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Conserved domains on  [gi|568971391|ref|XP_006532159|]
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carbonyl reductase [NADPH] 2 isoform X1 [Mus musculus]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
1-181 5.75e-97

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05351:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 244  Bit Score: 280.51  E-value: 5.75e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE------------------------------ 50
Cdd:cd05351    1 MELDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVREcpgiepvcvdlsdwdateealgsvgpvdll 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 ---------------------------------VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLT 97
Cdd:cd05351   81 vnnaavailqpflevtkeafdrsfdvnvravihVSQIVARGMIARGVPGSIVNVSSQASQRALTNHTVYCSTKAALDMLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  98 KAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd05351  161 KVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDGG 240

                 ....
gi 568971391 178 YLAS 181
Cdd:cd05351  241 FLAS 244
 
Name Accession Description Interval E-value
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
1-181 5.75e-97

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: 280.51  E-value: 5.75e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE------------------------------ 50
Cdd:cd05351    1 MELDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVREcpgiepvcvdlsdwdateealgsvgpvdll 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 ---------------------------------VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLT 97
Cdd:cd05351   81 vnnaavailqpflevtkeafdrsfdvnvravihVSQIVARGMIARGVPGSIVNVSSQASQRALTNHTVYCSTKAALDMLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  98 KAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd05351  161 KVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDGG 240

                 ....
gi 568971391 178 YLAS 181
Cdd:cd05351  241 FLAS 244
PRK07060 PRK07060
short chain dehydrogenase; Provisional
1-180 2.19e-54

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 172.59  E-value: 2.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE------------------------------ 50
Cdd:PRK07060   3 MAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGEtgceplrldvgddaairaalaaagafdglv 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 --------------------------------VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTK 98
Cdd:PRK07060  83 ncagiaslesaldmtaegfdrvmavnargaalVARHVARAMIAAGRGGSIVNVSSQAALVGLPDHLAYCASKAALDAITR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  99 AMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK07060 163 VLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLPVDGGY 242

                 ..
gi 568971391 179 LA 180
Cdd:PRK07060 243 TA 244
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
5-180 7.31e-48

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: 156.10  E-value: 7.31e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEV--------------------------------- 51
Cdd:COG1028    4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaggralavaadvtdeaavealvaaavaafgr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 --------------------------------------SQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAM 93
Cdd:COG1028   84 ldilvnnagitppgpleelteedwdrvldvnlkgpfllTRAALPHMRERG-GGRIVNISSIAGLRGSPGQAAYAASKAAV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  94 TMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGIL 173
Cdd:COG1028  163 VGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLA 242

                 ....*..
gi 568971391 174 VDAGYLA 180
Cdd:COG1028  243 VDGGLTA 249
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
44-178 1.21e-37

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: 129.47  E-value: 1.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   44 LVSLAKEvsqmvARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM 123
Cdd:pfam13561 108 LFLLAKA-----ALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLA 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568971391  124 GKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:pfam13561 181 ASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
62-178 6.43e-11

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: 59.17  E-value: 6.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   62 RGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVL--TDMGKKVSADpeFARKLke 139
Cdd:TIGR02685 149 RSTNLSIVNLCDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLlpDAMPFEVQED--YRRKV-- 224
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568971391  140 rhPL-RKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:TIGR02685 225 --PLgQREASAEQIADVVIFLVSPKAKYITGTCIKVDGGL 262
 
Name Accession Description Interval E-value
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
1-181 5.75e-97

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: 280.51  E-value: 5.75e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE------------------------------ 50
Cdd:cd05351    1 MELDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVREcpgiepvcvdlsdwdateealgsvgpvdll 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 ---------------------------------VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLT 97
Cdd:cd05351   81 vnnaavailqpflevtkeafdrsfdvnvravihVSQIVARGMIARGVPGSIVNVSSQASQRALTNHTVYCSTKAALDMLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  98 KAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd05351  161 KVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDGG 240

                 ....
gi 568971391 178 YLAS 181
Cdd:cd05351  241 FLAS 244
PRK07060 PRK07060
short chain dehydrogenase; Provisional
1-180 2.19e-54

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 172.59  E-value: 2.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE------------------------------ 50
Cdd:PRK07060   3 MAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGEtgceplrldvgddaairaalaaagafdglv 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 --------------------------------VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTK 98
Cdd:PRK07060  83 ncagiaslesaldmtaegfdrvmavnargaalVARHVARAMIAAGRGGSIVNVSSQAALVGLPDHLAYCASKAALDAITR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  99 AMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK07060 163 VLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLPVDGGY 242

                 ..
gi 568971391 179 LA 180
Cdd:PRK07060 243 TA 244
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
5-180 7.31e-48

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: 156.10  E-value: 7.31e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEV--------------------------------- 51
Cdd:COG1028    4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaggralavaadvtdeaavealvaaavaafgr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 --------------------------------------SQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAM 93
Cdd:COG1028   84 ldilvnnagitppgpleelteedwdrvldvnlkgpfllTRAALPHMRERG-GGRIVNISSIAGLRGSPGQAAYAASKAAV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  94 TMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGIL 173
Cdd:COG1028  163 VGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLA 242

                 ....*..
gi 568971391 174 VDAGYLA 180
Cdd:COG1028  243 VDGGLTA 249
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
44-178 1.21e-37

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: 129.47  E-value: 1.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   44 LVSLAKEvsqmvARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM 123
Cdd:pfam13561 108 LFLLAKA-----ALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLA 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568971391  124 GKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:pfam13561 181 ASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
10-175 1.95e-37

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: 128.94  E-value: 1.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDL-------------------VSLAKEVSQMVA-------------- 56
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALaelaaiealggnavavqadVSDEEDVEALVEealeefgrldilvn 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 ------------------RDMIN------------------RGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAM 100
Cdd:cd05233   81 nagiarpgpleeltdedwDRVLDvnltgvflltraalphmkKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568971391 101 AMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFaRKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVD 175
Cdd:cd05233  161 ALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAE-KELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
10-132 4.56e-34

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 118.87  E-value: 4.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE--------------------------------------- 50
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKElgalggkalfiqgdvtdraqvkalveqaverlgrldilv 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   51 --------------------------------VSQMVARDMINRGVpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTK 98
Cdd:pfam00106  83 nnagitglgpfselsdedwervidvnltgvfnLTRAVLPAMIKGSG-GRIVNISSVAGLVPYPGGSAYSASKAAVIGFTR 161
                         170       180       190
                  ....*....|....*....|....*....|....
gi 568971391   99 AMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPE 132
Cdd:pfam00106 162 SLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
FabG-like PRK07231
SDR family oxidoreductase;
5-180 6.02e-33

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 117.62  E-value: 6.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVV-------AVTRTNSDL------------VSLAKEVSQMVAR-------- 57
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVvtdrneeAAERVAAEIlaggraiavaadVSDEADVEAAVAAalerfgsv 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 D-MIN-----------------------------------RGVP-------GSIVNVSSMVAHVTFPNLITYSSTKGAMT 94
Cdd:PRK07231  83 DiLVNnagtthrngplldvdeaefdrifavnvkspylwtqAAVPamrgeggGAIVNVASTAGLRPRPGLGWYNASKGAVI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  95 MLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFAR--KLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGI 172
Cdd:PRK07231 163 TLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTPENraKFLATIPLGRLGTPEDIANAALFLASDEASWITGVTL 242

                 ....*...
gi 568971391 173 LVDAGYLA 180
Cdd:PRK07231 243 VVDGGRCV 250
PRK06172 PRK06172
SDR family oxidoreductase;
1-180 2.24e-31

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 113.69  E-value: 2.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTR---------------------TNSDlVSLAKEVSQMVARDM 59
Cdd:PRK06172   1 MSMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRdaaggeetvalireaggealfVACD-VTRDAEVKALVEQTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  60 -----------------------------------IN-RGV---------------PGSIVNVSSMVAHVTFPNLITYSS 88
Cdd:PRK06172  80 aaygrldyafnnagieieqgrlaegseaefdaimgVNvKGVwlcmkyqiplmlaqgGGAIVNTASVAGLGAAPKMSIYAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  89 TKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKV-SADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSAST 167
Cdd:PRK06172 160 SKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAyEADPRKAEFAAAMHPVGRIGKVEEVASAVLYLCSDGASFT 239
                        250
                 ....*....|...
gi 568971391 168 SGGGILVDAGYLA 180
Cdd:PRK06172 240 TGHALMVDGGATA 252
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
4-180 6.95e-31

