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Conserved domains on  [gi|99030931|ref|NP_014197|]
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2,4-dienoyl-CoA reductase (NADPH) [Saccharomyces cerevisiae S288C]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143283)

atypical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase that 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, similar to human peroxisomal 2,4-dienoyl-CoA reductase, an auxiliary enzyme of beta-oxidation that catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0070403|GO:0016491
PubMed:  12604210|19011750|19011748|19027726|20423462
SCOP:  4000029

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 22-270 4.19e-124

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: 354.20  E-value: 4.19e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkdkDAVLAIANVDVRNFEQVENAVKKTVE 101
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSAT---GGRAHPIQCDVRDPEAVEAAVDETLK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYYGVPFQGHVGAA 179
Cdd:cd05369  78 EFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKhgGSILNISATYAYTGSPFQVHSAAA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKE-KALAKIPLQRLGSTRDIAESTVYIFSPAASYVT 258
Cdd:cd05369 158 KAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEkKMIERVPLGRLGTPEEIANLALFLLSDAASYIN 237

                       250
                ....*....|..
gi 99030931 259 GTVLVVDGGMWH 270
Cdd:cd05369 238 GTTLVVDGGQWL 249
 
Name Accession Description Interval E-value
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 22-270 4.19e-124

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: 354.20  E-value: 4.19e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkdkDAVLAIANVDVRNFEQVENAVKKTVE 101
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSAT---GGRAHPIQCDVRDPEAVEAAVDETLK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYYGVPFQGHVGAA 179
Cdd:cd05369  78 EFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKhgGSILNISATYAYTGSPFQVHSAAA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKE-KALAKIPLQRLGSTRDIAESTVYIFSPAASYVT 258
Cdd:cd05369 158 KAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEkKMIERVPLGRLGTPEEIANLALFLLSDAASYIN 237

                       250
                ....*....|..
gi 99030931 259 GTVLVVDGGMWH 270
Cdd:cd05369 238 GTTLVVDGGQWL 249
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 22-272 1.64e-87

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 261.81  E-value: 1.64e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVE 101
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSA----DVRDYAAVEAAFAQIAD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK07576  83 EFGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVPMPMQAHVCAAKA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAK-IPLQRLGSTRDIAESTVYIFSPAASYVTGT 260
Cdd:PRK07576 163 GVDMLTRTLALEWGPEGIRVNSIVPGPIAGTEGMARLAPSPELQAAVAQsVPLKRNGTKQDIANAALFLASDMASYITGV 242

                        250
                 ....*....|..
gi 99030931  261 VLVVDGGmWHLG 272
Cdd:PRK07576 243 VLPVDGG-WSLG 253
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 20-268 1.89e-70

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: 218.12  E-value: 1.89e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  20 DLFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgisQLAKDKDAVLAIAnVDVRNFEQVENAVKKT 99
Cdd:COG1028   2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAA---ELRAAGGRALAVA-ADVTDEAAVEALVAAA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 100 VEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGA 178
Cdd:COG1028  78 VAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGQAAYAA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGK-KYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:COG1028 158 SKAAVVGLTRSLALELAPRGIRVNAVAPGPID-TPMTRALLGAeEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYI 236

                       250
                ....*....|.
gi 99030931 258 TGTVLVVDGGM 268
Cdd:COG1028 237 TGQVLAVDGGL 247
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 42-268 1.30e-56

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: 182.25  E-value: 1.30e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931    42 EALVLLGCKAAIVGRDQERTEQAAKgisqLAKDKDAvlAIANVDVRNFEQVENAVKKTVEKFGKIDFVI--AGAAGNFVC 119
Cdd:pfam13561  14 RALAEEGAEVVLTDLNEALAKRVEE----LAEELGA--AVLPCDVTDEEQVEALVAAAVEKFGRLDILVnnAGFAPKLKG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   120 DFANLSPNAFKSVVDIDLLGSFNTAKACLKeLKKSKGSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGI 199
Cdd:pfam13561  88 PFLDTSREDFDRALDVNLYSLFLLAKAALP-LMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGI 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   200 RSNCIAPGAIDnTEGLKRLAG-KKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:pfam13561 167 RVNAISPGPIK-TLAASGIPGfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
fabG_rel TIGR01831
3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well ...
 85-268 1.18e-18

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


Pssm-ID: 273825 [Multi-domain]  Cd Length: 239  Bit Score: 83.03  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931    85 DVRNFEQVENAVKKTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVS 162
Cdd:TIGR01831  56 DVADRVACREVLEADIAQHGAYYGVVLNAGIARDAAFPALSEDDWDAVIHTNLDGFYNVIHPCIMPMIGARqgGRIITLA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   163 ATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLagKKYKEKALAKIPLQRLGSTRDI 242
Cdd:TIGR01831 136 SVSGVMGNRGQVNYSAAKAGLIGATKALAIELAKRKITVNCIAPGLID-TGMIAME--ESALKEALSMVPMKRMGQPEEV 212

                         170       180
                  ....*....|....*....|....*.
gi 99030931   243 AESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:TIGR01831 213 AGLASFLMSDIAGYVTRQVISVNGGM 238
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 29-187 4.62e-05

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: 43.24  E-value: 4.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931     29 VTGGAGTICRVQTEALVLLGCKA-AIVGRDQERTEQAAKGISQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKFGKID 107
Cdd:smart00822   5 ITGGLGGLGRALARWLAERGARRlVLLSRSGPDAPGAAALLAELEAAGARVTVVA-CDVADRDALAAVLAAIPAVEGPLT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931    108 FVI--AGAAGNFVcdFANLSPNAFKSVVDIDLLGSFNTAKACL-KELKkskgsiLFV-----SATFhyyGVPFQGHVGAA 179
Cdd:smart00822  84 GVIhaAGVLDDGV--LASLTPERFAAVLAPKAAGAWNLHELTAdLPLD------FFVlfssiAGVL---GSPGQANYAAA 152


                   ....*...
gi 99030931    180 KAGIDALA 187
Cdd:smart00822 153 NAFLDALA 160
 
Name Accession Description Interval E-value
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 22-270 4.19e-124

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: 354.20  E-value: 4.19e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkdkDAVLAIANVDVRNFEQVENAVKKTVE 101
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSAT---GGRAHPIQCDVRDPEAVEAAVDETLK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYYGVPFQGHVGAA 179
Cdd:cd05369  78 EFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKhgGSILNISATYAYTGSPFQVHSAAA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKE-KALAKIPLQRLGSTRDIAESTVYIFSPAASYVT 258
Cdd:cd05369 158 KAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEkKMIERVPLGRLGTPEEIANLALFLLSDAASYIN 237

                       250
                ....*....|..
gi 99030931 259 GTVLVVDGGMWH 270
Cdd:cd05369 238 GTTLVVDGGQWL 249
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 22-272 1.64e-87

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 261.81  E-value: 1.64e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVE 101
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSA----DVRDYAAVEAAFAQIAD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK07576  83 EFGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVPMPMQAHVCAAKA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAK-IPLQRLGSTRDIAESTVYIFSPAASYVTGT 260
Cdd:PRK07576 163 GVDMLTRTLALEWGPEGIRVNSIVPGPIAGTEGMARLAPSPELQAAVAQsVPLKRNGTKQDIANAALFLASDMASYITGV 242

                        250
                 ....*....|..
gi 99030931  261 VLVVDGGmWHLG 272
Cdd:PRK07576 243 VLPVDGG-WSLG 253
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 20-268 1.89e-70

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: 218.12  E-value: 1.89e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  20 DLFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgisQLAKDKDAVLAIAnVDVRNFEQVENAVKKT 99
Cdd:COG1028   2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAA---ELRAAGGRALAVA-ADVTDEAAVEALVAAA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 100 VEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGA 178
Cdd:COG1028  78 VAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGQAAYAA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGK-KYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:COG1028 158 SKAAVVGLTRSLALELAPRGIRVNAVAPGPID-TPMTRALLGAeEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYI 236

                       250
                ....*....|.
gi 99030931 258 TGTVLVVDGGM 268
Cdd:COG1028 237 TGQVLAVDGGL 247
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 24-269 1.21e-61

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 195.67  E-value: 1.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLakdkDAVLAIANVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQF----PGQVLTVQMDVRNPEDVQKMVEQIDEKF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL--KKSKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK07677  77 GRIDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWieKGIKGNIINMVATYAWDAGPGVIHSAAAKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  182 GIDALAKNLAVELG-PLGIRSNCIAPGAIDNTEGLKRLA-GKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:PRK07677 157 GVLAMTRTLAVEWGrKYGIRVNAIAPGPIERTGGADKLWeSEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYING 236

                        250
                 ....*....|
gi 99030931  260 TVLVVDGGMW 269
Cdd:PRK07677 237 TCITMDGGQW 246
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
21-268 7.79e-60

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 190.76  E-value: 7.79e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   21 LFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKdavlAIANVDVRNFEQVENAVKKTV 100
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEA----RVLVFDVSDEAAVRALIEAAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  101 EKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPFQGHVGAA 179
Cdd:PRK05653  78 EAFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKArYGRIVNISSVSGVTGNPGQTNYSAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLaGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:PRK05653 158 KAGVIGFTKALALELASRGITVNAVAPGFID-TDMTEGL-PEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITG 235


                 ....*....
gi 99030931  260 TVLVVDGGM 268
Cdd:PRK05653 236 QVIPVNGGM 244
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 27-265 2.05e-59

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: 189.42  E-value: 2.05e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  27 AFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgisqLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKFGKI 106
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAA----IEALGGNAVAVQ-ADVSDEEDVEALVEEALEEFGRL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 107 DFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAGIDA 185
Cdd:cd05233  76 DILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPLPGQAAYAASKAALEG 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 186 LAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVD 265
Cdd:cd05233 156 LTRSLALELAPYGIRVNAVAPGLVD-TPMLAKLGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 42-268 1.30e-56

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: 182.25  E-value: 1.30e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931    42 EALVLLGCKAAIVGRDQERTEQAAKgisqLAKDKDAvlAIANVDVRNFEQVENAVKKTVEKFGKIDFVI--AGAAGNFVC 119
Cdd:pfam13561  14 RALAEEGAEVVLTDLNEALAKRVEE----LAEELGA--AVLPCDVTDEEQVEALVAAAVEKFGRLDILVnnAGFAPKLKG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   120 DFANLSPNAFKSVVDIDLLGSFNTAKACLKeLKKSKGSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGI 199
Cdd:pfam13561  88 PFLDTSREDFDRALDVNLYSLFLLAKAALP-LMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGI 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   200 RSNCIAPGAIDnTEGLKRLAG-KKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:pfam13561 167 RVNAISPGPIK-TLAASGIPGfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
PRK12826 PRK12826
SDR family oxidoreductase;
22-268 6.24e-54

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 175.88  E-value: 6.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQErteQAAKGISQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGD---DAAATAELVEAAGGKARARQ-VDVRDRAALKAAVAAGVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFV-SATFHYYGVPFQGHVGAA 179
Cdd:PRK12826  80 DFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTsSVAGPRVGYPGLAHYAAS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:PRK12826 160 KAGLVGFTRALALELAARNITVNSVHPGGVD-TPMAGNLGDAQWAEAIAAAIPLGRLGEPEDIAAAVLFLASDEARYITG 238


                 ....*....
gi 99030931  260 TVLVVDGGM 268
Cdd:PRK12826 239 QTLPVDGGA 247
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 22-268 5.34e-52

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 170.76  E-value: 5.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQER-TEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTV 100
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAgAEALVAEIGALGGKALAVQG----DVSDAESVERAVDEAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  101 EKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAA 179
Cdd:PRK05557  79 AEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMGNPGQANYAAS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  180 KAGIDALAKNLAVELGPLGIRSNCIAPGAI--DNTEGLKrlagKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:PRK05557 159 KAGVIGFTKSLARELASRGITVNAVAPGFIetDMTDALP----EDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYI 234

                        250
                 ....*....|.
gi 99030931  258 TGTVLVVDGGM 268
Cdd:PRK05557 235 TGQTLHVNGGM 245
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 24-268 7.06e-50

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 165.43  E-value: 7.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGR-DQERTEQAAKgisQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEK 102
Cdd:PRK12825   6 GRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVE---AVEALGRRAQAVQ-ADVTDKAALEAAVAAAVER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK12825  82 FGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGRSNYAAAKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKyKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTV 261
Cdd:PRK12825 162 GLVGLTKALARELAEYGITVNMVAPGDID-TDMKEATIEEA-REAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQV 239


                 ....*..
gi 99030931  262 LVVDGGM 268
Cdd:PRK12825 240 IEVTGGV 246
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 23-282 6.84e-49

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: 162.94  E-value: 6.84e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGR-DQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVE 101
Cdd:cd05358   2 KGKVALVTGASSGIGKAIAIRLATAGANVVVNYRsKEDAAEEVVEEIKAVGGKAIAVQA----DVSKEEDVVALFQSAIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYygVPFQGHV--G 177
Cdd:cd05358  78 EFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKikGKIINMSSVHEK--IPWPGHVnyA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAGKKYKEKA-LAKIPLQRLGSTRDIAESTVYIFSPAASY 256
Cdd:cd05358 156 ASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAI-NTPINAEAWDDPEQRADlLSLIPMGRIGEPEEIAAAAAWLASDEASY 234

                       250       260
                ....*....|....*....|....*.
gi 99030931 257 VTGTVLVVDGGMwhlgtyfghELYPE 282
Cdd:cd05358 235 VTGTTLFVDGGM---------TLYPS 251
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 25-268 3.32e-48

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: 160.79  E-value: 3.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLaianVDVRNFEQVENAVKKTVEKFG 104
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALE----ADVSDREAVEALVEKVEAEFG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 105 KIDFVIAgAAG----NFvcdFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPFQGHVGAA 179
Cdd:cd05333  77 PVDILVN-NAGitrdNL---LMRMSEEDWDAVINVNLTGVFNVTQAVIRAmIKRRSGRIINISSVVGLIGNPGQANYAAS 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLaGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:cd05333 153 KAGVIGFTKSLAKELASRGITVNAVAPGFID-TDMTDAL-PEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITG 230


                ....*....
gi 99030931 260 TVLVVDGGM 268
Cdd:cd05333 231 QVLHVNGGM 239
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-268 1.56e-46

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 156.54  E-value: 1.56e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVG-RDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTV 100
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAVKA----DVSSEEDVENLVEQIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  101 EKFGKIDFVIAGAA-GNFVcDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPFQGHVGA 178
Cdd:PRK05565  79 EKFGKIDILVNNAGiSNFG-LVTDMTDEEWDRVIDVNLTGVMLLTRYALPYmIKRKSGVIVNISSIWGLIGASCEVLYSA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLagKKYKEKALAK-IPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:PRK05565 158 SKGAVNAFTKALAKELAPSGIRVNAVAPGAID-TEMWSSF--SEEDKEGLAEeIPLGRLGKPEEIAKVVLFLASDDASYI 234

                        250
                 ....*....|.
gi 99030931  258 TGTVLVVDGGM 268
Cdd:PRK05565 235 TGQIITVDGGW 245
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 22-267 8.13e-46

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: 154.80  E-value: 8.13e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlakdKDAVLAIA-NVDVRNFEQVENAVKKTV 100
Cdd:cd05352   6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAK----KYGVKTKAyKCDVSSQESVEKTFKQIQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 101 EKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFV-SATFHYYGVPF-QGHVG 177
Cdd:cd05352  82 KDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQgKGSLIITaSMSGTIVNRPQpQAAYN 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNteGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:cd05352 162 ASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDT--DLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYT 239

                       250
                ....*....|
gi 99030931 258 TGTVLVVDGG 267
Cdd:cd05352 240 TGSDLIIDGG 249
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 22-267 1.69e-44

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 151.75  E-value: 1.69e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkdkdaVLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:PRK12829   9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAK-----VTATV-ADVADPAQVERVFDTAVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAaGNFVCDFA--NLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYYGVPFQGHVG 177
Cdd:PRK12829  83 RFGGLDVLVNNA-GIAGPTGGidEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhgGVIIALSSVAGRLGYPGRTPYA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKA----------LAKIPLQRLGSTRDIAESTV 247
Cdd:PRK12829 162 ASKWAVVGLVKSLAIELGPLGIRVNAILPGIVR-GPRMRRVIEARAQQLGigldemeqeyLEKISLGRMVEPEDIAATAL 240

                        250       260
                 ....*....|....*....|
gi 99030931  248 YIFSPAASYVTGTVLVVDGG 267
Cdd:PRK12829 241 FLASPAARYITGQAISVDGN 260
FabG-like PRK07231
SDR family oxidoreductase;
21-268 1.03e-43

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 149.21  E-value: 1.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   21 LFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISqlakDKDAVLAIAnVDVRNFEQVENAVKKTV 100
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEIL----AGGRAIAVA-ADVSDEADVEAAVAAAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  101 EKFGKIDFVIAGAAGNFVCD-FANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGA 178
Cdd:PRK07231  77 ERFGSVDILVNNAGTTHRNGpLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGLRPRPGLGWYNA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKE---KALAKIPLQRLGSTRDIAESTVYIFSPAAS 255
Cdd:PRK07231 157 SKGAVITLTKALAAELGPDKIRVNAVAPVVVE-TGLLEAFMGEPTPEnraKFLATIPLGRLGTPEDIANAALFLASDEAS 235

                        250
                 ....*....|...
gi 99030931  256 YVTGTVLVVDGGM 268
Cdd:PRK07231 236 WITGVTLVVDGGR 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 25-210 3.41e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 146.22  E-value: 3.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931    25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgisQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKFG 104
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAK---ELGALGGKALFIQ-GDVTDRAQVKALVEQAVERLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   105 KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKK-SKGSILFVSATFHYYGVPFQGHVGAAKAGI 183
Cdd:pfam00106  77 RLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKgSGGRIVNISSVAGLVPYPGGSAYSASKAAV 156

                         170       180
                  ....*....|....*....|....*..
gi 99030931   184 DALAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVD 183
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 23-263 6.07e-42

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: 144.55  E-value: 6.07e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISqlakdkDAVLAIAnVDVRNFEQVENAVKKTVEK 102
Cdd:COG4221   4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELG------GRALAVP-LDVTDEAAVEAAVAAAVAE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:COG4221  77 FGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGsGHIVNISSIAGLRPYPGGAVYAATKA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 182 GIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAKIPLQRLgSTRDIAESTVYIFSPAASYVTGTV 261
Cdd:COG4221 157 AVRGLSESLRAELRPTGIRVTVIEPGAVD-TEFLDSVFDGDAEAAAAVYEGLEPL-TPEDVAEAVLFALTQPAHVNVNEL 234


                ..
gi 99030931 262 LV 263
Cdd:COG4221 235 VL 236
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 22-267 1.98e-41

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: 143.71  E-value: 1.98e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKILLVV-ADLTEEEGQDRIISTTLA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVS---ATFHYYGVPFqghVGA 178
Cdd:cd05364  80 KFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSsvaGGRSFPGVLY---YCI 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAI----DNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAA 254
Cdd:cd05364 157 SKAALDQFTRCTALELAPKGVRVNSVSPGVIvtgfHRRMGMPEEQYIKFLSRAKETHPLGRPGTVDEVAEAIAFLASDAS 236

                       250
                ....*....|...
gi 99030931 255 SYVTGTVLVVDGG 267
Cdd:cd05364 237 SFITGQLLPVDGG 249
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 24-268 6.75e-41

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: 142.03  E-value: 6.75e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgisQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKF 103
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAAS---ELRAGGAGVLAVV-ADLTDPEDIDRLVEKAGDAF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAG 182
Cdd:cd05344  77 GRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSNVARAG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 183 IDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLA----------GKKYKEKALAKIPLQRLGSTRDIAESTVYIFSP 252
Cdd:cd05344 157 LIGLVKTLSRELAPDGVTVNSVLPGYID-TERVRRLLearaekegisVEEAEKEVASQIPLGRVGKPEELAALIAFLASE 235

                       250
                ....*....|....*.
gi 99030931 253 AASYVTGTVLVVDGGM 268
Cdd:cd05344 236 KASYITGQAILVDGGL 251
PRK07774 PRK07774
SDR family oxidoreductase;
22-267 1.65e-40

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 141.04  E-value: 1.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISqlAKDKDAVLAiaNVDVRNFEQVENAVKKTVE 101
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIV--ADGGTAIAV--QVDVSDPDSAKAMADATVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAA--GNFVCDFA-NLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYygvPFQGHVG 177
Cdd:PRK07774  80 AFGGIDYLVNNAAiyGGMKLDLLiTVPWDYYKKFMSVNLDGALVCTRAVYKHMaKRGGGAIVNQSSTAAW---LYSNFYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:PRK07774 157 LAKVGLNGLTQQLARELGGMNIRVNAIAPGPID-TEATRTVTPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWI 235

                        250
                 ....*....|
gi 99030931  258 TGTVLVVDGG 267
Cdd:PRK07774 236 TGQIFNVDGG 245
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 27-267 2.50e-40

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: 140.18  E-value: 2.50e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  27 AFVTGGAGTICRVQTEALVLLGCKAAIVGR-DQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVEKFGK 105
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRkSKDAAAEVAAEIEELGGKAVVVRA----DVSQPQDVEEMFAAVKERFGR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 106 IDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAGID 184
Cdd:cd05359  77 LDVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGSIRALPNYLAVGTAKAALE 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 185 ALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKY-KEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLV 263
Cdd:cd05359 157 ALVRYLAVELGPRGIRVNAVSPGVID-TDALAHFPNREDlLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLV 235


                ....
gi 99030931 264 VDGG 267
Cdd:cd05359 236 VDGG 239
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 24-268 3.84e-40

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 140.24  E-value: 3.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGckAAIVGRDQE--RTEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVE 101
Cdd:PRK12827   6 SRRVLITGGSGGLGRAIAVRLAADG--ADVIVLDIHpmRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYYGVPFQGHVGAA 179
Cdd:PRK12827  84 EFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGVRGNRGQVNYAAS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAgkkYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:PRK12827 164 KAGLIGLTKTLANELAPRGITVNAVAPGAI-NTPMADNAA---PTEHLLNPVPVQRLGEPDEVAALVAFLVSDAASYVTG 239


                 ....*....
gi 99030931  260 TVLVVDGGM 268
Cdd:PRK12827 240 QVIPVDGGF 248
PRK06484 PRK06484
short chain dehydrogenase; Validated
 24-277 3.86e-38

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 140.75  E-value: 3.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQErteqAAKGISQLAKDKDAVLaiaNVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAE----GAKKLAEALGDEHLSV---QADITDEAAVESAFAQIQARW 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVI--AGAAGNFVcDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSkGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK06484 342 GRLDVLVnnAGIAEVFK-PSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPRNAYCASKA 419

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRL--AGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:PRK06484 420 AVTMLSRSLACEWAPAGIRVNTVAPGYIE-TPAVLALkaSGRADFDSIRRRIPLGRLGDPEEVAEAIAFLASPAASYVNG 498

                        250
                 ....*....|....*...
gi 99030931  260 TVLVVDGGMwhlgTYFGH 277
Cdd:PRK06484 499 ATLTVDGGW----TAFGD 512
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 23-268 7.99e-37

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: 131.33  E-value: 7.99e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLaianVDVRNFEQVENAVKKTVEK 102
Cdd:cd05347   4 KGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFT----CDVSDEEAIKAAVEAIEED 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:cd05347  80 FGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGhGKIINICSLLSELGGPPVPAYAASKG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 182 GIDALAKNLAVELGPLGIRSNCIAPG--AIDNTEGLKrlAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:cd05347 160 GVAGLTKALATEWARHGIQVNAIAPGyfATEMTEAVV--ADPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNG 237


                ....*....
gi 99030931 260 TVLVVDGGM 268
Cdd:cd05347 238 QIIFVDGGW 246
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 23-267 6.98e-36

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: 128.99  E-value: 6.98e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIanvDVRNFEQVENAVKKTVEK 102
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALEL---DITSKESIKELIESYLEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 103 FGKIDFVIAGAA-GNFVCD--FANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATF--------HYYGV 170
Cdd:cd08930  78 FGRIDILINNAYpSPKVWGsrFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQgKGSIINIASIYgviapdfrIYENT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 171 PFQGHV--GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLagKKYKEkalaKIPLQRLGSTRDIAESTVY 248
Cdd:cd08930 158 QMYSPVeySVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSEFL--EKYTK----KCPLKRMLNPEDLRGAIIF 231

                       250
                ....*....|....*....
gi 99030931 249 IFSPAASYVTGTVLVVDGG 267
Cdd:cd08930 232 LLSDASSYVTGQNLVIDGG 250
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 22-267 9.61e-36

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: 128.79  E-value: 9.61e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDkdAVLAIANVDVRNFEQVENAVKKTVE 101
Cdd:cd05330   1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPD--AEVLLIKADVSDEAQVEAYVDATVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKID--FVIAGAAG--NFVCDFanlSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHV 176
Cdd:cd05330  79 QFGRIDgfFNNAGIEGkqNLTEDF---GADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNQSGY 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDN---TEGLKRLAGKKYKEKALAKI---PLQRLGSTRDIAESTVYIF 250
Cdd:cd05330 156 AAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTpmvEGSLKQLGPENPEEAGEEFVsvnPMKRFGEPEEVAAVVAFLL 235

                       250
                ....*....|....*..
gi 99030931 251 SPAASYVTGTVLVVDGG 267
Cdd:cd05330 236 SDDAGYVNAAVVPIDGG 252
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 21-270 1.02e-35

