKAvfVQADLSDVEDCRRVVAAADEafg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALL-DGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:PRK06198  84 RLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIkLMRRRKAEGTIVNIGSMSAHGGQPFLAAYCASKGA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  364 LIGLAQAWAPALGKRGITINAVAPGFIETQMTAAI--------PLTIREAGRRMnSMSQGGLPQDVAETVAWFAQPSSGA 435
Cdd:PRK06198 164 LATLTRNAAYALLRNRIRVNGLNIGWMATEGEDRIqrefhgapDDWLEKAAATQ-PFGRLLDPDEVARAVAFLLSDESGL 242

                        250
                 ....*....|....*.
gi 15599980  436 VSGQVLRVcGQSLLGA 451
Cdd:PRK06198 243 MTGSVIDF-DQSVWGA 257
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 234-396 8.97e-15

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: 73.52  E-value: 8.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 234 LARDGAEVVL--LDVPPAREALEGLAARLGG-RAVALDICAADAGQQLVEALP---EGVDIVVHNAGITRDKTLAKMSSD 307
Cdd:cd05350  18 FAKAGYNVALaaRRTDRLDELKAELLNPNPSvEVEILDVTDEERNQLVIAELEaelGGLDLVIINAGVGKGTSLGDLSFK 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 308 FWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAP 387
Cdd:cd05350  98 AFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAESLRYDVKKRGIRVTVINP 177


                ....*....
gi 15599980 388 GFIETQMTA 396
Cdd:cd05350 178 GFIDTPLTA 186
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 210-445 1.35e-14

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 73.61  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  210 KPLAGQRALVTGAARGIGAAIAETLARDGAEVV---LLDVPPAREALEGLaARLGGRAVAL--DICAADAGQQLVE-ALP 283
Cdd:PRK08936   3 SDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVinyRSDEEEANDVAEEI-KKAGGEAIAVkgDVTVESDVVNLIQtAVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  284 E--GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHD-NGRVVLLASISGIAGNLGQSNYAVS 360
Cdd:PRK08936  82 EfgTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDiKGNIINMSSVHEQIPWPLFVHYAAS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTA---AIPlTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVS 437
Cdd:PRK08936 162 KGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAekfADP-KQRADVESMIPMGYIGKPEEIAAVAAWLASSEASYVT 240


                 ....*...
gi 15599980  438 GQVLRVCG 445
Cdd:PRK08936 241 GITLFADG 248
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 212-445 1.41e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 73.25  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPP--AREALEGLAAR-LGGRAVALDICAADAGQQLVEALPE---G 285
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAerAELAVAKLRQEgIKAHAAPFNVTHKQEVEAAIEHIEKdigP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:PRK08085  87 IDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGAVK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  366 GLAQAWAPALGKRGITINAVAPGFIETQMTAAIP--------LTIREAGRRMnsmsqgGLPQDVAETVAWFAQPSSGAVS 437
Cdd:PRK08085 167 MLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVedeaftawLCKRTPAARW------GDPQELIGAAVFLSSKASDFVN 240


                 ....*...
gi 15599980  438 GQVLRVCG 445
Cdd:PRK08085 241 GHLLFVDG 248
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 212-450 2.51e-14

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 72.45  E-value: 2.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLA--ARLGGRAVAL--DICAADAGQQLVEALPE--- 284
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKmvKENGGEGIGVlaDVSTREGCETLAKATIDryg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGI--------TRDKTLAKMSSDFWNSVINVNlnapQVLTQALLDGGKlhdngrVVLLASISGIAGNLGQSN 356
Cdd:PRK06077  84 VADILVNNAGLglfspflnVDDKLIDKHISTDFKSVIYCS----QELAKEMREGGA------IVNIASVAGIRPAYGLSI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  357 YAVSKAGLIGLAQAWAPALGKRgITINAVAPGFIETQMTAAIP----LTIREAGRRMNSMSQGGLPQDVAETVAWFAqpS 432
Cdd:PRK06077 154 YGAMKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKLGESLFkvlgMSEKEFAEKFTLMGKILDPEEVAEFVAAIL--K 230

                        250
                 ....*....|....*....
gi 15599980  433 SGAVSGQVLRV-CGQSLLG 450
Cdd:PRK06077 231 IESITGQVFVLdSGESLKG 249
PRK08628 PRK08628
SDR family oxidoreductase;
232-445 3.56e-14

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 72.30  E-value: 3.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  232 ETLARDGAEVVLLDVPPAREALEGLAARLGGRA--VALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSS 306
Cdd:PRK08628  25 LRLAEEGAIPVIFGRSAPDDEFAEELRALQPRAefVQVDLTDDAQCRDAVEQTVAkfgRIDGLVNNAGVNDGVGLEAGRE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  307 DFWNSvINVNLNAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVA 386
Cdd:PRK08628 105 AFVAS-LERNLIHYYVMAHYCLPHLK-ASRGAIVNISSKTALTGQGGTSGYAAAKGAQLALTREWAVALAKDGVRVNAVI 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599980  387 PG---------FIET---------QMTAAIPLtireaGRRMNSmsqgglPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PRK08628 183 PAevmtplyenWIATfddpeaklaAITAKIPL-----GHRMTT------AEEIADTAVFLLSERSSHTTGQWLFVDG 248
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 212-442 4.99e-14

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: 71.42  E-value: 4.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLldVPPAREALEGLAARL---GGRA--VALDIC----AADAGQQLVEAL 282
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAI--AARRVDRLEALADELeaeGGKAlvLELDVTdeqqVDAAVERTVEAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 283 pEGVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:cd08934  79 -GRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 363 GLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAG--RRMNSMSQGGlPQDVAETVAW-FAQPSSGAVSGQ 439
Cdd:cd08934 158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAyeERISTIRKLQ-AEDIAAAVRYaVTAPHHVTVNEI 236


                ...
gi 15599980 440 VLR 442
Cdd:cd08934 237 LIR 239
PRK08219 PRK08219
SDR family oxidoreductase;
234-426 5.00e-14

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 71.12  E-value: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  234 LARDGAE---VVLLDVPParEALEGLAARL-GGRAVALDICAADAGQQLVEALPEgVDIVVHNAGITRDKTLAKMSSDFW 309
Cdd:PRK08219  19 IARELAPthtLLLGGRPA--ERLDELAAELpGATPFPVDLTDPEAIAAAVEQLGR-LDVLVHNAGVADLGPVAESTVDEW 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  310 NSVINVNLNAPQVLTQALLdgGKLHDN-GRVVLLASISGIAGNLGQSNYAVSKAGLiglaQAWAPAL--GKRG-ITINAV 385
Cdd:PRK08219  96 RATLEVNVVAPAELTRLLL--PALRAAhGHVVFINSGAGLRANPGWGSYAASKFAL----RALADALreEEPGnVRVTSV 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15599980  386 APGFIETQMTAAIpltIREAGRRMNSmSQGGLPQDVAETVA 426
Cdd:PRK08219 170 HPGRTDTDMQRGL---VAQEGGEYDP-ERYLRPETVAKAVR 206
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 212-394 5.44e-14

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: 71.50  E-value: 5.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPParEALEGLAARLG--GRAVALDICAADAGQQLVEALPE---GV 286
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINL--EAARATAAEIGpaACAISLDVTDQASIDRCVAALVDrwgSI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 287 DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAP----QVLTQALLDGGKlhdNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:cd05363  79 DILVNNAALFDLAPIVDITRESYDRLFAINVSGTlfmmQAVARAMIAQGR---GGKIINMASQAGRRGEALVGVYCATKA 155

                       170       180       190
                ....*....|....*....|....*....|..
gi 15599980 363 GLIGLAQAWAPALGKRGITINAVAPGFIETQM 394
Cdd:cd05363 156 AVISLTQSAGLNLIRHGINVNAIAPGVVDGEH 187
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 218-399 6.92e-14

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 71.06  E-value: 6.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  218 LVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLA---ARLGGRAVA---LDICAADAG--QQLVEALPEGV- 286
Cdd:PRK08945  16 LVTGAGDGIGREAALTYARHGATVILL----GRteEKLEAVYdeiEAAGGPQPAiipLDLLTATPQnyQQLADTIEEQFg 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 --DIVVHNAGITRDKT-LAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:PRK08945  92 rlDGVLHNAGLLGELGpMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYAVSKFA 171

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15599980  364 LIGLAQAWAPALGKRGITINAVAPGFIETQMTA-AIP 399
Cdd:PRK08945 172 TEGMMQVLADEYQGTNLRVNCINPGGTRTAMRAsAFP 208
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 234-383 8.74e-14

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: 69.43  E-value: 8.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980    234 LARDGAE-VVLL-----DVPPAREALEGLAARLGG-RAVALDICAADAGQQLVEALPEG---VDIVVHNAGITRDKTLAK 303
Cdd:smart00822  20 LAERGARrLVLLsrsgpDAPGAAALLAELEAAGARvTVVACDVADRDALAAVLAAIPAVegpLTGVIHAAGVLDDGVLAS 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980    304 MSSDFWNSVINVNLNAPQVLTQALLDggklHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWApALGKRGITIN 383
Cdd:smart00822 100 LTPERFAAVLAPKAAGAWNLHELTAD----LPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRR-ARGLPALSIA 174
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 251-396 1.13e-13

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: 70.34  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 251 EALEGLAARL--GGRAVALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQ 325
Cdd:cd05374  35 DKLESLGELLndNLEVLELDVTDEESIKAAVKEVIErfgRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTR 114

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599980 326 ALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTA 396
Cdd:cd05374 115 AFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFAD 185
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 212-425 1.16e-13

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: 70.69  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAARLGGRA------VALDICAADAGQQLVEALP 283
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLS----ARreERLEEVKSECLELGapsphvVPLDMSDLEDAEQVVEEAL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 284 E---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVS 360
Cdd:cd05332  77 KlfgGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAAS 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980 361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAiplTIREAGRRMNSM----SQGGLPQDVAETV 425
Cdd:cd05332 157 KHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMN---ALSGDGSMSAKMddttANGMSPEECALEI 222
PRK06949 PRK06949
SDR family oxidoreductase;
212-441 2.27e-13

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 69.79  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLldvpPAR--EALEGLAARL---GGRA--VALDICAADAGQQLV---EA 281
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVL----ASRrvERLKELRAEIeaeGGAAhvVSLDVTDYQSIKAAVahaET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  282 LPEGVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLN---------APQVLTQALLDGGKLhDNGRVVLLASISG--IAG 350
Cdd:PRK06949  83 EAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRgaffvaqevAKRMIARAKGAGNTK-PGGRIINIASVAGlrVLP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  351 NLGQsnYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTirEAGRRMNSM---SQGGLPQDVAETVAW 427
Cdd:PRK06949 162 QIGL--YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWET--EQGQKLVSMlprKRVGKPEDLDGLLLL 237

                        250
                 ....*....|....
gi 15599980  428 FAQPSSGAVSGQVL 441
Cdd:PRK06949 238 LAADESQFINGAII 251
PRK07069 PRK07069
short chain dehydrogenase; Validated
 216-445 3.90e-13

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 68.97  E-value: 3.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  216 RALVTGAARGIGAAIAETLARDGAEVVLLDVPPArEALEGLAARLGGR-------AVALDICAADAGQQLVEALPE---G 285
Cdd:PRK07069   1 RAFITGAAGGLGRAIARRMAEQGAKVFLTDINDA-AGLDAFAAEINAAhgegvafAAVQDVTDEAQWQALLAQAADamgG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:PRK07069  80 LSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  366 GLAQAWAPALGKRGITI--NAVAPGFIETQMTAAIPLTI--REAGRRMNS---MSQGGLPQDVAETVAWFAQPSSGAVSG 438
Cdd:PRK07069 160 SLTKSIALDCARRGLDVrcNSIHPTFIRTGIVDPIFQRLgeEEATRKLARgvpLGRLGEPDDVAHAVLYLASDESRFVTG 239


                 ....*..
gi 15599980  439 QVLRVCG 445
Cdd:PRK07069 240 AELVIDG 246
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 234-383 4.00e-13

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: 67.59  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   234 LARDGAE-VVLL-----DVPPAREALEGLAARLGG-RAVALDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAK 303
Cdd:pfam08659  20 LAERGARhLVLLsrsaaPRPDAQALIAELEARGVEvVVVACDVSDPDAVAALLAEIKAegpPIRGVIHAAGVLRDALLEN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   304 MSSDFWNSVINVNLNAPQVLTQALLDGgklhDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWApALGKRGITIN 383
Cdd:pfam08659 100 MTDEDWRRVLAPKVTGTWNLHEATPDE----PLDFFVLFSSIAGLLGSPGQANYAAANAFLDALAEYRR-SQGLPATSIN 174
PRK09730 PRK09730
SDR family oxidoreductase;
217-445 4.08e-13