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


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 112.45  E-value: 6.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRtNSDLVSLAKE--------------------------------- 50
Cdd:cd05347    2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSR-NEEKAEEAQQliekegveataftcdvsdeeaikaaveaieedf 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 ---------------------------------------VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKG 91
Cdd:cd05347   81 gkidilvnnagiirrhpaeefpeaewrdvidvnlngvffVSQAVARHMIKQG-HGKIINICSLLSELGGPPVPAYAASKG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  92 AMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGG 171
Cdd:cd05347  160 GVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQI 239

                 ....*....
gi 568971391 172 ILVDAGYLA 180
Cdd:cd05347  240 IFVDGGWLA 248
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
4-177 5.79e-30

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 109.86  E-value: 5.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE--------------------VSQMVARDM---- 59
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAElraaggearvlvfdvsdeaaVRALIEAAVeafg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  60 ----------INRGVP------------------------------------GSIVNVSSMVAHVTFPNLITYSSTKGAM 93
Cdd:PRK05653  82 aldilvnnagITRDALlprmseedwdrvidvnltgtfnvvraalppmikaryGRIVNISSVSGVTGNPGQTNYSAAKAGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  94 TMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEfARKLKERhPLRKFAEVEDVVNSILFLLSDRSASTSGGGIL 173
Cdd:PRK05653 162 IGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVK-AEILKEI-PLGRLGQPEEVANAVAFLASDAASYITGQVIP 239

                 ....
gi 568971391 174 VDAG 177
Cdd:PRK05653 240 VNGG 243
PRK06841 PRK06841
short chain dehydrogenase; Provisional
3-178 1.47e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 108.98  E-value: 1.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   3 LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTR-----------------------TNSDLVS------------- 46
Cdd:PRK06841  11 FDLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRsedvaevaaqllggnakglvcdvSDSQSVEaavaavisafgri 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  47 -----------LAKEVS---------------------QMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMT 94
Cdd:PRK06841  91 dilvnsagvalLAPAEDvseedwdktidinlkgsflmaQAVGRHMIAAG-GGKIVNLASQAGVVALERHVAYCASKAGVV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  95 MLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADpEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILV 174
Cdd:PRK06841 170 GMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAG-EKGERAKKLIPAGRFAYPEEIAAAALFLASDAAAMITGENLVI 248

                 ....
gi 568971391 175 DAGY 178
Cdd:PRK06841 249 DGGY 252
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
10-177 5.62e-28

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: 104.55  E-value: 5.62e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE--------------------------------------- 50
Cdd:cd05333    3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEikalggnaaaleadvsdreavealvekveaefgpvdilv 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 --------------------------------VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTK 98
Cdd:cd05333   83 nnagitrdnllmrmseedwdavinvnltgvfnVTQAVIRAMIKRR-SGRIINISSVVGLIGNPGQANYAASKAGVIGFTK 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568971391  99 AMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEfaRKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd05333  162 SLAKELASRGITVNAVAPGFIDTDMTDALPEKVK--EKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGG 238
PRK12826 PRK12826
SDR family oxidoreductase;
5-179 6.02e-28

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 104.61  E-value: 6.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAK--------------------EVSQMVA-------- 56
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAElveaaggkararqvdvrdraALKAAVAagvedfgr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 ------------------------RDMIN------------------RGVPGSIVNVSSMVAHVT-FPNLITYSSTKGAM 93
Cdd:PRK12826  84 ldilvanagifpltpfaemddeqwERVIDvnltgtflltqaalpaliRAGGGRIVLTSSVAGPRVgYPGLAHYAASKAGL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  94 TMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADpEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGIL 173
Cdd:PRK12826 164 VGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDA-QWAEAIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQTLP 242

                 ....*.
gi 568971391 174 VDAGYL 179
Cdd:PRK12826 243 VDGGAT 248
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
52-180 8.81e-28

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 104.15  E-value: 8.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 SQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADP 131
Cdd:PRK05565 122 TRYALPYMIKRK-SGVIVNISSIWGLIGASCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEED 200
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568971391 132 EFArkLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLA 180
Cdd:PRK05565 201 KEG--LAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIITVDGGWTC 247
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
1-177 1.42e-27

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 103.81  E-value: 1.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDL-----------VSLAKEVSQMVAR--------DM-- 59
Cdd:PRK08220   2 NAMDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQedypfatfvldVSDAAAVAQVCQRllaetgplDVlv 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  60 ------------------------INRGVP----------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKA 99
Cdd:PRK08220  82 naagilrmgatdslsdedwqqtfaVNAGGAfnlfravmpqfrrqrsGAIVTVGSNAAHVPRIGMAAYGASKAALTSLAKC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391 100 MAMELGPHKIRVNSVNPTVVLTDMGKKVSADPE--------FARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGG 171
Cdd:PRK08220 162 VGLELAPYGVRCNVVSPGSTDTDMQRTLWVDEDgeqqviagFPEQFKLGIPLGKIARPQEIANAVLFLASDLASHITLQD 241

                 ....*.
gi 568971391 172 ILVDAG 177
Cdd:PRK08220 242 IVVDGG 247
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
4-177 2.81e-27

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 102.96  E-value: 2.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSD-------------------------------LVSLAKE-- 50
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAgaealvaeigalggkalavqgdvsdaesverAVDEAKAef 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 ---------------------------------------VSQMVARDMINRGVpGSIVNVSSMVAHVTFPNLITYSSTKG 91
Cdd:PRK05557  82 ggvdilvnnagitrdnllmrmkeedwdrvidtnltgvfnLTKAVARPMMKQRS-GRIINISSVVGLMGNPGQANYAASKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  92 AMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSadPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGG 171
Cdd:PRK05557 161 GVIGFTKSLARELASRGITVNAVAPGFIETDMTDALP--EDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQT 238

                 ....*.
gi 568971391 172 ILVDAG 177
Cdd:PRK05557 239 LHVNGG 244
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
4-180 5.67e-27

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: 102.14  E-value: 5.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE-------VSQMVA-------RDMI--------- 60
Cdd:cd05329    3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEwrekgfkVEGSVCdvssrseRQELmdtvashfg 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  61 --------NRGV----------------------------------------PGSIVNVSSMVAHVTFPNLITYSSTKGA 92
Cdd:cd05329   83 gklnilvnNAGTnirkeakdyteedyslimstnfeaayhlsrlahpllkasgNGNIVFISSVAGVIAVPSGAPYGATKGA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  93 MTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGI 172
Cdd:cd05329  163 LNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQII 242

                 ....*...
gi 568971391 173 LVDAGYLA 180
Cdd:cd05329  243 AVDGGLTA 250
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
66-177 5.88e-27

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


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 102.10  E-value: 5.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTD----MGKKVSADPEFARKLKERH 141
Cdd:cd05364  134 GEIVNVSSVAGGRSFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGfhrrMGMPEEQYIKFLSRAKETH 213
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568971391 142 PLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd05364  214 PLGRPGTVDEVAEAIAFLASDASSFITGQLLPVDGG 249
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
10-162 4.73e-26

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: 99.49  E-value: 4.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE--------------------------------------- 50
Cdd:COG4221    8 ALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAElggralavpldvtdeaaveaavaaavaefgrldvlvnna 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 -----------------------------VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMA 101
Cdd:COG4221   88 gvallgpleeldpedwdrmidvnvkgvlyVTRAALPAMRARG-SGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLR 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971391 102 MELGPHKIRVNSVNPTVVLTDMGKKVSadPEFARKLKERHPLRKFAEVEDVVNSILFLLSD 162
Cdd:COG4221  167 AELRPTGIRVTVIEPGAVDTEFLDSVF--DGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQ 225
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
51-180 4.24e-25

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: 97.40  E-value: 4.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGvPGSIVNVSSMVAH-VTFPNLIT-YSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVs 128
Cdd:cd05352  124 CAQAAAKIFKKQG-KGSLIITASMSGTiVNRPQPQAaYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFV- 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568971391 129 aDPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLA 180
Cdd:cd05352  202 -DKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYTTGSDLIIDGGYTC 252
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
7-177 9.21e-25

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


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 96.30  E-value: 9.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDL---------------------VSLAKEVSQMVA--------- 56
Cdd:cd05358    3 GKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAaeevveeikavggkaiavqadVSKEEDVVALFQsaikefgtl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 ------------------------------------------RDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMT 94
Cdd:cd05358   83 dilvnnaglqgdasshemtledwnkvidvnltgqflcareaiKRFRKSKIKGKIINMSSVHEKIPWPGHVNYAASKGGVK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  95 MLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILV 174
Cdd:cd05358  163 MMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGTTLFV 242

                 ...
gi 568971391 175 DAG 177
Cdd:cd05358  243 DGG 245
PRK06138 PRK06138
SDR family oxidoreductase;
1-181 1.06e-24