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 128.92  E-value: 1.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   21 LFKGKVAFVTG-GAG---TICRVQTEAlvllGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAV 96
Cdd:PRK07890   2 LLKGKVVVVSGvGPGlgrTLAVRAARA----GADVVLAARTAERLDEVAAEIDDLGRRALAVPT----DITDEDQCANLV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   97 KKTVEKFGKIDFVIAGAA--GNFVcDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFV--SATFHyyGVPF 172
Cdd:PRK07890  74 ALALERFGRVDALVNNAFrvPSMK-PLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMInsMVLRH--SQPK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  173 QGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAI--DNTEGLKRLAGKK--------YKEKAlAKIPLQRLGSTRDI 242
Cdd:PRK07890 151 YGAYKMAKGALLAASQSLATELGPQGIRVNSVAPGYIwgDPLKGYFRHQAGKygvtveqiYAETA-ANSDLKRLPTDDEV 229

                        250       260
                 ....*....|....*....|....*...
gi 99030931  243 AESTVYIFSPAASYVTGTVLVVDGGMWH 270
Cdd:PRK07890 230 ASAVLFLASDLARAITGQTLDVNCGEYH 257
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 22-267 2.17e-35

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 128.48  E-value: 2.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVE 101
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKA----DVLDKESLEQARQQILE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNF---------------VCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATF 165
Cdd:PRK08277  84 DFGPCDILINGAGGNHpkattdnefheliepTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDmVGRKGGNIINISSMN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  166 HYygVPFQGHVG--AAKAGIDALAKNLAVELGPLGIRSNCIAPGAI--DNTEGLKRLAGKKYKEKA---LAKIPLQRLGS 238
Cdd:PRK08277 164 AF--TPLTKVPAysAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFltEQNRALLFNEDGSLTERAnkiLAHTPMGRFGK 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 99030931  239 TRDIAESTVYIFSP-AASYVTGTVLVVDGG 267
Cdd:PRK08277 242 PEELLGTLLWLADEkASSFVTGVVLPVDGG 271
PRK07326 PRK07326
SDR family oxidoreductase;
22-251 1.26e-34

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 125.51  E-value: 1.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKdkdaVLAIANvDVRNFEQVENAVKKTVE 101
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGN----VLGLAA-DVRDEADVQRAVDAIVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAA-GNFVcDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSAtfhYYGV-PFQGHVG-- 177
Cdd:PRK07326  79 AFGGLDVLIANAGvGHFA-PVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISS---LAGTnFFAGGAAyn 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEglkrLAGKKYKEKALAKIplqrlgSTRDIAESTVYIFS 251
Cdd:PRK07326 155 ASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVA-TH----FNGHTPSEKDAWKI------QPEDIAQLVLDLLK 217
PRK08628 PRK08628
SDR family oxidoreductase;
23-271 8.67e-34

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 123.92  E-value: 8.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDqERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVEK 102
Cdd:PRK08628   6 KDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRS-APDDEFAEELRALQPRAEFVQV----DLTDDAQCRDAVEQTVAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNfvcDFANL--SPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGvpfQGHVG--- 177
Cdd:PRK08628  81 FGRIDGLVNNAGVN---DGVGLeaGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTALTG---QGGTSgya 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPG-----AIDNTegLKRLAGKKYKEKAL-AKIPL-QRLGSTRDIAESTVYIF 250
Cdd:PRK08628 155 AAKGAQLALTREWAVALAKDGVRVNAVIPAevmtpLYENW--IATFDDPEAKLAAItAKIPLgHRMTTAEEIADTAVFLL 232

                        250       260
                 ....*....|....*....|.
gi 99030931  251 SPAASYVTGTVLVVDGGMWHL 271
Cdd:PRK08628 233 SERSSHTTGQWLFVDGGYVHL 253
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
22-210 9.26e-34

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 123.44  E-value: 9.26e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgisQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAA---ELRAAGARVEVVA-LDVTDPDAVAALAEAVLA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPFQGHVGAAK 180
Cdd:COG0300  79 RFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSSVAGLRGLPGMAAYAASK 158

                       170       180       190
                ....*....|....*....|....*....|
gi 99030931 181 AGIDALAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:COG0300 159 AALEGFSESLRAELAPTGVRVTAVCPGPVD 188
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 22-267 8.11e-33

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: 121.41  E-value: 8.11e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDkdaVLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGR---AIALA-ADVLDRASLERAREEIVA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGN--------------FVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFH 166
Cdd:cd08935  79 QFGTVDILINGAGGNhpdattdpehyepeTEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDmLEQKGGSIINISSMNA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 167 YygVPFQGHVG--AAKAGIDALAKNLAVELGPLGIRSNCIAPG---------AIDNTEGLKRLAGKkykeKALAKIPLQR 235
Cdd:cd08935 159 F--SPLTKVPAysAAKAAVSNFTQWLAVEFATTGVRVNAIAPGffvtpqnrkLLINPDGSYTDRSN----KILGRTPMGR 232

                       250       260       270
                ....*....|....*....|....*....|...
gi 99030931 236 LGSTRDIAESTVYIFS-PAASYVTGTVLVVDGG 267
Cdd:cd08935 233 FGKPEELLGALLFLASeKASSFVTGVVIPVDGG 265
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
18-267 1.00e-32

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 126.88  E-value: 1.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   18 RPDLFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlakdKDAVLAIAnVDVRNFEQVENAVK 97
Cdd:PRK08324 416 KPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGG----PDRALGVA-CDVTDEAAVQAAFE 490

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDFVI--AGAAgnFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILF-VSATFHYYGVPF 172
Cdd:PRK08324 491 EAALAFGGVDIVVsnAGIA--ISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlgGSIVFiASKNAVNPGPNF 568

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  173 QGHvGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLkrLAGKKYKEKALA-KIPLQRLGST------------ 239
Cdd:PRK08324 569 GAY-GAAKAAELHLVRQLALELGPDGIRVNGVNPDAVVRGSGI--WTGEWIEARAAAyGLSEEELEEFyrarnllkrevt 645

                        250       260
                 ....*....|....*....|....*....
gi 99030931  240 -RDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK08324 646 pEDVAEAVVFLASGLLSKTTGAIITVDGG 674
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 19-267 1.32e-32

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 120.72  E-value: 1.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   19 PDLFK--GKVAFVTGGAGTICRVQTEALVLLGckAAIVGRD--QERTEQAAKGISQLAKDKDAVlaiaNVDVRNFEQVEN 94
Cdd:PRK06113   4 SDNLRldGKCAIITGAGAGIGKEIAITFATAG--ASVVVSDinADAANHVVDEIQQLGGQAFAC----RCDITSEQELSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   95 AVKKTVEKFGKIDFVIAGAAGNFVCDFaNLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKG-SILFVSATFHYYGVPFQ 173
Cdd:PRK06113  78 LADFALSKLGKVDILVNNAGGGGPKPF-DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGgVILTITSMAAENKNINM 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  174 GHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPA 253
Cdd:PRK06113 157 TSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAI-LTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPA 235

                        250
                 ....*....|....
gi 99030931  254 ASYVTGTVLVVDGG 267
Cdd:PRK06113 236 ASWVSGQILTVSGG 249
PRK06138 PRK06138
SDR family oxidoreductase;
23-267 1.68e-32

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 120.26  E-value: 1.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgiSQLAKDKDAVLAIAnvDVRNFEQVENAVKKTVEK 102
Cdd:PRK06138   4 AGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVA---AAIAAGGRAFARQG--DVGSAEAVEALVDFVAAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK06138  79 WGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTASQLALAGGRGRAAYVASKG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAID---NTEGLKRLAG-KKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:PRK06138 159 AIASLTRAMALDHATDGIRVNAVAPGTIDtpyFRRIFARHADpEALREALRARHPMNRFGTAEEVAQAALFLASDESSFA 238

                        250
                 ....*....|
gi 99030931  258 TGTVLVVDGG 267
Cdd:PRK06138 239 TGTTLVVDGG 248
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 23-267 1.99e-32

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 119.52  E-value: 1.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVlaianvDVRNFEQVENAVKKTVEK 102
Cdd:PRK12828   6 QGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGI------DLVDPQAARRAVDEVNRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAgAAGNFVCD-FANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAK 180
Cdd:PRK12828  80 FGRLDALVN-IAGAFVWGtIADGDADTWDRMYGVNVKTTLNASKAALPALTASGgGRIVNIGAGAALKAGPGMGAYAAAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  181 AGIDALAKNLAVELGPLGIRSNCIAPGAIDNteglkrlagkkykEKALAKIPLQRLGS---TRDIAESTVYIFSPAASYV 257
Cdd:PRK12828 159 AGVARLTEALAAELLDRGITVNAVLPSIIDT-------------PPNRADMPDADFSRwvtPEQIAAVIAFLLSDEAQAI 225

                        250
                 ....*....|
gi 99030931  258 TGTVLVVDGG 267
Cdd:PRK12828 226 TGASIPVDGG 235
PRK07062 PRK07062
SDR family oxidoreductase;
23-267 3.46e-32

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 119.76  E-value: 3.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlaKDKDAVLAIANVDVRNFEQVENAVKKTVEK 102
Cdd:PRK07062   7 EGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLRE--KFPGARLLAARCDVLDEADVAAFAAAVEAR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK07062  85 FGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNSLLALQPEPHMVATSAARA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEK-------ALAK---IPLQRLGSTRDIAESTVYIFS 251
Cdd:PRK07062 165 GLLNLVKSLATELAPKGVRVNSILLGLVESGQWRRRYEARADPGQsweawtaALARkkgIPLGRLGRPDEAARALFFLAS 244

                        250
                 ....*....|....*.
gi 99030931  252 PAASYVTGTVLVVDGG 267
Cdd:PRK07062 245 PLSSYTTGSHIDVSGG 260
PRK06124 PRK06124
SDR family oxidoreductase;
24-268 4.34e-32

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 119.05  E-value: 4.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgiSQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK06124  11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAV---AALRAAGGAAEALA-FDIADEEAVAAAFARIDAEH 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSAtfhyygvpFQGHVG----- 177
Cdd:PRK06124  87 GRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGyGRIIAITS--------IAGQVAragda 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 ---AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAA 254
Cdd:PRK06124 159 vypAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPAVGPWLAQRTPLGRWGRPEEIAGAAVFLASPAA 238

                        250
                 ....*....|....
gi 99030931  255 SYVTGTVLVVDGGM 268
Cdd:PRK06124 239 SYVNGHVLAVDGGY 252
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 22-269 6.73e-32

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 118.57  E-value: 6.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIvgrDQERTEQAAKGI-SQLAKDKDAVLAIaNVDVRNFEQVENAVKKTV 100
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAENLvNELGKEGHDVYAV-QADVSKVEDANRLVEEAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  101 EKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAA 179
Cdd:PRK12935  80 NHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGQTNYSAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAgKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAAsYVTG 259
Cdd:PRK12935 160 KAGMLGFTKSLALELAKTNVTVNAICPGFID-TEMVAEVP-EEVRQKIVAKIPKKRFGQADEIAKGVVYLCRDGA-YITG 236

                        250
                 ....*....|
gi 99030931  260 TVLVVDGGMW 269
Cdd:PRK12935 237 QQLNINGGLY 246
PRK06484 PRK06484
short chain dehydrogenase; Validated
 23-267 6.99e-32

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 123.42  E-value: 6.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgiSQLAKDKDAVlaiaNVDVRNFEQVENAVKKTVEK 102
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERA---DSLGPDHHAL----AMDVSDEAQIREGFEQLHRE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVI--AGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYYGVPFQGHVGA 178
Cdd:PRK06484  77 FGRIDVLVnnAGVTDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKRTAYSA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRL--AGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASY 256
Cdd:PRK06484 157 SKAAVISLTRSLACEWAAKGIRVNAVLPGYVR-TQMVAELerAGKLDPSAVRSRIPLGRLGRPEEIAEAVFFLASDQASY 235

                        250
                 ....*....|.
gi 99030931  257 VTGTVLVVDGG 267
Cdd:PRK06484 236 ITGSTLVVDGG 246
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 23-268 7.10e-32

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 118.90  E-value: 7.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgisqlAKDKDAVLAIANvDVRNFEQVENAVKKTVEK 102
Cdd:PRK06200   5 HGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLR------QRFGDHVLVVEG-DVTSYADNQRAVDQTVDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAgnfVCDF----ANLSPN----AFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYY----GV 170
Cdd:PRK06200  78 FGKLDCFVGNAG---IWDYntslVDIPAEtldtAFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYpgggGP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  171 PFQghvgAAKAGIDALAKNLAVELGPlGIRSNCIAPGAIdNTEgLKRLAGKKYKEKALAKI-----------PLQRLGST 239
Cdd:PRK06200 155 LYT----ASKHAVVGLVRQLAYELAP-KIRVNGVAPGGT-VTD-LRGPASLGQGETSISDSpgladmiaaitPLQFAPQP 227

                        250       260       270
                 ....*....|....*....|....*....|
gi 99030931  240 RDIAESTVYIFSPAAS-YVTGTVLVVDGGM 268
Cdd:PRK06200 228 EDHTGPYVLLASRRNSrALTGVVINADGGL 257
PRK09135 PRK09135
pteridine reductase; Provisional
 23-267 1.35e-31

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 117.72  E-value: 1.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGA----GTICRV--QTEALVLLGCKaaivgRDQERTEQAAKGISQLAKDKDAVLAianVDVRNFEQVENAV 96
Cdd:PRK09135   5 SAKVALITGGArrigAAIARTlhAAGYRVAIHYH-----RSAAEADALAAELNALRPGSAAALQ---ADLLDPDALPELV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   97 KKTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSIlfVSATFHYYGVPFQGHV 176
Cdd:PRK09135  77 AACVAAFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRGAI--VNITDIHAERPLKGYP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  177 --GAAKAGIDALAKNLAVELGPlGIRSNCIAPGAIDNTEGLKRLAgKKYKEKALAKIPLQRLGSTRDIAEsTVYIFSPAA 254
Cdd:PRK09135 155 vyCAAKAALEMLTRSLALELAP-EVRVNAVAPGAILWPEDGNSFD-EEARQAILARTPLKRIGTPEDIAE-AVRFLLADA 231

                        250
                 ....*....|...
gi 99030931  255 SYVTGTVLVVDGG 267
Cdd:PRK09135 232 SFITGQILAVDGG 244
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 20-268 1.37e-31

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 118.13  E-value: 1.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLF--KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVK 97
Cdd:PRK08213   6 ELFdlSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAA----DVADEADIERLAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE--LKKSKGSILFVSATFHYYGVP--FQ 173
Cdd:PRK08213  82 ETLERFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsmIPRGYGRIINVASVAGLGGNPpeVM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  174 GHVG--AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDN--TEGLKRLAGkkykEKALAKIPLQRLGSTRDIAESTVYI 249
Cdd:PRK08213 162 DTIAynTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTkmTRGTLERLG----EDLLAHTPLGRLGDDEDLKGAALLL 237

                        250
                 ....*....|....*....
gi 99030931  250 FSPAASYVTGTVLVVDGGM 268
Cdd:PRK08213 238 ASDASKHITGQILAVDGGV 256
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 19-268 1.43e-31

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 117.90  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   19 PDLfKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGR-DQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVK 97
Cdd:PRK08936   3 SDL-EGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIKKAGGEAIAVKG----DVTVESDVVNLIQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS--KGSILFVSATFHYYGVPFQGH 175
Cdd:PRK08936  78 TAVKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdiKGNIINMSSVHEQIPWPLFVH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  176 VGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAAS 255
Cdd:PRK08936 158 YAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRADVESMIPMGYIGKPEEIAAVAAWLASSEAS 237

                        250
                 ....*....|...
gi 99030931  256 YVTGTVLVVDGGM 268
Cdd:PRK08936 238 YVTGITLFADGGM 250
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 24-268 1.74e-31

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: 117.30  E-value: 1.74e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTeqaakgiSQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKF 103
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERG-------ADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGAAKAGI 183
Cdd:cd09761  74 GRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 184 DALAKNLAVELGPlGIRSNCIAPGAIDNTEGLKRLAgKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLV 263
Cdd:cd09761 154 VALTHALAMSLGP-DIRVNCISPGWINTTEQQEFTA-APLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFI 231


                ....*
gi 99030931 264 VDGGM 268
Cdd:cd09761 232 VDGGM 236
PRK07856 PRK07856
SDR family oxidoreductase;
22-267 2.12e-31

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 117.34  E-value: 2.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRdqerteqaakgiSQLAKDKDAVLAIANVDVRNFEQVENAVKKTVE 101
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGR------------RAPETVDGRPAEFHAADVRDPDQVAALVDAIVE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKK--SKGSILFVSATFHYYGVPFQGHVGAA 179
Cdd:PRK07856  72 RHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqpGGGSIVNIGSVSGRRPSPGTAAYGAA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  180 KAGIDALAKNLAVELGPlGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAK-IPLQRLGSTRDIAESTVYIFSPAASYVT 258
Cdd:PRK07856 152 KAGLLNLTRSLAVEWAP-KVRVNAVVVGLVR-TEQSELHYGDAEGIAAVAAtVPLGRLATPADIAWACLFLASDLASYVS 229


                 ....*....
gi 99030931  259 GTVLVVDGG 267
Cdd:PRK07856 230 GANLEVHGG 238
PRK05867 PRK05867
SDR family oxidoreductase;
20-267 2.27e-31

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 117.44  E-value: 2.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLF--KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgiSQLAKDKDAVLAIaNVDVRNFEQVENAVK 97
Cdd:PRK05867   3 DLFdlHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLA---DEIGTSGGKVVPV-CCDVSQHQQVTSMLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATF--HYYGVPFQ- 173
Cdd:PRK05867  79 QVTAELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMvKQGQGGVIINTASMsgHIINVPQQv 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  174 GHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAgkKYKEKALAKIPLQRLGSTRDIAESTVYIFSPA 253
Cdd:PRK05867 159 SHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYI-LTELVEPYT--EYQPLWEPKIPLGRLGRPEELAGLYLYLASEA 235

                        250
                 ....*....|....
gi 99030931  254 ASYVTGTVLVVDGG 267
Cdd:PRK05867 236 SSYMTGSDIVIDGG 249
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 23-267 2.32e-31

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 117.29  E-value: 2.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVEK 102
Cdd:PRK12429   3 KGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAM----DVTDEEAINAGIDYAVET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVsATFHyygvpfqGHVG---- 177
Cdd:PRK12429  79 FGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINM-ASVH-------GLVGsagk 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 ----AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTeglkrLAGKKYKEKA---------------LAKIPLQRLGS 238
Cdd:PRK12429 151 aayvSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTP-----LVRKQIPDLAkergiseeevledvlLPLVPQKRFTT 225

                        250       260
                 ....*....|....*....|....*....
gi 99030931  239 TRDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK12429 226 VEEIADYALFLASFAAKGVTGQAWVVDGG 254
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 25-268 4.22e-31

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: 116.40  E-value: 4.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTGGAGTICRVQTEALVLLGCKAAIvgrDQERTEQAAKGISQLAKDKdAVLAIAnvDVRNFEQVENAVKKTVEKFG 104
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVV---NYYRSTESAEAVAAEAGER-AIAIQA--DVRDRDQVQAMIEEAKNHFG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 105 KIDFVIAGAAGNFVCDfanlsPNAFKSVVDID-----------LLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPF 172
Cdd:cd05349  75 PVDTIVNNALIDFPFD-----PDQRKTFDTIDwedyqqqlegaVKGALNLLQAVLPDFKERGsGRVINIGTNLFQNPVVP 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 173 QGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSP 252
Cdd:cd05349 150 YHDYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLK-VTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASP 228

                       250
                ....*....|....*.
gi 99030931 253 AASYVTGTVLVVDGGM 268
Cdd:cd05349 229 WARAVTGQNLVVDGGL 244
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-268 4.32e-31

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 116.60  E-value: 4.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDkdaVLAIAnVDVRNFEQVENAVKKTVEK 102
Cdd:PRK08217   4 KDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTE---VRGYA-ANVTDEEDVEATFAQIAED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAA----GNFVCD-----FANLSPNAFKSVVDIDLLGSFNT---AKACLKELKkSKGSILFVSaTFHYYGV 170
Cdd:PRK08217  80 FGQLNGLINNAGilrdGLLVKAkdgkvTSKMSLEQFQSVIDVNLTGVFLCgreAAAKMIESG-SKGVIINIS-SIARAGN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  171 PFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDN--TEGLKRLAgkkyKEKALAKIPLQRLGSTRDIAESTVY 248
Cdd:PRK08217 158 MGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETemTAAMKPEA----LERLEKMIPVGRLGEPEEIAHTVRF 233

                        250       260
                 ....*....|....*....|
gi 99030931  249 IFspAASYVTGTVLVVDGGM 268
Cdd:PRK08217 234 II--ENDYVTGRVLEIDGGL 251
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 21-267 4.96e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 116.18  E-value: 4.96e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   21 LFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlakDKDAVLAIANvDVRNFEQVENAVKKTV 100
Cdd:PRK07478   3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRA---EGGEAVALAG-DVRDEAYAKALVALAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  101 EKFGKID--FVIAGAAGNfVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSaTF--HYYGVPFQGH 175
Cdd:PRK07478  79 ERFGGLDiaFNNAGTLGE-MGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAmLARGGGSLIFTS-TFvgHTAGFPGMAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  176 VGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAAS 255
Cdd:PRK07478 157 YAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEALAFVAGLHALKRMAQPEEIAQAALFLASDAAS 236

                        250
                 ....*....|..
gi 99030931  256 YVTGTVLVVDGG 267
Cdd:PRK07478 237 FVTGTALLVDGG 248
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 23-268 5.87e-31

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: 116.30  E-value: 5.87e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERteqaakgISQLAKD-KDAVLAIANvDVRNFEQVENAVKKTVE 101
Cdd:cd05348   3 KGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEK-------VAELRADfGDAVVGVEG-DVRSLADNERAVARCVE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIaGAAG--NFVCDFANLSPN----AFKSVVDIDLLGSFNTAKACLKELKKSKGSILF-VSATFHYygvPFQG 174
Cdd:cd05348  75 RFGKLDCFI-GNAGiwDYSTSLVDIPEEkldeAFDELFHINVKGYILGAKAALPALYATEGSVIFtVSNAGFY---PGGG 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 175 HV--GAAKAGIDALAKNLAVELGPLgIRSNCIAPGAI--DNTEGLKRLAGKKYKEKAL------AKIPLQRLGSTRDIAE 244
Cdd:cd05348 151 GPlyTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMvtDLRGPASLGQGETSISTPPlddmlkSILPLGFAPEPEDYTG 229

                       250       260
                ....*....|....*....|....*
gi 99030931 245 STVYIFSPAAS-YVTGTVLVVDGGM 268
Cdd:cd05348 230 AYVFLASRGDNrPATGTVINYDGGM 254
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 23-268 8.00e-31

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: 115.63  E-value: 8.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGIsqlakdKDAVLAIANVDVRNFEQVENAVKKTVEK 102
Cdd:cd05326   3 DGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAEL------GDPDISFVHCDVTVEADVRAAVDTAVAR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 103 FGKIDFVI--AGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAK-ACLKELKKSKGSILFVSATFHYYGvPFQGHV-GA 178
Cdd:cd05326  77 FGRLDIMFnnAGVLGAPCYSILETSLEEFERVLDVNVYGAFLGTKhAARVMIPAKKGSIVSVASVAGVVG-GLGPHAyTA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLkrLAGKKYKEKALAKI------PLQRLGSTRDIAESTVYIFSP 252
Cdd:cd05326 156 SKHAVLGLTRSAATELGEHGIRVNCVSPYGV-ATPLL--TAGFGVEDEAIEEAvrgaanLKGTALRPEDIAAAVLYLASD 232

                       250
                ....*....|....*.
gi 99030931 253 AASYVTGTVLVVDGGM 268
Cdd:cd05326 233 DSRYVSGQNLVVDGGL 248
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 24-217 9.98e-31

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: 115.04  E-value: 9.98e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKF 103
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASGQKVSYISADLSDYEEVEQAFAQAVEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 104 GKIDFVIAgAAGNFVC-DFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:cd08939  81 GPPDLVVN-CAGISIPgLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGYSAYCPSKF 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 99030931 182 GIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKR 217
Cdd:cd08939 160 ALRGLAESLRQELKPYNIRVSVVYPPDTD-TPGFEE 194
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 20-268 1.13e-30

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: 115.51  E-value: 1.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  20 DLFKGKVAFVTGGA-------GTicrvqTEALVLLGCKAAIVGRDqertEQAAKGISQLAKDKDAVLAIaNVDVRNFEQV 92
Cdd:COG0623   1 GLLKGKRGLITGVAndrsiawGI-----AKALHEEGAELAFTYQG----EALKKRVEPLAEELGSALVL-PCDVTDDEQI 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  93 ENAVKKTVEKFGKIDFV---IAGA-----AGNFVcdfaNLSPNAFKSVVDIDLLgSF-NTAKAClKELKKSKGSILfvsa 163
Cdd:COG0623  71 DALFDEIKEKWGKLDFLvhsIAFApkeelGGRFL----DTSREGFLLAMDISAY-SLvALAKAA-EPLMNEGGSIV---- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 164 TFHYYG----VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdnteglKRLAGK------KYKEKALAKIPL 233
Cdd:COG0623 141 TLTYLGaervVPNYNVMGVAKAALEASVRYLAADLGPKGIRVNAISAGPI------KTLAASgipgfdKLLDYAEERAPL 214

                       250       260       270
                ....*....|....*....|....*....|....*
gi 99030931 234 QRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:COG0623 215 GRNVTIEEVGNAAAFLLSDLASGITGEIIYVDGGY 249
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 23-267 1.20e-30