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 68.72  E-value: 4.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVV---LLDVPPAREALEgLAARLGGRAVALDICAADAGQ-----QLVEALPEGVDI 288
Cdd:PRK09730   4 ALVTGGSRGIGRATALLLAQEGYTVAvnyQQNLHAAQEVVN-LITQAGGKAFVLQADISDENQvvamfTAIDQHDEPLAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 VVHNAGIT-RDKTLAKMSSDFWNSVINVNLNA------PQVLTQALLDGGKlhdNGRVVLLASISGIAGNLGQS-NYAVS 360
Cdd:PRK09730  83 LVNNAGILfTQCTVENLTAERINRVLSTNVTGyflccrEAVKRMALKHGGS---GGAIVNVSSAASRLGAPGEYvDYAAS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  361 KAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAaiplTIREAGR--RMNS---MSQGGLPQDVAETVAWFAQPSSGA 435
Cdd:PRK09730 160 KGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHA----SGGEPGRvdRVKSnipMQRGGQPEEVAQAIVWLLSDKASY 235

                        250
                 ....*....|
gi 15599980  436 VSGQVLRVCG 445
Cdd:PRK09730 236 VTGSFIDLAG 245
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
211-450 4.28e-13

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 68.98  E-value: 4.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVLL---DVPPAREALEGLAArLGGRAVALDicaADAGQQ-----LVEAL 282
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyarSRKAAEETAEEIEA-LGRKALAVK---ANVGDVekikeMFAQI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  283 PE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQallDGGKL---HDNGRVVllaSISGIAGNLGQSN 356
Cdd:PRK08063  77 DEefgRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQ---EAAKLmekVGGGKII---SLSSLGSIRYLEN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  357 YA---VSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIP--LTIREAGRRMNSMSQGGLPQDVAETVAWFAQP 431
Cdd:PRK08063 151 YTtvgVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPnrEELLEDARAKTPAGRMVEPEDVANAVLFLCSP 230

                        250       260
                 ....*....|....*....|
gi 15599980  432 SSGAVSGQVLRV-CGQSLLG 450
Cdd:PRK08063 231 EADMIRGQTIIVdGGRSLLV 250
PRK07832 PRK07832
SDR family oxidoreductase;
216-395 5.87e-13

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 68.92  E-value: 5.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  216 RALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAARLGGRAV----ALDICAADA----GQQLVEALPeGVD 287
Cdd:PRK07832   2 RCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVpehrALDISDYDAvaafAADIHAAHG-SMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  288 IVVHNAGITRDKTLAKMSSDFWNSVINVNLNAP----QVLTQALLDGGKlhdNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:PRK07832  81 VVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPihviETFVPPMVAAGR---GGHLVNVSSAAGLVALPWHAAYSASKFG 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15599980  364 LIGLAQAWAPALGKRGITINAVAPGFIETQMT 395
Cdd:PRK07832 158 LRGLSEVLRFDLARHGIGVSVVVPGAVKTPLV 189
PRK07326 PRK07326
SDR family oxidoreductase;
212-392 8.93e-13

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 67.73  E-value: 8.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLL--DVPPAREALEGLAARLGGRAVALDICAADAGQQLVEALPE---GV 286
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITarDQKELEEAAAELNNKGNVLGLAADVRDEADVQRAVDAIVAafgGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIG 366
Cdd:PRK07326  84 DVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALK-RGGGYIINISSLAGTNFFAGGAAYNASKFGLVG 162

                        170       180
                 ....*....|....*....|....*.
gi 15599980  367 LAQAWAPALGKRGITINAVAPGFIET 392
Cdd:PRK07326 163 FSEAAMLDLRQYGIKVSTIMPGSVAT 188
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 214-447 9.22e-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: 68.02  E-value: 9.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 214 GQRALVTGAARGIGAAIAETLARDGAEVVLL--DVPPAREALEGLAARLGGRAV---ALDICAAD----AGQQLVEALPE 284
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIAcrNEEKGEEAAAEIKKETGNAKVeviQLDLSSLAsvrqFAEEFLARFPR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 285 gVDIVVHNAGITRDKTlaKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLG-----QSN--- 356
Cdd:cd05327  81 -LDILINNAGIMAPPR--RLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPIDfndldLENnke 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 357 ------YAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIET--QMTAAIPLTIREAGRRM--NSMSQGglpqdvAETVA 426
Cdd:cd05327 158 yspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTelLRRNGSFFLLYKLLRPFlkKSPEQG------AQTAL 231

                       250       260
                ....*....|....*....|..
gi 15599980 427 WFA-QPSSGAVSGQVLRVCGQS 447
Cdd:cd05327 232 YAAtSPELEGVSGKYFSDCKIK 253
PRK05650 PRK05650
SDR family oxidoreductase;
215-392 1.09e-12

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 68.14  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  215 QRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAR--EALEGLAArLGGRA--VALDICAADAGQQLVEALPE---GVD 287
Cdd:PRK05650   1 NRVMITGAASGLGRAIALRWAREGWRLALADVNEEGgeETLKLLRE-AGGDGfyQRCDVRDYSQLTALAQACEEkwgGID 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  288 IVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGL 367
Cdd:PRK05650  80 VIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVAL 159

                        170       180
                 ....*....|....*....|....*
gi 15599980  368 AQAWAPALGKRGITINAVAPGFIET 392
Cdd:PRK05650 160 SETLLVELADDEIGVHVVCPSFFQT 184
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 209-445 1.38e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 68.14  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  209 SKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAA--RLGGRAVAL--DICAA----DAGQQLVE 280
Cdd:PRK06701  41 SGKLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRveKEGVKCLLIpgDVSDEafckDAVEETVR 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  281 ALpEGVDIVVHNAGITRDKT-LAKMSSDFWNSVINVNLNAPQVLTQALLDggKLHDNGRVVLLASISGIAGNLGQSNYAV 359
Cdd:PRK06701 121 EL-GRLDILVNNAAFQYPQQsLEDITAEQLDKTFKTNIYSYFHMTKAALP--HLKQGSAIINTGSITGYEGNETLIDYSA 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  360 SKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMtaaIPLT-----IREAGRRmNSMSQGGLPQDVAETVAWFAQPSSG 434
Cdd:PRK06701 198 TKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPL---IPSDfdeekVSQFGSN-TPMQRPGQPEELAPAYVFLASPDSS 273

                        250
                 ....*....|.
gi 15599980  435 AVSGQVLRVCG 445
Cdd:PRK06701 274 YITGQMLHVNG 284
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 212-449 1.47e-12

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: 67.44  E-value: 1.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLL--DVPPARE-ALEGLAARLGGR---AVALDICAADAGQQLVEALPEG 285
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTgrDAERLEEtRQSCLQAGVSEKkilLVVADLTEEEGQDRIISTTLAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 ---VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDgGKLHDNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:cd05364  81 fgrLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVP-HLIKTKGEIVNVSSVAGGRSFPGVLYYCISKA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 363 GLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPL------TIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAV 436
Cdd:cd05364 160 ALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMpeeqyiKFLSRAKETHPLGRPGTVDEVAEAIAFLASDASSFI 239

                       250
                ....*....|...
gi 15599980 437 SGQVLRVCGQSLL 449
Cdd:cd05364 240 TGQLLPVDGGRHL 252
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 214-445 1.95e-12

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 66.98  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDV--PPAREALEGLAARLG-GRAVALDICAADagQQLVEALPEGV---- 286
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADInsEKAANVAQEINAEYGeGMAYGFGADATS--EQSVLALSRGVdeif 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 ---DIVVHNAGITRDKTLAKMSSDFWNSVINVNLN-----APQVLTQALLDGGKlhdnGRVVLLASISGIAGNLGQSNYA 358
Cdd:PRK12384  80 grvDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVgyflcAREFSRLMIRDGIQ----GRIIQINSKSGKVGSKHNSGYS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  359 VSKAGLIGLAQAWAPALGKRGITINAVAPG-FIETQM------TAAIPLTIREAGRRMNSMSQGGLP-----QDVAETVA 426
Cdd:PRK12384 156 AAKFGGVGLTQSLALDLAEYGITVHSLMLGnLLKSPMfqsllpQYAKKLGIKPDEVEQYYIDKVPLKrgcdyQDVLNMLL 235

                        250
                 ....*....|....*....
gi 15599980  427 WFAQPSSGAVSGQVLRVCG 445
Cdd:PRK12384 236 FYASPKASYCTGQSINVTG 254
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 250-441 2.43e-12

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 66.73  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  250 REALEGLAARLGGraVALDICAADAGQQLVEALPEGV---DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQA 326
Cdd:PRK12859  60 QEELLKNGVKVSS--MELDLTQNDAPKELLNKVTEQLgypHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQ 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  327 LLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQ-MTAaiplTIREA 405
Cdd:PRK12859 138 FARGFDKKSGGRIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGwMTE----EIKQG 213

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15599980  406 GRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVL 441
Cdd:PRK12859 214 LLPMFPFGRIGEPKDAARLIKFLASEEAEWITGQII 249
PRK05855 PRK05855
SDR family oxidoreductase;
203-396 3.13e-12

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 68.47  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  203 AQVHDWSKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAR-EALEGLAARLGGRAVA--LDICAADAGQQLV 279
Cdd:PRK05855 304 ARVGRPRGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAaERTAELIRAAGAVAHAyrVDVSDADAMEAFA 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  280 EALPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNL----NAPQVLTQALLDGGKlhdNGRVVLLASISGIAGNL 352
Cdd:PRK05855 384 EWVRAehgVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLwgviHGCRLFGRQMVERGT---GGHIVNVASAAAYAPSR 460

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15599980  353 GQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTA 396
Cdd:PRK05855 461 SLPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 212-445 3.76e-12

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: 66.33  E-value: 3.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARL---GGRAVAL--DICAADAGQQLVEALPE-- 284
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGR--NQEKGDKVAKEItalGGRAIALaaDVLDRASLERAREEIVAqf 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 285 -GVDIVVHNAG--------------ITRDKTLAKMSSDFWNSVINVNLN----APQVLTQALLDGGKlhdnGRVVLLASI 345
Cdd:cd08935  81 gTVDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNgsflPSQVFGKDMLEQKG----GSIINISSM 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 346 SGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIET-QMTAAIPLTIREAGRRMNS------MSQGGLP 418
Cdd:cd08935 157 NAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTpQNRKLLINPDGSYTDRSNKilgrtpMGRFGKP 236

                       250       260
                ....*....|....*....|....*...
gi 15599980 419 QDVAETVAWFA-QPSSGAVSGQVLRVCG 445
Cdd:cd08935 237 EELLGALLFLAsEKASSFVTGVVIPVDG 264
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 212-445 5.17e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 65.91  E-value: 5.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREalEGLAARLGGRAVALDICAADAGQQLVEALPE---GVDI 288
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAG--KAAADEVGGLFVPTDVTDEDAVNALFDTAAEtygSVDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 VVHNAGIT--RDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGN-LGQSNYAVSKAGLI 365
Cdd:PRK06057  83 AFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSaTSQISYTASKGGVL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  366 GLAQAWAPALGKRGITINAVAPGFIET----QMTAAIPltiREAGRRMNSMSQG--GLPQDVAETVAWFAQPSSGAVSGQ 439
Cdd:PRK06057 163 AMSRELGVQFARQGIRVNALCPGPVNTpllqELFAKDP---ERAARRLVHVPMGrfAEPEEIAAAVAFLASDDASFITAS 239


                 ....*.
gi 15599980  440 VLRVCG 445
Cdd:PRK06057 240 TFLVDG 245
PRK07035 PRK07035
SDR family oxidoreductase;
212-448 5.19e-12

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 65.81  E-value: 5.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLldVPPAREALEGLAARL---GGRAVALDICAADAGQqlVEALPEGV-- 286
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIV--SSRKLDGCQAVADAIvaaGGKAEALACHIGEMEQ--IDALFAHIre 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 -----DIVVHNA------GITRDKTLAKmssdfWNSVINVNLNAPQVLTQAlldGGKL---HDNGRVVLLASISGIAGNL 352
Cdd:PRK07035  82 rhgrlDILVNNAaanpyfGHILDTDLGA-----FQKTVDVNIRGYFFMSVE---AGKLmkeQGGGSIVNVASVNGVSPGD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  353 GQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLT--IREAGRRMNSMSQGGLPQDVAETVAWFAQ 430
Cdd:PRK07035 154 FQGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNdaILKQALAHIPLRRHAEPSEMAGAVLYLAS 233

                        250
                 ....*....|....*...
gi 15599980  431 PSSGAVSGQVLRVCGQSL 448
Cdd:PRK07035 234 DASSYTTGECLNVDGGYL 251
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
 217-445 6.44e-12