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 96.37  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNfsGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDL-------------------VSLAKEVSQMVARDMIN 61
Cdd:PRK06138   1 MRLA--GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAervaaaiaaggrafarqgdVGSAEAVEALVDFVAAR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  62 RG-------------------------------------------VP-------GSIVNVSSMVAHVTFPNLITYSSTKG 91
Cdd:PRK06138  79 WGrldvlvnnagfgcggtvvttdeadwdavmrvnvggvflwakyaIPimqrqggGSIVNTASQLALAGGRGRAAYVASKG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  92 AMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKV---SADPEFARK-LKERHPLRKFAEVEDVVNSILFLLSDRSAST 167
Cdd:PRK06138 159 AIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIfarHADPEALREaLRARHPMNRFGTAEEVAQAALFLASDESSFA 238
                        250
                 ....*....|....
gi 568971391 168 SGGGILVDAGYLAS 181
Cdd:PRK06138 239 TGTTLVVDGGWLAA 252
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-177 2.95e-24

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 94.94  E-value: 2.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE--------------------------------- 50
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEavealgrraqavqadvtdkaaleaavaaaverf 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 ---------------------------------------VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKG 91
Cdd:PRK12825  83 gridilvnnagifedkpladmsddewdevidvnlsgvfhLLRAVVPPMRKQR-GGRIVNISSVAGLPGWPGRSNYAAAKA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  92 AMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMgkkVSADPEFARKLKERH-PLRKFAEVEDVVNSILFLLSDRSASTSGG 170
Cdd:PRK12825 162 GLVGLTKALARELAEYGITVNMVAPGDIDTDM---KEATIEEAREAKDAEtPLGRSGTPEDIARAVAFLCSDASDYITGQ 238

                 ....*..
gi 568971391 171 GILVDAG 177
Cdd:PRK12825 239 VIEVTGG 245
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
10-177 7.04e-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: 94.07  E-value: 7.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTR-------------------TNSDLV------------------------- 45
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLpfvllleygdplrltpldvADAAAVrevcsrllaehgpidalvncagvlr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  46 -----SLAKE---------------VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELG 105
Cdd:cd05331   81 pgatdPLSTEdweqtfavnvtgvfnLLQAVAPHMKDRR-TGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391 106 PHKIRVNSVNPTVVLTDMGKKVSADPE--------FARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd05331  160 PYGVRCNVVSPGSTDTAMQRTLWHDEDgaaqviagVPEQFRLGIPLGKIAQPADIANAVLFLASDQAGHITMHDLVVDGG 239
PRK05867 PRK05867
SDR family oxidoreductase;
3-178 9.80e-24

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 93.95  E-value: 9.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   3 LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVS------------------------------ 52
Cdd:PRK05867   5 FDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGtsggkvvpvccdvsqhqqvtsmldqvtael 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  53 -----------------------------------------QMVARDMINRGVPGSIVNVSSMVAHV-TFPNLIT-YSST 89
Cdd:PRK05867  85 ggidiavcnagiitvtpmldmpleefqrlqntnvtgvfltaQAAAKAMVKQGQGGVIINTASMSGHIiNVPQQVShYCAS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  90 KGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMgkkVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSG 169
Cdd:PRK05867 165 KAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL---VEPYTEYQPLWEPKIPLGRLGRPEELAGLYLYLASEASSYMTG 241

                 ....*....
gi 568971391 170 GGILVDAGY 178
Cdd:PRK05867 242 SDIVIDGGY 250
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
10-178 2.13e-23

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: 92.80  E-value: 2.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDL---------------------VSLAKEVSQMV------------- 55
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAaaevaaeieelggkavvvradVSQPQDVEEMFaavkerfgrldvl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  56 --------------------------------------ARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLT 97
Cdd:cd05359   81 vsnaaagafrplseltpahwdakmntnlkalvhcaqqaAKLMRERG-GGRIVAISSLGSIRALPNYLAVGTAKAALEALV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  98 KAMAMELGPHKIRVNSVNPTVVLTDMGKKVsADPEFARK-LKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDA 176
Cdd:cd05359  160 RYLAVELGPRGIRVNAVSPGVIDTDALAHF-PNREDLLEaAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDG 238

                 ..
gi 568971391 177 GY 178
Cdd:cd05359  239 GL 240
PRK12743 PRK12743
SDR family oxidoreductase;
5-180 7.36e-23

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 91.63  E-value: 7.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVtrtNSDLVSLAkevSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLI 84
Cdd:PRK12743  78 LGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTV---DVDGAFLC---SQIAARHMVKQGQGGRIINITSVHEHTPLPGAS 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  85 TYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPefarKLKERH--PLRKFAEVEDVVNSILFLLSD 162
Cdd:PRK12743 152 AYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDV----KPDSRPgiPLGRPGDTHEIASLVAWLCSE 227
                        170
                 ....*....|....*...
gi 568971391 163 RSASTSGGGILVDAGYLA 180
Cdd:PRK12743 228 GASYTTGQSLIVDGGFML 245
PRK06124 PRK06124
SDR family oxidoreductase;
7-180 1.72e-22

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 90.54  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   7 GLRALVTGAGkgiGRDTVKALHASGAKVVAVTRTnsDLVSlAKEVSQMVARDMiNRGVPGSIVNVSSMVAHVTFPNLITY 86
Cdd:PRK06124  88 RLDILVNNVG---ARDRRPLAELDDAAIRALLET--DLVA-PILLSRLAAQRM-KRQGYGRIIAITSIAGQVARAGDAVY 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  87 SSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDrSAS 166
Cdd:PRK06124 161 PAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPAVGPWLAQRTPLGRWGRPEEIAGAAVFLASP-AAS 239
                        170
                 ....*....|....*
gi 568971391 167 TSGGGIL-VDAGYLA 180
Cdd:PRK06124 240 YVNGHVLaVDGGYSV 254
PRK07478 PRK07478
short chain dehydrogenase; Provisional
10-177 1.94e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 90.37  E-value: 1.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQ------MVARD------------------------- 58
Cdd:PRK07478   9 AIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAeggeavALAGDvrdeayakalvalaverfggldiaf 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 -----------------------------------------MINRGvPGSIVNVSSMVAH-VTFPNLITYSSTKGAMTML 96
Cdd:PRK07478  89 nnagtlgemgpvaemslegwretlatnltsaflgakhqipaMLARG-GGSLIFTSTFVGHtAGFPGMAAYAASKAGLIGL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  97 TKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDA 176
Cdd:PRK07478 168 TQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEALAFVAGLHALKRMAQPEEIAQAALFLASDAASFVTGTALLVDG 247

                 .
gi 568971391 177 G 177
Cdd:PRK07478 248 G 248
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
7-177 2.34e-22

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: 90.03  E-value: 2.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQ--------------------------------- 53
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAggagvlavvadltdpedidrlvekagdafgrvd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  54 ------------------------------MVARDMINRGVP-------GSIVNVSSMVAHVTFPNLITYSSTKGAMTML 96
Cdd:cd05344   81 ilvnnaggpppgpfaeltdedwleafdlklLSVIRIVRAVLPgmkergwGRIVNISSLTVKEPEPNLVLSNVARAGLIGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  97 TKAMAMELGPHKIRVNSVNPTVVLTD--------MGKKVSADPEFARKLKERH-PLRKFAEVEDVVNSILFLLSDRSAST 167
Cdd:cd05344  161 VKTLSRELAPDGVTVNSVLPGYIDTErvrrlleaRAEKEGISVEEAEKEVASQiPLGRVGKPEELAALIAFLASEKASYI 240
                        250
                 ....*....|
gi 568971391 168 SGGGILVDAG 177
Cdd:cd05344  241 TGQAILVDGG 250
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4-165 5.02e-22

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 89.16  E-value: 5.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE--------------------------------- 50
Cdd:COG0300    2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAElraagarvevvaldvtdpdavaalaeavlarfg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 --------------------------------------VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGA 92
Cdd:COG0300   82 pidvlvnnagvggggpfeeldledlrrvfevnvfgpvrLTRALLPLMRARG-RGRIVNVSSVAGLRGLPGMAAYAASKAA 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971391  93 MTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEfarklkerhplRKFAEVEDVVNSILFLLSDRSA 165
Cdd:COG0300  161 LEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAG-----------RPLLSPEEVARAILRALERGRA 222
PRK12939 PRK12939
short chain dehydrogenase; Provisional
1-180 5.62e-22