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: 115.06  E-value: 1.20e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAI-VGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVE 101
Cdd:cd05362   2 AGKVALVTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAEIEAAGGKAIAVQA----DVSDPSQVARLFDAAEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKkSKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:cd05362  78 AFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR-DGGRIINISSSLTAAYTPNYGAYAGSKA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 182 GIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTV 261
Cdd:cd05362 157 AVEAFTRVLAKELGGRGITVNAVAPGPVD-TDMFYAGKTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQV 235


                ....*.
gi 99030931 262 LVVDGG 267
Cdd:cd05362 236 IRANGG 241
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 26-267 1.23e-30

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: 114.97  E-value: 1.23e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  26 VAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVlaiaNVDVRNFEQVENAVKKTVEKFGK 105
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGL----ECNVTSEQDLEAVVKATVSQFGG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 106 IDFVIAGAAGNFVCDFA-NLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAGI 183
Cdd:cd05365  77 ITILVNNAGGGGPKPFDmPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGgGAILNISSMSSENKNVRIAAYGSSKAAV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 184 DALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLV 263
Cdd:cd05365 157 NHMTRNLAFDLGPKGIRVNAVAPGAV-KTDALASVLTPEIERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLT 235


                ....
gi 99030931 264 VDGG 267
Cdd:cd05365 236 VSGG 239
PRK12743 PRK12743
SDR family oxidoreductase;
25-279 1.39e-30

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 115.13  E-value: 1.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRdqeRTEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKFG 104
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITWH---SDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  105 KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS--KGSILFVSATFHYYGVPFQGHVGAAKAG 182
Cdd:PRK12743  80 RIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgqGGRIINITSVHEHTPLPGASAYTAAKHA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  183 IDALAKNLAVELGPLGIRSNCIAPGAI-------DNTEGlkrlagkkyKEKALAKIPLQRLGSTRDIAESTVYIFSPAAS 255
Cdd:PRK12743 160 LGGLTKAMALELVEHGILVNAVAPGAIatpmngmDDSDV---------KPDSRPGIPLGRPGDTHEIASLVAWLCSEGAS 230

                        250       260
                 ....*....|....*....|....
gi 99030931  256 YVTGTVLVVDGGMWHLGTYFGHEL 279
Cdd:PRK12743 231 YTTGQSLIVDGGFMLANPQFNSEL 254
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 22-267 2.88e-30

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 114.37  E-value: 2.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDqERTEQAAKGIsqlakDKDAVLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRS-EDVAEVAAQL-----LGGNAKGLV-CDVSDSQSVEAAVAAVIS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPfqGHVG--A 178
Cdd:PRK06841  86 AFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHmIAAGGGKIVNLASQAGVVALE--RHVAycA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKyKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVT 258
Cdd:PRK06841 164 SKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAGEK-GERAKKLIPAGRFAYPEEIAAAALFLASDAAAMIT 242


                 ....*....
gi 99030931  259 GTVLVVDGG 267
Cdd:PRK06841 243 GENLVIDGG 251
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 23-268 4.15e-30

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: 113.70  E-value: 4.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQvENAVKKTVEK 102
Cdd:cd05329   5 EGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVC----DVSSRSE-RQELMDTVAS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 103 F--GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPFQGHVGAA 179
Cdd:cd05329  80 HfgGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASgNGNIVFISSVAGVIAVPSGAPYGAT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDN--TEGLkrLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:cd05329 160 KGALNQLTRSLACEWAKDNIRVNAVAPWVIATplVEPV--IQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYI 237

                       250
                ....*....|.
gi 99030931 258 TGTVLVVDGGM 268
Cdd:cd05329 238 TGQIIAVDGGL 248
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 24-268 4.75e-30

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: 114.01  E-value: 4.75e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTeqaAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKF 103
Cdd:cd05366   2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEA---AKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKK--SKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:cd05366  79 GSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKlgHGGKIINASSIAGVQGFPNLGAYSASKF 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 182 GIDALAKNLAVELGPLGIRSNCIAPGAID------NTEGLKRLAGKKY---KEKALAKIPLQRLGSTRDIAESTVYIFSP 252
Cdd:cd05366 159 AVRGLTQTAAQELAPKGITVNAYAPGIVKtemwdyIDEEVGEIAGKPEgegFAEFSSSIPLGRLSEPEDVAGLVSFLASE 238

                       250
                ....*....|....*.
gi 99030931 253 AASYVTGTVLVVDGGM 268
Cdd:cd05366 239 DSDYITGQTILVDGGM 254
PRK07035 PRK07035
SDR family oxidoreductase;
19-268 6.69e-30

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 113.19  E-value: 6.69e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   19 PDLF--KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGIsqlAKDKDAVLAIAnVDVRNFEQVENAV 96
Cdd:PRK07035   1 TNLFdlTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAI---VAAGGKAEALA-CHIGEMEQIDALF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   97 KKTVEKFGKIDFVIAGAAGN-FVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPFQG 174
Cdd:PRK07035  77 AHIRERHGRLDILVNNAAANpYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQgGGSIVNVASVNGVSPGDFQG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  175 HVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAA 254
Cdd:PRK07035 157 IYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAILKQALAHIPLRRHAEPSEMAGAVLYLASDAS 236

                        250
                 ....*....|....
gi 99030931  255 SYVTGTVLVVDGGM 268
Cdd:PRK07035 237 SYTTGECLNVDGGY 250
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 24-268 7.47e-30

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 113.14  E-value: 7.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVEKF 103
Cdd:PRK12939   7 GKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAA----DLADPASVQRFFDAAAAAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAG 182
Cdd:PRK12939  83 GGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGrGRIVNLASDTALWGAPKLGAYVASKGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  183 IDALAKNLAVELGPLGIRSNCIAPG--AIDNTEGLKRLAGKKYKEKAlakIPLQRLGSTRDIAESTVYIFSPAASYVTGT 260
Cdd:PRK12939 163 VIGMTRSLARELGGRGITVNAIAPGltATEATAYVPADERHAYYLKG---RALERLQVPDDVAGAVLFLLSDAARFVTGQ 239


                 ....*...
gi 99030931  261 VLVVDGGM 268
Cdd:PRK12939 240 LLPVNGGF 247
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 22-267 3.25e-29

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: 111.43  E-value: 3.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkdkdavLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGA------LALR-VDVTDEQQVAALFERAVE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGA-AGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKG-SILFVSATFHYYGVPFQGHVGAA 179
Cdd:cd08944  74 EFGGLDLLVNNAgAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGgSIVNLSSIAGQSGDPGYGAYGAS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAG-----KKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAA 254
Cdd:cd08944 154 KAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGfegalGPGGFHLLIHQLQGRLGRPEDVAAAVVFLLSDDA 233

                       250
                ....*....|...
gi 99030931 255 SYVTGTVLVVDGG 267
Cdd:cd08944 234 SFITGQVLCVDGG 246
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-267 8.83e-28

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 107.95  E-value: 8.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVgrdQERTEQAAKGIsqlaKDKDAVlaIANVDVRNFEQVENAVKKTVE 101
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVL---YNSAENEAKEL----REKGVF--TIKCDVGNRDQVKKSKEVVEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGAA-- 179
Cdd:PRK06463  76 EFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEGTTFYAit 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  180 KAGIDALAKNLAVELGPLGIRSNCIAPGAI--DNTEGLK-RLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASY 256
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPGWVetDMTLSGKsQEEAEKLRELFRNKTVLKTTGKPEDIANIVLFLASDDARY 235

                        250
                 ....*....|.
gi 99030931  257 VTGTVLVVDGG 267
Cdd:PRK06463 236 ITGQVIVADGG 246
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
24-267 1.29e-27

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 107.58  E-value: 1.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQErTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVEKF 103
Cdd:PRK08226   6 GKTALITGALQGIGEGIARVFARHGANLILLDISPE-IEKLADELCGRGHRCTAVVA----DVRDPASVAAAIKRAKEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSA-TFHYYGVPFQGHVGAAKA 181
Cdd:PRK08226  81 GRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEmIARKDGRIVMMSSvTGDMVADPGETAYALTKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAIDN--TEGLKRLAGKKYKEKALAKI----PLQRLGSTRDIAESTVYIFSPAAS 255
Cdd:PRK08226 161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRTpmAESIARQSNPEDPESVLTEMakaiPLRRLADPLEVGELAAFLASDESS 240

                        250
                 ....*....|..
gi 99030931  256 YVTGTVLVVDGG 267
Cdd:PRK08226 241 YLTGTQNVIDGG 252
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 24-210 1.70e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 108.13  E-value: 1.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgiSQLAKDKDAVLAIAnvDVRNFEQVENAVKKTVEKF 103
Cdd:PRK05872   9 GKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALA---AELGGDDRVLTVVA--DVTDLAAMQAAAEEAVERF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGAAKAGI 183
Cdd:PRK05872  84 GGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAAAPGMAAYCASKAGV 163

                        170       180
                 ....*....|....*....|....*..
gi 99030931  184 DALAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:PRK05872 164 EAFANALRLEVAHHGVTVGSAYLSWID 190
PRK07814 PRK07814
SDR family oxidoreductase;
20-268 1.73e-27

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 107.17  E-value: 1.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLFK--GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVK 97
Cdd:PRK07814   4 DRFRldDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAA----DLAHPEATAGLAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATF-HYYGVPFQG 174
Cdd:PRK07814  80 QAVEAFGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSggGSVINISSTMgRLAGRGFAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  175 HvGAAKAGIDALAKNLAVELGPlGIRSNCIAPGAIdNTEGLKRLAGKKYKEKALAK-IPLQRLGSTRDIAESTVYIFSPA 253
Cdd:PRK07814 160 Y-GTAKAALAHYTRLAALDLCP-RIRVNAIAPGSI-LTSALEVVAANDELRAPMEKaTPLRRLGDPEDIAAAAVYLASPA 236

                        250
                 ....*....|....*
gi 99030931  254 ASYVTGTVLVVDGGM 268
Cdd:PRK07814 237 GSYLTGKTLEVDGGL 251
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 23-267 2.10e-27

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 106.60  E-value: 2.10e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKdkdavlaiANVDVRNFEQVENAVKKTVEK 102
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGDNCRF--------VPVDVTSEKDVKAALALAKAK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 103 FGKIDFVIAGAAGNFVCDFANL------SPNAFKSVVDIDLLGSFNTAKACLKELKKS-------KGSILFVSATFHYYG 169
Cdd:cd05371  73 FGRLDIVVNCAGIAVAAKTYNKkgqqphSLELFQRVINVNLIGTFNVIRLAAGAMGKNepdqggeRGVIINTASVAAFEG 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 170 VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYI 249
Cdd:cd05371 153 QIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFD-TPLLAGLPEKVRDFLAKQVPFPSRLGDPAEYAHLVQHI 231

                       250
                ....*....|....*...
gi 99030931 250 FSpaASYVTGTVLVVDGG 267
Cdd:cd05371 232 IE--NPYLNGEVIRLDGA 247
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 22-267 2.24e-27

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: 106.84  E-value: 2.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDqERTEQAAKGISQLAkdkDAVLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:cd08937   2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEILAAG---DAAHVHT-ADLETYAGAQGVVRAAVE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNA-FKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVS--ATFHYYGVPFqghvG 177
Cdd:cd08937  77 RFGRVDVLINNVGGTIWAKPYEHYEEEqIEAEIRRSLFPTLWCCRAVLPHmLERQQGVIVNVSsiATRGIYRIPY----S 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRL---AGKKYKEKALAK---------IPLQRLGSTRDIAES 245
Cdd:cd08937 153 AAKGGVNALTASLAFEHARDGIRVNAVAPGGT-EAPPRKIPrnaAPMSEQEKVWYQrivdqtldsSLMGRYGTIDEQVRA 231

                       250       260
                ....*....|....*....|..
gi 99030931 246 TVYIFSPAASYVTGTVLVVDGG 267
Cdd:cd08937 232 ILFLASDEASYITGTVLPVGGG 253
PRK07063 PRK07063
SDR family oxidoreductase;
23-271 2.99e-27

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 106.67  E-value: 2.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIAnvDVRNFEQVENAVKKTVEK 102
Cdd:PRK07063   6 AGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAGARVLAVPA--DVTDAASVAAAVAAAEEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK07063  84 FGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGmVERGRGSIVNIASTHAFKIIPGCFPYPVAKH 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAG----KKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:PRK07063 164 GLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAqpdpAAARAETLALQPMKRIGRPEEVAMTAVFLASDEAPFI 243

                        250
                 ....*....|....
gi 99030931  258 TGTVLVVDGGMWHL 271
Cdd:PRK07063 244 NATCITIDGGRSVL 257
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 24-267 3.65e-27

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: 105.94  E-value: 3.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTG-----GAGTICRVQTEalvllGCKAAIVGRDQERTEQAAKGISqlakdkDAVLAIAnVDVRNFEQVENAVKK 98
Cdd:cd05345   5 GKVAIVTGagsgfGEGIARRFAQE-----GARVVIADINADGAERVAADIG------EAAIAIQ-ADVTKRADVEAMVEA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  99 TVEKFGKIDFVIAGAA-GNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKK-SKGSILFVSATFHYYGVPFQGHV 176
Cdd:cd05345  73 ALSKFGRLDILVNNAGiTHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEqGGGVIINIASTAGLRPRPGLTWY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAiDNTEGLKRLAGK---KYKEKALAKIPLQRLGSTRDIAESTVYIFSPA 253
Cdd:cd05345 153 NASKGWVVTATKAMAVELAPRNIRVNCLCPVA-GETPLLSMFMGEdtpENRAKFRATIPLGRLSTPDDIANAALYLASDE 231

                       250
                ....*....|....
gi 99030931 254 ASYVTGTVLVVDGG 267
Cdd:cd05345 232 ASFITGVALEVDGG 245
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 15-268 3.94e-27

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: 106.09  E-value: 3.94e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  15 GSWRPDLFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAakgISQLAKDKDAVLAIAnVDVRNFEQVEN 94
Cdd:cd08936   1 GVTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRA---VATLQGEGLSVTGTV-CHVGKAEDRER 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  95 AVKKTVEKFGKIDFVIAGAAGN-FVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYYGVPF 172
Cdd:cd08936  77 LVATAVNLHGGVDILVSNAAVNpFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMeKRGGGSVVIVSSVAAFHPFPG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 173 QGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSP 252
Cdd:cd08936 157 LGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSE 236

                       250
                ....*....|....*.
gi 99030931 253 AASYVTGTVLVVDGGM 268
Cdd:cd08936 237 DASYITGETVVVGGGT 252
PRK09242 PRK09242
SDR family oxidoreductase;
17-268 6.02e-27

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 105.60  E-value: 6.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   17 WRPDlfkGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIANV-DVRNFEQVENA 95
Cdd:PRK09242   5 WRLD---GQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVsDDEDRRAILDW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   96 VKKTvekFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGS----ILFVSATFHY-YGV 170
Cdd:PRK09242  82 VEDH---WDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSaivnIGSVSGLTHVrSGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  171 PFqghvGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDN--TEGLkrLAGKKYKEKALAKIPLQRLGSTRDIAESTVY 248
Cdd:PRK09242 159 PY----GMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTplTSGP--LSDPDYYEQVIERTPMRRVGEPEEVAAAVAF 232

                        250       260
                 ....*....|....*....|
gi 99030931  249 IFSPAASYVTGTVLVVDGGM 268
Cdd:PRK09242 233 LCMPAASYITGQCIAVDGGF 252
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
25-269 6.35e-27

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 105.23  E-value: 6.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRVQTEALVLLGCKaaIVGRDQERTEQAAKGISQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKFG 104
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYR--VIATYFSGNDCAKDWFEEYGFTEDQVRLKE-LDVTDTEECAEALAEIEEEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  105 KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELK-KSKGSILFVSATFHYYGVPFQGHVGAAKAGI 183
Cdd:PRK12824  80 PVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQTNYSAAKAGM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  184 DALAKNLAVELGPLGIRSNCIAPGAIdNTEgLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLV 263
Cdd:PRK12824 160 IGFTKALASEGARYGITVNCIAPGYI-ATP-MVEQMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFITGETIS 237


                 ....*.
gi 99030931  264 VDGGMW 269
Cdd:PRK12824 238 INGGLY 243
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 22-267 7.94e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 105.65  E-value: 7.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkDKDAVLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALK-GAGAVRYEP-ADVTDEDQVARAVDAATA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGN-FVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSA-----TFHYYGVpfqg 174
Cdd:PRK05875  83 WHGRLHGVVHCAGGSeTIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELvRGGGGSFVGISSiaasnTHRWFGA---- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  175 hVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAA 254
Cdd:PRK05875 159 -YGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSADYRACTPLPRVGEVEDVANLAMFLLSDAA 237

                        250
                 ....*....|...
gi 99030931  255 SYVTGTVLVVDGG 267
Cdd:PRK05875 238 SWITGQVINVDGG 250
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
23-269 9.13e-27

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 105.11  E-value: 9.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlakdkdAVLAIAnVDVRNFEQVENAVKKTVEK 102
Cdd:PRK07067   5 QGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGP------AAIAVS-LDVTRQDSIDRIVAAAVER 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAgnfVCDFANL---SPNAFKSVVDIDLLGSFNTAKACLKEL--KKSKGSILFVSATFHYYGVPFQGHVG 177
Cdd:PRK07067  78 FGGIDILFNNAA---LFDMAPIldiSRDSYDRLFAVNVKGLFFLMQAVARHMveQGRGGKIINMASQAGRRGEALVSHYC 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNT------------EGLKRlaGKKYKEKALAkIPLQRLGSTRDIAES 245
Cdd:PRK07067 155 ATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPmwdqvdalfaryENRPP--GEKKRLVGEA-VPLGRMGVPDDLTGM 231

                        250       260
                 ....*....|....*....|....
gi 99030931  246 TVYIFSPAASYVTGTVLVVDGGMW 269
Cdd:PRK07067 232 ALFLASADADYIVAQTYNVDGGNW 255
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 23-267 1.26e-26

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: 104.39  E-value: 1.26e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKdkdavlaIANVDVRNFEQVENAVKKTVEK 102
Cdd:cd05341   4 KGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAAR-------FFHLDVTDEDGWTAVVDTAREA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 103 FGKIDfVIAGAAGNFVCDFANLSPNA-FKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPFQGHVGAAK 180
Cdd:cd05341  77 FGRLD-VLVNNAGILTGGTVETTTLEeWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPALAAYNASK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 181 AGIDALAKNLAVELGP--LGIRSNCIAPGAIdNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVT 258
Cdd:cd05341 156 GAVRGLTKSAALECATqgYGIRVNSVHPGYI-YTPMTDELLIAQGEMGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVT 234


                ....*....
gi 99030931 259 GTVLVVDGG 267
Cdd:cd05341 235 GSELVVDGG 243
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
21-267 1.27e-26

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 104.42  E-value: 1.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   21 LFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIV-GRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKT 99
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKALAVKA----NVGDVEKIKEMFAQI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  100 VEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGS-ILFVSATFHYYGVPFQGHVGA 178
Cdd:PRK08063  77 DEEFGRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGkIISLSSLGSIRYLENYTTVGV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGK-KYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:PRK08063 157 SKAALEALTRYLAVELAPKGIAVNAVSGGAVD-TDALKHFPNReELLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMI 235

                        250
                 ....*....|
gi 99030931  258 TGTVLVVDGG 267
Cdd:PRK08063 236 RGQTIIVDGG 245
PRK07074 PRK07074
SDR family oxidoreductase;
25-268 1.28e-26

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 104.85  E-value: 1.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlakdkDAVLAIAnVDVRNFEQVENAVKKTVEKFG 104
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGD-----ARFVPVA-CDLTDAASLAAALANAAAERG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  105 KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATfhyYGVPFQGH--VGAAKA 181
Cdd:PRK07074  77 PVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGmLKRSRGAVVNIGSV---NGMAALGHpaYSAAKA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGK-KYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGT 260
Cdd:PRK07074 154 GLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAANpQVFEELKKWYPLQDFATPDDVANAVLFLASPAARAITGV 233


                 ....*...
gi 99030931  261 VLVVDGGM 268
Cdd:PRK07074 234 CLPVDGGL 241
PRK06114 PRK06114
SDR family oxidoreductase;
19-267 1.94e-26

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 104.09  E-value: 1.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   19 PDLFK--GKVAFVTGGAGTICrvQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIANvDVRNFEQVENAV 96
Cdd:PRK06114   1 PQLFDldGQVAFVTGAGSGIG--QRIAIGLAQAGADVALFDLRTDDGLAETAEHIEAAGRRAIQIAA-DVTSKADLRAAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   97 KKTVEKFGKIDfVIAGAAGnfvcdFANLSP------NAFKSVVDIDLLGSFNTAKA-CLKELKKSKGSILFV---SATFH 166
Cdd:PRK06114  78 ARTEAELGALT-LAVNAAG-----IANANPaeemeeEQWQTVMDINLTGVFLSCQAeARAMLENGGGSIVNIasmSGIIV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  167 YYGVpFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAID---NTEGLKRLAGKKYKEKAlakiPLQRLGSTRDIA 243
Cdd:PRK06114 152 NRGL-LQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTAtpmNTRPEMVHQTKLFEEQT----PMQRMAKVDEMV 226

                        250       260
                 ....*....|....*....|....
gi 99030931  244 ESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK06114 227 GPAVFLLSDAASFCTGVDLLVDGG 250
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 23-267 2.36e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 104.73  E-value: 2.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgiSQLAKDKDAVLAIANvDVRNFEQVENAVKKTVEK 102
Cdd:PRK06701  45 KGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETK--QRVEKEGVKCLLIPG-DVSDEAFCKDAVEETVRE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNF-VCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATfhyygvPFQGHV----- 176
Cdd:PRK06701 122 LGRLDILVNNAAFQYpQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQGSAIINTGSIT------GYEGNEtlidy 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAI-------DNTEGLKRLAGkkykekalAKIPLQRLGSTRDIAESTVYI 249
Cdd:PRK06701 196 SATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIwtplipsDFDEEKVSQFG--------SNTPMQRPGQPEELAPAYVFL 267

                        250
                 ....*....|....*...
gi 99030931  250 FSPAASYVTGTVLVVDGG 267
Cdd:PRK06701 268 ASPDSSYITGQMLHVNGG 285
PRK06172 PRK06172
SDR family oxidoreductase;
22-267 3.19e-26

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 103.68  E-value: 3.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVlaiaNVDVRNFEQVENAVKKTVE 101
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFV----ACDVTRDAEVKALVEQTIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFV-----IAGAAGNFvcdfANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPFQGH 175
Cdd:PRK06172  81 AYGRLDYAfnnagIEIEQGRL----AEGSEAEFDAIMGVNVKGVWLCMKYQIPLmLAQGGGAIVNTASVAGLGAAPKMSI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  176 VGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGK--KYKEKALAKIPLQRLGSTRDIAESTVYIFSPA 253
Cdd:PRK06172 157 YAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVID-TDMFRRAYEAdpRKAEFAAAMHPVGRIGKVEEVASAVLYLCSDG 235

                        250
                 ....*....|....
gi 99030931  254 ASYVTGTVLVVDGG 267
Cdd:PRK06172 236 ASFTTGHALMVDGG 249
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 23-272 3.91e-26

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 103.55  E-value: 3.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISqlakdkDAVLAIAnVDVRNFEQVENAVKKTVEK 102
Cdd:PRK08265   5 AGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLG------ERARFIA-TDITDDAAIERAVATVVAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIagaagNFVCDFANlspNAFKS-------VVDIDLLGSFNTAKACLKELKKSKGSIL---FVSATFhyygvpf 172
Cdd:PRK08265  78 FGRVDILV-----NLACTYLD---DGLASsradwlaALDVNLVSAAMLAQAAHPHLARGGGAIVnftSISAKF------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  173 qGHVG-----AAKAGIDALAKNLAVELGPLGIRSNCIAPG-----AIDNTEGlkrlaGKKYKEKALAKI--PLQRLGSTR 240
Cdd:PRK08265 143 -AQTGrwlypASKAAIRQLTRSMAMDLAPDGIRVNSVSPGwtwsrVMDELSG-----GDRAKADRVAAPfhLLGRVGDPE 216

                        250       260       270
                 ....*....|....*....|....*....|..
gi 99030931  241 DIAESTVYIFSPAASYVTGTVLVVDGGMWHLG 272
Cdd:PRK08265 217 EVAQVVAFLCSDAASFVTGADYAVDGGYSALG 248
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
23-268 4.13e-26

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 103.27  E-value: 4.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVlaiaNVDVRNFEQVENAVKKTVEK 102
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAV----KADVSDRDQVFAAVRQVVDT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVI--AGAAGNFVCDfaNLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYYGVPFQGHVGA 178
Cdd:PRK08643  77 FGDLNVVVnnAGVAPTTPIE--TITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhgGKIINATSQAGVVGNPELAVYSS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAI------DNTEGLKRLAGK--KYKEKALAK-IPLQRLGSTRDIAESTVYI 249
Cdd:PRK08643 155 TKFAVRGLTQTAARDLASEGITVNAYAPGIVktpmmfDIAHQVGENAGKpdEWGMEQFAKdITLGRLSEPEDVANCVSFL 234

                        250
                 ....*....|....*....
gi 99030931  250 FSPAASYVTGTVLVVDGGM 268
Cdd:PRK08643 235 AGPDSDYITGQTIIVDGGM 253
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 24-267 2.32e-25

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: 101.31  E-value: 2.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGisqlAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKF 103
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEA----AQGGPRALGVQ-CDVTSEAQVQSAFEQAVLEF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:cd08943  76 GGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNAVAPGPNAAAYSAAKA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 182 GIDALAKNLAVELGPLGIRSNCIAP-----GAIDNTEGLKRLAGKKYK---EKALAKIPLQRLGSTRDIAESTVYIFSPA 253
Cdd:cd08943 156 AEAHLARCLALEGGEDGIRVNTVNPdavfrGSKIWEGVWRAARAKAYGlleEEYRTRNLLKREVLPEDVAEAVVAMASED 235