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: 65.47  E-value: 6.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVVLLDV--------PPAREA-LEGLAARLGGRAVAL-----DICAADAGQQLVEAL 282
Cdd:NF040491   3 ALVTGAARGIGAATVRRLAARGYAVVAVDAcagdpapyPLGTEAdLDALVASSPGRVETVvadvrDRAALAAAVALALDR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  283 PEGVDIVVHNAG-ITRDKTLAKMSSDFWNSVINVNL----NAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSNY 357
Cdd:NF040491  83 WGRLDAAVAAAAvIAGGRPLWETPPEELDALWDVDVrgvwNLAAAAVPALLAGPD-PRGCRFVAVASAAGHRGLFHLAAY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  358 AVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQM---TAAI-------PLTIREAGRRMNSmsqgglPQDVAETVAW 427
Cdd:NF040491 162 CAAKHAVVGLVRGLAADLAGTGVTACAVSPGSTDTPMlaaTAALyglddvtELAAHQLVRRLLD------PDEVAAVVAF 235

                        250
                 ....*....|....*...
gi 15599980  428 FAQPSSGAVSGQVLRVCG 445
Cdd:NF040491 236 ACSPGGAAVNGSVVHADG 253
PRK07985 PRK07985
SDR family oxidoreductase;
209-450 8.60e-12

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 65.79  E-value: 8.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  209 SKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAARL---GGRAVAL--DICAADAGQQLV---- 279
Cdd:PRK07985  44 SGRLKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDAQDVKKIIeecGRKAVLLpgDLSDEKFARSLVheah 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  280 EALpEGVDIVVHNAGI-TRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDggKLHDNGRVVLLASISGIAGNLGQSNYA 358
Cdd:PRK07985 124 KAL-GGLDIMALVAGKqVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIP--LLPKGASIITTSSIQAYQPSPHLLDYA 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  359 VSKAGLIGLAQAWAPALGKRGITINAVAPGFIET--QMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAV 436
Cdd:PRK07985 201 ATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTalQISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQESSYV 280

                        250
                 ....*....|....
gi 15599980  437 SGQVLRVCGQSLLG 450
Cdd:PRK07985 281 TAEVHGVCGGEHLG 294
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 217-409 9.79e-12

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: 64.62  E-value: 9.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLDV--PPAREALEGLAARLGG-RAVALDI--CAADAGQQLVEALPE-GVDIVV 290
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCrdPSAATELAALGASHSRlHILELDVtdEIAESAEAVAERLGDaGLDVLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 291 HNAGI-TRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISG-IAGN--LGQSNYAVSKAGLIG 366
Cdd:cd05325  81 NNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsIGDNtsGGWYSYRASKAALNM 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15599980 367 LAQAWAPALGKRGITINAVAPGFIETQMTAAI-----PLTIREAGRRM 409
Cdd:cd05325 161 LTKSLAVELKRDGITVVSLHPGWVRTDMGGPFaknkgPITPEESVAGL 208
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 212-398 1.53e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 64.40  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAReaLEGLAARLGG-----RAVALDICAADAGQQLVEALPE-- 284
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAK--LAAAAESLKGqglsaHALAFDVTDHDAVRAAIDAFEAei 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 -GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNL----NAPQVLTQALLDGGKlhdnGRVVLLASISGIAGNLGQSNYAV 359
Cdd:PRK07523  86 gPIDILVNNAGMQFRTPLEDFPADAFERLLRTNIssvfYVGQAVARHMIARGA----GKIINIASVQSALARPGIAPYTA 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15599980  360 SKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAI 398
Cdd:PRK07523 162 TKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAAL 200
PRK07814 PRK07814
SDR family oxidoreductase;
212-445 1.56e-11

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 64.41  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLldVPPAREALEGLAARL---GGRA--VALDICAADAGQQLVEALPEG- 285
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLI--AARTESQLDEVAEQIraaGRRAhvVAADLAHPEATAGLAGQAVEAf 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 --VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLH-DNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:PRK07814  86 grLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHsGGGSVINISSTMGRLAGRGFAAYGTAKA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  363 GLIGLAQAWAPALGKRgITINAVAPGFIetqMTAAIPLT-----IREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVS 437
Cdd:PRK07814 166 ALAHYTRLAALDLCPR-IRVNAIAPGSI---LTSALEVVaandeLRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLT 241


                 ....*...
gi 15599980  438 GQVLRVCG 445
Cdd:PRK07814 242 GKTLEVDG 249
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 212-451 3.05e-11

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 63.36  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAArlggRAVALDICAADAGQQLVEALPE---GVDI 288
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQ--AFLTQEDYPF----ATFVLDVSDAAAVAQVCQRLLAetgPLDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 VVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLA 368
Cdd:PRK08220  80 LVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  369 QAWAPALGKRGITINAVAPGFIETQMT-------AAIPLTIR---EAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSG 438
Cdd:PRK08220 160 KCVGLELAPYGVRCNVVSPGSTDTDMQrtlwvdeDGEQQVIAgfpEQFKLGIPLGKIARPQEIANAVLFLASDLASHITL 239

                        250
                 ....*....|...
gi 15599980  439 QVLRVCGQSLLGA 451
Cdd:PRK08220 240 QDIVVDGGATLGA 252
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 234-394 3.25e-11

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: 63.04  E-value: 3.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 234 LARDGAEVVLldvpPAR--EALEGLAARLGGRAV---------ALDICAADAGQQLVEALPEG---VDIVVHNAGITRDK 299
Cdd:cd08939  21 LVKEGANVII----VARseSKLEEAVEEIEAEANasgqkvsyiSADLSDYEEVEQAFAQAVEKggpPDLVVNCAGISIPG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 300 TLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRG 379
Cdd:cd08939  97 LFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFALRGLAESLRQELKPYN 176

                       170
                ....*....|....*
gi 15599980 380 ITINAVAPGFIETQM 394
Cdd:cd08939 177 IRVSVVYPPDTDTPG 191
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 119-441 4.39e-11

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: 64.33  E-value: 4.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 119 DKCPKVVVLGRPPES-LKDPVTASVQRSLEGFTRSLGKE--IRRGGNVQLLYVGKGAE-DQLEGAL-RFFLSPKSAYVSG 193
Cdd:cd05274  46 STGPPLWLVTRGAEAvSADDVAALAQAALWGLLRVLALEhpELWGGLVDLDAADAADEaAALAALLaGAPGEDELALRGG 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 194 Q--VIRLAANSAQVHDW-SKPLAGQRA-LVTGAARGIGAAIAETLARDGA-EVVLLDVPPAREALEGLAARLGGRAVALD 268
Cdd:cd05274 126 QrlVPRLVRAPAAALELaAAPGGLDGTyLITGGLGGLGLLVARWLAARGArHLVLLSRRGPAPRAAARAALLRAGGARVS 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 269 ICAADAG-----QQLVEALPEG--VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDggklHDNGRVVL 341
Cdd:cd05274 206 VVRCDVTdpaalAALLAELAAGgpLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPD----LPLDFFVL 281

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 342 LASISGIAGNLGQSNYAVSKAGLIGLAQAWApalgKRGITINAVAPGFIETQMTAAIPLTIREAGRRmnsmsqGGLPQDV 421
Cdd:cd05274 282 FSSVAALLGGAGQAAYAAANAFLDALAAQRR----RRGLPATSVQWGAWAGGGMAAAAALRARLARS------GLGPLAP 351

                       330       340
                ....*....|....*....|
gi 15599980 422 AETVAWFAQPSSGAVSGQVL 441
Cdd:cd05274 352 AEALEALEALLASDAPQAVV 371
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 234-445 4.51e-11

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: 62.87  E-value: 4.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 234 LARDGAEVVLLDV--PPAREALEGLAARLGGRAVALDICAADagQQLVEALPEGV-------DIVVHNAGITRDKTLAKM 304
Cdd:cd05322  22 LAEAGYDVAVADInsENAEKVADEINAEYGEKAYGFGADATN--EQSVIALSKGVdeifkrvDLLVYSAGIAKSAKITDF 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 305 SSDFWNSVINVNLN-----APQVLTQALLDGGKlhdnGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRG 379
Cdd:cd05322 100 ELGDFDRSLQVNLVgyflcAREFSKLMIRDGIQ----GRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEHG 175

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599980 380 ITINAVAPG-FIETQM-TAAIPLTIREAGRRMNSMSQ----------GGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:cd05322 176 ITVNSLMLGnLLKSPMfQSLLPQYAKKLGIKESEVEQyyidkvplkrGCDYQDVLNMLLFYASPKASYCTGQSINITG 253
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 254-393 5.26e-11

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: 62.86  E-value: 5.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 254 EGLAARLGGRA------VALDICAADAGQQLVEALPEG-VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQA 326
Cdd:cd09806  41 GRLWEAAGALAggtletLQLDVCDSKSVAAAVERVTERhVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQA 120

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599980 327 LLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQ 393
Cdd:cd09806 121 FLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTA 187
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 234-445 7.82e-11

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 62.61  E-value: 7.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  234 LARDGAEVVLLDVppAREALEGLAARL---GGRAVAL--DICAAD----AGQQLVEALpEGVDIVVHNAG---------- 294
Cdd:PRK08277  30 LARAGAKVAILDR--NQEKAEAVVAEIkaaGGEALAVkaDVLDKEsleqARQQILEDF-GPCDILINGAGgnhpkattdn 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  295 -----ITRDKTLAKMSSDFWNSVINVNLN----APQVLTQALLDGGKlhdnGRVVLLASISG------IAGnlgqsnYAV 359
Cdd:PRK08277 107 efhelIEPTKTFFDLDEEGFEFVFDLNLLgtllPTQVFAKDMVGRKG----GNIINISSMNAftpltkVPA------YSA 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  360 SKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAipLTIREAGR---RMNS------MSQGGLPQDVAETVAWFAQ 430
Cdd:PRK08277 177 AKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRA--LLFNEDGSlteRANKilahtpMGRFGKPEELLGTLLWLAD 254

                        250
                 ....*....|....*.
gi 15599980  431 P-SSGAVSGQVLRVCG 445
Cdd:PRK08277 255 EkASSFVTGVVLPVDG 270
PRK07454 PRK07454
SDR family oxidoreductase;
215-392 1.11e-10

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 61.51  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  215 QRALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAARL---GGRAVALDI---CAADAGQQLVEALPEG- 285
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALV----ARsqDALEALAAELrstGVKAAAYSIdlsNPEAIAPGIAELLEQFg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 -VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK07454  83 cPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAAL 162

                        170       180
                 ....*....|....*....|....*...
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIET 392
Cdd:PRK07454 163 AAFTKCLAEEERSHGIRVCTITLGAVNT 190
PLN02253 PLN02253
xanthoxin dehydrogenase
 199-445 1.27e-10

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 62.15  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  199 AANSAQVHDWSKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVppAREALEGLAARLGGRAVAL----DICAADA 274
Cdd:PLN02253   3 TASSSASSLPSQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDL--QDDLGQNVCDSLGGEPNVCffhcDVTVEDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  275 GQQLVEALPE---GVDIVVHNAGITRDKTLAKMSSDF--WNSVINVNL--------NAPQVLTQalldggklHDNGRVVL 341
Cdd:PLN02253  81 VSRAVDFTVDkfgTLDIMVNNAGLTGPPCPDIRNVELseFEKVFDVNVkgvflgmkHAARIMIP--------LKKGSIVS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  342 LASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAA-IPLTIRE----------AGRRMN 410
Cdd:PLN02253 153 LCSVASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAhLPEDERTedalagfrafAGKNAN 232

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15599980  411 SMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PLN02253 233 LKGVELTVDDVANAVLFLASDEARYISGLNLMIDG 267
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 212-445 1.97e-10

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: 60.95  E-value: 1.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAReaLEGLAARLGG-RAVALDICAADAGQQLVEALPEgVDIVV 290
Cdd:cd05351   5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQAD--LDSLVRECPGiEPVCVDLSDWDATEEALGSVGP-VDLLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 291 HNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHD-NGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQ 369
Cdd:cd05351  82 NNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCSTKAALDMLTK 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599980 370 AWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLP--QDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:cd05351 162 VMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKMLNRIPLGKFAevEDVVNAILFLLSDKSSMTTGSTLPVDG 239
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 234-445 2.23e-10

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 60.55  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  234 LARDGAEVVLLDVPParEALEGLAARLGG----RAVALDICAADAGQQLVE----ALPEGVDIVVHNAGITRD-----KT 300
Cdd:PRK05786  25 ALKEGAQVCINSRNE--NKLKRMKKTLSKygniHYVVGDVSSTESARNVIEkaakVLNAIDGLVVTVGGYVEDtveefSG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  301 LAKMssdfwnsvINVNLNAPQVLTQALLDggKLHDNGRVVLLASISGI-AGNLGQSNYAVSKAGLIGLAQAWAPALGKRG 379
Cdd:PRK05786 103 LEEM--------LTNHIKIPLYAVNASLR--FLKEGSSIVLVSSMSGIyKASPDQLSYAVAKAGLAKAVEILASELLGRG 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  380 ITINAVAPGFIETQMtaaipltirEAGRRMNSMSQGGLPQ----DVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PRK05786 173 IRVNGIAPTTISGDF---------EPERNWKKLRKLGDDMappeDFAKVIIWLLTDEADWVDGVVIPVDG 233
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 217-430 3.30e-10