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 88.88  E-value: 5.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVV----------------------------------AVTR------- 39
Cdd:PRK12939   1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAfndglaaearelaaaleaaggrahaiaadladpaSVQRffdaaaa 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  40 ---------------TNSDLVSLAKE---------------VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSST 89
Cdd:PRK12939  81 alggldglvnnagitNSKSATELDIDtwdavmnvnvrgtflMLRAALPHLRDSG-RGRIVNLASDTALWGAPKLGAYVAS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  90 KGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADpEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSG 169
Cdd:PRK12939 160 KGAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPAD-ERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTG 238
                        250
                 ....*....|.
gi 568971391 170 GGILVDAGYLA 180
Cdd:PRK12939 239 QLLPVNGGFVM 249
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
5-177 6.01e-22

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 91.83  E-value: 6.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTR-------------------------TNSD---------------- 43
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLdeeaaeaaaaelggpdralgvacdvTDEAavqaafeeaalafggv 499
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  44 --LVSLA---------------------------KEVSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMT 94
Cdd:PRK08324 500 diVVSNAgiaisgpieetsdedwrrsfdvnatghFLVAREAVRIMKAQGLGGSIVFIASKNAVNPGPNFGAYGAAKAAEL 579
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  95 MLTKAMAMELGPHKIRVNSVNPTVVLTD-------MGKKVSAdpefARKLKERHPLRKFA-------EV--EDVVNSILF 158
Cdd:PRK08324 580 HLVRQLALELGPDGIRVNGVNPDAVVRGsgiwtgeWIEARAA----AYGLSEEELEEFYRarnllkrEVtpEDVAEAVVF 655
                        250
                 ....*....|....*....
gi 568971391 159 LLSDRSASTSGGGILVDAG 177
Cdd:PRK08324 656 LASGLLSKTTGAIITVDGG 674
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
39-181 6.27e-22

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 89.06  E-value: 6.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  39 RTNsdlVSLAKEVSQMVARDMINRGVpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTV 118
Cdd:PRK07523 116 RTN---ISSVFYVGQAVARHMIARGA-GKIINIASVQSALARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGY 191
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971391 119 VLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS 181
Cdd:PRK07523 192 FDTPLNAALVADPEFSAWLEKRTPAGRWGKVEELVGACVFLASDASSFVNGHVLYVDGGITAS 254
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
66-178 7.25e-22

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: 88.60  E-value: 7.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKK--VSADPEFARKLKERHPL 143
Cdd:cd05345  132 GVIINIASTAGLRPRPGLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMfmGEDTPENRAKFRATIPL 211
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568971391 144 RKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:cd05345  212 GRLSTPDDIANAALYLASDEASFITGVALEVDGGR 246
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
52-180 2.93e-21

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: 87.51  E-value: 2.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 SQMVARDMINRGVpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADP 131
Cdd:cd08935  135 SQVFGKDMLEQKG-GSIINISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINP 213
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568971391 132 E-----FARKLKERHPLRKFAEVEDVVNSILFLLSDRSAS-TSGGGILVDAGYLA 180
Cdd:cd08935  214 DgsytdRSNKILGRTPMGRFGKPEELLGALLFLASEKASSfVTGVVIPVDGGFSA 268
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
51-181 5.15e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 86.73  E-value: 5.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSAD 130
Cdd:PRK08085 124 VSQAVARYMVKRQ-AGKIINICSMQSELGRDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVED 202
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568971391 131 PEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS 181
Cdd:PRK08085 203 EAFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFVDGGMLVA 253
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
5-177 1.12e-20

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: 85.31  E-value: 1.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAG-KGIGRDTVKALHASGAKVVAVtrtnsDLVSLAKeVSQMVARDMINRGvPGSIVNVSSMVAHVTFPNL 83
Cdd:cd05365   74 FGGITILVNNAGgGGPKPFDMPMTEEDFEWAFKL-----NLFSAFR-LSQLCAPHMQKAG-GGAILNISSMSSENKNVRI 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  84 ITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSAdPEFARKLKERHPLRKFAEVEDVVNSILFLLSDR 163
Cdd:cd05365  147 AAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLT-PEIERAMLKHTPLGRLGEPEDIANAALFLCSPA 225
                        170
                 ....*....|....
gi 568971391 164 SASTSGGGILVDAG 177
Cdd:cd05365  226 SAWVSGQVLTVSGG 239
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
5-180 1.57e-20

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: 85.13  E-value: 1.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVtrtNSDLVSLAkevSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLI 84
Cdd:cd05341   77 FGRLDVLVNNAGILTGGTVETTTLEEWRRLLDI---NLTGVFLG---TRAVIPPMKEAG-GGSIINMSSIEGLVGDPALA 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  85 TYSSTKGAMTMLTKAMAMELGPHK--IRVNSVNPTVVLTDMGKKVSADPEfARKLKERHPLRKFAEVEDVVNSILFLLSD 162
Cdd:cd05341  150 AYNASKGAVRGLTKSAALECATQGygIRVNSVHPGYIYTPMTDELLIAQG-EMGNYPNTPMGRAGEPDEIAYAVVYLASD 228
                        170
                 ....*....|....*...
gi 568971391 163 RSASTSGGGILVDAGYLA 180
Cdd:cd05341  229 ESSFVTGSELVVDGGYTA 246
PRK06198 PRK06198
short chain dehydrogenase; Provisional
53-169 1.77e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 85.44  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  53 QMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTD-----MGKKV 127
Cdd:PRK06198 124 QEAIKLMRRRKAEGTIVNIGSMSAHGGQPFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEgedriQREFH 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568971391 128 SADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSG 169
Cdd:PRK06198 204 GAPDDWLEKAAATQPFGRLLDPDEVARAVAFLLSDESGLMTG 245
PRK06523 PRK06523
short chain dehydrogenase; Provisional
3-177 1.44e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 82.64  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   3 LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRT-----NSDLVSLAKEVS-----QMVAR--------------- 57
Cdd:PRK06523   5 LELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSrpddlPEGVEFVAADLTtaegcAAVARavlerlggvdilvhv 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 ---------------------------------------DMINRGvPGSIVNVSSMVAHVTFPNLIT-YSSTKGAMTMLT 97
Cdd:PRK06523  85 lggssapaggfaaltdeewqdelnlnllaavrldrallpGMIARG-SGVIIHVTSIQRRLPLPESTTaYAAAKAALSTYS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  98 KAMAMELGPHKIRVNSVNPTVVLTD--------MGKKVSADPEFARKLKERH----PLRKFAEVEDVVNSILFLLSDRSA 165
Cdd:PRK06523 164 KSLSKEVAPKGVRVNTVSPGWIETEaavalaerLAEAAGTDYEGAKQIIMDSlggiPLGRPAEPEEVAELIAFLASDRAA 243
                        250
                 ....*....|..
gi 568971391 166 STSGGGILVDAG 177
Cdd:PRK06523 244 SITGTEYVIDGG 255
PRK09242 PRK09242
SDR family oxidoreductase;
4-180 1.48e-19

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 82.87  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLV----------------SLAKEVSQMVARDMI------- 60
Cdd:PRK09242   6 RLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAqardelaeefperevhGLAADVSDDEDRRAIldwvedh 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  61 ---------NRGV----------------------------------------PGSIVNVSSMVAHVTFPNLITYSSTKG 91
Cdd:PRK09242  86 wdglhilvnNAGGnirkaaidytedewrgifetnlfsafelsryahpllkqhaSSAIVNIGSVSGLTHVRSGAPYGMTKA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  92 AMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGG 171
Cdd:PRK09242 166 ALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPAASYITGQC 245

                 ....*....
gi 568971391 172 ILVDAGYLA 180
Cdd:PRK09242 246 IAVDGGFLR 254
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
51-177 1.88e-19

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 82.59  E-value: 1.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSAd 130
Cdd:PRK06113 125 LSQLVAPEMEKNG-GGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVIT- 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568971391 131 PEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK06113 203 PEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGG 249
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
52-177 2.07e-19

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: 82.38  E-value: 2.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 SQMVARDMINRGvPGSIVNVSSMVAhVTFPNL-----------ITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVL 120
Cdd:cd08930  122 SQAFIKLFKKQG-KGSIINIASIYG-VIAPDFriyentqmyspVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIL 199
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568971391 121 TDMgkkvsaDPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd08930  200 NNQ------PSEFLEKYTKKCPLKRMLNPEDLRGAIIFLLSDASSYVTGQNLVIDGG 250
PRK07035 PRK07035
SDR family oxidoreductase;
4-180 3.81e-19

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 81.60  E-value: 3.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQ------------------------------ 53
Cdd:PRK07035   5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAaggkaealachigemeqidalfahirerhg 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  54 -----------------MVARD-----------------MINRGVP-------GSIVNVSSMVAHVTFPNLITYSSTKGA 92
Cdd:PRK07035  85 rldilvnnaaanpyfghILDTDlgafqktvdvnirgyffMSVEAGKlmkeqggGSIVNVASVNGVSPGDFQGIYSITKAA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  93 MTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGI 172
Cdd:PRK07035 165 VISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTGECL 244