                       250
                ....*....|....
gi 99030931 254 ASYVTGTVLVVDGG 267
Cdd:cd08943 236 FGKTTGAIVTVDGG 249
PRK06947 PRK06947
SDR family oxidoreductase;
25-267 3.98e-25

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 100.65  E-value: 3.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRVQTealVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKFG 104
Cdd:PRK06947   3 KVVLITGASRGIGRATA---VLAAARGWSVGINYARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  105 KIDFVI--AGAAGNFVcDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKG----SILFVSATFHYYGVPFQgHV-- 176
Cdd:PRK06947  80 RLDALVnnAGIVAPSM-PLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGgrggAIVNVSSIASRLGSPNE-YVdy 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEgLKRLAGKKYKEKAL-AKIPLQRLGSTRDIAESTVYIFSPAAS 255
Cdd:PRK06947 158 AGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIE-TE-IHASGGQPGRAARLgAQTPLGRAGEADEVAETIVWLLSDAAS 235

                        250
                 ....*....|..
gi 99030931  256 YVTGTVLVVDGG 267
Cdd:PRK06947 236 YVTGALLDVGGG 247
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 19-269 5.43e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 100.46  E-value: 5.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   19 PDLFKGKVAFVTGGAGTICRVQTEALVLLGCKA-AIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVK 97
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAGlVICGRNAEKGEAQAAELEALGAKAVFVQA----DLSDVEDCRRVVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDfVIAGAAGnfVCDFANL---SPNAFKSVVDIDLLGSFNTAKACLKEL--KKSKGSILFVSATFHYYGVPF 172
Cdd:PRK06198  77 AADEAFGRLD-ALVNAAG--LTDRGTIldtSPELFDRHFAVNVRAPFFLMQEAIKLMrrRKAEGTIVNIGSMSAHGGQPF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  173 QGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRL------AGKKYKEKALAKIPLQRLGSTRDIAEST 246
Cdd:PRK06198 154 LAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMA-TEGEDRIqrefhgAPDDWLEKAAATQPFGRLLDPDEVARAV 232

                        250       260
                 ....*....|....*....|...
gi 99030931  247 VYIFSPAASYVTGTVLVVDGGMW 269
Cdd:PRK06198 233 AFLLSDESGLMTGSVIDFDQSVW 255
PRK06500 PRK06500
SDR family oxidoreductase;
22-268 5.58e-25

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 100.03  E-value: 5.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISqlakdkDAVLAIAN--VDVRNFEQVENAVKkt 99
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELG------ESALVIRAdaGDVAAQKALAQALA-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  100 vEKFGKID--FVIAGAAgnfvcDFANL---SPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYyGVPFQG 174
Cdd:PRK06500  76 -EAFGRLDavFINAGVA-----KFAPLedwDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLNGSINAHI-GMPNSS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  175 HVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAK-----IPLQRLGSTRDIAESTVYI 249
Cdd:PRK06500 149 VYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQ-TPLYGKLGLPEATLDAVAAqiqalVPLGRFGTPEEIAKAVLYL 227

                        250
                 ....*....|....*....
gi 99030931  250 FSPAASYVTGTVLVVDGGM 268
Cdd:PRK06500 228 ASDESAFIVGSEIIVDGGM 246
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 23-269 1.00e-24

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: 100.06  E-value: 1.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQErtEQAAKGISQLAK-DKDAVLAIANvDVRNFEQVENAVKKTVE 101
Cdd:cd05355  25 KGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEE--EDDAEETKKLIEeEGRKCLLIPG-DLGDESFCRDLVKEVVK 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVC-DFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKsKGSILFVSATFHYYGVPFQGHVGAAK 180
Cdd:cd05355 102 EFGKLDILVNNAAYQHPQeSIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK-GSSIINTTSVTAYKGSPHLLDYAATK 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 181 AGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGT 260
Cdd:cd05355 181 GAIVAFTRGLSLQLAEKGIRVNAVAPGPI-WTPLIPSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQDSSYVTGQ 259


                ....*....
gi 99030931 261 VLVVDGGMW 269
Cdd:cd05355 260 VLHVNGGEI 268
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
20-267 1.03e-24

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 99.81  E-value: 1.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLF--KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEqaakgISQLAKDKDAVLAIANVDVRNFEQVENAVK 97
Cdd:PRK06935   9 DFFslDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDE-----TRRLIEKEGRKVTFVQVDLTKPESAEKVVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPFQGHV 176
Cdd:PRK06935  84 EALEEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVmAKQGSGKIINIASMLSFQGGKFVPAY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAI--DNTEGLKrlAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAA 254
Cdd:PRK06935 164 TASKHGVAGLTKAFANELAAYNIQVNAIAPGYIktANTAPIR--ADKNRNDEILKRIPAGRWGEPDDLMGAAVFLASRAS 241

                        250
                 ....*....|...
gi 99030931  255 SYVTGTVLVVDGG 267
Cdd:PRK06935 242 DYVNGHILAVDGG 254
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 22-268 1.27e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 99.02  E-value: 1.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISqlakdkDAVLAianVDVRNFEQVENAVKKtve 101
Cdd:PRK07060   7 FSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETG------CEPLR---LDVGDDAAIRAALAA--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 kFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS--KGSILFVSATFHYYGVPFQGHVGAA 179
Cdd:PRK07060  75 -AGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAgrGGSIVNVSSQAALVGLPDHLAYCAS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:PRK07060 154 KAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSG 233


                 ....*....
gi 99030931  260 TVLVVDGGM 268
Cdd:PRK07060 234 VSLPVDGGY 242
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-268 1.81e-24

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 99.01  E-value: 1.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRVQTEALVLLGCKAAIvgrDQERTEQAAKGISQLAKDKdaVLAIaNVDVRNFEQVENAVKKTVEKFG 104
Cdd:PRK08642   6 QTVLVTGGSRGLGAAIARAFAREGARVVV---NYHQSEDAAEALADELGDR--AIAL-QADVTDREQVQAMFATATEHFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  105 K-IDFVIAGAAGNFVCD------FANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSAT-FHYYGVPFQGH 175
Cdd:PRK08642  80 KpITTVVNNALADFSFDgdarkkADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGTNlFQNPVVPYHDY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  176 VgAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEglkrlAGKKYKEKALAKI----PLQRLGSTRDIAESTVYIFS 251
Cdd:PRK08642 160 T-TAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTD-----ASAATPDEVFDLIaattPLRKVTTPQEFADAVLFFAS 233

                        250
                 ....*....|....*..
gi 99030931  252 PAASYVTGTVLVVDGGM 268
Cdd:PRK08642 234 PWARAVTGQNLVVDGGL 250
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 22-267 2.94e-24

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: 98.38  E-value: 2.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgiSQLAKDKDAVLAIANVDVRNFEQVENAVKKTVE 101
Cdd:cd08933   7 YADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALE---SELNRAGPGSCKFVPCDVTKEEDIKTLISVTVE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFAN-LSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGAAK 180
Cdd:cd08933  84 RFGRIDCLVNNAGWHPPHQTTDeTSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATK 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 181 AGIDALAKNLAVELGPLGIRSNCIAPGAIDNT--EGLKRLAGK---KYKEKALAKiPLQRLGSTRDIAESTVYIFSpAAS 255
Cdd:cd08933 164 GAITAMTKALAVDESRYGVRVNCISPGNIWTPlwEELAAQTPDtlaTIKEGELAQ-LLGRMGTEAESGLAALFLAA-EAT 241

                       250
                ....*....|..
gi 99030931 256 YVTGTVLVVDGG 267
Cdd:cd08933 242 FCTGIDLLLSGG 253
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 20-268 3.83e-24

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 98.21  E-value: 3.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLF--KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgisqlAKDKDAVLAIANV-DVRNFEQVENAV 96
Cdd:PRK07097   4 NLFslKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLA-----AYRELGIEAHGYVcDVTDEDGVQAMV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   97 KKTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYYGVPFQGH 175
Cdd:PRK07097  79 SQIEKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMiKKGHGKIINICSMMSELGRETVSA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  176 VGAAKAGIDALAKNLAVELGPLGIRSNCIAPG--AIDNTEGLKRLA----GKKYKEKALAKIPLQRLGSTRDIAESTVYI 249
Cdd:PRK07097 159 YAAAKGGLKMLTKNIASEYGEANIQCNGIGPGyiATPQTAPLRELQadgsRHPFDQFIIAKTPAARWGDPEDLAGPAVFL 238

                        250
                 ....*....|....*....
gi 99030931  250 FSPAASYVTGTVLVVDGGM 268
Cdd:PRK07097 239 ASDASNFVNGHILYVDGGI 257
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 27-267 4.47e-24

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 97.54  E-value: 4.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  27 AFVTGGAGTICRVQTEALVLLGckAAIVGRDQERTEQAAKGisqlakdkdAVLAIANVDVRNFEQVENAVKKTVEKFGKI 106
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAG--ATVIALDLPFVLLLEYG---------DPLRLTPLDVADAAAVREVCSRLLAEHGPI 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 107 DFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELK-KSKGSIlfVSATFHYYGVPF--QGHVGAAKAGI 183
Cdd:cd05331  70 DALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKdRRTGAI--VTVASNAAHVPRisMAAYGASKAAL 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 184 DALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAK---------IPLQRLGSTRDIAESTVYIFSPAA 254
Cdd:cd05331 148 ASLSKCLGLELAPYGVRCNVVSPGSTD-TAMQRTLWHDEDGAAQVIAgvpeqfrlgIPLGKIAQPADIANAVLFLASDQA 226

                       250
                ....*....|...
gi 99030931 255 SYVTGTVLVVDGG 267
Cdd:cd05331 227 GHITMHDLVVDGG 239
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 23-267 5.91e-24

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 97.77  E-value: 5.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQerteqaakgisqlAKDKDAVLAIANVDVRNFEQVENAVKKTVEK 102
Cdd:PRK06171   8 QGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHG-------------GDGQHENYQFVPTDVSSAEEVNHTVAEIIEK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNF---VCDFAN------LSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYYGVPF 172
Cdd:PRK06171  75 FGRIDGLVNNAGINIprlLVDEKDpagkyeLNEAAFDKMFNINQKGVFLMSQAVARQMvKQHDGVIVNMSSEAGLEGSEG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  173 QGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTeGLKRLAgkkYkEKALA------------------KIPLQ 234
Cdd:PRK06171 155 QSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEAT-GLRTPE---Y-EEALAytrgitveqlragytktsTIPLG 229

                        250       260       270
                 ....*....|....*....|....*....|...
gi 99030931  235 RLGSTRDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK06171 230 RSGKLSEVADLVCYLLSDRASYITGVTTNIAGG 262
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 23-268 6.22e-24

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: 97.15  E-value: 6.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGisqlakdkdAVLAIANVDVRNFEQVENAVKKtvek 102
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERG---------PGITTRVLDVTDKEQVAALAKE---- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 103 FGKIDfVIAGAAGnFV--CDFANLSPNAFKSVVDIDLLGSFNTAKACL-KELKKSKGSIL-FVSATFHYYGVPFQGHVGA 178
Cdd:cd05368  68 EGRID-VLFNCAG-FVhhGSILDCEDDDWDFAMNLNVRSMYLMIKAVLpKMLARKDGSIInMSSVASSIKGVPNRFVYST 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKAL----AKIPLQRLGSTRDIAESTVYIFSPAA 254
Cdd:cd05368 146 TKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALkafaARQPLGRLATPEEVAALAVYLASDES 225

                       250
                ....*....|....
gi 99030931 255 SYVTGTVLVVDGGM 268
Cdd:cd05368 226 AYVTGTAVVIDGGW 239
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 23-267 7.48e-24

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: 97.17  E-value: 7.48e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKdkdaVLAIAnVDVRNFEQVENAVKKTVEK 102
Cdd:cd08942   5 AGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGE----CIAIP-ADLSSEEGIEALVARVAER 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-----------GSI--LFVSA--TFHY 167
Cdd:cd08942  80 SDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenparviniGSIagIVVSGleNYSY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 168 ygvpfqghvGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTV 247
Cdd:cd08942 160 ---------GASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNDPAALEAEEKSIPLGRWGRPEDMAGLAI 230

                       250       260
                ....*....|....*....|
gi 99030931 248 YIFSPAASYVTGTVLVVDGG 267
Cdd:cd08942 231 MLASRAGAYLTGAVIPVDGG 250
PRK09186 PRK09186
flagellin modification protein A; Provisional
 23-267 8.29e-24

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 97.37  E-value: 8.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlaKDKDAVLAIANVDVRNFEQVENAVKKTVEK 102
Cdd:PRK09186   3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGK--EFKSKKLSLVELDITDQESLEEFLSKSAEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGA---AGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATF--------HYYGV 170
Cdd:PRK09186  81 YGKIDGAVNCAyprNKDYGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGgGNLVNISSIYgvvapkfeIYEGT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  171 PFQGHV--GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAI-DN--TEGLkrlagKKYKEKALAKIPLqrlgSTRDIAES 245
Cdd:PRK09186 161 SMTSPVeyAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGIlDNqpEAFL-----NAYKKCCNGKGML----DPDDICGT 231

                        250       260
                 ....*....|....*....|..
gi 99030931  246 TVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK09186 232 LVFLLSDQSKYITGQNIIVDDG 253
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 24-268 9.73e-24

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 96.73  E-value: 9.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGckAAIVGRDQERTEQAAKGISQLAKDKDAVLAIaNVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADG--FAVAVNYAGSAAAADELVAEIEAAGGRAIAV-QADVADAAAVTRLFDAAETAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSkGSILFVSATFHYYGVPFQGHVGAAKAGI 183
Cdd:PRK12937  82 GRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGPYAASKAAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  184 DALAKNLAVELGPLGIRSNCIAPGAIdNTEGLkrLAGKKYKEKA-LAKI-PLQRLGSTRDIAESTVYIFSPAASYVTGTV 261
Cdd:PRK12937 161 EGLVHVLANELRGRGITVNAVAPGPV-ATELF--FNGKSAEQIDqLAGLaPLERLGTPEEIAAAVAFLAGPDGAWVNGQV 237


                 ....*..
gi 99030931  262 LVVDGGM 268
Cdd:PRK12937 238 LRVNGGF 244
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 24-268 1.25e-23

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 96.52  E-value: 1.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTIcrvQTEALVLLGCKAAIVGRDQERTEQaakgISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK12936   6 GRKALVTGASGGI---GEEIARLLHAQGAIVGLHGTRVEK----LEALAAELGERVKIFPANLSDRDEVKALGQKAEADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAG 182
Cdd:PRK12936  79 EGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRyGRIINITSVVGVTGNPGQANYCASKAG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  183 IDALAKNLAVELGPLGIRSNCIAPGAIDNTeglkrLAGK---KYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:PRK12936 159 MIGFSKSLAQEIATRNVTVNCVAPGFIESA-----MTGKlndKQKEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTG 233


                 ....*....
gi 99030931  260 TVLVVDGGM 268
Cdd:PRK12936 234 QTIHVNGGM 242
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 25-209 2.40e-23

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 95.76  E-value: 2.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgisqlAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKFG 104
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLG------ELLNDNLEVLE-LDVTDEESIKAAVKEVIERFG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 105 KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAGI 183
Cdd:cd05374  74 RIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTPFLGPYCASKAAL 153

                       170       180
                ....*....|....*....|....*.
gi 99030931 184 DALAKNLAVELGPLGIRSNCIAPGAI 209
Cdd:cd05374 154 EALSESLRLELAPFGIKVTIIEPGPV 179
PLN02253 PLN02253
xanthoxin dehydrogenase
 24-267 4.51e-23

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 95.66  E-value: 4.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTIcrvqTEALVLL----GCKAAIVGRDQERTEQAAKGISqlakDKDAVLAIaNVDVRNFEQVENAVKKT 99
Cdd:PLN02253  18 GKVALVTGGATGI----GESIVRLfhkhGAKVCIVDLQDDLGQNVCDSLG----GEPNVCFF-HCDVTVEDDVSRAVDFT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  100 VEKFGKIDFVI--AGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAK-ACLKELKKSKGSIL-FVSATFHYYGVPFQGH 175
Cdd:PLN02253  89 VDKFGTLDIMVnnAGLTGPPCPDIRNVELSEFEKVFDVNVKGVFLGMKhAARIMIPLKKGSIVsLCSVASAIGGLGPHAY 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  176 VGAaKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALA--------KIPLQRLGST-RDIAEST 246
Cdd:PLN02253 169 TGS-KHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTEDALAgfrafagkNANLKGVELTvDDVANAV 247

                        250       260
                 ....*....|....*....|.
gi 99030931  247 VYIFSPAASYVTGTVLVVDGG 267
Cdd:PLN02253 248 LFLASDEARYISGLNLMIDGG 268
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 22-268 5.23e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 94.97  E-value: 5.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRdqERTEQAAKGISQLAkdkdavlaianVDVRNFEQVENAVKKTVE 101
Cdd:PRK06523   7 LAGKRALVTGGTKGIGAATVARLLEAGARVVTTAR--SRPDDLPEGVEFVA-----------ADLTTAEGCAAVARAVLE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVI--AGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVS----------ATFHYy 168
Cdd:PRK06523  74 RLGGVDILVhvLGGSSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMiARGSGVIIHVTsiqrrlplpeSTTAY- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  169 gvpfqghvGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEG----LKRLA---------GKKYKEKALAKIPLQR 235
Cdd:PRK06523 153 --------AAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWI-ETEAavalAERLAeaagtdyegAKQIIMDSLGGIPLGR 223

                        250       260       270
                 ....*....|....*....|....*....|...
gi 99030931  236 LGSTRDIAESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:PRK06523 224 PAEPEEVAELIAFLASDRAASITGTEYVIDGGT 256
PRK05717 PRK05717
SDR family oxidoreductase;
24-268 9.85e-23

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 94.19  E-value: 9.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkdkdavLAIAnVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENA------WFIA-MDVADEAQVAAGVAEVLGQF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAgnfVCD-----FANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGA 178
Cdd:PRK05717  83 GRLDALVCNAA---IADphnttLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  179 AKAGIDALAKNLAVELGPlGIRSNCIAPGAIDNTEGLKRLAgKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVT 258
Cdd:PRK05717 160 SKGGLLALTHALAISLGP-EIRVNAVSPGWIDARDPSQRRA-EPLSEADHAQHPAGRVGTVEDVAAMVAWLLSRQAGFVT 237

                        250
                 ....*....|
gi 99030931  259 GTVLVVDGGM 268
Cdd:PRK05717 238 GQEFVVDGGM 247
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 23-267 1.76e-22

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: 93.67  E-value: 1.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVG-RDQERTEQAAKGIsqLAKDKDAVLAIaNVDVRNFEQVENAVKKTVE 101
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGfGDAAEIEAVRAGL--AAKHGVKVLYH-GADLSKPAAIEDMVAYAQR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAK 180
Cdd:cd08940  78 QFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVASANKSAYVAAK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 181 AGIDALAKNLAVELGPLGIRSNCIAPG------------AIDNTEGLKRLAGKKykEKALAKIPLQRLGSTRDIAESTVY 248
Cdd:cd08940 158 HGVVGLTKVVALETAGTGVTCNAICPGwvltplvekqisALAQKNGVPQEQAAR--ELLLEKQPSKQFVTPEQLGDTAVF 235

                       250
                ....*....|....*....
gi 99030931 249 IFSPAASYVTGTVLVVDGG 267
Cdd:cd08940 236 LASDAASQITGTAVSVDGG 254
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 24-268 1.82e-22

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: 93.42  E-value: 1.82e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGT------ICRVQTEAlvllGCKAAIVGRDqertEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVK 97
Cdd:cd05372   1 GKRILITGIANDrsiawgIAKALHEA----GAELAFTYQP----EALRKRVEKLAERLGESALVLPCDVSNDEEIKELFA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  98 KTVEKFGKIDFV---IAGAAGN-FVCDFANLSPNAFKSVVDIDLLgSFNT-AKACLKELKKSkGSILfvsaTFHYYG--- 169
Cdd:cd05372  73 EVKKDWGKLDGLvhsIAFAPKVqLKGPFLDTSRKGFLKALDISAY-SLVSlAKAALPIMNPG-GSIV----TLSYLGser 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 170 -VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdnteglKRLAGKKYK--EKAL----AKIPLQRLGSTRDI 242
Cdd:cd05372 147 vVPGYNVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPI------KTLAASGITgfDKMLeyseQRAPLGRNVTAEEV 220

                       250       260
                ....*....|....*....|....*.
gi 99030931 243 AESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:cd05372 221 GNTAAFLLSDLSSGITGEIIYVDGGY 246
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 22-269 1.96e-22

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: 93.30  E-value: 1.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQaakgisqLAKDKDAVLAIAnVDVRNFEqvenAVKKTVE 101
Cdd:cd05351   5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDS-------LVRECPGIEPVC-VDLSDWD----ATEEALG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS--KGSILFVSATFHYygVPFQGHV--G 177
Cdd:cd05351  73 SVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARgvPGSIVNVSSQASQ--RALTNHTvyC 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:cd05351 151 STKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMT 230

                       250
                ....*....|..
gi 99030931 258 TGTVLVVDGGMW 269
Cdd:cd05351 231 TGSTLPVDGGFL 242
PRK08416 PRK08416
enoyl-ACP reductase;
22-267 2.69e-22

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 93.30  E-value: 2.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVgrdQERTEQAAKGISQLAKDKDAVLAIA-NVDVRNFEQVENAVKKTV 100
Cdd:PRK08416   6 MKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFT---YNSNVEEANKIAEDLEQKYGIKAKAyPLNILEPETYKELFKKID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  101 EKFGKIDFVIAGA-------AGNFVcDFANLSP----NAFKSVVDIDLLGSFNTAKaclKELKKSKGSILFVSATFHYYG 169
Cdd:PRK08416  83 EDFDRVDFFISNAiisgravVGGYT-KFMRLKPkglnNIYTATVNAFVVGAQEAAK---RMEKVGGGSIISLSSTGNLVY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  170 VP-FQGHvGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAG-KKYKEKALAKIPLQRLGSTRDIAESTV 247
Cdd:PRK08416 159 IEnYAGH-GTSKAAVETMVKYAATELGEKNIRVNAVSGGPID-TDALKAFTNyEEVKAKTEELSPLNRMGQPEDLAGACL 236

                        250       260
                 ....*....|....*....|
gi 99030931  248 YIFSPAASYVTGTVLVVDGG 267
Cdd:PRK08416 237 FLCSEKASWLTGQTIVVDGG 256
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 24-263 5.40e-22

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 92.07  E-value: 5.40e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKG-----ISQLAKDKDAV----LAIAnVDVRNFEQVEN 94
Cdd:cd05338   3 GKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDNGSAKslpgtIEETAEEIEAAggqaLPIV-VDVRDEDQVRA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  95 AVKKTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFhyYGVPFQ 173
Cdd:cd05338  82 LVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAgQGHILNISPPL--SLRPAR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 174 GHV--GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKykekalaKIPLQRlgSTRDIAESTVYIFS 251
Cdd:cd05338 160 GDVayAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPAATELSGGS-------DPARAR--SPEILSDAVLAILS 230

                       250
                ....*....|..
gi 99030931 252 PAASYVTGTVLV 263
Cdd:cd05338 231 RPAAERTGLVVI 242
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 25-267 5.83e-22

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: 91.98  E-value: 5.83e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgiSQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKFG 104
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAE---LQAINPKVKATFVQ-CDVTSWEQLAAAFKKAIEKFG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 105 KIDFVIAGAAGNFVCD--FANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK----GSILFVSATFHYYGVPFQGHVGA 178
Cdd:cd05323  77 RVDILINNAGILDEKSylFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGLYPAPQFPVYSA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 179 AKAGIDALAKNLAVEL-GPLGIRSNCIAPGAIdNTEGLKRLagKKYKEKALAKIPLQrlgSTRDIAESTVYIFSPAASyv 257
Cdd:cd05323 157 SKHGVVGFTRSLADLLeYKTGVRVNAICPGFT-NTPLLPDL--VAKEAEMLPSAPTQ---SPEVVAKAIVYLIEDDEK-- 228

                       250
                ....*....|
gi 99030931 258 TGTVLVVDGG 267
Cdd:cd05323 229 NGAIWIVDGG 238
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 23-267 2.65e-21

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 90.48  E-value: 2.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGIsqlAKDKDAVLAIA-NVDVRNFEQVENAVKKTVE 101
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEI---NAEYGEGMAYGfGADATSEQSVLALSRGVDE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVI--AGAA-GNFVCDFanlSPNAFKSVVDIDLLGSFNTAKACLKEL--KKSKGSILFVSATFHYYGVPFQGHV 176
Cdd:PRK12384  78 IFGRVDLLVynAGIAkAAFITDF---QLGDFDRSLQVNLVGYFLCAREFSRLMirDGIQGRIIQINSKSGKVGSKHNSGY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRL----AGK------KYKEKALAKIPLQRLGSTRDIAEST 246
Cdd:PRK12384 155 SAAKFGGVGLTQSLALDLAEYGITVHSLMLGNLLKSPMFQSLlpqyAKKlgikpdEVEQYYIDKVPLKRGCDYQDVLNML 234

                        250       260
                 ....*....|....*....|.
gi 99030931  247 VYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK12384 235 LFYASPKASYCTGQSINVTGG 255
PRK07577 PRK07577
SDR family oxidoreductase;
84-267 3.39e-21