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: 60.37  E-value: 3.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAARLGGR------AVALDICAADAGQQLVEALPEG--- 285
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKLILT----GRraERLQELADELGAKfpvkvlPLQLDVSDRESIEAALENLPEEfrd 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 VDIVVHNAGITRD-KTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:cd05346  79 IDILVNNAGLALGlDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAV 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599980 365 IGLAQAWAPALGKRGITINAVAPGFIETQMTaaiplTIREAG--RRMNSMSQGG---LPQDVAETVAWFAQ 430
Cdd:cd05346 159 RQFSLNLRKDLIGTGIRVTNIEPGLVETEFS-----LVRFHGdkEKADKVYEGVeplTPEDIAETILWVAS 224
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 210-385 3.37e-10

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 62.24  E-value: 3.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 210 KPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPParEALEGLAARLGGRAVALDICAADAGQQLVEALPE----- 284
Cdd:COG3347 421 KPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDG--EAAEAAAAELGGGYGADAVDATDVDVTAEAAVAAafgfa 498

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 285 -----GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGgklhdnGRVVLLASISGIAGNLGQSNYAV 359
Cdd:COG3347 499 gldigGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQG------TGGQGLGGSSVFAVSKNAAAAAY 572

                       170       180       190
                ....*....|....*....|....*....|.
gi 15599980 360 SKAGLIGLAQA-----WAPALGKRGITINAV 385
Cdd:COG3347 573 GAAAAATAKAAaqhllRALAAEGGANGINAN 603
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 217-392 3.60e-10

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: 59.83  E-value: 3.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLdvppAREA--LEGLAARLGGRA--VALDICAADAGQQLVEALPE---GVDIV 289
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGIC----ARDEarLAAAAAQELEGVlgLAGDVRDEADVRRAVDAMEEafgGLDAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 290 VHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQ 369
Cdd:cd08929  79 VNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSE 158

                       170       180
                ....*....|....*....|...
gi 15599980 370 AWAPALGKRGITINAVAPGFIET 392
Cdd:cd08929 159 AAMLDLREANIRVVNVMPGSVDT 181
PRK09135 PRK09135
pteridine reductase; Provisional
 217-445 3.91e-10

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 59.94  E-value: 3.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREAlEGLAARL----GGRAVAL--DICAADAGQQLVEALPE---GVD 287
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEA-DALAAELnalrPGSAAALqaDLLDPDALPELVAACVAafgRLD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  288 IVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDggKLHDN-GRVVLLASISGIAGNLGQSNYAVSKAGLIG 366
Cdd:PRK09135  88 ALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAP--QLRKQrGAIVNITDIHAERPLKGYPVYCAAKAALEM 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  367 LAQAWAPALGKRgITINAVAPGFIE-TQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSgAVSGQVLRVCG 445
Cdd:PRK09135 166 LTRSLALELAPE-VRVNAVAPGAILwPEDGNSFDEEARQAILARTPLKRIGTPEDIAEAVRFLLADAS-FITGQILAVDG 243
PRK06947 PRK06947
SDR family oxidoreductase;
249-445 5.08e-10

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 59.82  E-value: 5.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  249 AREALEGLAARLGGRA--VALDICAADAGQQLVEALPE---GVDIVVHNAGITR------DKTLAKMSSDFWNSVINVNL 317
Cdd:PRK06947  39 AAEETADAVRAAGGRAcvVAGDVANEADVIAMFDAVQSafgRLDALVNNAGIVApsmplaDMDAARLRRMFDTNVLGAYL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  318 NAPQVLTQALLDGGklhdnGRVVLLASISGIAGNLGQSN----YAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQ 393
Cdd:PRK06947 119 CAREAARRLSTDRG-----GRGGAIVNVSSIASRLGSPNeyvdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETE 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15599980  394 MTAAIPLTIREAgrRMNS---MSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PRK06947 194 IHASGGQPGRAA--RLGAqtpLGRAGEADEVAETIVWLLSDAASYVTGALLDVGG 246
PRK08267 PRK08267
SDR family oxidoreductase;
227-436 5.52e-10

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 59.95  E-value: 5.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  227 GAAIAETLARDGAEVVLLDVppAREALEGLAARLGGRAV---ALDICAADAGQQLVEALPE----GVDIVVHNAGITRDK 299
Cdd:PRK08267  14 GRATALLFAAEGWRVGAYDI--NEAGLAALAAELGAGNAwtgALDVTDRAAWDAALADFAAatggRLDVLFNNAGILRGG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  300 TLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQA----WApal 375
Cdd:PRK08267  92 PFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEAldleWR--- 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599980  376 gKRGITINAVAPGFIETQMTAAIPLTIREAgrrmnSMSQGGL---PQDVAEtVAWFAQPSSGAV 436
Cdd:PRK08267 169 -RHGIRVADVMPLFVDTAMLDGTSNEVDAG-----STKRLGVrltPEDVAE-AVWAAVQHPTRL 225
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 216-445 6.57e-10

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: 59.43  E-value: 6.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 216 RALVTGAARGIGAAIAETLARDGAEVVLLDVPPAReaLEGLAARLGGRAVALDicaadagqQLVEALPEGVDIVVHNAGI 295
Cdd:cd05328   1 TIVITGAASGIGAATAELLEDAGHTVIGIDLREAD--VIADLSTPEGRAAAIA--------DVLARCSGVLDGLVNCAGV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 296 TRDKTLakmssdfwNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGI--------------------------- 348
Cdd:cd05328  71 GGTTVA--------GLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAgwaqdklelakalaagtearavalaeh 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 349 AGNLGQSNYAVSKAGLIGLAQAWAPA-LGKRGITINAVAPGFIETQMTAAIPLTIR--EAGRRMNS-MSQGGLPQDVAET 424
Cdd:cd05328 143 AGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRggESVDAFVTpMGRRAEPDEIAPV 222

                       250       260
                ....*....|....*....|.
gi 15599980 425 VAWFAQPSSGAVSGQVLRVCG 445
Cdd:cd05328 223 IAFLASDAASWINGANLFVDG 243
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 235-429 1.18e-09

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: 58.23  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 235 ARDGAEVVLLDVppAREALEGLAARLGGRAV---ALDICAADAGQQLV----EALPEGVDIVVHNAGITRDKTLAKMSSD 307
Cdd:cd08931  21 ARNGWFVGLYDI--DEDGLAALAAELGAENVvagALDVTDRAAWAAALadfaAATGGRLDALFNNAGVGRGGPFEDVPLA 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 308 FWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAP 387
Cdd:cd08931  99 AHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEALDVEWARHGIRVADVWP 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15599980 388 GFIETQMTaaipltirEAGRRMNSMSQGGL----PQDVAETVaWFA 429
Cdd:cd08931 179 WFVDTPIL--------TKGETGAAPKKGLGrvlpVSDVAKVV-WAA 215
PRK06123 PRK06123
SDR family oxidoreductase;
217-445 1.49e-09

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 58.25  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVVL--LDVPPAREALEGLAARLGGRAVALDICAADAGQqlVEALPEGVD------- 287
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVCLnyLRNRDAAEAVVQAIRRQGGEALAVAADVADEAD--VLRLFEAVDrelgrld 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  288 IVVHNAGI-TRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSN----YAVSKA 362
Cdd:PRK06123  83 ALVNNAGIlEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRGGAIVNVSSMAARLGSPGeyidYAASKG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  363 GLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPltirEAGR--RMNS---MSQGGLPQDVAETVAWFAQPSSGAVS 437
Cdd:PRK06123 163 AIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGG----EPGRvdRVKAgipMGRGGTAEEVARAILWLLSDEASYTT 238


                 ....*...
gi 15599980  438 GQVLRVCG 445
Cdd:PRK06123 239 GTFIDVSG 246
PRK07024 PRK07024
SDR family oxidoreductase;
235-396 2.25e-09

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 58.02  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  235 ARDGAEVVLLdvppAR--EALEGLAARLGGRA----VALDICAADAGQQLVEALPE---GVDIVVHNAGITRDkTLAKMS 305
Cdd:PRK07024  23 ARQGATLGLV----ARrtDALQAFAARLPKAArvsvYAADVRDADALAAAAADFIAahgLPDVVIANAGISVG-TLTEER 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  306 SDF--WNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITIN 383
Cdd:PRK07024  98 EDLavFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLESLRVELRPAGVRVV 177

                        170
                 ....*....|...
gi 15599980  384 AVAPGFIETQMTA 396
Cdd:PRK07024 178 TIAPGYIRTPMTA 190
PRK12744 PRK12744
SDR family oxidoreductase;
212-392 2.39e-09

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 57.83  E-value: 2.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLL------DVPPAREALEGLAArLGGRAVAL--DICAADAGQQLVEALP 283
Cdd:PRK12744   6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIhynsaaSKADAEETVAAVKA-AGAKAVAFqaDLTTAAAVEKLFDDAK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  284 E---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQV-LTQAlldGGKLHDNGRVV-----LLASISGiagnlGQ 354
Cdd:PRK12744  85 AafgRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFfIKEA---GRHLNDNGKIVtlvtsLLGAFTP-----FY 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15599980  355 SNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIET 392
Cdd:PRK12744 157 SAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDT 194
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 264-406 3.47e-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: 57.03  E-value: 3.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 264 AVALDICAADAGQQLVEALPEgVDIVVHNAGITRDKTLakMSSDFWNSV---INVNLNAPQVLTQALLDGGKLHDNGRVV 340
Cdd:cd05354  54 PLRLDVTDPESIKAAAAQAKD-VDVVINNAGVLKPATL--LEEGALEALkqeMDVNVFGLLRLAQAFAPVLKANGGGAIV 130

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599980 341 LLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAI------PLTIREAG 406
Cdd:cd05354 131 NLNSVASLKNFPAMGTYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAggpkesPETVAEAV 202
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 211-426 4.64e-09

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 57.26  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVL--LDVPPAREAleglAARLGG-RAVALDICAADAGQQL---VEALPE 284
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIgdLDEALAKET----AAELGLvVGGPLDVTDPASFAAFldaVEADLG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:PRK07825  78 PIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTireagrrmnsmsqGGL----PQDVAETVA 426
Cdd:PRK07825 158 VGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGGA-------------KGFknvePEDVAAAIV 210
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
234-445 4.79e-09

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 56.55  E-value: 4.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  234 LARD-GAEVVLLDVPPAREALEGLaarlggraVALDICAADAGQQLVEALPEGVDIVVHNAGI--TRDKTLakmssdfwn 310
Cdd:PRK12428   4 LLRFlGARVIGVDRREPGMTLDGF--------IQADLGDPASIDAAVAALPGRIDALFNIAGVpgTAPVEL--------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  311 sVINVNLNAPQVLTQALLDggKLHDNGRVVLLASISG------------IAGNLG---------------QSNYAVSKAG 363
Cdd:PRK12428  67 -VARVNFLGLRHLTEALLP--RMAPGGAIVNVASLAGaewpqrlelhkaLAATASfdegaawlaahpvalATGYQLSKEA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  364 LI--GLAQAWaPALGKRGITINAVAPGFIETQM-----TAAIPLTIREAGRRmnsMSQGGLPQDVAETVAWFAQPSSGAV 436
Cdd:PRK12428 144 LIlwTMRQAQ-PWFGARGIRVNCVAPGPVFTPIlgdfrSMLGQERVDSDAKR---MGRPATADEQAAVLVFLCSDAARWI 219


                 ....*....
gi 15599980  437 SGQVLRVCG 445
Cdd:PRK12428 220 NGVNLPVDG 228
PRK07102 PRK07102
SDR family oxidoreductase;
235-400 5.03e-09

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 56.47  E-value: 5.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  235 ARDGAEVVLLdvppAR--EALEGLAARL---GGRAVA---LDICAADAGQQLVEALPEGVDIVVHNAGITRDKTLAKMSS 306
Cdd:PRK07102  22 AAAGARLYLA----ARdvERLERLADDLrarGAVAVStheLDILDTASHAAFLDSLPALPDIVLIAVGTLGDQAACEADP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  307 DFWNSVINVNLNAPQVLTQALLDGGKLHDNGrvvLLASISGIAGNLG-QSNY--AVSKAGLIGLAQAWAPALGKRGITIN 383
Cdd:PRK07102  98 ALALREFRTNFEGPIALLTLLANRFEARGSG---TIVGISSVAGDRGrASNYvyGSAKAALTAFLSGLRNRLFKSGVHVL 174

                        170
                 ....*....|....*..
gi 15599980  384 AVAPGFIETQMTAAIPL 400
Cdd:PRK07102 175 TVKPGFVRTPMTAGLKL 191
PRK05866 PRK05866
SDR family oxidoreductase;
211-409 5.78e-09