                 ....*...
gi 568971391 173 LVDAGYLA 180
Cdd:PRK07035 245 NVDGGYLS 252
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
53-178 5.25e-19

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 81.30  E-value: 5.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  53 QMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPE 132
Cdd:PRK08063 122 QEAAKLMEKVG-GGKIISLSSLGSIRYLENYTTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREE 200
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568971391 133 FARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK08063 201 LLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMIRGQTIIVDGGR 246
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
4-177 5.89e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 81.15  E-value: 5.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVS---------------------------LAKEV----- 51
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEaaahlealgidalwiaadvadeadierLAEETlerfg 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 ---------------------------------------SQMVARDMINRGVPGSIVNVSSmVA-----HVTFPNLITYS 87
Cdd:PRK08213  89 hvdilvnnagatwgapaedhpveawdkvmnlnvrglfllSQAVAKRSMIPRGYGRIINVAS-VAglggnPPEVMDTIAYN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  88 STKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEfaRKLKERHPLRKFAEVEDVVNSILFLLSDRSAST 167
Cdd:PRK08213 168 TSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERLG--EDLLAHTPLGRLGDDEDLKGAALLLASDASKHI 245
                        250
                 ....*....|
gi 568971391 168 SGGGILVDAG 177
Cdd:PRK08213 246 TGQILAVDGG 255
PRK05875 PRK05875
short chain dehydrogenase; Provisional
1-179 1.17e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 80.62  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQM-------------------------- 54
Cdd:PRK05875   1 MQLSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALkgagavryepadvtdedqvaravdaa 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  55 ------------------------------------------------VARDMInRGVPGSIVNVSSMVAHVTFPNLITY 86
Cdd:PRK05875  81 tawhgrlhgvvhcaggsetigpitqidsdawrrtvdlnvngtmyvlkhAARELV-RGGGGSFVGISSIAASNTHRWFGAY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  87 SSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSAS 166
Cdd:PRK05875 160 GVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSADYRACTPLPRVGEVEDVANLAMFLLSDAASW 239
                        250
                 ....*....|...
gi 568971391 167 TSGGGILVDAGYL 179
Cdd:PRK05875 240 ITGQVINVDGGHM 252
PRK12829 PRK12829
short chain dehydrogenase; Provisional
5-177 1.57e-18

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 80.10  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQM-----------------VARDMINR----- 62
Cdd:PRK12829   9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAkvtatvadvadpaqverVFDTAVERfggld 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  63 ------------------------------------------------GVPGSIVNVSSMVAHVTFPNLITYSSTKGAMT 94
Cdd:PRK12829  89 vlvnnagiagptggideitpeqweqtlavnlngqfyfaraavpllkasGHGGVIIALSSVAGRLGYPGRTPYAASKWAVV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  95 MLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSAD---------PEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSA 165
Cdd:PRK12829 169 GLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEAraqqlgiglDEMEQEYLEKISLGRMVEPEDIAATALFLASPAAR 248
                        250
                 ....*....|..
gi 568971391 166 STSGGGILVDAG 177
Cdd:PRK12829 249 YITGQAISVDGN 260
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
7-178 1.87e-18

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: 79.44  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAK---------------EVSQMVAR-------------- 57
Cdd:cd05368    2 GKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERgpgittrvldvtdkeQVAALAKEegridvlfncagfv 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 ---------------------------------DMINRGvPGSIVNVSSMVAHV-TFPNLITYSSTKGAMTMLTKAMAME 103
Cdd:cd05368   82 hhgsildcedddwdfamnlnvrsmylmikavlpKMLARK-DGSIINMSSVASSIkGVPNRFVYSTTKAAVIGLTKSVAAD 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568971391 104 LGPHKIRVNSVNPTVVLTDMGK---KVSADPEFARK-LKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:cd05368  161 FAQQGIRCNAICPGTVDTPSLEeriQAQPDPEEALKaFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVIDGGW 239
PRK07069 PRK07069
short chain dehydrogenase; Validated
65-177 2.01e-18

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 79.75  E-value: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  65 PGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHK--IRVNSVNPTVVLTDMGKKVSA---DPEFARKLKE 139
Cdd:PRK07069 130 PASIVNISSVAAFKAEPDYTAYNASKAAVASLTKSIALDCARRGldVRCNSIHPTFIRTGIVDPIFQrlgEEEATRKLAR 209
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568971391 140 RHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK07069 210 GVPLGRLGEPDDVAHAVLYLASDESRFVTGAELVIDGG 247
PRK06947 PRK06947
SDR family oxidoreductase;
48-177 2.83e-18

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 79.08  E-value: 2.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  48 AKEVSQMVARDMINRGvpGSIVNVSSMVAHVTFPN-LITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMgKK 126
Cdd:PRK06947 120 AREAARRLSTDRGGRG--GAIVNVSSIASRLGSPNeYVDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI-HA 196
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568971391 127 VSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK06947 197 SGGQPGRAARLGAQTPLGRAGEADEVAETIVWLLSDAASYVTGALLDVGGG 247
PRK07856 PRK07856
SDR family oxidoreductase;
3-177 3.01e-18

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 79.21  E-value: 3.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   3 LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAK------------EVSQMVAR--------DM-IN 61
Cdd:PRK07856   2 LDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRPaefhaadvrdpdQVAALVDAiverhgrlDVlVN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  62 R--GVP----------------------------------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKA 99
Cdd:PRK07856  82 NagGSPyalaaeasprfhekivelnllapllvaqaanavmqqqpggGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNLTRS 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568971391 100 MAMELGPhKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK07856 162 LAVEWAP-KVRVNAVVVGLVRTEQSELHYGDAEGIAAVAATVPLGRLATPADIAWACLFLASDLASYVSGANLEVHGG 238
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
10-177 3.42e-18

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: 78.96  E-value: 3.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSD-LVSLAKEVSQ----------------------------------M 54
Cdd:cd05366    5 AIITGAAQGIGRAIAERLAADGFNIVLADLNLEEaAKSTIQEISEagynavavgadvtdkddvealidqavekfgsfdvM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  55 V-------------------------------------ARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLT 97
Cdd:cd05366   85 VnnagiapitplltiteedlkkvyavnvfgvlfgiqaaARQFKKLGHGGKIINASSIAGVQGFPNLGAYSASKFAVRGLT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  98 KAMAMELGPHKIRVNSVNPTVVLTDM------------GKKV-SADPEFARKLkerhPLRKFAEVEDVVNSILFLLSDRS 164
Cdd:cd05366  165 QTAAQELAPKGITVNAYAPGIVKTEMwdyideevgeiaGKPEgEGFAEFSSSI----PLGRLSEPEDVAGLVSFLASEDS 240
                        250
                 ....*....|...
gi 568971391 165 ASTSGGGILVDAG 177
Cdd:cd05366  241 DYITGQTILVDGG 253
PRK06114 PRK06114
SDR family oxidoreductase;
1-180 4.34e-18

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 78.67  E-value: 4.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKL-NFSGLRALVTGAGKGIGRDTVKALHASGAKVV---------------------------------------AVTRT 40
Cdd:PRK06114   1 PQLfDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVAlfdlrtddglaetaehieaagrraiqiaadvtskadlraAVART 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  41 NSDLVSL--------------AKEVS-------------------QMVARDMINRGvPGSIVNVSSMVAHVTFPNLIT-- 85
Cdd:PRK06114  81 EAELGALtlavnaagiananpAEEMEeeqwqtvmdinltgvflscQAEARAMLENG-GGSIVNIASMSGIIVNRGLLQah 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  86 YSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKvsadPEFA---RKLKERHPLRKFAEVEDVVNSILFLLSD 162
Cdd:PRK06114 160 YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTR----PEMVhqtKLFEEQTPMQRMAKVDEMVGPAVFLLSD 235
                        250
                 ....*....|....*...
gi 568971391 163 RSASTSGGGILVDAGYLA 180
Cdd:PRK06114 236 AASFCTGVDLLVDGGFVC 253
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
5-177 5.92e-18

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: 78.40  E-value: 5.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE---------------------------------- 50
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEissatggrahpiqcdvrdpeaveaavdetlkefg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 --------------------------------------VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGA 92
Cdd:cd05369   81 kidilinnaagnflapaeslspngfktvididlngtfnTTKAVGKRLIEAKHGGSILNISATYAYTGSPFQVHSAAAKAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  93 MTMLTKAMAMELGPHKIRVNSVNPTVVLTDMG-KKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGG 171
Cdd:cd05369  161 VDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGmERLAPSGKSEKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTT 240