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 89.79  E-value: 3.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   84 VDVRNFEQVENAVKKTVEKFGkIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFV- 161
Cdd:PRK07577  48 CDLADIEQTAATLAQINEIHP-VDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNIc 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  162 SATFHyyGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLK--RLAGKKYKEKALAKIPLQRLGST 239
Cdd:PRK07577 127 SRAIF--GALDRTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIE-TELFRqtRPVGSEEEKRVLASIPMRRLGTP 203

                        170       180
                 ....*....|....*....|....*...
gi 99030931  240 RDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK07577 204 EEVAAAIAFLLSDDAGFITGQVLGVDGG 231
PRK08589 PRK08589
SDR family oxidoreductase;
25-267 4.80e-21

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 90.22  E-value: 4.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICrvQTEALVLLGCKAAIVGRD-QERTEQAAKGISQLAKDKDAVlaiaNVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK08589   7 KVAVITGASTGIG--QASAIALAQEGAYVLAVDiAEAVSETVDKIKSNGGKAKAY----HVDISDEQQVKDFASEIKEQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGA----AGNFVCDFAnlsPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGAA 179
Cdd:PRK08589  81 GRVDVLFNNAgvdnAAGRIHEYP---VDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYNAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  180 KAGIDALAKNLAVELGPLGIRSNCIAPGAI-----DNTEGLKR-LAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPA 253
Cdd:PRK08589 158 KGAVINFTKSIAIEYGRDGIRANAIAPGTIetplvDKLTGTSEdEAGKTFRENQKWMTPLGRLGKPEEVAKLVVFLASDD 237

                        250
                 ....*....|....
gi 99030931  254 ASYVTGTVLVVDGG 267
Cdd:PRK08589 238 SSFITGETIRIDGG 251
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 22-267 5.24e-21

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 89.62  E-value: 5.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgisQLAKDKDAVLAIaNVDVRNFEQVENAVKKTVE 101
Cdd:PRK12823   6 FAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEVAA----ELRAAGGEALAL-TADLETYAGAQAAMAAAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGN-FVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVS--ATFHYYGVPFqghvG 177
Cdd:PRK12823  81 AFGRIDVLINNVGGTiWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHmLAQGGGAIVNVSsiATRGINRVPY----S 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAID--------NTEGLKRLAGKKYKE---KALAKIPLQRLGSTRDIAEST 246
Cdd:PRK12823 157 AAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEapprrvprNAAPQSEQEKAWYQQivdQTLDSSLMKRYGTIDEQVAAI 236

                        250       260
                 ....*....|....*....|.
gi 99030931  247 VYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK12823 237 LFLASDEASYITGTVLPVGGG 257
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 23-267 6.87e-21

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 89.57  E-value: 6.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlAKDKDAVLAIanvDVRNFEQVENAVKKTVEK 102
Cdd:PRK13394   6 NGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINK-AGGKAIGVAM---DVTNEDAVNAGIDKVAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYYGVPFQGHVGAAK 180
Cdd:PRK13394  82 FGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLKSAYVTAK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  181 AGIDALAKNLAVELGPLGIRSNCIAPGAIdntegLKRLAGKKYKEKA---------------LAKIPLQRLGSTRDIAES 245
Cdd:PRK13394 162 HGLLGLARVLAKEGAKHNVRSHVVCPGFV-----RTPLVDKQIPEQAkelgiseeevvkkvmLGKTVDGVFTTVEDVAQT 236

                        250       260
                 ....*....|....*....|..
gi 99030931  246 TVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK13394 237 VLFLSSFPSAALTGQSFVVSHG 258
PRK07041 PRK07041
SDR family oxidoreductase;
29-267 6.98e-21

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 88.56  E-value: 6.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   29 VTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGIsqlakDKDAVLAIANVDVRNFEQVENAVKKTvekfGKIDF 108
Cdd:PRK07041   2 VVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARAL-----GGGAPVRTAALDITDEAAVDAFFAEA----GPFDH 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  109 VIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKElkkSKGSILFVSATFHYYGVPFQGHVGAAKAGIDALAK 188
Cdd:PRK07041  73 VVITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAARIA---PGGSLTFVSGFAAVRPSASGVLQGAINAALEALAR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  189 NLAVELGPlgIRSNCIAPGAIDnTEGLKRLAGKKYKE---KALAKIPLQRLGSTRDIAESTVYIFspAASYVTGTVLVVD 265
Cdd:PRK07041 150 GLALELAP--VRVNTVSPGLVD-TPLWSKLAGDAREAmfaAAAERLPARRVGQPEDVANAILFLA--ANGFTTGSTVLVD 224


                 ..
gi 99030931  266 GG 267
Cdd:PRK07041 225 GG 226
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 24-249 1.14e-20

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: 88.36  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgisQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKF 103
Cdd:cd08934   3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALAD---ELEAEGGKALVLE-LDVTDEQQVDAAVERTVEAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELK-KSKGSILFVSATFHYYGVPFQGHVGAAKAG 182
Cdd:cd08934  79 GRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNSAVYNATKFG 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 183 IDALAKNLAVELGPLGIRSNCIAPGAIDN--TEGLKRLAGKKYKEKALAKI-PLQrlgsTRDIAESTVYI 249
Cdd:cd08934 159 VNAFSEGLRQEVTERGVRVVVIEPGTVDTelRDHITHTITKEAYEERISTIrKLQ----AEDIAAAVRYA 224
PRK06398 PRK06398
aldose dehydrogenase; Validated
 22-268 1.28e-20

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 88.74  E-value: 1.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERteqaakgisqlakdkDAVLAIANVDVRNFEQVENAVKKTVE 101
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS---------------YNDVDYFKVDVSNKEQVIKGIDYVIS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPFQGHVGAAK 180
Cdd:PRK06398  69 KYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYmLKQDKGVIINIASVQSFAVTRNAAAYVTSK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  181 AGIDALAKNLAVELGPLgIRSNCIAPGAIDN--TEGLKRLAGKKYKEKALAKI-------PLQRLGSTRDIAESTVYIFS 251
Cdd:PRK06398 149 HAVLGLTRSIAVDYAPT-IRCVAVCPGSIRTplLEWAAELEVGKDPEHVERKIrewgemhPMKRVGKPEEVAYVVAFLAS 227

                        250
                 ....*....|....*..
gi 99030931  252 PAASYVTGTVLVVDGGM 268
Cdd:PRK06398 228 DLASFITGECVTVDGGL 244
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 22-267 1.51e-20

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 88.40  E-value: 1.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGckAAIVGRDQERTEQaakgisqlakdKDAVLAIANVDVRNFEQVENAVKKTVE 101
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAG--AKVIGFDQAFLTQ-----------EDYPFATFVLDVSDAAAVAQVCQRLLA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDfVIAGAAGNF-VCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSAtfHYYGVPFQGHV--G 177
Cdd:PRK08220  73 ETGPLD-VLVNAAGILrMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRsGAIVTVGS--NAAHVPRIGMAayG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAK---------IPLQRLGSTRDIAESTVY 248
Cdd:PRK08220 150 ASKAALTSLAKCVGLELAPYGVRCNVVSPGSTD-TDMQRTLWVDEDGEQQVIAgfpeqfklgIPLGKIARPQEIANAVLF 228

                        250
                 ....*....|....*....
gi 99030931  249 IFSPAASYVTGTVLVVDGG 267
Cdd:PRK08220 229 LASDLASHITLQDIVVDGG 247
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-213 1.71e-20

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 87.82  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLakdkDAVLAIANVDVRNFEQVENAVKKTVEK 102
Cdd:PRK07666   6 QGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAY----GVKVVIATADVSDYEEVTAAIEQLKNE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVI--AGAA--GNFVcdfaNLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVG 177
Cdd:PRK07666  82 LGSIDILInnAGISkfGKFL----ELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQsGDIINISSTAGQKGAAVTSAYS 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTE 213
Cdd:PRK07666 158 ASKFGVLGLTESLMQEVRKHNIRVTALTPSTV-ATD 192
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 22-269 2.10e-20

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: 88.06  E-value: 2.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkdkdavLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAA------CAIS-LDVTDQASIDRCVAALVD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL--KKSKGSILFVSATFHYYGVPFQGHVGAA 179
Cdd:cd05363  74 RWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMiaQGRGGKIINMASQAGRRGEALVGVYCAT 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDNT--EGL--------KRLAGKKyKEKALAKIPLQRLGSTRDIAESTVYI 249
Cdd:cd05363 154 KAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEhwDGVdakfaryeNRPRGEK-KRLVGEAVPFGRMGRAEDLTGMAIFL 232

                       250       260
                ....*....|....*....|
gi 99030931 250 FSPAASYVTGTVLVVDGGMW 269
Cdd:cd05363 233 ASTDADYIVAQTYNVDGGNW 252
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 21-208 2.92e-20

(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: 87.38  E-value: 2.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  21 LFKGKVAFVTGGAGTICRVQTEALVLLGCKaaIVGRDQeRTEQAAKGISQLAKDK--DAVLAIANVDVRNFEQVENA--- 95
Cdd:cd05353   2 RFDGRVVLVTGAGGGLGRAYALAFAERGAK--VVVNDL-GGDRKGSGKSSSAADKvvDEIKAAGGKAVANYDSVEDGeki 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  96 VKKTVEKFGKIDFVIAGAAgnFVCD--FANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPF 172
Cdd:cd05353  79 VKTAIDAFGRVDILVNNAG--ILRDrsFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGLYGNFG 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 99030931 173 QGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGA 208
Cdd:cd05353 157 QANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAA 192
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 22-268 7.25e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 86.32  E-value: 7.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLakdkdavlaIANVDVRNFEQVENAVKKTVE 101
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGL---------FVPTDVTDEDAVNALFDTAAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKID--FVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSIL----FV----SATFhyygv 170
Cdd:PRK06057  76 TYGSVDiaFNNAGISPPEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQgKGSIIntasFVavmgSATS----- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  171 pfQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAGKKyKEKA---LAKIPLQRLGSTRDIAESTV 247
Cdd:PRK06057 151 --QISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPV-NTPLLQELFAKD-PERAarrLVHVPMGRFAEPEEIAAAVA 226

                        250       260
                 ....*....|....*....|.
gi 99030931  248 YIFSPAASYVTGTVLVVDGGM 268
Cdd:PRK06057 227 FLASDDASFITASTFLVDGGI 247
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 25-274 1.25e-19

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: 86.05  E-value: 1.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVEKFG 104
Cdd:cd08945   4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTC----DVRSVPEIEALVAAAVARYG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 105 KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE---LKKSKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:cd08945  80 PIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggmLERGTGRIINIASTGGKQGVVHAAPYSASKH 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 182 GIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAG-----KKYKEKAL----AKIPLQRLGSTRDIAESTVYIFSP 252
Cdd:cd08945 160 GVVGFTKALGLELARTGITVNAVCPGFVETPMAASVREHyadiwEVSTEEAFdritARVPLGRYVTPEEVAGMVAYLIGD 239

                       250       260
                ....*....|....*....|..
gi 99030931 253 AASYVTGTVLVVDGGmwhLGTY 274
Cdd:cd08945 240 GAAAVTAQALNVCGG---LGNY 258
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 21-262 3.72e-19

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: 84.17  E-value: 3.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  21 LFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIaNVDVRNFEQVENAVKKTV 100
Cdd:cd05340   1 LLNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFIL-DLLTCTSENCQQLAQRIA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 101 EKFGKIDFVIAGAAGNF-VCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGA 178
Cdd:cd05340  80 VNYPRLDGVLHNAGLLGdVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYAV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEglkrlagkkyKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVT 258
Cdd:cd05340 160 SKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAM----------RASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKT 229


                ....
gi 99030931 259 GTVL 262
Cdd:cd05340 230 GMTF 233
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
24-267 3.98e-19

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 84.57  E-value: 3.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTG---GAGticrvQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTV 100
Cdd:PRK12481   8 GKVAIITGcntGLG-----QGMAIGLAKAGADIVGVGVAEAPETQAQVEALGRKFHFITA----DLIQQKDIDSIVSQAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  101 EKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKK--SKGSILFVSATFHYYGVPFQGHVGA 178
Cdd:PRK12481  79 EVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKqgNGGKIINIASMLSFQGGIRVPSYTA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  179 AKAGIDALAKNLAVELGPLGIRSNCIAPG--AIDNTEGLKrlAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASY 256
Cdd:PRK12481 159 SKSAVMGLTRALATELSQYNINVNAIAPGymATDNTAALR--ADTARNEAILERIPASRWGTPDDLAGPAIFLSSSASDY 236

                        250
                 ....*....|.
gi 99030931  257 VTGTVLVVDGG 267
Cdd:PRK12481 237 VTGYTLAVDGG 247
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 25-210 5.85e-19

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: 83.33  E-value: 5.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgisqlAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKFG 104
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAA------AQELEGVLGLA-GDVRDEADVRRAVDAMEEAFG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 105 KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSF-NTAKACLKELKKSKGSILFVSAtfhYYGV-PFQGHVG--AAK 180
Cdd:cd08929  74 GLDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFyCIHKAAPALLRRGGGTIVNVGS---LAGKnAFKGGAAynASK 150

                       170       180       190
                ....*....|....*....|....*....|
gi 99030931 181 AGIDALAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:cd08929 151 FGLLGLSEAAMLDLREANIRVVNVMPGSVD 180
fabG_rel TIGR01831
3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well ...
 85-268 1.18e-18

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


Pssm-ID: 273825 [Multi-domain]  Cd Length: 239  Bit Score: 83.03  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931    85 DVRNFEQVENAVKKTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVS 162
Cdd:TIGR01831  56 DVADRVACREVLEADIAQHGAYYGVVLNAGIARDAAFPALSEDDWDAVIHTNLDGFYNVIHPCIMPMIGARqgGRIITLA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   163 ATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLagKKYKEKALAKIPLQRLGSTRDI 242
Cdd:TIGR01831 136 SVSGVMGNRGQVNYSAAKAGLIGATKALAIELAKRKITVNCIAPGLID-TGMIAME--ESALKEALSMVPMKRMGQPEEV 212

                         170       180
                  ....*....|....*....|....*.
gi 99030931   243 AESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:TIGR01831 213 AGLASFLMSDIAGYVTRQVISVNGGM 238
PRK07985 PRK07985
SDR family oxidoreductase;
15-272 1.51e-18

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 83.51  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   15 GSWRpdlFKGKVAFVTGGAGTICRVQTEALVLLGCKAAI--VGRDQERTEQAAKGISQLAKDkdAVLAIANVDVRNFEQv 92
Cdd:PRK07985  43 GSGR---LKDRKALVTGGDSGIGRAAAIAYAREGADVAIsyLPVEEEDAQDVKKIIEECGRK--AVLLPGDLSDEKFAR- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   93 eNAVKKTVEKFGKIDfVIAGAAGNFVC--DFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSkGSILFVSATFHYYGV 170
Cdd:PRK07985 117 -SLVHEAHKALGGLD-IMALVAGKQVAipDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKG-ASIITTSSIQAYQPS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  171 PFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTeglKRLAGKKYKEKALA---KIPLQRLGSTRDIAESTV 247
Cdd:PRK07985 194 PHLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTA---LQISGGQTQDKIPQfgqQTPMKRAGQPAELAPVYV 270

                        250       260
                 ....*....|....*....|....*
gi 99030931  248 YIFSPAASYVTGTVLVVDGGMwHLG 272
Cdd:PRK07985 271 YLASQESSYVTAEVHGVCGGE-HLG 294
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
25-272 3.89e-18

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 81.60  E-value: 3.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAG----TIC-RVQTEAL-VLLGCKAAIVGRDQERTEQAAKGISQLAKDKDavlaianvdVRNFEQVENAVKK 98
Cdd:PRK12938   4 RIAYVTGGMGgigtSICqRLHKDGFkVVAGCGPNSPRRVKWLEDQKALGFDFIASEGN---------VGDWDSTKAAFDK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   99 TVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYYGVPFQGHVG 177
Cdd:PRK12938  75 VKAEVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMvERGWGRIINISSVNGQKGQFGQTNYS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAgKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:PRK12938 155 TAKAGIHGFTMSLAQEVATKGVTVNTVSPGYI-GTDMVKAIR-PDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFS 232

                        250
                 ....*....|....*
gi 99030931  258 TGTVLVVDGGMwHLG 272
Cdd:PRK12938 233 TGADFSLNGGL-HMG 246
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
44-267 5.45e-18

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 81.71  E-value: 5.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   44 LVLLGCKAAIVGRDQERTeqAAKGISQLAKDKDAVLA--------------IAN---------VDVRNFEQVENAVKKTV 100
Cdd:PRK08415   1 MIMKGKKGLIVGVANNKS--IAYGIAKACFEQGAELAftylnealkkrvepIAQelgsdyvyeLDVSKPEHFKSLAESLK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  101 EKFGKIDFVIAGAA--------GNFVcdfaNLSPNAFKSVVDIDLLGSFNTAKACLKELKKsKGSILfvsaTFHYYG--- 169
Cdd:PRK08415  79 KDLGKIDFIVHSVAfapkealeGSFL----ETSKEAFNIAMEISVYSLIELTRALLPLLND-GASVL----TLSYLGgvk 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  170 -VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdnteglKRLAGK---------KYKEkalAKIPLQRLGST 239
Cdd:PRK08415 150 yVPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNAISAGPI------KTLAASgigdfrmilKWNE---INAPLKKNVSI 220

                        250       260
                 ....*....|....*....|....*...
gi 99030931  240 RDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK08415 221 EEVGNSGMYLLSDLSSGVTGEIHYVDAG 248
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
62-268 7.24e-18

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 81.14  E-value: 7.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   62 EQAAKGISQLAKDKDAVLaIANVDVRNFEQVENAVKKTVEKFGKIDFVIAGAAgnfvcdFA----------NLSPNAFKS 131
Cdd:PRK07533  46 DKARPYVEPLAEELDAPI-FLPLDVREPGQLEAVFARIAEEWGRLDFLLHSIA------FApkedlhgrvvDCSREGFAL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  132 VVDIDLlGSFnTAKACLKE-LKKSKGSILFVSatfhYYG----VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAP 206
Cdd:PRK07533 119 AMDVSC-HSF-IRMARLAEpLMTNGGSLLTMS----YYGaekvVENYNLMGPVKAALESSVRYLAAELGPKGIRVHAISP 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 99030931  207 GAIDN--TEGLKRLagKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:PRK07533 193 GPLKTraASGIDDF--DALLEDAAERAPLRRLVDIDDVGAVAAFLASDAARRLTGNTLYIDGGY 254
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 22-225 1.14e-17

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: 80.32  E-value: 1.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTG---GAGTICrvqteALVL--LGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIanvDVRNFEQVENAV 96
Cdd:cd05332   1 LQGKVVIITGassGIGEEL-----AYHLarLGARLVLSARREERLEEVKSECLELGAPSPHVVPL---DMSDLEDAEQVV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  97 KKTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELK-KSKGSILFVSATFHYYGVPFQGH 175
Cdd:cd05332  73 EEALKLFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIeRSQGSIVVVSSIAGKIGVPFRTA 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 99030931 176 VGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKE 225
Cdd:cd05332 153 YAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGSMS 202
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 26-268 1.41e-17

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: 80.20  E-value: 1.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  26 VAFVTGGAGTICRVQTEALVLLGCKAAIV-GRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVEKFG 104
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINdLPDDDQATEVVAEVLAAGRRAIYFQA----DIGELSDHEALLDQAWEDFG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 105 KIDFVI--AGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-------KKSKGSILFVSATFHYYGVPFQGH 175
Cdd:cd05337  79 RLDCLVnnAGIAVRPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMveqpdrfDGPHRSIIFVTSINAYLVSPNRGE 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 176 VGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNteGLKRLAGKKYKEK-ALAKIPLQRLGSTRDIAESTVYIFSPAA 254
Cdd:cd05337 159 YCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHT--DMTAPVKEKYDELiAAGLVPIRRWGQPEDIAKAVRTLASGLL 236

                       250
                ....*....|....
gi 99030931 255 SYVTGTVLVVDGGM 268
Cdd:cd05337 237 PYSTGQPINIDGGL 250
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 25-267 1.78e-17

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 79.63  E-value: 1.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQErtEQAAKGISQLAKDKDAVLAIaNVDVRNFEQVENAVKKTVEKFG 104
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSE--AEAQRLKDELNALRNSAVLV-QADLSDFAACADLVAAAFRAFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 105 KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPfqGHVG--AAKA 181
Cdd:cd05357  78 RCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSrNGSIINIIDAMTDRPLT--GYFAycMSKA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 182 GIDALAKNLAVELGPLgIRSNCIAPGAIDNTEGLkrlaGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPaaSYVTGTV 261
Cdd:cd05357 156 ALEGLTRSAALELAPN-IRVNGIAPGLILLPEDM----DAEYRENALRKVPLKRRPSAEEIADAVIFLLDS--NYITGQI 228


                ....*.
gi 99030931 262 LVVDGG 267
Cdd:cd05357 229 IKVDGG 234
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 26-212 7.97e-17

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: 77.81  E-value: 7.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  26 VAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVEKFGK 105
Cdd:cd05360   2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVA----DVADAAQVERAADTAVERFGR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 106 IDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKK-SKGSILFVSATFHYYGVPFQGHVGAAKAGID 184
Cdd:cd05360  78 IDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRrGGGALINVGSLLGYRSAPLQAAYSASKHAVR 157

                       170       180       190
                ....*....|....*....|....*....|
gi 99030931 185 ALAKNLAVELGPLG--IRSNCIAPGAIDNT 212
Cdd:cd05360 158 GFTESLRAELAHDGapISVTLVQPTAMNTP 187
PRK07069 PRK07069
short chain dehydrogenase; Validated
 27-268 1.06e-16

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 77.83  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   27 AFVTGGAGTICRVQTEALVLLGCKAAIVgrDQERTEQAAKGISQLAKDKDAVLAIANV-DVRNFEQVENAVKKTVEKFGK 105
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLT--DINDAAGLDAFAAEINAAHGEGVAFAAVqDVTDEAQWQALLAQAADAMGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  106 IDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAGID 184
Cdd:PRK07069  80 LSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAFKAEPDYTAYNASKAAVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  185 ALAKNLAVELGP--LGIRSNCIAPGAIDN--TEGLKRLAGKKYKEKALAK-IPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:PRK07069 160 SLTKSIALDCARrgLDVRCNSIHPTFIRTgiVDPIFQRLGEEEATRKLARgVPLGRLGEPDDVAHAVLYLASDESRFVTG 239


                 ....*....
gi 99030931  260 TVLVVDGGM 268
Cdd:PRK07069 240 AELVIDGGI 248
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
22-267 1.22e-16

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 77.61  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTG---GAGticrvQTEALVLLGCKAAIVGRD-QERTEQAAKgISQLAKDKDAVLAianvDVRNFEQVENAVK 97
Cdd:PRK08993   8 LEGKVAVVTGcdtGLG-----QGMALGLAEAGCDIVGINiVEPTETIEQ-VTALGRRFLSLTA----DLRKIDGIPALLE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKK--SKGSILFVSATFHYYG---VPf 172
Cdd:PRK08993  78 RAVAEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAqgNGGKIINIASMLSFQGgirVP- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  173 qgHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPG--AIDNTEGLKrlAGKKYKEKALAKIPLQRLGSTRDIAESTVYIF 250
Cdd:PRK08993 157 --SYTASKSGVMGVTRLMANEWAKHNINVNAIAPGymATNNTQQLR--ADEQRSAEILDRIPAGRWGLPSDLMGPVVFLA 232

                        250
                 ....*....|....*..
gi 99030931  251 SPAASYVTGTVLVVDGG 267
Cdd:PRK08993 233 SSASDYINGYTIAVDGG 249
PRK07775 PRK07775
SDR family oxidoreductase;
27-207 1.58e-16

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 77.49  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   27 AFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISqlAKDKDAVlAIAnVDVRNFEQVENAVKKTVEKFGKI 106
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIR--ADGGEAV-AFP-LDVTDPDSVKSFVAQAEEALGEI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  107 DFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPFQGHVGAAKAGIDA 185
Cdd:PRK07775  89 EVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGmIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEA 168

                        170       180
                 ....*....|....*....|..
gi 99030931  186 LAKNLAVELGPLGIRSNCIAPG 207
Cdd:PRK07775 169 MVTNLQMELEGTGVRASIVHPG 190
PRK06181 PRK06181
SDR family oxidoreductase;
24-207 2.58e-16

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 76.94  E-value: 2.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkdkDAVLAIAnVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHG---GEALVVP-TDVSDAEACERLIEAAVARF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLS-PNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGAAKAG 182
Cdd:PRK06181  77 GGIDILVNNAGITMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHA 156

                        170       180
                 ....*....|....*....|....*
gi 99030931  183 IDALAKNLAVELGPLGIRSNCIAPG 207
Cdd:PRK06181 157 LHGFFDSLRIELADDGVAVTVVCPG 181
PRK08278 PRK08278
SDR family oxidoreductase;
22-211 2.95e-16

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 76.87  E-value: 2.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDA----VLAIAnVDVRNFEQVENAVK 97
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHPKLPGTIHTAAEEIEAaggqALPLV-GDVRDEDQVAAAVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGS-ILFVSATFHYYGVPFQGHV 176
Cdd:PRK08278  83 KAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPhILTLSPPLNLDPKWFAPHT 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 99030931  177 G--AAKAGIDALAKNLAVELGPLGIRSNC------IAPGAIDN 211
Cdd:PRK08278 163 AytMAKYGMSLCTLGLAEEFRDDGIAVNAlwprttIATAAVRN 205
PRK07831 PRK07831
SDR family oxidoreductase;
20-264 3.46e-16