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 57.06  E-value: 5.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVLldVPPAREALEGLAARL---GG--RAVALDICAADAGQQLVEALPE- 284
Cdd:PRK05866  37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVA--VARREDLLDAVADRItraGGdaMAVPCDLSDLDAVDALVADVEKr 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 --GVDIVVHNAGITRDKTLAKmSSDFWNSV---INVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQ-SNYA 358
Cdd:PRK05866 115 igGVDILINNAGRSIRRPLAE-SLDRWHDVertMVLNYYAPLRLIRGLAPGMLERGDGHIINVATWGVLSEASPLfSVYN 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599980  359 VSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTA------AIP-LTIREAGRRM 409
Cdd:PRK05866 194 ASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIAptkaydGLPaLTADEAAEWM 251
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 212-445 1.01e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 55.82  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLldVPPAREALEGLAARLGGR------AVALDICAADAGQQLVEALPEg 285
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHL--VARDADALEALAADLRAAhgvdvaVHALDLSSPEAREQLAAEAGD- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVllaSISGIAGNLGQSNY---AVSKA 362
Cdd:PRK06125  82 IDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIV---NVIGAAGENPDADYicgSAGNA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  363 GLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAipLTIREAGRRMNSMS-----QGGLP-------QDVAETVAWFAQ 430
Cdd:PRK06125 159 ALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLT--LLKGRARAELGDESrwqelLAGLPlgrpatpEEVADLVAFLAS 236

                        250
                 ....*....|....*
gi 15599980  431 PSSGAVSGQVLRVCG 445
Cdd:PRK06125 237 PRSGYTSGTVVTVDG 251
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 205-425 1.39e-08

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: 55.60  E-value: 1.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 205 VHDWSkplaGQRALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAARLGGR------AVALDICAADAGQ 276
Cdd:cd05343   1 MERWR----GRVALVTGASVGIGAAVARALVQHGMKVVGC----ARrvDKIEALAAECQSAgyptlfPYQCDLSNEEQIL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 277 QLVEALPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLH--DNGRVVLLASISG---I 348
Cdd:cd05343  73 SMFSAIRTqhqGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERnvDDGHIININSMSGhrvP 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980 349 AGNLgQSNYAVSKAGLIGLAQAWAPAL--GKRGITINAVAPGFIETQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETV 425
Cdd:cd05343 153 PVSV-FHFYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANAV 230
PRK09134 PRK09134
SDR family oxidoreductase;
216-445 1.51e-08

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 55.32  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  216 RALVTGAARGIGAAIAETLARDGAEVVlLDVPPAREALEGLAA---RLGGRAVAL--DICAADAGQQLVEALPEG---VD 287
Cdd:PRK09134  11 AALVTGAARRIGRAIALDLAAHGFDVA-VHYNRSRDEAEALAAeirALGRRAVALqaDLADEAEVRALVARASAAlgpIT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  288 IVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDggklhdngrvVLLASISGIAGNL----------GQSNY 357
Cdd:PRK09134  90 LLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFAR----------ALPADARGLVVNMidqrvwnlnpDFLSY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  358 AVSKAGLIGLAQAWAPALGKRgITINAVAPGfietqmtaaipLTIR---------EAGRRMNSMSQGGLPQDVAETVAWF 428
Cdd:PRK09134 160 TLSKAALWTATRTLAQALAPR-IRVNAIGPG-----------PTLPsgrqspedfARQHAATPLGRGSTPEEIAAAVRYL 227

                        250
                 ....*....|....*..
gi 15599980  429 AqpSSGAVSGQVLRVCG 445
Cdd:PRK09134 228 L--DAPSVTGQMIAVDG 242
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 233-449 2.18e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 55.19  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  233 TLARDGAEVVLLDVPPAR--EALEGLAARLGGRAV---ALDICAADAGQQLVEALPE---GVDIVVHNAGITRD-KTLAK 303
Cdd:PRK05875  26 GLVAAGAAVMIVGRNPDKlaAAAEEIEALKGAGAVryePADVTDEDQVARAVDAATAwhgRLHGVVHCAGGSETiGPITQ 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  304 MSSDFWNSVINVNLNAPQVL----TQALLDGGklhdNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRG 379
Cdd:PRK05875 106 IDSDAWRRTVDLNVNGTMYVlkhaARELVRGG----GGSFVGISSIAASNTHRWFGAYGVTKSAVDHLMKLAADELGPSW 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599980  380 ITINAVAPGFIETQMTAAIPLT--IREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCGQSLL 449
Cdd:PRK05875 182 VRVNSIRPGLIRTDLVAPITESpeLSADYRACTPLPRVGEVEDVANLAMFLLSDAASWITGQVINVDGGHML 253
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 217-445 3.93e-08

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: 54.12  E-value: 3.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREA-LEGLAARLGGravaLDICAADAGQQLVEALPEG---VDIVVHN 292
Cdd:cd05361   4 ALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAeRQAFESENPG----TKALSEQKPEELVDAVLQAggaIDVLVSN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 293 AGITRDKT-LAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAW 371
Cdd:cd05361  80 DYIPRPMNpIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESL 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980 372 APALGKRGITINAVAPGFIETQMTAAIPL-----TIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:cd05361 160 AKELSRDNILVYAIGPNFFNSPTYFPTSDwennpELRERVKRDVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFAG 238
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 218-371 4.05e-08

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: 55.07  E-value: 4.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 218 LVTGAARGIGAAIAETLARD-GAEVVLL-------DVPPAREALEGLAArLGGRA--VALDICAADAGQQLVEALPE--- 284
Cdd:cd08953 209 LVTGGAGGIGRALARALARRyGARLVLLgrsplppEEEWKAQTLAALEA-LGARVlyISADVTDAAAVRRLLEKVREryg 287

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 285 GVDIVVHNAGITRDKTLAKMSSDFWNSVInvnlnAPQVL-TQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAG 363
Cdd:cd08953 288 AIDGVIHAAGVLRDALLAQKTAEDFEAVL-----APKVDgLLNLAQALADEPLDFFVLFSSVSAFFGGAGQADYAAANAF 362


                ....*...
gi 15599980 364 LIGLAQAW 371
Cdd:cd08953 363 LDAFAAYL 370
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 211-448 4.99e-08

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: 53.69  E-value: 4.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPparEALEGLAARLGGRAVALDICAAD----AGQQLVEALPEG- 285
Cdd:cd08937   1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS---ELVHEVLAEILAAGDAAHVHTADletyAGAQGVVRAAVEr 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 ---VDIVVHNAGIT-RDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNlgQSNYAVSK 361
Cdd:cd08937  78 fgrVDVLINNVGGTiWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGIY--RIPYSAAK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 362 AGLIGLAQAWAPALGKRGITINAVAPGFIETQ----MTAAIPLT---------IREAGRRMNSMSQGGLPQDVAETVAWF 428
Cdd:cd08937 156 GGVNALTASLAFEHARDGIRVNAVAPGGTEAPprkiPRNAAPMSeqekvwyqrIVDQTLDSSLMGRYGTIDEQVRAILFL 235

                       250       260
                ....*....|....*....|
gi 15599980 429 AQPSSGAVSGQVLRVCGQSL 448
Cdd:cd08937 236 ASDEASYITGTVLPVGGGDL 255
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 212-448 8.25e-08

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 53.32  E-value: 8.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLL-----DVPPAREALEGlAARLGGRAVALDICAADAGQQLVEALPE-G 285
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLsrneeNLKKAREKIKS-ESNVDVSYIVADLTKREDLERTVKELKNiG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 V-DIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLAS--ISGIAGNLGQSNyaVSKA 362
Cdd:PRK08339  85 EpDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSvaIKEPIPNIALSN--VVRI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  363 GLIGLAQAWAPALGKRGITINAVAPGFIETQMTaaIPLTIREAGRRMNSMSQG-------------GLPQDVAETVAWFA 429
Cdd:PRK08339 163 SMAGLVRTLAKELGPKGITVNGIMPGIIRTDRV--IQLAQDRAKREGKSVEEAlqeyakpiplgrlGEPEEIGYLVAFLA 240

                        250
                 ....*....|....*....
gi 15599980  430 QPSSGAVSGQVLRVCGQSL 448
Cdd:PRK08339 241 SDLGSYINGAMIPVDGGRL 259
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 214-395 1.24e-07

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: 52.61  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 214 GQRALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAARL------GGRAVALDICAADAGQQLVEALPEG 285
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILI----SRtqEKLDAVAKEIeekygvETKTIAADFSAGDDIYERIEKELEG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 VDI--VVHNAGITRD--KTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSK 361
Cdd:cd05356  77 LDIgiLVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASK 156

                       170       180       190
                ....*....|....*....|....*....|....
gi 15599980 362 AGLIGLAQAWAPALGKRGITINAVAPGFIETQMT 395
Cdd:cd05356 157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMS 190
PRK08264 PRK08264
SDR family oxidoreductase;
264-399 1.74e-07

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 51.81  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  264 AVALDICAADAGQQLVEALPEgVDIVVHNAGITR------DKTLAKMSSDFwnsviNVNLNAPQVLTQALLDGGKLHDNG 337
Cdd:PRK08264  53 PLQLDVTDPASVAAAAEAASD-VTILVNNAGIFRtgslllEGDEDALRAEM-----ETNYFGPLAMARAFAPVLAANGGG 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599980  338 RVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIP 399
Cdd:PRK08264 127 AIVNVLSVLSWVNFPNLGTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGLD 188
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 234-450 1.93e-07

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: 51.81  E-value: 1.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 234 LARDGAEVVLLDVPPAREA-LEGLAARLGGRAVALDICAADagQQLVEALPEGV-------DIVVHNAG----ITRDKTL 301
Cdd:cd05372  23 LHEAGAELAFTYQPEALRKrVEKLAERLGESALVLPCDVSN--DEEIKELFAEVkkdwgklDGLVHSIAfapkVQLKGPF 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 302 AKMSSDFWNSVINVNLNAPQVLTQALLDggKLHDNGRVVllaSISGIAGNLGQSNY---AVSKAGLIGLAQAWAPALGKR 378
Cdd:cd05372 101 LDTSRKGFLKALDISAYSLVSLAKAALP--IMNPGGSIV---TLSYLGSERVVPGYnvmGVAKAALESSVRYLAYELGRK 175

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599980 379 GITINAVAPGFIETQMTAAIPL--TIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRV-CGQSLLG 450
Cdd:cd05372 176 GIRVNAISAGPIKTLAASGITGfdKMLEYSEQRAPLGRNVTAEEVGNTAAFLLSDLSSGITGEIIYVdGGYHIMG 250
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 231-443 2.96e-07

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: 50.66  E-value: 2.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 231 AETLARDGAEVVlldvpparealeglAARLGGRAVALDICAADAgqqlVEALPEG---VDIVVHNAGITRDKTLAKMSSD 307
Cdd:cd11731  15 AQLLSAHGHEVI--------------TAGRSSGDYQVDITDEAS----IKALFEKvghFDAIVSTAGDAEFAPLAELTDA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 308 FWNSVINVNLNAPQVLTQALLDggKLHDNGRVVLlasISGIAG---NLGQSNYAVSKAGLIGLAQAWAPALGkRGITINA 384
Cdd:cd11731  77 DFQRGLNSKLLGQINLVRHGLP--YLNDGGSITL---TSGILAqrpIPGGAAAATVNGALEGFVRAAAIELP-RGIRINA 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980 385 VAPGFIETQMTAAipltireagrrMNSMSqGGLPQDVAETVAWFAQPSSGAVSGQVLRV 443
Cdd:cd11731 151 VSPGVVEESLEAY-----------GDFFP-GFEPVPAEDVAKAYVRSVEGAFTGQVLHV 197
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 234-369 3.20e-07

ketoreductase (KR), subgroup 1, 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 KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. 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: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 52.56  E-value: 3.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 234 LARDGAEVVLL------DVPPAREALEGLAArLGGRA--VALDICAADAGQQLVEALPEGVDI--VVHNAGITRDKTLAK 303
Cdd:cd08952 250 LARRGAEHLVLtsrrgpDAPGAAELVAELTA-LGARVtvAACDVADRDALAALLAALPAGHPLtaVVHAAGVLDDGPLDD 328

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599980 304 MSSDFWNSVINVNLNAPQVLTQALLDggklHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQ 369
Cdd:cd08952 329 LTPERLAEVLRAKVAGARHLDELTRD----RDLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAE 390
PRK08251 PRK08251
SDR family oxidoreductase;
249-401 4.05e-07

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 51.09  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  249 AR--EALEGLAARL----GGRAVA---LDICAADAGQQLVEALPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVN 316
Cdd:PRK08251  33 ARrtDRLEELKAELlaryPGIKVAvaaLDVNDHDQVFEVFAEFRDelgGLDRVIVNAGIGKGARLGTGKFWANKATAETN 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  317 LNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLG-QSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMT 395
Cdd:PRK08251 113 FVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGvKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMN 192