                 ....*.
gi 568971391 172 ILVDAG 177
Cdd:cd05369  241 LVVDGG 246
PRK06123 PRK06123
SDR family oxidoreductase;
5-177 7.24e-18

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 78.28  E-value: 7.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGkgIGRDTVKALHASGAKVVAVTRTN--SDLVSLAKEVSQMVARdmiNRGVPGSIVNVSSMVAHVTFPN 82
Cdd:PRK06123  78 LGRLDALVNNAG--ILEAQMRLEQMDAARLTRIFATNvvGSFLCAREAVKRMSTR---HGGRGGAIVNVSSMAARLGSPG 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  83 -LITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMgKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLS 161
Cdd:PRK06123 153 eYIDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI-HASGGEPGRVDRVKAGIPMGRGGTAEEVARAILWLLS 231
                        170
                 ....*....|....*.
gi 568971391 162 DRSASTSGGGILVDAG 177
Cdd:PRK06123 232 DEASYTTGTFIDVSGG 247
PRK08265 PRK08265
short chain dehydrogenase; Provisional
10-180 7.38e-18

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 78.13  E-value: 7.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVV-----------------------------------AVTRT-------------- 40
Cdd:PRK08265   9 AIVTGGATLIGAAVARALVAAGARVAivdidadngaavaaslgerarfiatditddaaierAVATVvarfgrvdilvnla 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  41 -------------------NSDLVSlAKEVSQMVARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMA 101
Cdd:PRK08265  89 ctylddglassradwlaalDVNLVS-AAMLAQAAHPHLARGG--GAIVNFTSISAKFAQTGRWLYPASKAAIRQLTRSMA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391 102 MELGPHKIRVNSVNP----TVVLTDM--GKKVSADpefaRKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVD 175
Cdd:PRK08265 166 MDLAPDGIRVNSVSPgwtwSRVMDELsgGDRAKAD----RVAAPFHLLGRVGDPEEVAQVVAFLCSDAASFVTGADYAVD 241

                 ....*
gi 568971391 176 AGYLA 180
Cdd:PRK08265 242 GGYSA 246
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-181 8.21e-18

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 78.24  E-value: 8.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKgIGRDtvKALHASGAKVVAVTRTNSDLVSLakeVSQMVARDMINRGvPGSIVNVSSMVAHVTFPNL 83
Cdd:PRK06935  88 EFGKIDILVNNAGT-IRRA--PLLEYKDEDWNAVMDINLNSVYH---LSQAVAKVMAKQG-SGKIINIASMLSFQGGKFV 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  84 ITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDR 163
Cdd:PRK06935 161 PAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNRNDEILKRIPAGRWGEPDDLMGAAVFLASRA 240
                        170
                 ....*....|....*...
gi 568971391 164 SASTSGGGILVDAGYLAS 181
Cdd:PRK06935 241 SDYVNGHILAVDGGWLVR 258
PRK06500 PRK06500
SDR family oxidoreductase;
5-177 8.58e-18

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 77.69  E-value: 8.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKV--------------------VAVTRTNSDLVSLAKEVSQMVARD------ 58
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVaitgrdpasleaaraelgesALVIRADAGDVAAQKALAQALAEAfgrlda 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 -MINRGV--------------------------------------PGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKA 99
Cdd:PRK06500  84 vFINAGVakfapledwdeamfdrsfntnvkgpyfliqallpllanPASIVLNGSINAHIGMPNSSVYAASKAALLSLAKT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391 100 MAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEF----ARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVD 175
Cdd:PRK06500 164 LSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATldavAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFIVGSEIIVD 243

                 ..
gi 568971391 176 AG 177
Cdd:PRK06500 244 GG 245
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
10-178 1.33e-17

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: 77.32  E-value: 1.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDL---------------------VSLAKEVSQMV------------- 55
Cdd:cd05362    6 ALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAaeevvaeieaaggkaiavqadVSDPSQVARLFdaaekafggvdil 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  56 -------------------------------------ARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTK 98
Cdd:cd05362   86 vnnagvmlkkpiaetseeefdrmftvntkgaffvlqeAAKRLRDG--GRIINISSSLTAAYTPNYGAYAGSKAAVEAFTR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  99 AMAMELGPHKIRVNSVNPTVVLTDM--GKKVSADPEFarkLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDA 176
Cdd:cd05362  164 VLAKELGGRGITVNAVAPGPVDTDMfyAGKTEEAVEG---YAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQVIRANG 240

                 ..
gi 568971391 177 GY 178
Cdd:cd05362  241 GY 242
PRK07577 PRK07577
SDR family oxidoreductase;
9-177 1.63e-17

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 77.07  E-value: 1.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   9 RALVTGAGKGIGRDTVKALHASGAKVVAVTRTNS---------------------------------------------- 42
Cdd:PRK07577   5 TVLVTGATKGIGLALSLRLANLGHQVIGIARSAIddfpgelfacdladieqtaatlaqineihpvdaivnnvgialpqpl 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  43 ---DLVSL----------AKEVSQMVARDMINRGVpGSIVNVSSMVAHVTfPNLITYSSTKGAMTMLTKAMAMELGPHKI 109
Cdd:PRK07577  85 gkiDLAALqdvydlnvraAVQVTQAFLEGMKLREQ-GRIVNICSRAIFGA-LDRTSYSAAKSALVGCTRTWALELAEYGI 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568971391 110 RVNSVNPTVVLTDMGKKVS-ADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK07577 163 TVNAVAPGPIETELFRQTRpVGSEEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDGG 231
PRK12828 PRK12828
short chain dehydrogenase; Provisional
66-177 2.07e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 76.76  E-value: 2.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARklkerhplrk 145
Cdd:PRK12828 134 GRIVNIGAGAALKAGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMPDADFSR---------- 203
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568971391 146 FAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK12828 204 WVTPEQIAAVIAFLLSDEAQAITGASIPVDGG 235
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
44-178 2.12e-17

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


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 76.99  E-value: 2.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  44 LVSLAKEvsqmvARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM 123
Cdd:COG0623  122 LVALAKA-----AEPLMNEG--GSIVTLTYLGAERVVPNYNVMGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKTLA 194
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568971391 124 GKKVsadPEFARKLK---ERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:COG0623  195 ASGI---PGFDKLLDyaeERAPLGRNVTIEEVGNAAAFLLSDLASGITGEIIYVDGGY 249
PRK07890 PRK07890
short chain dehydrogenase; Provisional
51-177 3.23e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 76.53  E-value: 3.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKK---- 126
Cdd:PRK07890 121 LTQAFTPALAESG--GSIVMINSMVLRHSQPKYGAYKMAKGALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKGyfrh 198
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568971391 127 ------VSADPEFARkLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK07890 199 qagkygVTVEQIYAE-TAANSDLKRLPTDDEVASAVLFLASDLARAITGQTLDVNCG 254
PRK06484 PRK06484
short chain dehydrogenase; Validated
56-181 3.39e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 78.35  E-value: 3.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  56 ARDMINRGVpgsIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEF-A 134
Cdd:PRK06484 387 ARLMSQGGV---IVNLGSIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLALKASGRAdF 463
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568971391 135 RKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS 181
Cdd:PRK06484 464 DSIRRRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTVDGGWTAF 510
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
51-180 3.73e-17

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 76.10  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSAD 130
Cdd:PRK12481 121 LSQAVAKQFVKQGNGGKIINIASMLSFQGGIRVPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRAD 200
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568971391 131 PEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLA 180
Cdd:PRK12481 201 TARNEAILERIPASRWGTPDDLAGPAIFLSSSASDYVTGYTLAVDGGWLA 250
PRK09135 PRK09135
pteridine reductase; Provisional
10-177 3.83e-17

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 76.12  E-value: 3.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVA-----------------VTRTNS---------DLVSLAKEVSQMVAR------ 57
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVAIhyhrsaaeadalaaelnALRPGSaaalqadllDPDALPELVAACVAAfgrlda 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 ----------------------DMI--NRGVP---------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTK 98
Cdd:PRK09135  89 lvnnassfyptplgsiteaqwdDLFasNLKAPfflsqaaapqlrkqrGAIVNITDIHAERPLKGYPVYCAAKAALEMLTR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  99 AMAMELGPHkIRVNSVNPTVVLTDMGKKvSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTsgGGIL-VDAG 177
Cdd:PRK09135 169 SLALELAPE-VRVNAVAPGAILWPEDGN-SFDEEARQAILARTPLKRIGTPEDIAEAVRFLLADASFIT--GQILaVDGG 244
PRK09730 PRK09730
SDR family oxidoreductase;
8-177 4.36e-17