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 76.61  E-value: 3.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLFKGKVAFVTGGAGT-ICRVQTEALVLLGCKAAIVGRDQERTEQAAkgiSQLAKD--KDAVLAIAnVDVRNFEQVENAV 96
Cdd:PRK07831  13 GLLAGKVVLVTAAAGTgIGSATARRALEEGARVVISDIHERRLGETA---DELAAElgLGRVEAVV-CDVTSEAQVDALI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   97 KKTVEKFGKIDFVI--AGAAGNfvCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELK--KSKGSILFVSATFHYYGVPF 172
Cdd:PRK07831  89 DAAVERLGRLDVLVnnAGLGGQ--TPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRarGHGGVIVNNASVLGWRAQHG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  173 QGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGaidnteglkrLAGKKYKEKALAKIPLQRLGSTR---------DIA 243
Cdd:PRK07831 167 QAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPS----------IAMHPFLAKVTSAELLDELAAREafgraaepwEVA 236

                        250       260
                 ....*....|....*....|.
gi 99030931  244 ESTVYIFSPAASYVTGTVLVV 264
Cdd:PRK07831 237 NVIAFLASDYSSYLTGEVVSV 257
PRK05650 PRK05650
SDR family oxidoreductase;
28-250 5.47e-16

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 75.85  E-value: 5.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   28 FVTGGAGTICRvqteALVLL----GCKAAIVGRDQERTEQAAKGISQLAKDKdavlAIANVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK05650   4 MITGAASGLGR----AIALRwareGWRLALADVNEEGGEETLKLLREAGGDG----FYQRCDVRDYSQLTALAQACEEKW 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVI--AG-AAGNFvcdFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAA 179
Cdd:PRK05650  76 GGIDVIVnnAGvASGGF---FEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGPAMSSYNVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  180 KAGIDALAKNLAVELGPLGIRSNCIAPG---------AIDNTEGLKRLAGkkykeKALAKIPLqrlgSTRDIAEstvYIF 250
Cdd:PRK05650 153 KAGVVALSETLLVELADDEIGVHVVCPSffqtnlldsFRGPNPAMKAQVG-----KLLEKSPI----TAADIAD---YIY 220
PRK09730 PRK09730
SDR family oxidoreductase;
25-267 1.10e-15

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 74.89  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRvqtEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKFG 104
Cdd:PRK09730   2 AIALVTGGSRGIGR---ATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  105 KIDFVIAGAAGNFV-CDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKK----SKGSILFVSATFHYYGVPFQgHV--G 177
Cdd:PRK09730  79 PLAALVNNAGILFTqCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALkhggSGGAIVNVSSAASRLGAPGE-YVdyA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEgLKRLAGKKYK-EKALAKIPLQRLGSTRDIAESTVYIFSPAASY 256
Cdd:PRK09730 158 ASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFI-YTE-MHASGGEPGRvDRVKSNIPMQRGGQPEEVAQAIVWLLSDKASY 235

                        250
                 ....*....|.
gi 99030931  257 VTGTVLVVDGG 267
Cdd:PRK09730 236 VTGSFIDLAGG 246
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 27-210 3.42e-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: 73.13  E-value: 3.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  27 AFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKdavlAIANVDVRNFEQVENAVKKTVEKFGKI 106
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSV----EVEILDVTDEERNQLVIAELEAELGGL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 107 DFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELK-KSKGSILFVSATFHYYGVPFQGHVGAAKAGIDA 185
Cdd:cd05350  77 DLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRaKGRGHLVLISSVAALRGLPGAAAYSASKAALSS 156

                       170       180
                ....*....|....*....|....*
gi 99030931 186 LAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:cd05350 157 LAESLRYDVKKRGIRVTVINPGFID 181
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 140-267 4.57e-15

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: 72.99  E-value: 4.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 140 SFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDN-----TE 213
Cdd:cd05361 108 PFALLQAAIAQMKKAGgGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSptyfpTS 187

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 99030931 214 GLKrlAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:cd05361 188 DWE--NNPELRERVKRDVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFAGG 239
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
58-267 5.96e-15

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 72.84  E-value: 5.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   58 QERTEQAAKGI-SQLAKDKDAVLAIanvDVRNFEQVENAVKKTVEKFGKIDFV---IAGAAGNFVC-DFANLSPNAFKSV 132
Cdd:PRK08594  42 GERLEKEVRELaDTLEGQESLLLPC---DVTSDEEITACFETIKEEVGVIHGVahcIAFANKEDLRgEFLETSRDGFLLA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  133 VDIDLLGSFNTAKAcLKELKKSKGSILfvsaTFHYYG----VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGA 208
Cdd:PRK08594 119 QNISAYSLTAVARE-AKKLMTEGGSIV----TLTYLGgervVQNYNVMGVAKASLEASVKYLANDLGKDGIRVNAISAGP 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 99030931  209 IdNTEGLKRLAG-----KKYKEKAlakiPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK08594 194 I-RTLSAKGVGGfnsilKEIEERA----PLRRTTTQEEVGDTAAFLFSDLSRGVTGENIHVDSG 252
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 24-272 6.80e-15

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 73.17  E-value: 6.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQteALVLLGCKAAIVGRDQERT-EQAAKGISQLAKDKDAVL-----AIANV-DVRNFEQVENAV 96
Cdd:PRK07791   6 GRVVIVTGAGGGIGRAH--ALAFAAEGARVVVNDIGVGlDGSASGGSAAQAVVDEIVaaggeAVANGdDIADWDGAANLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   97 KKTVEKFGKIDFVIAGAAgnFVCD--FANLSPNAFKSVVDIDLLGSFNTA-------KACLKELKKSKGSILFVSATFHY 167
Cdd:PRK07791  84 DAAVETFGGLDVLVNNAG--ILRDrmIANMSEEEWDAVIAVHLKGHFATLrhaaaywRAESKAGRAVDARIINTSSGAGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  168 YGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDN-TEGLKRLAGKKYKEKALakiplqRLGSTRDIAEST 246
Cdd:PRK07791 162 QGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAARTRmTETVFAEMMAKPEEGEF------DAMAPENVSPLV 235

                        250       260       270
                 ....*....|....*....|....*....|..
gi 99030931  247 VYIFSPAASYVTGTVLVVDGGM------WHLG 272
Cdd:PRK07791 236 VWLGSAESRDVTGKVFEVEGGKisvaegWRHG 267
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 20-268 8.54e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 72.49  E-value: 8.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLF--KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGIsqlaKDKDAVLAIANVDVRNFEQVENAVK 97
Cdd:PRK07523   4 NLFdlTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESL----KGQGLSAHALAFDVTDHDAVRAAID 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYYGVPFQGHV 176
Cdd:PRK07523  80 AFEAEIGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMiARGAGKIINIASVQSALARPGIAPY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASY 256
Cdd:PRK07523 160 TATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALVADPEFSAWLEKRTPAGRWGKVEELVGACVFLASDASSF 239

                        250
                 ....*....|..
gi 99030931  257 VTGTVLVVDGGM 268
Cdd:PRK07523 240 VNGHVLYVDGGI 251
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 23-194 1.29e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 73.03  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDkdaVLAIAnVDVRNFEQVENAVKKTVEK 102
Cdd:PRK07109   7 GRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGE---ALAVV-ADVADAEAVQAAADRAEEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELK-KSKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK07109  83 LGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRpRDRGAIIQVGSALAYRSIPLQSAYCAAKH 162

                        170
                 ....*....|...
gi 99030931  182 GIDALAKNLAVEL 194
Cdd:PRK07109 163 AIRGFTDSLRCEL 175
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 22-236 1.60e-14

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: 71.18  E-value: 1.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISqlakdkdAVLAIAnVDVRNFEQVENAVKKTVE 101
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELP-------NIHTIV-LDVGDAESVEALAEALLS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVI--AGAAGNFvcDFANLSP--NAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYygVPFQGH- 175
Cdd:cd05370  75 EYPNLDILInnAGIQRPI--DLRDPASdlDKADTEIDTNLIGPIRLIKAFLPHLKKQpEATIVNVSSGLAF--VPMAANp 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 99030931 176 -VGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGkkyKEKALAKIPLQRL 236
Cdd:cd05370 151 vYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNP---DGGTPRKMPLDEF 209
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 20-268 2.25e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 71.32  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLF--KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAvlaiANVDVRNFEQVENAVK 97
Cdd:PRK08085   3 DLFslAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHA----APFNVTHKQEVEAAIE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYYGVPFQGHV 176
Cdd:PRK08085  79 HIEKDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMvKRQAGKIINICSMQSELGRDTITPY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAGKKYKEKALAK-IPLQRLGSTRDIAESTVYIFSPAAS 255
Cdd:PRK08085 159 AASKGAVKMLTRGMCVELARHNIQVNGIAPGYF-KTEMTKALVEDEAFTAWLCKrTPAARWGDPQELIGAAVFLSSKASD 237

                        250
                 ....*....|...
gi 99030931  256 YVTGTVLVVDGGM 268
Cdd:PRK08085 238 FVNGHLLFVDGGM 250
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
85-267 2.25e-14

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 71.28  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   85 DVRNFEQVENAVKKTVEKFGKIDFVI-----AGAAGnFVCDFANLSPNAFKSVVDIDLLGSFNTAKAClKELKKSKGSIL 159
Cdd:PRK07370  67 DVQDDAQIEETFETIKQKWGKLDILVhclafAGKEE-LIGDFSATSREGFARALEISAYSLAPLCKAA-KPLMSEGGSIV 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  160 fvsaTFHYYG----VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAG-----KKYKEKAlak 230
Cdd:PRK07370 145 ----TLTYLGgvraIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPI-RTLASSAVGGildmiHHVEEKA--- 216

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 99030931  231 iPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK07370 217 -PLRRTVTQTEVGNTAAFLLSDLASGITGQTIYVDAG 252
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
66-267 2.37e-14

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 71.32  E-value: 2.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   66 KGISQLAKDKDAVLAiANVDVRNFEQVENAVKKTVEKFGKIDFVIAGAA----GNFVCDFANLSPNAFKSVVDIDLLgSF 141
Cdd:PRK08159  50 KRVEPLAAELGAFVA-GHCDVTDEASIDAVFETLEKKWGKLDFVVHAIGfsdkDELTGRYVDTSRDNFTMTMDISVY-SF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  142 NTAKACLKELKKSKGSILfvsaTFHYYG----VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdnteglKR 217
Cdd:PRK08159 128 TAVAQRAEKLMTDGGSIL----TLTYYGaekvMPHYNVMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPI------KT 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 99030931  218 LAGK---------KYKEkalAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK08159 198 LAASgigdfryilKWNE---YNAPLRRTVTIEEVGDSALYLLSDLSRGVTGEVHHVDSG 253
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-267 3.22e-14

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 70.91  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKaaIVGRDQERTEQAAKGISQLAK-DKDAVLAIANVDVRnfEQVENAVKKTVE 101
Cdd:PRK06077   5 KDKVVVVTGSGRGIGRAIAVRLAKEGSL--VVVNAKKRAEEMNETLKMVKEnGGEGIGVLADVSTR--EGCETLAKATID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSkGSILFVSATfhyYGV-PFQGH--VGA 178
Cdd:PRK06077  81 RYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREG-GAIVNIASV---AGIrPAYGLsiYGA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  179 AKAGIDALAKNLAVELGPlGIRSNCIAPGAIDNT--EGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAAsy 256
Cdd:PRK06077 157 MKAAVINLTKYLALELAP-KIRVNAIAPGFVKTKlgESLFKVLGMSEKEFAEKFTLMGKILDPEEVAEFVAAILKIES-- 233

                        250
                 ....*....|.
gi 99030931  257 VTGTVLVVDGG 267
Cdd:PRK06077 234 ITGQVFVLDSG 244
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-268 5.93e-14

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 69.99  E-value: 5.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRdqeRTEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKFG 104
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDR---PDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  105 KIDFVI--AGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKG-------SILFVSATFHYYGVPFQGH 175
Cdd:PRK12745  80 RIDCLVnnAGVGVKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphrSIVFVSSVNAIMVSPNRGE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  176 VGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAI--DNTEGLKrlagKKYKEKALAKI-PLQRLGSTRDIAESTVYIFSP 252
Cdd:PRK12745 160 YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIktDMTAPVT----AKYDALIAKGLvPMPRWGEPEDVARAVAALASG 235

                        250
                 ....*....|....*.
gi 99030931  253 AASYVTGTVLVVDGGM 268
Cdd:PRK12745 236 DLPYSTGQAIHVDGGL 251
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 24-268 6.85e-14

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 70.58  E-value: 6.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVqtEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIANvDVRNFEQVENAVKKTVEkF 103
Cdd:PRK07792  12 GKVAVVTGAAAGLGRA--EALGLARLGATVVVNDVASALDASDVLDEIRAAGAKAVAVAG-DISQRATADELVATAVG-L 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAK-ACLKELKKSK-------GSILFVSATFHYYGVPFQGH 175
Cdd:PRK07792  88 GGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRnAAAYWRAKAKaaggpvyGRIVNTSSEAGLVGPVGQAN 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  176 VGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAidNTEGLKRLAGKKYKEKALAKIPLqrlgSTRDIAESTVYIFSPAAS 255
Cdd:PRK07792 168 YGAAKAGITALTLSAARALGRYGVRANAICPRA--RTAMTADVFGDAPDVEAGGIDPL----SPEHVVPLVQFLASPAAA 241

                        250
                 ....*....|...
gi 99030931  256 YVTGTVLVVDGGM 268
Cdd:PRK07792 242 EVNGQVFIVYGPM 254
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 25-251 1.36e-13

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: 68.85  E-value: 1.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianVDVRNFEQVENAVKKTVEKFG 104
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQ---LDVSDRESIEAALENLPEEFR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 105 KIDFVI--AG-AAGnfVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYYGVPfQGHV-GAA 179
Cdd:cd05346  78 DIDILVnnAGlALG--LDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMiARNQGHIINLGSIAGRYPYA-GGNVyCAT 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 99030931 180 KAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAK--IPLQrlgsTRDIAESTVYIFS 251
Cdd:cd05346 155 KAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLVRFHGDKEKADKVYEgvEPLT----PEDIAETILWVAS 224
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 20-246 1.47e-13

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 69.21  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKT 99
Cdd:PRK05876   2 DGFPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMC----DVRHREEVTHLADEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  100 VEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACL-KELKKSKGSILFVSATFHYYgVPFQ--GHV 176
Cdd:PRK05876  78 FRLLGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLpRLLEQGTGGHVVFTASFAGL-VPNAglGAY 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 99030931  177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAID-----NTEGLKRLA-GKKYKEKALAKIPLQRLG-STRDIAEST 246
Cdd:PRK05876 157 GVAKYGVVGLAETLAREVTADGIGVSVLCPMVVEtnlvaNSERIRGAAcAQSSTTGSPGPLPLQDDNlGVDDIAQLT 233
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-272 1.60e-13

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 68.45  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALvlLGCKAAIVGRDQERTEQAAKGISQLAKDkdavlaianvdvrnfeqVENAVKKTVE 101
Cdd:PRK06550   3 FMTKTVLITGAASGIGLAQARAF--LAQGAQVYGVDKQDKPDLSGNFHFLQLD-----------------LSDDLEPLFD 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDfVIAGAAGnFVCDFANL---SPNAFKSVVDIDLLGSFNTAKACL-KELKKSKGSILFVS--ATFHYYGvpfqGH 175
Cdd:PRK06550  64 WVPSVD-ILCNTAG-ILDDYKPLldtSLEEWQHIFDTNLTSTFLLTRAYLpQMLERKSGIIINMCsiASFVAGG----GG 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  176 VG--AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPA 253
Cdd:PRK06550 138 AAytASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAADFEPGGLADWVARETPIKRWAEPEEVAELTLFLASGK 217

                        250
                 ....*....|....*....
gi 99030931  254 ASYVTGTVLVVDGGmWHLG 272
Cdd:PRK06550 218 ADYMQGTIVPIDGG-WTLK 235
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 23-267 2.15e-13

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 68.65  E-value: 2.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgisQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEK 102
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVAD---EINAEYGEKAYGFGADATNEQSVIALSKGVDEI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 103 FGKIDFVI--AG-AAGNFVCDFANlspNAFKSVVDIDLLGSFNTAKACLKELKK--SKGSILFVSATFHYYGVPFQGHVG 177
Cdd:cd05322  78 FKRVDLLVysAGiAKSAKITDFEL---GDFDRSLQVNLVGYFLCAREFSKLMIRdgIQGRIIQINSKSGKVGSKHNSGYS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRL----AGK------KYKEKALAKIPLQRLGSTRDIAESTV 247
Cdd:cd05322 155 AAKFGGVGLTQSLALDLAEHGITVNSLMLGNLLKSPMFQSLlpqyAKKlgikesEVEQYYIDKVPLKRGCDYQDVLNMLL 234

                       250       260
                ....*....|....*....|
gi 99030931 248 YIFSPAASYVTGTVLVVDGG 267
Cdd:cd05322 235 FYASPKASYCTGQSINITGG 254
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
48-271 2.16e-13

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 68.21  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   48 GCKAAIVGRDQE-----RTEQAAKGISQLAKDKDAVLAianVDVRNFEQVENAVKKTVEKFGKIDFVIAGAA----GNFV 118
Cdd:PRK06079  24 GCAQAIKDQGATviytyQNDRMKKSLQKLVDEEDLLVE---CDVASDESIERAFATIKERVGKIDGIVHAIAyakkEELG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  119 CDFANLSPNAFKSVVDIDLLGSFNTAKAClKELKKSKGSILfvsaTFHYYG----VPFQGHVGAAKAGIDALAKNLAVEL 194
Cdd:PRK06079 101 GNVTDTSRDGYALAQDISAYSLIAVAKYA-RPLLNPGASIV----TLTYFGseraIPNYNVMGIAKAALESSVRYLARDL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  195 GPLGIRSNCIAPGAIdnteglKRLAGKKYKE-KALAKIPLQRLG-----STRDIAESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:PRK06079 176 GKKGIRVNAISAGAV------KTLAVTGIKGhKDLLKESDSRTVdgvgvTIEEVGNTAAFLLSDLSTGVTGDIIYVDKGV 249


                 ...
gi 99030931  269 wHL 271
Cdd:PRK06079 250 -HL 251
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
81-273 3.17e-13

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 68.11  E-value: 3.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   81 IANVDVRNFEQVENAVKKTVEKFGKIDFVIAGAAgnfvcdFANlsPNAFKS-VVDIDLlGSFNTAK--AC--LKELKKSK 155
Cdd:PRK06603  62 VSELDVTNPKSISNLFDDIKEKWGSFDFLLHGMA------FAD--KNELKGrYVDTSL-ENFHNSLhiSCysLLELSRSA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  156 -------GSILfvsaTFHYYG----VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdnteglKRLAGKK-- 222
Cdd:PRK06603 133 ealmhdgGSIV----TLTYYGaekvIPNYNVMGVAKAALEASVKYLANDMGENNIRVNAISAGPI------KTLASSAig 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 99030931  223 -----YKEKAlAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGGMWHLGT 273
Cdd:PRK06603 203 dfstmLKSHA-ATAPLKRNTTQEDVGGAAVYLFSELSKGVTGEIHYVDCGYNIMGS 257
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 26-210 3.24e-13

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: 67.65  E-value: 3.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  26 VAFVTGGAGTICRVQTEALVLLGCKAAIVGRDqertEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKFGK 105
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDIN----EKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 106 IDFVI--AG-AAGNFvcdFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:cd05339  77 VTILInnAGvVSGKK---LLELPDEEIEKTFEVNTLAHFWTTKAFLPDmLERNHGHIVTIASVAGLISPAGLADYCASKA 153

                       170       180       190
                ....*....|....*....|....*....|..
gi 99030931 182 GIDALAKNLAVEL---GPLGIRSNCIAPGAID 210
Cdd:cd05339 154 AAVGFHESLRLELkayGKPGIKTTLVCPYFIN 185
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 24-267 5.10e-13

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 69.18  E-value: 5.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkDKDAVLAIANVDVRNfEQVENAVKKTVEKF 103
Cdd:COG3347 425 GRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGY-GADAVDATDVDVTAE-AAVAAAFGFAGLDI 502

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKG---SILFVSATFHYYGVPFQGHVGAAK 180
Cdd:COG3347 503 GGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLggsSVFAVSKNAAAAAYGAAAAATAKA 582

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 181 AGIDALAKnLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGT 260
Cdd:COG3347 583 AAQHLLRA-LAAEGGANGINANRVNPDAVLDGSAIWASAARAERAAAYGIGNLLLEEVYRKRVALAVLVLAEDIAEAAAF 661


                ....*..
gi 99030931 261 VLVVDGG 267
Cdd:COG3347 662 FASDGGN 668
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 48-210 6.26e-13

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: 67.02  E-value: 6.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  48 GCKAAIVGRDQERTEQAAKGISQLAKDkdAVLAIAnVDVRNFEQVENAVKKTVEKFGKIDFVIAGAAGNFVCDFANLSPN 127
Cdd:cd05373  23 GFSVALAARREAKLEALLVDIIRDAGG--SAKAVP-TDARDEDEVIALFDLIEEEIGPLEVLVYNAGANVWFPILETTPR 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 128 AFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIR-SNCIA 205
Cdd:cd05373 100 VFEKVWEMAAFGGFLAAREAAKRmLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALAQSMARELGPKGIHvAHVII 179


                ....*
gi 99030931 206 PGAID 210
Cdd:cd05373 180 DGGID 184
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 22-220 6.58e-13

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 66.70  E-value: 6.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAV----LAIAnVDVRNFEQVENAVK 97
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGTIYTAAEEIEAAggkaLPCI-VDIRDEDQVRAAVE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGS-ILFVSATFHYYGVPFQGHV 176
Cdd:cd09762  80 KAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPhILNLSPPLNLNPKWFKNHT 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 99030931 177 G--AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAG 220
Cdd:cd09762 160 AytMAKYGMSMCVLGMAEEFKPGGIAVNALWPRTAIATAAMNMLGG 205
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 27-212 1.02e-12

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: 65.68  E-value: 1.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  27 AFVTGGAGTICRVQTEALVLLGCKAAIVGRDQErteqaakgisqlakdkdavlaIANVDVRNfeqvENAVKKTVEKFGKI 106
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSG---------------------DYQVDITD----EASIKALFEKVGHF 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 107 DFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKsKGSILFVSATFHYYGVPFQGHVGAAKAGIDAL 186
Cdd:cd11731  56 DAIVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLND-GGSITLTSGILAQRPIPGGAAAATVNGALEGF 134

                       170       180
                ....*....|....*....|....*.
gi 99030931 187 AKNLAVELgPLGIRSNCIAPGAIDNT 212
Cdd:cd11731 135 VRAAAIEL-PRGIRINAVSPGVVEES 159
PRK12742 PRK12742
SDR family oxidoreductase;
22-267 1.03e-12

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 66.32  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAgticrvqtealvlLGCKAAIVGRdqeRTEQAAKGISQLAKDKDAVLAIA--------NVDVRNfeqvE 93
Cdd:PRK12742   4 FTGKKVLVLGGS-------------RGIGAAIVRR---FVTDGANVRFTYAGSKDAAERLAqetgatavQTDSAD----R 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   94 NAVKKTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSkGSILFVSATfHYYGVPFQ 173
Cdd:PRK12742  64 DAVIDVVRKSGALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG-GRIIIIGSV-NGDRMPVA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  174 GHV--GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTeglKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFS 251
Cdd:PRK12742 142 GMAayAASKSALQGMARGLARDFGPRGITINVVQPGPIDTD---ANPANGPMKDMMHSFMAIKRHGRPEEVAGMVAWLAG 218

                        250
                 ....*....|....*.
gi 99030931  252 PAASYVTGTVLVVDGG 267
Cdd:PRK12742 219 PEASFVTGAMHTIDGA 234
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 25-207 1.21e-12

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: 65.72  E-value: 1.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTG---GAG-TICRVQTEA---LVLLGCkaaivgRDQERTEQAAKGISQLAKDKDAVLaianVDVRNFEQVENAVK 97
Cdd:cd05324   1 KVALVTGanrGIGfEIVRQLAKSgpgTVILTA------RDVERGQAAVEKLRAEGLSVRFHQ----LDVTDDASIEAAAD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  98 KTVEKFGKIDFVI--AGAAGNfVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFqg 174
Cdd:cd05324  71 FVEEKYGGLDILVnnAGIAFK-GFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSLTSAY-- 147

                       170       180       190
                ....*....|....*....|....*....|...
gi 99030931 175 hvGAAKAGIDALAKNLAVELGPLGIRSNCIAPG 207
Cdd:cd05324 148 --GVSKAALNALTRILAKELKETGIKVNACCPG 178
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 24-267 1.37e-12

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 66.25  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTG-----GAGT-ICRVqteaLVLLGCKAAIVGRDQERTEQAAKGISQLA-------KDKDAVLAIANVDVRNFE 90
Cdd:PRK12748   5 KKIALVTGasrlnGIGAaVCRR----LAAKGIDIFFTYWSPYDKTMPWGMHDKEPvllkeeiESYGVRCEHMEIDLSQPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   91 QVENAVKKTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYYG 169
Cdd:PRK12748  81 APNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYdGKAGGRIINLTSGQSLGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  170 VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTeglkrLAGKKYKEKALAKIPLQRLGSTRDIAESTVYI 249
Cdd:PRK12748 161 MPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTG-----WITEELKHHLVPKFPQGRVGEPVDAARLIAFL 235

                        250
                 ....*....|....*...
gi 99030931  250 FSPAASYVTGTVLVVDGG 267
Cdd:PRK12748 236 VSEEAKWITGQVIHSEGG 253
PRK08340 PRK08340
SDR family oxidoreductase;
44-268 1.81e-12