                 ....*.
gi 15599980  396 AAIPLT 401
Cdd:PRK08251 193 AKAKST 198
PRK09186 PRK09186
flagellin modification protein A; Provisional
 212-390 4.82e-07

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 50.76  E-value: 4.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVL--LDVPPAREALEGLAARLGGRA---VALDICAADAGQQLVEALPE-- 284
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAadIDKEALNELLESLGKEFKSKKlslVELDITDQESLEEFLSKSAEky 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  285 -GVDIVVHNAgITRDKTLAK----MSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIA--------GN 351
Cdd:PRK09186  82 gKIDGAVNCA-YPRNKDYGKkffdVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVapkfeiyeGT 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15599980  352 LGQS--NYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFI 390
Cdd:PRK09186 161 SMTSpvEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGI 201
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 212-397 6.13e-07

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: 50.38  E-value: 6.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLldVPPAREALEGLAARLGG-RAVALDICAADAGQQLVEAL----PEgV 286
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLEAGNTVII--TGRREERLAEAKKELPNiHTIVLDVGDAESVEALAEALlseyPN-L 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 287 DIVVHNAGITRDKTLAKMSSDF--WNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:cd05370  80 DILINNAGIQRPIDLRDPASDLdkADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAAL 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 15599980 365 IGLAQAWAPALGKRGITINAVAPGFIETQMTAA 397
Cdd:cd05370 160 HSYTLALRHQLKDTGVEVVEIVPPAVDTELHEE 192
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
216-445 6.94e-07

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 50.75  E-value: 6.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 216 RALVTGAARGIGAAIAETLARDGAEVVLLDVPPAReaLEGLAARLGGRAVALDICAADAgqqlVEALPEGVDIVVHNAGI 295
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPG--AANLAALPGVEFVRGDLRDPEA----LAAALAGVDAVVHLAAP 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 296 TRDKTlakmssDFWNSVINVNLNApqvlTQALLDGGKLHDNGRVVlLASISGIAGNLG-----------QSNYAVSKAGL 364
Cdd:COG0451  75 AGVGE------EDPDETLEVNVEG----TLNLLEAARAAGVKRFV-YASSSSVYGDGEgpidedtplrpVSPYGASKLAA 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 365 IGLAQAWAPALGKRGITINavAPGFIETQMTAAIPLTIREA--GRRMNSMSQGGLP------QDVAETVAWFAQpsSGAV 436
Cdd:COG0451 144 ELLARAYARRYGLPVTILR--PGNVYGPGDRGVLPRLIRRAlaGEPVPVFGDGDQRrdfihvDDVARAIVLALE--APAA 219


                ....*....
gi 15599980 437 SGQVLRVCG 445
Cdd:COG0451 220 PGGVYNVGG 228
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 242-424 9.85e-07

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: 49.97  E-value: 9.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 242 VLLDVPPAREALEGLAA-RLggRAVALDICAA----DAGQQLVEALPE-GVDIVVHNAGITRDKTLAKMSS-DFWNSVIN 314
Cdd:cd09805  31 CLTKNGPGAKELRRVCSdRL--RTLQLDVTKPeqikRAAQWVKEHVGEkGLWGLVNNAGILGFGGDEELLPmDDYRKCME 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 315 VNLNAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQM 394
Cdd:cd09805 109 VNLFGTVEVTKAFLPLLR-RAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGI 187

                       170       180       190
                ....*....|....*....|....*....|
gi 15599980 395 TAAIPLTIreagRRMNSMSQgGLPQDVAET 424
Cdd:cd09805 188 TGNSELWE----KQAKKLWE-RLPPEVKKD 212
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 217-392 1.23e-06

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: 49.06  E-value: 1.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAreALEGLAARLGGRAVALDICAADAGQQLVEALPEgVDIVVHNAGIT 296
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAG--ALAGLAAEVGALARPADVAAELEVWALAQELGP-LDLLVYAAGAI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 297 RDKTLAKMSSDFWNSVINVNL-NAPQVLTQALLdggKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPAL 375
Cdd:cd11730  78 LGKPLARTKPAAWRRILDANLtGAALVLKHALA---LLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVARKEV 154

                       170
                ....*....|....*..
gi 15599980 376 GKRGITInaVAPGFIET 392
Cdd:cd11730 155 RGLRLTL--VRPPAVDT 169
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 218-425 1.24e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 49.65  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  218 LVTGAARGIGAAIAETLARDGAEVvlldVPPAR--EALEGLAARLGGR--AVALDICAADAGQQLVEALPEGV---DIVV 290
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRV----VATARdtATLADLAEKYGDRllPLALDVTDRAAVFAAVETAVEHFgrlDIVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  291 HNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQA 370
Cdd:PRK08263  83 NNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSEA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599980  371 WAPALGKRGITINAVAPG-----FIETQMTAAIPL----TIREAGRRMNS-MSQGGLPQDVAETV 425
Cdd:PRK08263 163 LAQEVAEFGIKVTLVEPGgystdWAGTSAKRATPLdaydTLREELAEQWSeRSVDGDPEAAAEAL 227
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 232-451 1.50e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 49.57  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  232 ETLARDGAEVVLL--DVPPAREALEGLAArLGGRAVAL-----DICAADAG-QQLVEALPEgVDIVVHNAGITRDKTLAK 303
Cdd:PRK07576  27 QAFARAGANVAVAsrSQEKVDAAVAQLQQ-AGPEGLGVsadvrDYAAVEAAfAQIADEFGP-IDVLVSGAAGNFPAPAAG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  304 MSSDFWNSVINVNLNAP-QVLTQALldgGKLHDNGRVVLlaSIS-GIAGN--LGQSNYAVSKAGLIGLAQAWAPALGKRG 379
Cdd:PRK07576 105 MSANGFKTVVDIDLLGTfNVLKAAY---PLLRRPGASII--QISaPQAFVpmPMQAHVCAAKAGVDMLTRTLALEWGPEG 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  380 ITINAVAPGFI---------------ETQMTAAIPLtireagRRMnsmsqgGLPQDVAETVAWFAQPSSGAVSGQVLRV- 443
Cdd:PRK07576 180 IRVNSIVPGPIagtegmarlapspelQAAVAQSVPL------KRN------GTKQDIANAALFLASDMASYITGVVLPVd 247


                 ....*...
gi 15599980  444 CGQSLLGA 451
Cdd:PRK07576 248 GGWSLGGA 255
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 232-451 1.63e-06

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: 49.25  E-value: 1.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 232 ETLARDGAEVVLLDVPPA-REALEGLAARLGGRAVA-LDICAADAGQQLVEALPE---GVDIVVHNAGitrdktlakMS- 305
Cdd:COG0623  25 KALHEEGAELAFTYQGEAlKKRVEPLAEELGSALVLpCDVTDDEQIDALFDEIKEkwgKLDFLVHSIA---------FAp 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 306 -SDFWNSVINVN----LNAPQV-------LTQALLDggKLHDNGRVVLLaSISGiagnlGQ---SNY---AVSKAGLIGL 367
Cdd:COG0623  96 kEELGGRFLDTSregfLLAMDIsayslvaLAKAAEP--LMNEGGSIVTL-TYLG-----AErvvPNYnvmGVAKAALEAS 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 368 AQAWAPALGKRGITINAVAPGFIETQMTAAIP--LTIREAGRRMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRV-C 444
Cdd:COG0623 168 VRYLAADLGPKGIRVNAISAGPIKTLAASGIPgfDKLLDYAEERAPLGRNVTIEEVGNAAAFLLSDLASGITGEIIYVdG 247


                ....*..
gi 15599980 445 GQSLLGA 451
Cdd:COG0623 248 GYHIMGM 254
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 246-383 3.29e-06

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (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 oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase 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 consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses 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-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses 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 the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. 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: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 49.21  E-value: 3.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 246 VPPAREALEGLAARLGG-RAVALDICAADAGQQLVEALPEG---VDIVVHNAGITRDKTLAKMSSDFWNSVInvnlnAPQ 321
Cdd:cd08955 186 SAAARQAIAALEEAGAEvVVLAADVSDRDALAAALAQIRASlppLRGVIHAAGVLDDGVLANQDWERFRKVL-----APK 260

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599980 322 V--------LTQAL-LDggklhdngRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWApALGKRGITIN 383
Cdd:cd08955 261 VqgawnlhqLTQDLpLD--------FFVLFSSVASLLGSPGQANYAAANAFLDALAHYRR-ARGLPALSIN 322
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 212-444 3.57e-06

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: 48.21  E-value: 3.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLL--DVPPAREALEGLAARLGGRAVALDICAADAGQqlVEALPEGV--- 286
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITgrTILPQLPGTAEEIEARGGKCIPVRCDHSDDDE--VEALFERVare 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 287 -----DIVVHNAGITRDKTLAKMSSDF-------WNSVINVNLNAPQVL----TQALLDGGKlhdnGRVVLLASISGIAg 350
Cdd:cd09763  79 qqgrlDILVNNAYAAVQLILVGVAKPFweepptiWDDINNVGLRAHYACsvyaAPLMVKAGK----GLIVIISSTGGLE- 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 351 NLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIET-QMTAAIPLTIREAGRRMNS-MSQGGLPQDVAETVAWF 428
Cdd:cd09763 154 YLFNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTeLVLEMPEDDEGSWHAKERDaFLNGETTEYSGRCVVAL 233

                       250
                ....*....|....*..
gi 15599980 429 AQ-PSSGAVSGQVLRVC 444
Cdd:cd09763 234 AAdPDLMELSGRVLITG 250
PRK09291 PRK09291
SDR family oxidoreductase;
214-392 3.94e-06

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 48.07  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  214 GQRALVTGAARGIGAAIAETLARDGAEVVL-LDVPPAREALEGLAARLGG--RAVALDI-CAADAGQqlveALPEGVDIV 289
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIAgVQIAPQVTALRAEAARRGLalRVEKLDLtDAIDRAQ----AAEWDVDVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  290 VHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQ 369
Cdd:PRK09291  78 LNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEAIAE 157

                        170       180
                 ....*....|....*....|...
gi 15599980  370 AWAPALGKRGITINAVAPGFIET 392
Cdd:PRK09291 158 AMHAELKPFGIQVATVNPGPYLT 180
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 352-445 4.40e-06

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: 48.00  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980   352 LGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFieTQMTAAIPLTIREAGRRMNSMSQ-GGLPQDVAETVAWFAQ 430
Cdd:TIGR02685 168 LGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL--SLLPDAMPFEVQEDYRRKVPLGQrEASAEQIADVVIFLVS 245

                          90
                  ....*....|....*
gi 15599980   431 PSSGAVSGQVLRVCG 445
Cdd:TIGR02685 246 PKAKYITGTCIKVDG 260
PRK07023 PRK07023
SDR family oxidoreductase;
216-398 6.73e-06

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 47.32  E-value: 6.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  216 RALVTGAARGIGAAIAETLARDGAEVVLLdvppAREALEGLAARLGGR--AVALDI-----CAADAGQQLVEALPEGVDI 288
Cdd:PRK07023   3 RAIVTGHSRGLGAALAEQLLQPGIAVLGV----ARSRHPSLAAAAGERlaEVELDLsdaaaAAAWLAGDLLAAFVDGASR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  289 V--VHNAGITRD-KTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLI 365
Cdd:PRK07023  79 VllINNAGTVEPiGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAALD 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15599980  366 GLAQAWApALGKRGITINAVAPGFIETQMTAAI 398
Cdd:PRK07023 159 HHARAVA-LDANRALRIVSLAPGVVDTGMQATI 190
PRK07062 PRK07062
SDR family oxidoreductase;
211-445 6.77e-06

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 47.34  E-value: 6.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAReaLEGLAARLGGR-------AVALDICAADAGQQLVEALP 283
Cdd:PRK07062   5 QLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEER--LASAEARLREKfpgarllAARCDVLDEADVAAFAAAVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  284 E---GVDIVVHNAGITRDKTLAKMSSDFWN--------SVINVnlnapqvlTQALLDGGKLHDNGRVVLLASISGIAGNL 352
Cdd:PRK07062  83 ArfgGVDMLVNNAGQGRVSTFADTTDDAWRdelelkyfSVINP--------TRAFLPLLRASAAASIVCVNSLLALQPEP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  353 GQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIET------------------QMTAAIpltireAGRRMNSMSQ 414
Cdd:PRK07062 155 HMVATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVESgqwrrryearadpgqsweAWTAAL------ARKKGIPLGR 228

                        250       260       270
                 ....*....|....*....|....*....|.
gi 15599980  415 GGLPQDVAETVAWFAQPSSGAVSGQVLRVCG 445
Cdd:PRK07062 229 LGRPDEAARALFFLASPLSSYTTGSHIDVSG 259
PRK05884 PRK05884
SDR family oxidoreductase;
218-388 5.95e-05