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 76.04  E-value: 4.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   8 LRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQMVARdmiNRGVPGSIVNVSSMVAHVTFP-NLITY 86
Cdd:PRK09730  80 LAALVNNAGILFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALK---HGGSGGAIVNVSSAASRLGAPgEYVDY 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  87 SSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKvSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDrSAS 166
Cdd:PRK09730 157 AASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHAS-GGEPGRVDRVKSNIPMQRGGQPEEVAQAIVWLLSD-KAS 234
                        170
                 ....*....|.
gi 568971391 167 TSGGGILVDAG 177
Cdd:PRK09730 235 YVTGSFIDLAG 245
PRK07814 PRK07814
SDR family oxidoreductase;
10-177 5.16e-17

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 75.97  E-value: 5.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQ------MVARD------------------------- 58
Cdd:PRK07814  13 AVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAagrrahVVAADlahpeataglagqaveafgrldivv 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 ----------------------------------------MINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTK 98
Cdd:PRK07814  93 nnvggtmpnpllststkdladaftfnvatahaltvaavplMLEHSGGGSVINISSTMGRLAGRGFAAYGTAKAALAHYTR 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568971391  99 AMAMELGPhKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK07814 173 LAALDLCP-RIRVNAIAPGSILTSALEVVAANDELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKTLEVDGG 250
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
48-177 6.54e-17

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: 75.57  E-value: 6.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  48 AKEVSQMVARDMINRGVpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKV 127
Cdd:cd05349  116 ALNLLQAVLPDFKERGS-GRVINIGTNLFQNPVVPYHDYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAA 194
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568971391 128 SADpEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd05349  195 TPK-EVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQNLVVDGG 243
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
51-180 6.77e-17

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 75.68  E-value: 6.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSAD 130
Cdd:PRK08993 123 MSQAAAKHFIAQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRAD 202
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568971391 131 PEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLA 180
Cdd:PRK08993 203 EQRSAEILDRIPAGRWGLPSDLMGPVVFLASSASDYINGYTIAVDGGWLA 252
PRK07063 PRK07063
SDR family oxidoreductase;
7-177 7.38e-17

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 75.47  E-value: 7.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVV-------AVTRTNSDL---------------VSLAKEVSQMVAR------- 57
Cdd:PRK07063   7 GKVALVTGAAQGIGAAIARAFAREGAAVAladldaaLAERAAAAIardvagarvlavpadVTDAASVAAAVAAaeeafgp 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 --------------------------------------------DMINRGVpGSIVNVSSMVAHVTFPNLITYSSTKGAM 93
Cdd:PRK07063  87 ldvlvnnaginvfadplamtdedwrrcfavdldgawngcravlpGMVERGR-GSIVNIASTHAFKIIPGCFPYPVAKHGL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  94 TMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKV---SADPEFARKLKER-HPLRKFAEVEDVVNSILFLLSDRSASTSG 169
Cdd:PRK07063 166 LGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWwnaQPDPAAARAETLAlQPMKRIGRPEEVAMTAVFLASDEAPFINA 245

                 ....*...
gi 568971391 170 GGILVDAG 177
Cdd:PRK07063 246 TCITIDGG 253
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-179 1.42e-16

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 74.76  E-value: 1.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVtrtnsDLVSLAKeVSQMVARDMINrgvPGSIVNVSSMVAHVTFPNL 83
Cdd:PRK06077  81 RYGVADILVNNAGLGLFSPFLNVDDKLIDKHIST-----DFKSVIY-CSQELAKEMRE---GGAIVNIASVAGIRPAYGL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  84 ITYSSTKGAMTMLTKAMAMELGPhKIRVNSVNPTVVLTDMGK---KVS--ADPEFArklkERHPLR-KFAEVEDVVNSIL 157
Cdd:PRK06077 152 SIYGAMKAAVINLTKYLALELAP-KIRVNAIAPGFVKTKLGEslfKVLgmSEKEFA----EKFTLMgKILDPEEVAEFVA 226
                        170       180
                 ....*....|....*....|..
gi 568971391 158 FLLSdrSASTSGGGILVDAGYL 179
Cdd:PRK06077 227 AILK--IESITGQVFVLDSGES 246
PRK08628 PRK08628
SDR family oxidoreductase;
66-178 2.01e-16

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 74.22  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGK---KVSADPEfaRKLKE--- 139
Cdd:PRK08628 133 GAIVNISSKTALTGQGGTSGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYEnwiATFDDPE--AKLAAita 210
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568971391 140 RHPL-RKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK08628 211 KIPLgHRMTTAEEIADTAVFLLSERSSHTTGQWLFVDGGY 250
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
10-178 2.04e-16

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 74.03  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTN-------------------------SDLVSLAKEVSQMVARD------ 58
Cdd:PRK12824   5 ALVTGAKRGIGSAIARELLNDGYRVIATYFSGndcakdwfeeygftedqvrlkeldvTDTEECAEALAEIEEEEgpvdil 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 -----------------------------------------MINRGVpGSIVNVSSMVA---HVTFPNlitYSSTKGAMT 94
Cdd:PRK12824  85 vnnagitrdsvfkrmshqewndvintnlnsvfnvtqplfaaMCEQGY-GRIINISSVNGlkgQFGQTN---YSAAKAGMI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  95 MLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSadPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILV 174
Cdd:PRK12824 161 GFTKALASEGARYGITVNCIAPGYIATPMVEQMG--PEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFITGETISI 238

                 ....
gi 568971391 175 DAGY 178
Cdd:PRK12824 239 NGGL 242
PRK07074 PRK07074
SDR family oxidoreductase;
55-180 2.50e-16

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 74.04  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  55 VARDMINRGvPGSIVNVSSM--VAHVTFPnliTYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM-GKKVSADP 131
Cdd:PRK07074 119 VLEGMLKRS-RGAVVNIGSVngMAALGHP---AYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAwEARVAANP 194
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568971391 132 EFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLA 180
Cdd:PRK07074 195 QVFEELKKWYPLQDFATPDDVANAVLFLASPAARAITGVCLPVDGGLTA 243
PRK12827 PRK12827
short chain dehydrogenase; Provisional
36-178 4.68e-16

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 73.22  E-value: 4.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  36 AVTRTNSDLvslAKEVSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVN 115
Cdd:PRK12827 113 DVIDVNLDG---FFNVTQAALPPMIRARRGGRIVNIASVAGVRGNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVA 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971391 116 PTVVLTDMGKKVSADPefarKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK12827 190 PGAINTPMADNAAPTE----HLLNPVPVQRLGEPDEVAALVAFLVSDAASYVTGQVIPVDGGF 248
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-177 7.30e-16

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 72.89  E-value: 7.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSD----------------------LVSLAKEVSQMVAR- 57
Cdd:PRK06463   1 YSMRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENeakelrekgvftikcdvgnrdqVKKSKEVVEKEFGRv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 DMI--NRGV----------------------------------------PGSIVNVSSMVAHVTFPNLIT-YSSTKGAMT 94
Cdd:PRK06463  81 DVLvnNAGImylmpfeefdeekynkmikinlngaiyttyeflpllklskNGAIVNIASNAGIGTAAEGTTfYAITKAGII 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  95 MLTKAMAMELGPHKIRVNSVNPTVVLTDM---GKkvsaDPEFARKLKE----RHPLRKFAEVEDVVNSILFLLSDRSAST 167
Cdd:PRK06463 161 ILTRRLAFELGKYGIRVNAVAPGWVETDMtlsGK----SQEEAEKLRElfrnKTVLKTTGKPEDIANIVLFLASDDARYI 236
                        250
                 ....*....|
gi 568971391 168 SGGGILVDAG 177
Cdd:PRK06463 237 TGQVIVADGG 246
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
51-177 1.11e-15

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: 72.19  E-value: 1.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSAD 130
Cdd:cd08936  126 MTKAVVPEMEKRG-GGSVVIVSSVAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMD 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568971391 131 PEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd08936  205 KAVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASYITGETVVVGGG 251
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
10-147 1.15e-15

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: 72.26  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLA----------------------------------------- 48
Cdd:cd05374    3 VLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGellndnlevleldvtdeesikaavkevierfgridvlvnna 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  49 -------------KEVSQM--------------VARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMA 101
Cdd:cd05374   83 gyglfgpleetsiEEVRELfevnvfgplrvtraFLPLMRKQG-SGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESLR 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568971391 102 MELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFA 147
Cdd:cd05374  162 LELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPEISPYAPERKEI 207
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
52-180 1.23e-15