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 65.98  E-value: 1.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   44 LVLLGCKAAIVGRDQERTEQAAKGISQLAKdkdaVLAIaNVDVRNFEQVENAVKKTVEKFGKIDFVIAGAaGNFVCDFAN 123
Cdd:PRK08340  20 LLKKGARVVISSRNEENLEKALKELKEYGE----VYAV-KADLSDKDDLKNLVKEAWELLGGIDALVWNA-GNVRCEPCM 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  124 LSPNAFKSVVDIDLLGSfnTAKACLKEL-------KKSKGSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGP 196
Cdd:PRK08340  94 LHEAGYSDWLEAALLHL--VAPGYLTTLliqawleKKMKGVLVYLSSVSVKEPMPPLVLADVTRAGLVQLAKGVSRTYGG 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  197 LGIRSNCIAPGAIDNT---EGLKRLAGKK-------YKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDG 266
Cdd:PRK08340 172 KGIRAYTVLLGSFDTPgarENLARIAEERgvsfeetWEREVLERTPLKRTGRWEELGSLIAFLLSENAEYMLGSTIVFDG 251


                 ..
gi 99030931  267 GM 268
Cdd:PRK08340 252 AM 253
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 22-251 2.02e-12

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: 65.61  E-value: 2.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlaKDKDAVLAIaNVDVRNFEQVENAVKKTVE 101
Cdd:cd05343   4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQS--AGYPTLFPY-QCDLSNEEQILSMFSAIRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK---GSILFV-SATFHYYGVPFQGHVG 177
Cdd:cd05343  81 QHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvddGHIINInSMSGHRVPPVSVFHFY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 178 AA-KAGIDALAKNLAVEL--GPLGIRSNCIAPGAIDnTEGLKRLAGKKYK--EKALAKIP-LQRlgstRDIAESTVYIFS 251
Cdd:cd05343 161 AAtKHAVTALTEGLRQELreAKTHIRATSISPGLVE-TEFAFKLHDNDPEkaAATYESIPcLKP----EDVANAVLYVLS 235
PRK08703 PRK08703
SDR family oxidoreductase;
19-227 3.64e-12

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 64.57  E-value: 3.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   19 PDLFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAV--LAIANVDVRNFEQVENAV 96
Cdd:PRK08703   1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAirFDLMSAEEKEFEQFAATI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   97 KKtvEKFGKIDFVIAGAAgnfvcDFANLSPNAFKSVVD------IDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYG 169
Cdd:PRK08703  81 AE--ATQGKLDGIVHCAG-----YFYALSPLDFQTVAEwvnqyrINTVAPMGLTRALFPLLKQSpDASVIFVGESHGETP 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 99030931  170 VPFQGHVGAAKAGIDALAKNLAVELGPLG-IRSNCIAPGAIDNTEGLKRLAGKKYKEKA 227
Cdd:PRK08703 154 KAYWGGFGASKAALNYLCKVAADEWERFGnLRANVLVPGPINSPQRIKSHPGEAKSERK 212
PRK06949 PRK06949
SDR family oxidoreductase;
22-268 5.08e-12

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 64.40  E-value: 5.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVlaiaNVDVRNFEQVENAVKKTVE 101
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVV----SLDVTDYQSIKAAVAHAET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL---------KKSKGSILFVSATFHYYGVPF 172
Cdd:PRK06949  83 EAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMiarakgagnTKPGGRIINIASVAGLRVLPQ 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  173 QGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSP 252
Cdd:PRK06949 163 IGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYID-TEINHHHWETEQGQKLVSMLPRKRVGKPEDLDGLLLLLAAD 241

                        250
                 ....*....|....*.
gi 99030931  253 AASYVTGTVLVVDGGM 268
Cdd:PRK06949 242 ESQFINGAIISADDGF 257
PRK06123 PRK06123
SDR family oxidoreductase;
25-267 5.78e-12

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 64.41  E-value: 5.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTIcrvqTEALVLLGCKAAI-VGRDQERTEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK06123   3 KVMIITGASRGI----GAATALLAAERGYaVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDREL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDfVIAGAAGNFVCD--FANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK----GSILFVSATFHYYGVPFQG-HV 176
Cdd:PRK06123  79 GRLD-ALVNNAGILEAQmrLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHggrgGAIVNVSSMAARLGSPGEYiDY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASY 256
Cdd:PRK06123 158 AASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIY-TEIHASGGEPGRVDRVKAGIPMGRGGTAEEVARAILWLLSDEASY 236

                        250
                 ....*....|.
gi 99030931  257 VTGTVLVVDGG 267
Cdd:PRK06123 237 TTGTFIDVSGG 247
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 21-267 6.14e-12

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 64.33  E-value: 6.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   21 LFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIvgRDQERTEQAAKGISQLAKDKDAVLAI-ANVD-VRNFEQVENAVKK 98
Cdd:PRK12747   1 MLKGKVALVTGASRGIGRAIAKRLANDGALVAI--HYGNRKEEAEETVYEIQSNGGSAFSIgANLEsLHGVEALYSSLDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   99 TVEK---FGKIDFVIAGAA---GNFVcdfANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKgSILFVSATFHYYGVPF 172
Cdd:PRK12747  79 ELQNrtgSTKFDILINNAGigpGAFI---EETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNS-RIINISSAATRISLPD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  173 QGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSP 252
Cdd:PRK12747 155 FIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYATTISAFNRLGEVEDIADTAAFLASP 234

                        250
                 ....*....|....*
gi 99030931  253 AASYVTGTVLVVDGG 267
Cdd:PRK12747 235 DSRWVTGQLIDVSGG 249
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 179-268 6.36e-12

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: 64.56  E-value: 6.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   179 AKAGIDALAKNLAVELGPLGIRSNCIAPGaidnTEGLKRLAGKKYKEKALAKIPL-QRLGSTRDIAESTVYIFSPAASYV 257
Cdd:TIGR02685 176 AKHALEGLTRSAALELAPLQIRVNGVAPG----LSLLPDAMPFEVQEDYRRKVPLgQREASAEQIADVVIFLVSPKAKYI 251

                          90
                  ....*....|.
gi 99030931   258 TGTVLVVDGGM 268
Cdd:TIGR02685 252 TGTCIKVDGGL 262
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 24-267 7.21e-12

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 64.11  E-value: 7.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAakgisqlakdKDAVLAIANVDVRNF-------EQVENAV 96
Cdd:PRK08339   8 GKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKA----------REKIKSESNVDVSYIvadltkrEDLERTV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   97 KKtVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYYGVPFQGH 175
Cdd:PRK08339  78 KE-LKNIGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMeRKGFGRIIYSTSVAIKEPIPNIAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  176 VGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAGKKYK------EKALAK----IPLQRLGSTRDIAES 245
Cdd:PRK08339 157 SNVVRISMAGLVRTLAKELGPKGITVNGIMPGII-RTDRVIQLAQDRAKregksvEEALQEyakpIPLGRLGEPEEIGYL 235

                        250       260
                 ....*....|....*....|..
gi 99030931  246 TVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK08339 236 VAFLASDLGSYINGAMIPVDGG 257
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 24-208 7.75e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 64.29  E-value: 7.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgisqlAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLA------EKYGDRLLPLA-LDVTDRAAVFAAVETAVEHF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPFQGHVGAAKAG 182
Cdd:PRK08263  76 GRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQrSGHIIQISSIGGISAFPMSGIYHASKWA 155

                        170       180
                 ....*....|....*....|....*.
gi 99030931  183 IDALAKNLAVELGPLGIRSNCIAPGA 208
Cdd:PRK08263 156 LEGMSEALAQEVAEFGIKVTLVEPGG 181
PRK06128 PRK06128
SDR family oxidoreductase;
24-267 1.00e-11

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 64.11  E-value: 1.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQErtEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK06128  55 GRKALITGADSGIGRATAIAFAREGADIALNYLPEE--EQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKEL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGN-FVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSkGSILFVSATFHYYGVPFQGHVGAAKAG 182
Cdd:PRK06128 133 GGLDILVNIAGKQtAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPG-ASIINTGSIQSYQPSPTLLDYASTKAA 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  183 IDALAKNLAVELGPLGIRSNCIAPGAIDNtegLKRLAGKKYKEKAL---AKIPLQRLGSTRDIAESTVYIFSPAASYVTG 259
Cdd:PRK06128 212 IVAFTKALAKQVAEKGIRVNAVAPGPVWT---PLQPSGGQPPEKIPdfgSETPMKRPGQPVEMAPLYVLLASQESSYVTG 288


                 ....*...
gi 99030931  260 TVLVVDGG 267
Cdd:PRK06128 289 EVFGVTGG 296
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 24-210 1.61e-11

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: 62.73  E-value: 1.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALvlLGCKAAIVGRDQERTEQAAKGISQLAKDKDAvlaianvdvrnfEQVENAVKKTVEKF 103
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAF--KSRGWWVASIDLAENEEADASIIVLDSDSFT------------EQAKQVVASVARLS 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 104 GKIDFVIAGAAGnfvcdFANLSP------NAFKSVVDIDLLGSFNTAKACLKELKKSkGSILFVSATFHYYGVPFQGHVG 177
Cdd:cd05334  67 GKVDALICVAGG-----WAGGSAksksfvKNWDLMWKQNLWTSFIASHLATKHLLSG-GLLVLTGAKAALEPTPGMIGYG 140

                       170       180       190
                ....*....|....*....|....*....|....*
gi 99030931 178 AAKAGIDALAKNLAVELG--PLGIRSNCIAPGAID 210
Cdd:cd05334 141 AAKAAVHQLTQSLAAENSglPAGSTANAILPVTLD 175
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 25-249 1.90e-11

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: 62.38  E-value: 1.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQErteqaakGISQLAKDKDAVLAIaNVDVRNFEQVENAVKKTVEKFG 104
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPE-------DLAALSASGGDVEAV-PYDARDPEDARALVDALRDRFG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 105 KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPFQGHVGAAKAGI 183
Cdd:cd08932  73 RIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAgSGRVVFLNSLSGKRVLAGNAGYSASKFAL 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 99030931 184 DALAKNLAVELGPLGIRSNCIAPGAIDnTEGLKRLAgkkykekALAKIPLQRLGSTRDIAESTVYI 249
Cdd:cd08932 153 RALAHALRQEGWDHGVRVSAVCPGFVD-TPMAQGLT-------LVGAFPPEEMIQPKDIANLVRMV 210
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 24-259 2.39e-11

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: 62.63  E-value: 2.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGIsqLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKF 103
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEI--KKETGNAKVEVIQLDLSSLASVRQFAEEFLARF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 104 GKIDFVIAGaAGNFVCDFaNLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGS-ILFVSATFH---------------- 166
Cdd:cd05327  79 PRLDILINN-AGIMAPPR-RLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSrIVNVSSIAHragpidfndldlennk 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 167 -YYGVPFqghVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAGkkykekALAKIPLQRLGSTRDI--- 242
Cdd:cd05327 157 eYSPYKA---YGQSKLANILFTRELARRLEGTGVTVNALHPGVV-RTELLRRNGS------FFLLYKLLRPFLKKSPeqg 226

                       250
                ....*....|....*...
gi 99030931 243 AESTVY-IFSPAASYVTG 259
Cdd:cd05327 227 AQTALYaATSPELEGVSG 244
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-269 3.69e-11

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 62.11  E-value: 3.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTG-----GAGT-ICRVQTEAlvllGC-----------KAAIVGRDQERTEQAAKGISQLAkdkdavlaianVD 85
Cdd:PRK12859   5 KNKVAVVTGvsrldGIGAaICKELAEA----GAdifftywtaydKEMPWGVDQDEQIQLQEELLKNG-----------VK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   86 VRNFE---QVENAVKKTV----EKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGS 157
Cdd:PRK12859  70 VSSMEldlTQNDAPKELLnkvtEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFdKKSGGR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  158 ILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDN---TEGLkrlagkkyKEKALAKIPLQ 234
Cdd:PRK12859 150 IINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTgwmTEEI--------KQGLLPMFPFG 221

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 99030931  235 RLGSTRDIAESTVYIFSPAASYVTGTVLVVDGGMW 269
Cdd:PRK12859 222 RIGEPKDAARLIKFLASEEAEWITGQIIHSEGGFK 256
PRK07832 PRK07832
SDR family oxidoreductase;
25-210 6.04e-11

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 61.60  E-value: 6.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKdkdAVLAIANVDVRNFEQVENAVKKTVEKFG 104
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGG---TVPEHRALDISDYDAVAAFAADIHAAHG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  105 KIDFV--IAGAAGNFVCDfaNLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK--GSILFVSATFHYYGVPFQGHVGAAK 180
Cdd:PRK07832  78 SMDVVmnIAGISAWGTVD--RLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGrgGHLVNVSSAAGLVALPWHAAYSASK 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 99030931  181 AGIDALAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:PRK07832 156 FGLRGLSEVLRFDLARHGIGVSVVVPGAVK 185
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 18-208 6.68e-11

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 61.04  E-value: 6.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   18 RPDLFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAV--LAIANVDVRNFEQVENA 95
Cdd:PRK08945   6 KPDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIipLDLLTATPQNYQQLADT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   96 VKktvEKFGKIDFVI--AGAAGNfVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPF 172
Cdd:PRK08945  86 IE---EQFGRLDGVLhnAGLLGE-LGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSSVGRQGRAN 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 99030931  173 QGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGA 208
Cdd:PRK08945 162 WGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGG 197
PRK07454 PRK07454
SDR family oxidoreductase;
25-210 8.18e-11

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 60.74  E-value: 8.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQaakgISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEKFG 104
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEA----LAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  105 KIDFVI--AGAAgnFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK07454  83 CPDVLInnAGMA--YTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMrARGGGLIINVSSIAARNAFPQWGAYCVSKA 160

                        170       180
                 ....*....|....*....|....*....
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:PRK07454 161 ALAAFTKCLAEEERSHGIRVCTITLGAVN 189
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 23-216 1.09e-10

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: 60.92  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERT-EQAAKGISQLAKDKDAVLaianVDVRNFEQVENAVKKT-V 100
Cdd:cd09763   2 SGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQlPGTAEEIEARGGKCIPVR----CDHSDDDEVEALFERVaR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 101 EKFGKIDFVIAGAAGNFVCDFAN-------LSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATF---HYYG 169
Cdd:cd09763  78 EQQGRLDILVNNAYAAVQLILVGvakpfweEPPTIWDDINNVGLRAHYACSVYAAPLMVKAgKGLIVIISSTGgleYLFN 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 99030931 170 VPFqghvGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLK 216
Cdd:cd09763 158 VAY----GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFV-RTELVL 199
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 22-268 1.37e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 60.44  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAkgiSQLAKDKDAVLAIANVDVRNFEQVEnavkKTVE 101
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALA---ADLRAAHGVDVAVHALDLSSPEARE----QLAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVI--AGA--AGNFvcdfANLSPNAFKSVVDIDLLGSFNTAKACLKELKkSKGSILFVSATFHYYGVPFQGHV- 176
Cdd:PRK06125  78 EAGDIDILVnnAGAipGGGL----DDVDDAAWRAGWELKVFGYIDLTRLAYPRMK-ARGSGVIVNVIGAAGENPDADYIc 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  177 -GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGK---------KYKEkALAKIPLQRLGSTRDIAEST 246
Cdd:PRK06125 153 gSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLLKGRaraelgdesRWQE-LLAGLPLGRPATPEEVADLV 231

                        250       260
                 ....*....|....*....|..
gi 99030931  247 VYIFSPAASYVTGTVLVVDGGM 268
Cdd:PRK06125 232 AFLASPRSGYTSGTVVTVDGGI 253
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 23-207 2.46e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 59.92  E-value: 2.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTeQAAKGISQLAkdkdavlaianVDVRNFEQVENAVKKTVEK 102
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARA-APIPGVELLE-----------LDVTDDASVQAAVDEVIAR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVI-------AGAAGNFvcdfanlSPNAFKSVVDIDLLGSFNTAKACLKELKK-SKGSILFVSATFHYYGVPFQG 174
Cdd:PRK06179  71 AGRIDVLVnnagvglAGAAEES-------SIAQAQALFDTNVFGILRMTRAVLPHMRAqGSGRIINISSVLGFLPAPYMA 143

                        170       180       190
                 ....*....|....*....|....*....|...
gi 99030931  175 HVGAAKAGIDALAKNLAVELGPLGIRSNCIAPG 207
Cdd:PRK06179 144 LYAASKHAVEGYSESLDHEVRQFGIRVSLVEPA 176
PRK06139 PRK06139
SDR family oxidoreductase;
23-288 4.26e-10

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 59.35  E-value: 4.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDkdaVLAIANvDVRNFEQVENAVKKTVEK 102
Cdd:PRK06139   6 HGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAE---VLVVPT-DVTDADQVKALATQAASF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDF----VIAGAAGNFvcdfaNLSP-NAFKSVVDIDLLGSFNTAKACLKELKKSKGSIL--------FVSAtfhyyg 169
Cdd:PRK06139  82 GGRIDVwvnnVGVGAVGRF-----EETPiEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFinmislggFAAQ------ 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  170 vPFQGHVGAAKAGIDALAKNLAVELGPL-GIRSNCIAPGAIDnTEGLKRlaGKKYKEKALAKIPLqrLGSTRDIAESTVY 248
Cdd:PRK06139 151 -PYAAAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMD-TPGFRH--GANYTGRRLTPPPP--VYDPRRVAKAVVR 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 99030931  249 IF-SPAASYVTGTVLvvdggmwHLgTYFGHELYPEALIKSM 288
Cdd:PRK06139 225 LAdRPRATTTVGAAA-------RL-ARLAHFLAPGLTARLM 257
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
85-267 4.77e-10

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 58.99  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   85 DVRNFEQVENAVKKTVEKFGKIDFVIAGAA----GNFVCDFANLSPNAFKSVVDIDLLgSFNTAKACLKELKKSKGSILf 160
Cdd:PRK06505  65 DVEDIASVDAVFEALEKKWGKLDFVVHAIGfsdkNELKGRYADTTRENFSRTMVISCF-SFTEIAKRAAKLMPDGGSML- 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  161 vsaTFHYYG----VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdnteglKRLAGK---------KYKEKa 227
Cdd:PRK06505 143 ---TLTYGGstrvMPNYNVMGVAKAALEASVRYLAADYGPQGIRVNAISAGPV------RTLAGAgigdaraifSYQQR- 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 99030931  228 laKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK06505 213 --NSPLRRTVTIDEVGGSALYLLSDLSSGVTGEIHFVDSG 250
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 51-242 5.10e-10

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: 58.63  E-value: 5.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  51 AAIVGRDQERTEQAAKGISQLAKDKDAV----------LAIANVDVRNFEQVENAVKKTVEkfGKIDFVIAGAAGNFVCD 120
Cdd:cd09806  17 AVRLASDPSKRFKVYATMRDLKKKGRLWeaagalaggtLETLQLDVCDSKSVAAAVERVTE--RHVDVLVCNAGVGLLGP 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 121 FANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGI 199
Cdd:cd09806  95 LEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLPFNDVYCASKFALEGLCESLAVQLLPFNV 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 99030931 200 RSNCIAPGAIdNTEglkrlagkkYKEKALAKIPLQRLGSTRDI 242
Cdd:cd09806 175 HLSLIECGPV-HTA---------FMEKVLGSPEEVLDRTADDI 207
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
46-267 6.77e-10

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 58.44  E-value: 6.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   46 LLGCKAAIVGRDQERTeqAAKGISQLAKDKDAVLAIANV-----------------------DVRNFEQVENAVKKTVEK 102
Cdd:PRK08690   4 LQGKKILITGMISERS--IAYGIAKACREQGAELAFTYVvdkleervrkmaaeldselvfrcDVASDDEINQVFADLGKH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVI--------AGAAGNFVcdfANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQG 174
Cdd:PRK08690  82 WDGLDGLVhsigfapkEALSGDFL---DSISREAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSYLGAVRAIPNYN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  175 HVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIdNTEGLKRLAG-KKYKEKALAKIPLQRLGSTRDIAESTVYIFSPA 253
Cdd:PRK08690 159 VMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPI-KTLAASGIADfGKLLGHVAAHNPLRRNVTIEEVGNTAAFLLSDL 237

                        250
                 ....*....|....
gi 99030931  254 ASYVTGTVLVVDGG 267
Cdd:PRK08690 238 SSGITGEITYVDGG 251
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 84-207 1.14e-09

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: 58.06  E-value: 1.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  84 VDVRNFEQVENAVKKTVEKFGKIDF--VI--AGAAGnFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSIL 159
Cdd:cd09805  55 LDVTKPEQIKRAAQWVKEHVGEKGLwgLVnnAGILG-FGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVV 133

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 99030931 160 FVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPG 207
Cdd:cd09805 134 NVSSMGGRVPFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPG 181
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
68-267 1.39e-09

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 57.52  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   68 ISQLAKDKDAVLaIANVDVRNFEQVENAVKKTVEKFGKIDFVI--------AGAAGNFVcdfANLSPNAFKSVVDIDLLG 139
Cdd:PRK06997  48 ITEFAAEFGSDL-VFPCDVASDEQIDALFASLGQHWDGLDGLVhsigfaprEAIAGDFL---DGLSRENFRIAHDISAYS 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  140 SFNTAKACLKELKKsKGSILfvsaTFHYYG----VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDN--TE 213
Cdd:PRK06997 124 FPALAKAALPMLSD-DASLL----TLSYLGaervVPNYNTMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTlaAS 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 99030931  214 GLKRLAGK-KYKEKAlakIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK06997 199 GIKDFGKIlDFVESN---APLRRNVTIEEVGNVAAFLLSDLASGVTGEITHVDSG 250
PRK12746 PRK12746
SDR family oxidoreductase;
24-267 3.36e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 56.20  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAI-VGRDQERTEQAAKGISqlAKDKDAVLAIANVDV-----RNFEQVENAVK 97
Cdd:PRK12746   6 GKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIE--SNGGKAFLIEADLNSidgvkKLVEQLKNELQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   98 KTVEKfGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKeLKKSKGSILFVSATFHYYGVPFQGHVG 177
Cdd:PRK12746  84 IRVGT-SEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLP-LLRAEGRVINISSAEVRLGFTGSIAYG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  178 AAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNTEGLKRLAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYV 257
Cdd:PRK12746 162 LSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRNFATNSSVFGRIGQVEDIADAVAFLASSDSRWV 241

                        250
                 ....*....|
gi 99030931  258 TGTVLVVDGG 267
Cdd:PRK12746 242 TGQIIDVSGG 251
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 191-282 3.50e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 56.57  E-value: 3.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  191 AVELGPLGIRSNCIAPGAIDNTEGLKRLAGKK---YKeKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK06940 184 AVKWGERGARINSISPGIISTPLAQDELNGPRgdgYR-NMFAKSPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVDGG 262

                         90
                 ....*....|....*
gi 99030931  268 MwhLGTYFGHELYPE 282
Cdd:PRK06940 263 A--TASYRYGPLKPE 275
PRK08267 PRK08267
SDR family oxidoreductase;
28-210 4.56e-09

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 56.10  E-value: 4.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   28 FVTGGAGTICRVQTEALVLLGCKAAIVGRDQErteqaakGISQLAKDKDAV-LAIANVDVRNFEQVENAVKKTVEKF-GK 105
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGAYDINEA-------GLAALAAELGAGnAWTGALDVTDRAAWDAALADFAAATgGR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  106 IDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILF----VSATfhyYGVPFQGHVGAAKA 181
Cdd:PRK08267  78 LDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVIntssASAI---YGQPGLAVYSATKF 154

                        170       180
                 ....*....|....*....|....*....
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:PRK08267 155 AVRGLTEALDLEWRRHGIRVADVMPLFVD 183
PRK09072 PRK09072
SDR family oxidoreductase;
23-212 7.87e-09

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 55.33  E-value: 7.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKgisQLAKDKDAVLAIAnvDVRNFEQVEnAVKKTVEK 102
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAA---RLPYPGRHRWVVA--DLTSEAGRE-AVLARARE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKK-SKGSILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK09072  78 MGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAqPSAMVVNVGSTFGSIGYPGYASYCASKF 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGAIDNT 212
Cdd:PRK09072 158 ALRGFSEALRRELADTGVRVLYLAPRATRTA 188
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 60-267 8.73e-09

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 54.77  E-value: 8.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   60 RTEQAAKGISQLAKDKDAVLAIANvDVRNFEQVENAVKKTVEKFGKIDFVIAGAAG---NFVCDFANLSpNAFKSVVDID 136
Cdd:PRK05786  37 RNENKLKRMKKTLSKYGNIHYVVG-DVSSTESARNVIEKAAKVLNAIDGLVVTVGGyveDTVEEFSGLE-EMLTNHIKIP 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  137 LLgsfnTAKACLKELKKSKgSILFVSATFHYY-GVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNtegl 215
Cdd:PRK05786 115 LY----AVNASLRFLKEGS-SIVLVSSMSGIYkASPDQLSYAVAKAGLAKAVEILASELLGRGIRVNGIAPTTISG---- 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 99030931  216 KRLAGKKYKEkalakipLQRLGSTR----DIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK05786 186 DFEPERNWKK-------LRKLGDDMappeDFAKVIIWLLTDEADWVDGVVIPVDGG 234
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 198-268 1.30e-08

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: 54.42  E-value: 1.30e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 99030931 198 GIRSNCIAPGAIDnTEGLKRL-AGKKYKEKALAKI-PLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:cd05328 174 GVRVNTVAPGPVE-TPILQAFlQDPRGGESVDAFVtPMGRRAEPDEIAPVIAFLASDAASWINGANLFVDGGL 245
PRK07984 PRK07984
enoyl-ACP reductase FabI;
120-267 3.15e-08