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 44.03  E-value: 5.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  218 LVTGAARGIGAAIAETLARDGAEVVLldVPPAREALEGLAARLGGRAVALDICAADAGQQLVEALPEGVDIVVH------ 291
Cdd:PRK05884   4 LVTGGDTDLGRTIAEGFRNDGHKVTL--VGARRDDLEVAAKELDVDAIVCDNTDPASLEEARGLFPHHLDTIVNvpapsw 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  292 NAGITRDKTLAKMSSDfWNSVINVNLNAPQVLTQALldGGKLHDNGRVVLLASISGIAGnlgqSNYAVSKAGLIGLAQAW 371
Cdd:PRK05884  82 DAGDPRTYSLADTANA-WRNALDATVLSAVLTVQSV--GDHLRSGGSIISVVPENPPAG----SAEAAIKAALSNWTAGQ 154

                        170
                 ....*....|....*..
gi 15599980  372 APALGKRGITINAVAPG 388
Cdd:PRK05884 155 AAVFGTRGITINAVACG 171
PRK08703 PRK08703
SDR family oxidoreductase;
210-441 6.95e-05

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 44.15  E-value: 6.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  210 KPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAR-EALEGLAARLGG---RAVALDICAADAGQ------QLV 279
Cdd:PRK08703   2 ATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKlEKVYDAIVEAGHpepFAIRFDLMSAEEKEfeqfaaTIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  280 EALPEGVDIVVHNAGI------TRDKTLAKmssdfWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLG 353
Cdd:PRK08703  82 EATQGKLDGIVHCAGYfyalspLDFQTVAE-----WVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  354 QSNYAVSKAGLIGLAQAWAPALGKRG-ITINAVAPGFIET-QMTAAIPltiREAGRRMNSMSqgglpqDVAETVAWFAQP 431
Cdd:PRK08703 157 WGGFGASKAALNYLCKVAADEWERFGnLRANVLVPGPINSpQRIKSHP---GEAKSERKSYG------DVLPAFVWWASA 227

                        250
                 ....*....|
gi 15599980  432 SSGAVSGQVL 441
Cdd:PRK08703 228 ESKGRSGEIV 237
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 212-392 8.43e-05

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: 43.88  E-value: 8.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREAleGLAARLGGRAVAL--DICAADAGQQLVEALPEG---V 286
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVA--ELRADFGDAVVGVegDVRSLADNERAVARCVERfgkL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 287 DIVVHNAGI---------TRDKTLAKMSSDFWNsvINV--NLNAPQVLTQALLDGgklhdNGRVVLLASISGIAGNLGQS 355
Cdd:cd05348  80 DCFIGNAGIwdystslvdIPEEKLDEAFDELFH--INVkgYILGAKAALPALYAT-----EGSVIFTVSNAGFYPGGGGP 152

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15599980 356 NYAVSKAGLIGLAQAWAPALGKRgITINAVAPGFIET 392
Cdd:cd05348 153 LYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVT 188
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 217-433 8.46e-05

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: 43.91  E-value: 8.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAR-EALEGLAAR-LGGRAVAldiCAADAGQ-QLVEALPEGV------- 286
Cdd:cd05373   2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKlEALLVDIIRdAGGSAKA---VPTDARDeDEVIALFDLIeeeigpl 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 287 DIVVHNAGITRDKTLAKMSSDFWNSVINVN-----LNAPQVLTQALLDGGklhdnGRVVLLASISGIAGNLGQSNYAVSK 361
Cdd:cd05373  79 EVLVYNAGANVWFPILETTPRVFEKVWEMAafggfLAAREAAKRMLARGR-----GTIIFTGATASLRGRAGFAAFAGAK 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599980 362 AGLIGLAQAWAPALGKRGItinAVAPGFIETQMTAAIpltIREAGRRMNSMSQGGL---PQDVAETVaWF--AQPSS 433
Cdd:cd05373 154 FALRALAQSMARELGPKGI---HVAHVIIDGGIDTDF---IRERFPKRDERKEEDGildPDAIAEAY-WQlhTQPRS 223
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 210-366 9.73e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 44.14  E-value: 9.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  210 KPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAA---RLGGRAVALDICAADAGQ-----QLV 279
Cdd:PRK07109   4 KPIGRQVVVITGASAGVGRATARAFARRGAKVVLL----ARgeEGLEALAAeirAAGGEALAVVADVADAEAvqaaaDRA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  280 EALPEGVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAV 359
Cdd:PRK07109  80 EEELGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCA 159


                 ....*..
gi 15599980  360 SKAGLIG 366
Cdd:PRK07109 160 AKHAIRG 166
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 212-412 9.88e-05

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 43.79  E-value: 9.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREAleGLAARLGGRAVAL--DICAADAGQQLVEALPE---GV 286
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLA--SLRQRFGDHVLVVegDVTSYADNQRAVDQTVDafgKL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIVVHNAGI----TR--DKTLAKMSSDFwNSVINVNLNAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSNYAVS 360
Cdd:PRK06200  82 DCFVGNAGIwdynTSlvDIPAETLDTAF-DEIFNVNVKGYLLGAKAALPALK-ASGGSMIFTLSNSSFYPGGGGPLYTAS 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15599980  361 KAGLIGLAQAWAPALGKRgITINAVAPGFIETQMTAaiPLTIREAGRRMNSM 412
Cdd:PRK06200 160 KHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLRG--PASLGQGETSISDS 208
PRK08017 PRK08017
SDR family oxidoreductase;
316-395 1.51e-04

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 43.15  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  316 NLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLiglaQAWAPA----LGKRGITINAVAPGFIE 391
Cdd:PRK08017 105 NFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYAL----EAWSDAlrmeLRHSGIKVSLIEPGPIR 180


                 ....
gi 15599980  392 TQMT 395
Cdd:PRK08017 181 TRFT 184
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 215-392 1.68e-04

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: 42.76  E-value: 1.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 215 QRALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAA---RLGGRAVALDICAADAGQqlVEALPE----- 284
Cdd:cd05360   1 QVVVITGASSGIGRATALAFAERGAKVVLA----ARsaEALHELARevrELGGEAIAVVADVADAAQ--VERAADtaver 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 285 --GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:cd05360  75 fgRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKH 154

                       170       180       190
                ....*....|....*....|....*....|..
gi 15599980 363 GLIGLAQAWAPALGKRG--ITINAVAPGFIET 392
Cdd:cd05360 155 AVRGFTESLRAELAHDGapISVTLVQPTAMNT 186
PRK08278 PRK08278
SDR family oxidoreductase;
209-441 1.91e-04

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 42.97  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  209 SKPLAGQRALVTGAARGIGAAIAETLARDGAEVVLL---DVPPAReaLEGL---AAR----LGGRAVAL--DICAADAGQ 276
Cdd:PRK08278   1 MMSLSGKTLFITGASRGIGLAIALRAARDGANIVIAaktAEPHPK--LPGTihtAAEeieaAGGQALPLvgDVRDEDQVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  277 QLVEALPE---GVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLA-----SISGI 348
Cdd:PRK08278  79 AAVAKAVErfgGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSpplnlDPKWF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  349 AGNLGqsnYAVSKAGLIGLAQAWAPALGKRGITINAVAPgfiETQM-TAAipltIREAGRRMNSMSQGGLPQDVAETVAW 427
Cdd:PRK08278 159 APHTA---YTMAKYGMSLCTLGLAEEFRDDGIAVNALWP---RTTIaTAA----VRNLLGGDEAMRRSRTPEIMADAAYE 228

                        250
                 ....*....|....
gi 15599980  428 FAQPSSGAVSGQVL 441
Cdd:PRK08278 229 ILSRPAREFTGNFL 242
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 213-450 1.98e-04

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: 42.91  E-value: 1.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 213 AGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAR-EALEGLAARLG-GRAVAL--DICAADAGQQLVEALPEG--- 285
Cdd:cd08933   8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAgQALESELNRAGpGSCKFVpcDVTKEEDIKTLISVTVERfgr 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 VDIVVHNAGI-TRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:cd08933  88 IDCLVNNAGWhPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLR-KSQGNIINLSSLVGSIGQKQAAPYVATKGAI 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 365 IGLAQAWAPALGKRGITINAVAPGFIETQM-------TAAIPLTIREaGRRMNSMSQGGLPQDVAeTVAWFAQPSSGAVS 437
Cdd:cd08933 167 TAMTKALAVDESRYGVRVNCISPGNIWTPLweelaaqTPDTLATIKE-GELAQLLGRMGTEAESG-LAALFLAAEATFCT 244

                       250
                ....*....|...
gi 15599980 438 GQVLRVCGQSLLG 450
Cdd:cd08933 245 GIDLLLSGGAELG 257
PRK08177 PRK08177
SDR family oxidoreductase;
217-409 2.02e-04

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 42.71  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREalEGLAARLGGRAVALDICAADAGQQLVEALPEGV-DIVVHNAGI 295
Cdd:PRK08177   4 ALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQD--TALQALPGVHIEKLDMNDPASLDQLLQRLQGQRfDLLFVNAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  296 T--RDKTLAKMSSDFWNSVINVNLNAPQVLTQALLdgGKLHDNGRVvlLASISGIAGNLGQSN------YAVSKAGLIGL 367
Cdd:PRK08177  82 SgpAHQSAADATAAEIGQLFLTNAIAPIRLARRLL--GQVRPGQGV--LAFMSSQLGSVELPDggemplYKASKAALNSM 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15599980  368 AQAWAPALGKRGITINAVAPGFIETQM-TAAIPLTIREAGRRM 409
Cdd:PRK08177 158 TRSFVAELGEPTLTVLSMHPGWVKTDMgGDNAPLDVETSVKGL 200
PRK06194 PRK06194
hypothetical protein; Provisional
 210-370 2.62e-04

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 42.70  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  210 KPLAGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPParEALEGLAARL---GGRAVALDICAADAGQqlVEALPEG- 285
Cdd:PRK06194   2 KDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQ--DALDRAVAELraqGAEVLGVRTDVSDAAQ--VEALADAa 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 ------VDIVVHNAGITRDKTLAKMSSDFWNSVINVNL----NAPQVLTQALLDGGK--LHDNGRVVLLASISGIAGNLG 353
Cdd:PRK06194  78 lerfgaVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLwgviHGVRAFTPLMLAAAEkdPAYEGHIVNTASMAGLLAPPA 157

                        170
                 ....*....|....*..
gi 15599980  354 QSNYAVSKAGLIGLAQA 370
Cdd:PRK06194 158 MGIYNVSKHAVVSLTET 174
PRK06914 PRK06914
SDR family oxidoreductase;
234-430 3.08e-04

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 42.32  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  234 LARDGAEVVL-LDVPPAREALEGLAARLGG----RAVALDICAADAGQ--QLVEALPEGVDIVVHNAGITRDKTLAKMSS 306
Cdd:PRK06914  23 LAKKGYLVIAtMRNPEKQENLLSQATQLNLqqniKVQQLDVTDQNSIHnfQLVLKEIGRIDLLVNNAGYANGGFVEEIPV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  307 DFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVA 386
Cdd:PRK06914 103 EEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYALEGFSESLRLELKPFGIDVALIE 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980  387 PGFIET-------QMTAAIPLTIREAGRRMNSMSQ--------GGLPQDVAETVAWFAQ 430
Cdd:PRK06914 183 PGSYNTniwevgkQLAENQSETTSPYKEYMKKIQKhinsgsdtFGNPIDVANLIVEIAE 241
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 214-438 6.64e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 41.20  E-value: 6.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  214 GQRALVTGAARGIGAAIAETLARDGAEVVLldvpPAR--EALEGLAARL---GGRA--VALDICAADAGQQLVEALPEG- 285
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVI----TGRtkEKLEEAKLEIeqfPGQVltVQMDVRNPEDVQKMVEQIDEKf 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  286 --VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQAL-----LDGGKlhdnGRVV-LLASISGIAGnLGQSNY 357
Cdd:PRK07677  77 grIDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVgkywiEKGIK----GNIInMVATYAWDAG-PGVIHS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  358 AVSKAGLIGLAQAWAPALGKR-GITINAVAPGFIETQMTAAIPLTIREAGRR-MNSMSQG--GLPQDVAETVAWFAQPSS 433
Cdd:PRK07677 152 AAAKAGVLAMTRTLAVEWGRKyGIRVNAIAPGPIERTGGADKLWESEEAAKRtIQSVPLGrlGTPEEIAGLAYFLLSDEA 231


                 ....*
gi 15599980  434 GAVSG 438
Cdd:PRK07677 232 AYING 236
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 216-397 1.45e-03

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: 40.17  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 216 RALVTGAARGIGAAIAETLARDGAEVVLLDVPPAR-----EALEGLAARLGGRAVALDICAADAGQqlVEALPEgVDIVV 290
Cdd:cd08951   9 RIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRaadakAACPGAAGVLIGDLSSLAETRKLADQ--VNAIGR-FDAVI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 291 HNAGITRDKTLaKMSSDFWNSVINVNLNAPQVLTqALLDGGK--------LHDNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:cd08951  86 HNAGILSGPNR-KTPDTGIPAMVAVNVLAPYVLT-ALIRRPKrliylssgMHRGGNASLDDIDWFNRGENDSPAYSDSKL 163

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15599980 363 GLIGLAQAWAPALGKrgITINAVAPGFIETQMTAA 397
Cdd:cd08951 164 HVLTLAAAVARRWKD--VSSNAVHPGWVPTKMGGA 196
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 268-380 1.66e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) 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 consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis 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-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP 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 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: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 40.51  E-value: 1.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 268 DICAADAGQQLVEALPEGVDI--VVHNAGITRDKTLAKMSSDFWNSVinvnlNAPQVLTQALLD------GGKLhDNgrV 339
Cdd:cd08954 282 DVSSLEKAINLILNAPKIGPIggIFHLAFVLIDKVLEIDTESLFISV-----NKAKVMGAINLHnqsikrCWKL-DY--F 353

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15599980 340 VLLASISGIAGNLGQSNY--------AVSKA----GLIGLAQAWaPALGKRGI 380
Cdd:cd08954 354 VLFSSVSSIRGSAGQCNYvcansvldSLSRYrksiGLPSIAINW-GAIGDVGF 405
PRK05854 PRK05854
SDR family oxidoreductase;
212-417 1.89e-03

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 40.05  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLldvpPAREALEGLAARLGGRAVA---------LDICA----ADAGQQL 278
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVIL----PVRNRAKGEAAVAAIRTAVpdaklslraLDLSSlasvAALGEQL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  279 V-EALPegVDIVVHNAGI----TRDKTLAKMSSDF-WNSVINVNLNApQVLtqALLDGGklhdNGRVVLLASISGIAGNL 352
Cdd:PRK05854  88 RaEGRP--IHLLINNAGVmtppERQTTADGFELQFgTNHLGHFALTA-HLL--PLLRAG----RARVTSQSSIAARRGAI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  353 ------------GQSNYAVSK--AGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPLTIREAG----RRMNSMSQ 414
Cdd:PRK05854 159 nwddlnwersyaGMRAYSQSKiaVGLFALELDRRSRAAGWGITSNLAHPGVAPTNLLAARPEVGRDKDtlmvRLIRSLSA 238


                 ...
gi 15599980  415 GGL 417
Cdd:PRK05854 239 RGF 241
PRK06101 PRK06101
SDR family oxidoreductase;
265-402 2.10e-03

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 39.47  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  265 VALDICAADAGQQLVEALPEGVDIVVHNAGITRDKTLAKMSSDFWNSVINVNLnapqVLTQALLDGGKLH-DNG-RVVLL 342
Cdd:PRK06101  51 LAFDVTDHPGTKAALSQLPFIPELWIFNAGDCEYMDDGKVDATLMARVFNVNV----LGVANCIEGIQPHlSCGhRVVIV 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599980  343 ASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTA----AIPLTI 402
Cdd:PRK06101 127 GSIASELALPRAEAYGASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDkntfAMPMII 190
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 214-445 2.44e-03

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: 39.23  E-value: 2.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 214 GQRALVTGAARGIGAAIAETLARDGAEVVLLDVPPAREALEGLAArlggRAVALDICAADAGQQLVEALPEGVDIVVHNA 293
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEADASIIV----LDSDSFTEQAKQVVASVARLSGKVDALICVA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 294 G-----ITRDKTLAKMssdfWNSVINVNLN----APQVLTQALLDGgklhdnGRVVLLASISGIAGNLGQSNYAVSKAGL 364
Cdd:cd05334  77 GgwaggSAKSKSFVKN----WDLMWKQNLWtsfiASHLATKHLLSG------GLLVLTGAKAALEPTPGMIGYGAAKAAV 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 365 IGLAQAWAPALG--KRGITINAVAPGFIETQMTaaipltiREAGRRMNsMSQGGLPQDVAETVAWFAQPSSGAVSGQVLR 442
Cdd:cd05334 147 HQLTQSLAAENSglPAGSTANAILPVTLDTPAN-------RKAMPDAD-FSSWTPLEFIAELILFWASGAARPKSGSLIP 218


                ...
gi 15599980 443 VCG 445
Cdd:cd05334 219 VVT 221
PRK05693 PRK05693
SDR family oxidoreductase;
217-393 2.53e-03

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 39.77  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVvlldVPPAREA--LEGLAARlGGRAVALDICAADAGQQLVEALPE---GVDIVVH 291
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEV----WATARKAedVEALAAA-GFTAVQLDVNDGAALARLAEELEAehgGLDVLIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  292 NAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKlHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAW 371
Cdd:PRK05693  79 NAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLR-RSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDAL 157

                        170       180
                 ....*....|....*....|..
gi 15599980  372 APALGKRGITINAVAPGFIETQ 393
Cdd:PRK05693 158 RLELAPFGVQVMEVQPGAIASQ 179
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 257-443 2.92e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 38.64  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  257 AARLGGrAVALDICAADAGQQLVEALPEgVDIVVHNAGITRDKTLAKMSSDFWNSVIN------VNLnapqvltqALLDG 330
Cdd:PRK07578  29 AGRSSG-DVQVDITDPASIRALFEKVGK-VDAVVSAAGKVHFAPLAEMTDEDFNVGLQsklmgqVNL--------VLIGQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  331 GKLHDNGRVVLlasISGIAGN---LGQSNYAVSKAGLIGLAQAWAPALgKRGITINAVAPGFIEtqmtaaipltirEAGR 407
Cdd:PRK07578  99 HYLNDGGSFTL---TSGILSDepiPGGASAATVNGALEGFVKAAALEL-PRGIRINVVSPTVLT------------ESLE 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15599980  408 RMNSMSQGGLPQDVAETVAWFAQPSSGAVSGQVLRV 443
Cdd:PRK07578 163 KYGPFFPGFEPVPAARVALAYVRSVEGAQTGEVYKV 198
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 213-388 3.42e-03

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 39.16  E-value: 3.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  213 AGQRALVTGAARGIGAAIAETLARDGAEVVLLDVPP-AREALEGLAArLGGRAVAL--DICAADAGQQLVEALPE---GV 286
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSElVHEVAAELRA-AGGEALALtaDLETYAGAQAAMAAAVEafgRI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIVVHNAGIT-RDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVllaSISGIA-GNLGQSNYAVSKAGL 364
Cdd:PRK12823  86 DVLINNVGGTiWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIV---NVSSIAtRGINRVPYSAAKGGV 162

                        170       180
                 ....*....|....*....|....
gi 15599980  365 IGLAQAWAPALGKRGITINAVAPG 388
Cdd:PRK12823 163 NALTASLAFEYAEHGIRVNAVAPG 186
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 212-400 3.81e-03

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: 38.99  E-value: 3.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 212 LAGQRALVTGAARGIGAAIAETLARDGAEVVLLdvppAR--EALEGLAARLGG-RAVALDICAADAGQQLVEALPE---G 285
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIIT----GRreEKLEEAAAANPGlHTIVLDVADPASIAALAEQVTAefpD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 VDIVVHNAGITRDKTLAKmSSDFWNSV---INVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKA 362
Cdd:COG3967  79 LNVLINNAGIMRAEDLLD-EAEDLADAereITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKA 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15599980 363 GLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIPL 400
Cdd:COG3967 158 ALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGG 195
PRK06482 PRK06482
SDR family oxidoreductase;
218-398 4.12e-03

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 38.94  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  218 LVTGAARGIGAAIAETLARDGAEVVLLDVPPAreALEGLAARLGGR--AVALDICAADAGQQLVE---ALPEGVDIVVHN 292
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRVAATVRRPD--ALDDLKARYGDRlwVLQLDVTDSAAVRAVVDrafAALGRIDVVVSN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  293 AGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWA 372
Cdd:PRK06482  84 AGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAVA 163

                        170       180
                 ....*....|....*....|....*.
gi 15599980  373 PALGKRGITINAVAPGFIETQMTAAI 398
Cdd:PRK06482 164 QEVAPFGIEFTIVEPGPARTNFGAGL 189
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
 250-369 4.90e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); 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 consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis 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. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. 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: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 39.17  E-value: 4.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 250 REALEGLAARLggRAVALDICAADAGQQLVEALPEGVDI--VVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQAL 327
Cdd:cd08956 239 VAELAALGAEV--TVAACDVADRAALAALLAAVPADHPLtaVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWHLHELT 316

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15599980 328 LDggklHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQ 369
Cdd:cd08956 317 RD----LDLAAFVLFSSAAGVLGSPGQANYAAANAFLDALAQ 354
PRK07775 PRK07775
SDR family oxidoreductase;
211-399 4.94e-03

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 38.58  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  211 PLAGQR-ALVTGAARGIGAAIAETLARDGAEVVLldvpPAR--EALEGLAARL---GGRAVA--LDICAADAGQQLVEAL 282
Cdd:PRK07775   6 PHPDRRpALVAGASSGIGAATAIELAAAGFPVAL----GARrvEKCEELVDKIradGGEAVAfpLDVTDPDSVKSFVAQA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  283 PEG---VDIVVHNAGITRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAV 359
Cdd:PRK07775  82 EEAlgeIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15599980  360 SKAGLIGLAQAWAPALGKRGITINAVAPGFIETQMTAAIP 399
Cdd:PRK07775 162 AKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWSLP 201
PRK07041 PRK07041
SDR family oxidoreductase;
227-445 5.35e-03

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 38.48  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  227 GAAIAETLARDGAEVVLLDVPPAR--EALEGLAARLGGRAVALDICAADAGQQLVEALPEgVDIVVHNAGITRDKTLAKM 304
Cdd:PRK07041  10 GLALARAFAAEGARVTIASRSRDRlaAAARALGGGAPVRTAALDITDEAAVDAFFAEAGP-FDHVVITAADTPGGPVRAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  305 SSDFWNSVINVNLNAPQVLTQALldggKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAWAPALGKrgITINA 384
Cdd:PRK07041  89 PLAAAQAAMDSKFWGAYRVARAA----RIAPGGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLALELAP--VRVNT 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599980  385 VAPGFIETQMTAAIPLTIREAgrRMNSMSQG------GLPQDVAETVAWFAqpSSGAVSGQVLRVCG 445
Cdd:PRK07041 163 VSPGLVDTPLWSKLAGDAREA--MFAAAAERlparrvGQPEDVANAILFLA--ANGFTTGSTVLVDG 225
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
217-398 5.82e-03

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 38.51  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  217 ALVTGAARGIGAAIAETLARDGAEVVLLdvppAREALEGLAARLGGRAVALDICAAD------AGQQLVEAL----PEGV 286
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVISI----SRTENKELTKLAEQYNSNLTFHSLDlqdvheLETNFNEILssiqEDNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  287 DIV--VHNAGI-TRDKTLAKMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASiSGIAGNL--GQSNYAVSK 361
Cdd:PRK06924  80 SSIhlINNAGMvAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVDKRVINIS-SGAAKNPyfGWSAYCSSK 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15599980  362 AGL------IGLAQawapALGKRGITINAVAPGFIETQMTAAI 398
Cdd:PRK06924 159 AGLdmftqtVATEQ----EEEEYPVKIVAFSPGVMDTNMQAQI 197
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 218-429 7.81e-03

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 37.81  E-value: 7.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  218 LVTGAARGIGAAIAETLARDGAEVVLLDVPPAReaLEGLAARLGGR--AVALDICAADAGQQLVEALPEG---VDIVVHN 292
Cdd:PRK10538   4 LVTGATAGFGECITRRFIQQGHKVIATGRRQER--LQELKDELGDNlyIAQLDVRNRAAIEEMLASLPAEwrnIDVLVNN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980  293 AGITRDKTLA-KMSSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLGQSNYAVSKAGLIGLAQAW 371
Cdd:PRK10538  82 AGLALGLEPAhKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15599980  372 APALGKRGITINAVAPGFIE-TQMTAAIPLTIREAGRRMNSMSQGGLPQDVAETVAWFA 429
Cdd:PRK10538 162 RTDLHGTAVRVTDIEPGLVGgTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVA 220
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 214-394 8.24e-03

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: 37.83  E-value: 8.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 214 GQRALVTGAARGIGAAIAETLARDGAEVVLL--DVPPAREALEGLAARLGGRAV---ALDICAADAGQQLVE---ALPEG 285
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMAcrDMAKCEEAAAEIRRDTLNHEVivrHLDLASLKSIRAFAAeflAEEDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599980 286 VDIVVHNAGITR---DKTlakmsSDFWNSVINVNLNAPQVLTQALLDGGKLHDNGRVVLLASISGIAGNLG----QSN-- 356
Cdd:cd09807  81 LDVLINNAGVMRcpySKT-----EDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINfddlNSEks 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15599980 357 ------YAVSKAGLIGLAQAWAPALGKRGITINAVAPGFIETQM 394
Cdd:cd09807 156 yntgfaYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
 
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.
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