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 53.37  E-value: 3.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  120 DFAN-LSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSIlfvsaTFHYYG----VPFQGHVGAAKAGIDALAKNLAVEL 194
Cdd:PRK07984 103 DYVNaVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALL-----TLSYLGaeraIPNYNVMGLAKASLEANVRYMANAM 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 99030931  195 GPLGIRSNCIAPGAIDN--TEGLKRLagKKYKEKALAKIPLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGG 267
Cdd:PRK07984 178 GPEGVRVNAISAGPIRTlaASGIKDF--RKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGG 250
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 60-208 9.48e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 52.22  E-value: 9.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   60 RTEQAAKGISQLAKDKdaVLAIAnVDVRNFEQVENAVKKTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLG 139
Cdd:PRK06180  36 RSEAARADFEALHPDR--ALARL-LDVTDFDAIDAVVADAEATFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFG 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  140 SFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGA 208
Cdd:PRK06180 113 AVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPGS 182
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 175-267 1.08e-07

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 51.47  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  175 HVG--AAKAGIDALAKNLAVELGPLgIRSNCIAPGAIDNTEGlkrlAGKKYKEKALAKIPLQRLGSTRDIAESTVYIFsp 252
Cdd:PRK06483 145 HIAyaASKAALDNMTLSFAAKLAPE-VKVNSIAPALILFNEG----DDAAYRQKALAKSLLKIEPGEEEIIDLVDYLL-- 217

                         90
                 ....*....|....*
gi 99030931  253 AASYVTGTVLVVDGG 267
Cdd:PRK06483 218 TSCYVTGRSLPVDGG 232
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 24-213 1.13e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 51.87  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlakdkdaVLAIAnVDVRNFEQVENAVKKTVEKF 103
Cdd:PRK07825   5 GKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGL-------VVGGP-LDVTDPASFAAFLDAVEADL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKE-LKKSKGSILFVSATFHYYGVPFQGHVGAAKAG 182
Cdd:PRK07825  77 GPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRmVPRGRGHVVNVASLAGKIPVPGMATYCASKHA 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 99030931  183 IDALAKNLAVELGPLGIRSNCIAPGAIdNTE 213
Cdd:PRK07825 157 VVGFTDAARLELRGTGVHVSVVLPSFV-NTE 186
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
144-272 1.36e-07

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 51.48  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  144 AKACLkELKKSKGSIlfVSATFH-YYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNT-----EGLKR 217
Cdd:PRK07889 128 AKALL-PLMNEGGSI--VGLDFDaTVAWPAYDWMGVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLaakaiPGFEL 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 99030931  218 LAGkKYKEKAlakiPlqrLG-STRD---IAESTVYIFSPAASYVTGTVLVVDGGMWHLG 272
Cdd:PRK07889 205 LEE-GWDERA----P---LGwDVKDptpVARAVVALLSDWFPATTGEIVHVDGGAHAMG 255
PRK06914 PRK06914
SDR family oxidoreductase;
23-208 1.85e-07

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 51.18  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLakDKDAVLAIANVDVRNFEQVENaVKKTVEK 102
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQL--NLQQNIKVQQLDVTDQNSIHN-FQLVLKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVI--AG-AAGNFVCDfanLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGS-ILFVSATFHYYGVPFQGHVGA 178
Cdd:PRK06914  79 IGRIDLLVnnAGyANGGFVEE---IPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGkIINISSISGRVGFPGLSPYVS 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 99030931  179 AKAGIDALAKNLAVELGPLGIRSNCIAPGA 208
Cdd:PRK06914 156 SKYALEGFSESLRLELKPFGIDVALIEPGS 185
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
192-268 3.86e-07

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 50.00  E-value: 3.86e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 99030931  192 VELGPLGIRSNCIAPGAIDnTEGLKRLAgKKYKEKALAKI--PLQRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGGM 268
Cdd:PRK12428 154 PWFGARGIRVNCVAPGPVF-TPILGDFR-SMLGQERVDSDakRMGRPATADEQAAVLVFLCSDAARWINGVNLPVDGGL 230
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 21-147 3.95e-07

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: 50.83  E-value: 3.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  21 LFKGKVAFVTGGAGTICRVQTEALV-LLGCKAAIVGRDQE--RTEQAAKGISQLAKDKDAVLAIAnVDVRNFEQVENAVK 97
Cdd:cd08953 202 LKPGGVYLVTGGAGGIGRALARALArRYGARLVLLGRSPLppEEEWKAQTLAALEALGARVLYIS-ADVTDAAAVRRLLE 280

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 99030931  98 KTVEKFGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKAC 147
Cdd:cd08953 281 KVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQAL 330
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 27-210 4.04e-07

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: 49.44  E-value: 4.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  27 AFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDavlaianvdvrnfEQVENAVKKTVEKFGKI 106
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARPAD-------------VAAELEVWALAQELGPL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 107 DFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKeLKKSKGSILFVSATFHYYGVPFQGHVGAAKAGIDAL 186
Cdd:cd11730  68 DLLVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALA-LLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAY 146

                       170       180
                ....*....|....*....|....
gi 99030931 187 AKNLAVELGplGIRSNCIAPGAID 210
Cdd:cd11730 147 VEVARKEVR--GLRLTLVRPPAVD 168
PRK09134 PRK09134
SDR family oxidoreductase;
25-272 1.03e-06

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 48.77  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRVQTEALVLLGCKAAI-VGRDQERTEQAAKGISQLAKDKDAVLAianvDVRNFEQVENAVKKTVEKF 103
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAAEIRALGRRAVALQA----DLADEAEVRALVARASAAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  104 GKIDFVIAGAAgNFVCD-FANLSPNAFKSVVDIDLLGSFNTAKACLKEL-KKSKGSIL-------------FVSATFhyy 168
Cdd:PRK09134  86 GPITLLVNNAS-LFEYDsAASFTRASWDRHMATNLRAPFVLAQAFARALpADARGLVVnmidqrvwnlnpdFLSYTL--- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  169 gvpfqghvgaAKAGIDALAKNLAVELGPlGIRSNCIAPG----AIDNTEGlkrlagkkYKEKALAKIPLQRLGSTRDIAE 244
Cdd:PRK09134 162 ----------SKAALWTATRTLAQALAP-RIRVNAIGPGptlpSGRQSPE--------DFARQHAATPLGRGSTPEEIAA 222

                        250       260
                 ....*....|....*....|....*...
gi 99030931  245 STVYIFSPAAsyVTGTVLVVDGGMwHLG 272
Cdd:PRK09134 223 AVRYLLDAPS--VTGQMIAVDGGQ-HLA 247
PRK06194 PRK06194
hypothetical protein; Provisional
 20-146 1.21e-06

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 48.86  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLFKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDkdaVLAIAnVDVRNFEQVENAVKKT 99
Cdd:PRK06194   2 KDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAE---VLGVR-TDVSDAAQVEALADAA 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 99030931  100 VEKFGKIDFVI--AG-AAGNFVCDFanlSPNAFKSVVDIDLLGSFNTAKA 146
Cdd:PRK06194  78 LERFGAVHLLFnnAGvGAGGLVWEN---SLADWEWVLGVNLWGVIHGVRA 124
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 131-244 1.38e-06

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: 47.90  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 131 SVVDIDLLGSFNTAKACLKELK-KSKGSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAI 209
Cdd:cd02266  57 RAIRANVVGTRRLLEAARELMKaKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASEGWGNGLPATAVACGTW 136

                        90       100       110
                ....*....|....*....|....*....|....*
gi 99030931 210 DNTEGLKrlAGKKYKEKALAKIPLQRLGSTRDIAE 244
Cdd:cd02266 137 AGSGMAK--GPVAPEEILGNRRHGVRTMPPEEVAR 169
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 60-228 2.15e-06

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: 47.68  E-value: 2.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  60 RTEQAAKGISQLAKdKDAVLAIANVDVRNFEQVE-NAVKKTVeKFGKIDFVI--AGAAGNFvCDFANLSPNAFKSVVDID 136
Cdd:cd05325  31 RDPSAATELAALGA-SHSRLHILELDVTDEIAESaEAVAERL-GDAGLDVLInnAGILHSY-GPASEVDSEDLLEVFQVN 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 137 LLGSFNTAKACLKELKKSK-GSILFVSATFhyyG-----VPFQGHV-GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAI 209
Cdd:cd05325 108 VLGPLLLTQAFLPLLLKGArAKIINISSRV---GsigdnTSGGWYSyRASKAALNMLTKSLAVELKRDGITVVSLHPGWV 184

                       170
                ....*....|....*....
gi 99030931 210 DNteglkRLAGKKYKEKAL 228
Cdd:cd05325 185 RT-----DMGGPFAKNKGP 198
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 24-266 2.51e-06

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 48.29  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICrvQTEALVLLGCKAAIVGRD----QERTEQAAKGI--SQLAKD---KDAVLAIAnvdvrnfEQVen 94
Cdd:PRK08261 210 GKVALVTGAARGIG--AAIAEVLARDGAHVVCLDvpaaGEALAAVANRVggTALALDitaPDAPARIA-------EHL-- 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   95 avkktVEKFGKIDFVI--AGAAGnfvcD--FANLSPNAFKSVVDIDLLGSFNTAKACL-KELKKSKGSILFVSATFHYYG 169
Cdd:PRK08261 279 -----AERHGGLDIVVhnAGITR----DktLANMDEARWDSVLAVNLLAPLRITEALLaAGALGDGGRIVGVSSISGIAG 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  170 VPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGAIDNteglkrlagkkykeKALAKIPL------QRL------G 237
Cdd:PRK08261 350 NRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIET--------------QMTAAIPFatreagRRMnslqqgG 415

                        250       260
                 ....*....|....*....|....*....
gi 99030931  238 STRDIAESTVYIFSPAASYVTGTVLVVDG 266
Cdd:PRK08261 416 LPVDVAETIAWLASPASGGVTGNVVRVCG 444
PRK12744 PRK12744
SDR family oxidoreductase;
23-267 2.96e-06

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 47.43  E-value: 2.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVLAIANVDVRNFEQVENAVKKTVEK 102
Cdd:PRK12744   7 KGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYgVPFQGHVGAAKAG 182
Cdd:PRK12744  87 FGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDNGKIVTLVTSLLGAF-TPFYSAYAGSKAP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  183 IDALAKNLAVELGPLGIRSNCIAPGAIDN-----TEGLKRLAgkkYKEKALAKIPLQRLGSTR--DIAESTVYIFSpAAS 255
Cdd:PRK12744 166 VEHFTRAASKEFGARGISVTAVGPGPMDTpffypQEGAEAVA---YHKTAAALSPFSKTGLTDieDIVPFIRFLVT-DGW 241

                        250
                 ....*....|..
gi 99030931  256 YVTGTVLVVDGG 267
Cdd:PRK12744 242 WITGQTILINGG 253
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 22-162 5.92e-06

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: 46.69  E-value: 5.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAkdkdavlAIAnVDVRNFEQVENAVKKTVE 101
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLH-------TIV-LDVADPASIAALAEQVTA 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 99030931 102 KFGKIDFVIAGAAGNFVCDFAN--LSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGS-ILFVS 162
Cdd:COG3967  75 EFPDLNVLINNAGIMRAEDLLDeaEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAaIVNVS 138
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 25-210 7.10e-06

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: 46.29  E-value: 7.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQErteqaakGISQLAKDKDA-VLAIANVDVRNFEQVENAVKKTVEKF 103
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDED-------GLAALAAELGAeNVVAGALDVTDRAAWAAALADFAAAT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 104 G-KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILF-VSATFHYYGVPFQGHVGAAKA 181
Cdd:cd08931  74 GgRLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVInTASSSAIYGQPDLAVYSATKF 153

                       170       180
                ....*....|....*....|....*....
gi 99030931 182 GIDALAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:cd08931 154 AVRGLTEALDVEWARHGIRVADVWPWFVD 182
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 22-210 2.85e-05

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: 44.32  E-value: 2.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  22 FKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVG-RDQERTEQAakgisqLAKDKDAVLAIaNVDVRNFEQVENAVKKTV 100
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKKVYAAvRDPGSAAHL------VAKYGDKVVPL-RLDVTDPESIKAAAAQAK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 101 EkfgkIDFVIAGAAGNFVCD-FANLSPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPFQGHVGA 178
Cdd:cd05354  74 D----VDVVINNAGVLKPATlLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAMGTYSA 149

                       170       180       190
                ....*....|....*....|....*....|..
gi 99030931 179 AKAGIDALAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:cd05354 150 SKSAAYSLTQGLRAELAAQGTLVLSVHPGPID 181
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
 174-272 2.99e-05

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 44.77  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  174 GHVGAAKAGIDALAKNLAVELG-PLGIRSNCIAPGAidntegLKRLAGK------KYKEKALAKIPLQRLGSTRDIAEST 246
Cdd:PLN02730 191 GGMSSAKAALESDTRVLAFEAGrKYKIRVNTISAGP------LGSRAAKaigfidDMIEYSYANAPLQKELTADEVGNAA 264

                         90       100
                 ....*....|....*....|....*.
gi 99030931  247 VYIFSPAASYVTGTVLVVDGGMWHLG 272
Cdd:PLN02730 265 AFLASPLASAITGATIYVDNGLNAMG 290
PRK06482 PRK06482
SDR family oxidoreductase;
24-208 3.46e-05

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 44.34  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   24 GKVAFVTGGAGTICRVQTEALVLLGCK-AAIVgrdqeRTEQAAKGISQLAKDKdavLAIANVDVRNFEQVENAVKKTVEK 102
Cdd:PRK06482   2 SKTWFITGASSGFGRGMTERLLARGDRvAATV-----RRPDALDDLKARYGDR---LWVLQLDVTDSAAVRAVVDRAFAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  103 FGKIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGS-ILFVSATFHYYGVPFQGHVGAAKA 181
Cdd:PRK06482  74 LGRIDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGrIVQVSSEGGQIAYPGFSLYHATKW 153

                        170       180
                 ....*....|....*....|....*..
gi 99030931  182 GIDALAKNLAVELGPLGIRSNCIAPGA 208
Cdd:PRK06482 154 GIEGFVEAVAQEVAPFGIEFTIVEPGP 180
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
 92-272 4.04e-05

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 44.42  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   92 VENAVKKTVEKFGKIDFVIAGAAGnfvcdfanlSPNAFKSVVDIDLLG----------SFNTAKACLKELKKSKGSILFV 161
Cdd:PRK06300 106 ISEVAEQVKKDFGHIDILVHSLAN---------SPEISKPLLETSRKGylaalstssySFVSLLSHFGPIMNPGGSTISL 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  162 SATFHYYGVP-FQGHVGAAKAGIDALAKNLAVELG-PLGIRSNCIAPGAidntegLKRLAGK------KYKEKALAKIPL 233
Cdd:PRK06300 177 TYLASMRAVPgYGGGMSSAKAALESDTKVLAWEAGrRWGIRVNTISAGP------LASRAGKaigfieRMVDYYQDWAPL 250

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 99030931  234 QRLGSTRDIAESTVYIFSPAASYVTGTVLVVDGGMWHLG 272
Cdd:PRK06300 251 PEPMEAEQVGAAAAFLVSPLASAITGETLYVDHGANVMG 289
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 29-187 4.62e-05

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: 43.24  E-value: 4.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931     29 VTGGAGTICRVQTEALVLLGCKA-AIVGRDQERTEQAAKGISQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKFGKID 107
Cdd:smart00822   5 ITGGLGGLGRALARWLAERGARRlVLLSRSGPDAPGAAALLAELEAAGARVTVVA-CDVADRDALAAVLAAIPAVEGPLT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931    108 FVI--AGAAGNFVcdFANLSPNAFKSVVDIDLLGSFNTAKACL-KELKkskgsiLFV-----SATFhyyGVPFQGHVGAA 179
Cdd:smart00822  84 GVIhaAGVLDDGV--LASLTPERFAAVLAPKAAGAWNLHELTAdLPLD------FFVlfssiAGVL---GSPGQANYAAA 152


                   ....*...
gi 99030931    180 KAGIDALA 187
Cdd:smart00822 153 NAFLDALA 160
PRK06196 PRK06196
oxidoreductase; Provisional
 20-114 5.00e-05

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 43.90  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   20 DLfKGKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQlakdkdavLAIANVDVRNFEQVENAVKKT 99
Cdd:PRK06196  23 DL-SGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDG--------VEVVMLDLADLESVRAFAERF 93

                         90
                 ....*....|....*
gi 99030931  100 VEKFGKIDFVIAGAA 114
Cdd:PRK06196  94 LDSGRRIDILINNAG 108
PRK07201 PRK07201
SDR family oxidoreductase;
17-113 1.13e-04

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 43.40  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   17 WR----PDLFK---------GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGIsqlaKDKDAVLAIAN 83
Cdd:PRK07201 351 WErhldPDRARrrdlrgplvGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEI----RAKGGTAHAYT 426

                         90       100       110
                 ....*....|....*....|....*....|
gi 99030931   84 VDVRNFEQVENAVKKTVEKFGKIDFVIAGA 113
Cdd:PRK07201 427 CDLTDSAAVDHTVKDILAEHGHVDYLVNNA 456
PRK08264 PRK08264
SDR family oxidoreductase;
22-210 1.49e-04

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 42.18  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   22 FKGKVAFVTGGAGTICRvqteALVllgckAAIVGRDQERTEQAAKGISQLAKDKDAVLAIAnVDVRNFEQVENAVkktvE 101
Cdd:PRK08264   4 IKGKVVLVTGANRGIGR----AFV-----EQLLARGAAKVYAAARDPESVTDLGPRVVPLQ-LDVTDPASVAAAA----E 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  102 KFGKIDFVI--AGAA--GNFVCDFAnlsPNAFKSVVDIDLLGSFNTAKACLKELKKS-KGSILFVSATFHYYGVPFQGHV 176
Cdd:PRK08264  70 AASDVTILVnnAGIFrtGSLLLEGD---EDALRAEMETNYFGPLAMARAFAPVLAANgGGAIVNVLSVLSWVNFPNLGTY 146

                        170       180       190
                 ....*....|....*....|....*....|....
gi 99030931  177 GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAID 210
Cdd:PRK08264 147 SASKAAAWSLTQALRAELAPQGTRVLGVHPGPID 180
PRK07024 PRK07024
SDR family oxidoreductase;
52-210 1.55e-04

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 42.22  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   52 AIVGRdqeRTEQAAKGISQLAKDKDAvlAIANVDVRNFEQVENAVKKTVEKFGKIDFVIAGA---AGNFVCDFANLSpnA 128
Cdd:PRK07024  30 GLVAR---RTDALQAFAARLPKAARV--SVYAADVRDADALAAAAADFIAAHGLPDVVIANAgisVGTLTEEREDLA--V 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  129 FKSVVDIDLLGSFNTAKACLKELKKSK-GSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPG 207
Cdd:PRK07024 103 FREVMDTNYFGMVATFQPFIAPMRAARrGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPG 182


                 ...
gi 99030931  208 AID 210
Cdd:PRK07024 183 YIR 185
PRK08309 PRK08309
short chain dehydrogenase; Provisional
 27-111 1.91e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236232  Cd Length: 177  Bit Score: 41.27  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   27 AFVTGGAGTICRVqTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKdkdavLAIANVDVRNFEQVENAVKKTVEKFGKI 106
Cdd:PRK08309   3 ALVIGGTGMLKRV-SLWLCEKGFHVSVIARREVKLENVKRESTTPES-----ITPLPLDYHDDDALKLAIKSTIEKNGPF 76


                 ....*
gi 99030931  107 DFVIA 111
Cdd:PRK08309  77 DLAVA 81
PRK05693 PRK05693
SDR family oxidoreductase;
25-209 2.97e-04

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 41.70  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   25 KVAFVTGGAGTICRVQTEALvllgcKAAivGRDQERTEQAAKGISQLAKdkdAVLAIANVDVRNFEQVENAVKKTVEKFG 104
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAF-----KAA--GYEVWATARKAEDVEALAA---AGFTAVQLDVNDGAALARLAEELEAEHG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  105 KIDFVIAGAAGNFVCDFANLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGSILFVSATFHYYGVPFQGHVGAAKAGID 184
Cdd:PRK05693  72 GLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVH 151

                        170       180
                 ....*....|....*....|....*
gi 99030931  185 ALAKNLAVELGPLGIRSNCIAPGAI 209
Cdd:PRK05693 152 ALSDALRLELAPFGVQVMEVQPGAI 176
PRK09291 PRK09291
SDR family oxidoreductase;
149-208 1.46e-03

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 39.21  E-value: 1.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  149 KELKKSKGSILFVSATFHYYGVPFQGHVGAAKAGIDALAKNLAVELGPLGIRSNCIAPGA 208
Cdd:PRK09291 118 KMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEAIAEAMHAELKPFGIQVATVNPGP 177
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 29-187 1.79e-03

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: 39.58  E-value: 1.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  29 VTGGAGTICRVQTEALVLLGCKA-AIVGRDQERTEQAAKgISQLAKDKDAVLaIANVDVRNFEQVENAVKKTVEKFGKID 107
Cdd:cd08955 154 ITGGLGGLGLLVAEWLVERGARHlVLTGRRAPSAAARQA-IAALEEAGAEVV-VLAADVSDRDALAAALAQIRASLPPLR 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931 108 FVIAGAAgnfVCD---FANLSPNAFKSVVDIDLLGSFNtakacLKELKKSKGSILFV--SATFHYYGVPFQGHVGAAKAG 182
Cdd:cd08955 232 GVIHAAG---VLDdgvLANQDWERFRKVLAPKVQGAWN-----LHQLTQDLPLDFFVlfSSVASLLGSPGQANYAAANAF 303


                ....*
gi 99030931 183 IDALA 187
Cdd:cd08955 304 LDALA 308
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 29-187 1.82e-03

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: 38.31  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931    29 VTGGAGTICRVQTEALVLLGCKA-AIVGRDQERTEQAAKGISQLAKDKDAVLAIAnVDVRNFEQVENAVKKTVEKFGKID 107
Cdd:pfam08659   5 ITGGLGGLGRELARWLAERGARHlVLLSRSAAPRPDAQALIAELEARGVEVVVVA-CDVSDPDAVAALLAEIKAEGPPIR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   108 FVI--AGAAGNFVcdFANLSPNAFKSVVDIDLLGSFNTAKACLKE------LKKSKGSILfvsatfhyyGVPFQGHVGAA 179
Cdd:pfam08659  84 GVIhaAGVLRDAL--LENMTDEDWRRVLAPKVTGTWNLHEATPDEpldffvLFSSIAGLL---------GSPGQANYAAA 152


                  ....*...
gi 99030931   180 KAGIDALA 187
Cdd:pfam08659 153 NAFLDALA 160
PRK08251 PRK08251
SDR family oxidoreductase;
71-232 2.49e-03

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 38.76  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931   71 LAKDKDAVLAIANVDVRNFEQVENAVKKTVEKFGKIDFVIAGA---------AGNFvcdfanlspNAFKSVVDIDLLGSF 141
Cdd:PRK08251  47 LARYPGIKVAVAALDVNDHDQVFEVFAEFRDELGGLDRVIVNAgigkgarlgTGKF---------WANKATAETNFVAAL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  142 NTAKACLKELKKS-KGSILFVSATFHYYGVPfqGHV---GAAKAGIDALAKNLAVELGPLGIRSNCIAPGAI-------- 209
Cdd:PRK08251 118 AQCEAAMEIFREQgSGHLVLISSVSAVRGLP--GVKaayAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIrsemnaka 195

                        170       180       190
                 ....*....|....*....|....*....|
gi 99030931  210 -------DNTEGLKRLAGKKYKEKALAKIP 232
Cdd:PRK08251 196 kstpfmvDTETGVKALVKAIEKEPGRAAVP 225
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 24-172 4.02e-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: 38.22  E-value: 4.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  24 GKVAFVTGGAGTICRVQTEALVLLGCKAAIVGRDQERTEQAAKGISQLAKDKDAVlaIANVDVRNFEQVENAVKKTVEKF 103
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVI--VRHLDLASLKSIRAFAAEFLAEE 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 99030931 104 GKIDFVIaGAAGNFVCDFAnLSPNAFKSVVDIDLLGSFNTAKACLKELKKSKGS-ILFVSATFHYYG-VPF 172
Cdd:cd09807  79 DRLDVLI-NNAGVMRCPYS-KTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSrIVNVSSLAHKAGkINF 147
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 23-149 6.03e-03

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 37.60  E-value: 6.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  23 KGKVAFVTGGAGTICRVQTEALVLLGCKAAIV-GRDQerteqaaKGISQLAKDKDAVLAIANV-----DVRNFEQVENAV 96
Cdd:cd05237   1 KGKTILVTGGAGSIGSELVRQILKFGPKKLIVfDRDE-------NKLHELVRELRSRFPHDKLrfiigDVRDKERLRRAF 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 99030931  97 kktveKFGKIDFVIAGAAGNFV--CDFanlspnAFKSVVDIDLLGSFNTAKACLK 149
Cdd:cd05237  74 -----KERGPDIVFHAAALKHVpsMED------NPEEAIKTNVLGTKNVIDAAIE 117
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 25-114 8.33e-03

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic 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: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 36.98  E-value: 8.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 99030931  25 KVAFVTG-----GAGTICRV------QTEALVLLGCkaaivgRDQERTEQAAKGISQLAKDKDAVLAIANVDVRNFEQVE 93
Cdd:cd08941   2 KVVLVTGansglGLAICERLlaeddeNPELTLILAC------RNLQRAEAACRALLASHPDARVVFDYVLVDLSNMVSVF 75

                        90       100
                ....*....|....*....|.
gi 99030931  94 NAVKKTVEKFGKIDFVIAGAA 114
Cdd:cd08941  76 AAAKELKKRYPRLDYLYLNAG 96
 
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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