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 72.63  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 SQMVARDMINRGVpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADP 131
Cdd:PRK08277 141 TQVFAKDMVGRKG-GNIINISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALLFNE 219
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568971391 132 -----EFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGIL-VDAGYLA 180
Cdd:PRK08277 220 dgsltERANKILAHTPMGRFGKPEELLGTLLWLADEKASSFVTGVVLpVDGGFSA 274
PRK07774 PRK07774
SDR family oxidoreductase;
51-177 1.45e-15

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 72.08  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGvPGSIVNVSSMVAhvtFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSAD 130
Cdd:PRK07774 124 CTRAVYKHMAKRG-GGAIVNQSSTAA---WLYSNFYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPK 199
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568971391 131 pEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK07774 200 -EFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWITGQIFNVDGG 245
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
51-180 1.85e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 72.02  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNP-------TVVLTDM 123
Cdd:PRK07097 125 VSKAVIPSMIKKG-HGKIINICSMMSELGRETVSAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPgyiatpqTAPLREL 203
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568971391 124 GKKVSADPeFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLA 180
Cdd:PRK07097 204 QADGSRHP-FDQFIIAKTPAARWGDPEDLAGPAVFLASDASNFVNGHILYVDGGILA 259
PRK06484 PRK06484
short chain dehydrogenase; Validated
51-180 1.97e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 72.96  E-value: 1.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMgkkvSAD 130
Cdd:PRK06484 119 VAREALRLMIEQGHGAAIVNVASGAGLVALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQM----VAE 194
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568971391 131 PEFARKL-----KERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLA 180
Cdd:PRK06484 195 LERAGKLdpsavRSRIPLGRLGRPEEIAEAVFFLASDQASYITGSTLVVDGGWTV 249
PRK06398 PRK06398
aldose dehydrogenase; Validated
5-180 2.37e-15

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 71.40  E-value: 2.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLR---ALVTGAGKGIGRDTVKALHASGAKVVAVTR---------------TNSDLVSLAKE---------------- 50
Cdd:PRK06398   1 DLGLKdkvAIVTGGSQGIGKAVVNRLKEEGSNVINFDIkepsyndvdyfkvdvSNKEQVIKGIDyviskygridilvnna 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 -----------------------------VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMA 101
Cdd:PRK06398  81 giesygaihaveedewdriinvnvngiflMSKYTIPYMLKQD-KGVIINIASVQSFAVTRNAAAYVTSKHAVLGLTRSIA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391 102 MELGPhKIRVNSVNPTVVLTDM-----GKKVSADPE-FARKLKE---RHPLRKFAEVEDVVNSILFLLSDRSASTSGGGI 172
Cdd:PRK06398 160 VDYAP-TIRCVAVCPGSIRTPLlewaaELEVGKDPEhVERKIREwgeMHPMKRVGKPEEVAYVVAFLASDLASFITGECV 238

                 ....*...
gi 568971391 173 LVDAGYLA 180
Cdd:PRK06398 239 TVDGGLRA 246
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
50-177 2.43e-15

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: 71.07  E-value: 2.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  50 EVSQMVARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHkIRVNSVNPTVVLTDMGKKVSA 129
Cdd:cd09761  112 ELSRYCRDELIKNK--GRIINIASTRAFQSEPDSEAYAASKGGLVALTHALAMSLGPD-IRVNCISPGWINTTEQQEFTA 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568971391 130 DPeFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd09761  189 AP-LTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIVDGG 235
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
10-177 4.43e-15

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: 70.50  E-value: 4.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVA---------------------------VTRTNS---------------DLV-- 45
Cdd:cd08943    4 ALVTGGASGIGLAIAKRLAAEGAAVVVadidpeiaekvaeaaqggpralgvqcdVTSEAQvqsafeqavlefgglDIVvs 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  46 --SLAKE------------------------VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKA 99
Cdd:cd08943   84 naGIATSspiaetsledwnrsmdinltghflVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLARC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391 100 MAMELGPHKIRVNSVNPTVVL-----TDMGKKVS---ADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGG 171
Cdd:cd08943  164 LALEGGEDGIRVNTVNPDAVFrgskiWEGVWRAArakAYGLLEEEYRTRNLLKREVLPEDVAEAVVAMASEDFGKTTGAI 243

                 ....*.
gi 568971391 172 ILVDAG 177
Cdd:cd08943  244 VTVDGG 249
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
53-177 4.46e-15

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 70.76  E-value: 4.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  53 QMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSA--D 130
Cdd:PRK12745 127 RMLAQPEPEELPHRSIVFVSSVNAIMVSPNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAkyD 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568971391 131 PEFARKLKerhPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK12745 207 ALIAKGLV---PMPRWGEPEDVARAVAALASGDLPYSTGQAIHVDGG 250
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
44-178 6.42e-15

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 70.30  E-value: 6.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  44 LVSLAKEvsqmvARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVN--SVNPTvvlt 121
Cdd:cd05372  119 LVSLAKA-----ALPIMNPG--GSIVTLSYLGSERVVPGYNVMGVAKAALESSVRYLAYELGRKGIRVNaiSAGPI---- 187
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391 122 dMGKKVSADPEFARKLK---ERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:cd05372  188 -KTLAASGITGFDKMLEyseQRAPLGRNVTAEEVGNTAAFLLSDLSSGITGEIIYVDGGY 246
PRK08589 PRK08589
SDR family oxidoreductase;
51-180 6.50e-15

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 70.58  E-value: 6.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVS-- 128
Cdd:PRK08589 121 MTKMLLPLMMEQG--GSIINTSSFSGQAADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTgt 198
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568971391 129 ADPEFARKLKERH----PLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLA 180
Cdd:PRK08589 199 SEDEAGKTFRENQkwmtPLGRLGKPEEVAKLVVFLASDDSSFITGETIRIDGGVMA 254
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
4-178 7.19e-15

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: 70.18  E-value: 7.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKgIGRDTVKALHASGAKVVAVTRTNSDLVSLakeVSQMVARDMINRGvPGSIVNVSSMVAHVTFPNL 83
Cdd:cd05326   76 RFGRLDIMFNNAGV-LGAPCYSILETSLEEFERVLDVNVYGAFL---GTKHAARVMIPAK-KGSIVSVASVAGVVGGLGP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  84 ITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM-----GKKVSADPEFARKLKErhPLRKFAEVEDVVNSILF 158
Cdd:cd05326  151 HAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLltagfGVEDEAIEEAVRGAAN--LKGTALRPEDIAAAVLY 228
                        170       180
                 ....*....|....*....|
gi 568971391 159 LLSDRSASTSGGGILVDAGY 178
Cdd:cd05326  229 LASDDSRYVSGQNLVVDGGL 248
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
59-177 1.02e-14

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: 69.44  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 MINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLK 138
Cdd:cd08944  124 MIARG-GGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPG 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568971391 139 ERHPLR-----KFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd08944  203 GFHLLIhqlqgRLGRPEDVAAAVVFLLSDDASFITGQVLCVDGG 246
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
59-177 1.28e-14

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 69.37  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 MINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLK 138
Cdd:PRK08936 131 FVEHDIKGNIINMSSVHEQIPWPLFVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRADVE 210
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568971391 139 ERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK08936 211 SMIPMGYIGKPEEIAAVAAWLASSEASYVTGITLFADGG 249
PRK06949 PRK06949
SDR family oxidoreductase;
3-178 1.57e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 69.41  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   3 LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTR------------------------------------------- 39
Cdd:PRK06949   5 INLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRrverlkelraeieaeggaahvvsldvtdyqsikaavahaetea 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  40 -------------TNSDLVSLAKE---------------VSQMVARDMINRGV-------PGSIVNVSSMVAHVTFPNLI 84
Cdd:PRK06949  85 gtidilvnnsgvsTTQKLVDVTPAdfdfvfdtntrgaffVAQEVAKRMIARAKgagntkpGGRIINIASVAGLRVLPQIG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  85 TYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKvSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRS 164
Cdd:PRK06949 165 LYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHH-HWETEQGQKLVSMLPRKRVGKPEDLDGLLLLLAADES 243
                        250
                 ....*....|....
gi 568971391 165 ASTSGGGILVDAGY 178
Cdd:PRK06949 244 QFINGAIISADDGF 257
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
52-179 3.76e-14

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: 68.26  E-value: 3.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 SQMVARDMINR-----GVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMgkK 126
Cdd:cd05337  120 TQAVARRMVEQpdrfdGPHRSIIFVTSINAYLVSPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDM--T 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568971391 127 VSADPEFARKLKE-RHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYL 179
Cdd:cd05337  198 APVKEKYDELIAAgLVPIRRWGQPEDIAKAVRTLASGLLPYSTGQPINIDGGLS 251
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
1-167 3.93e-14

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: 68.33  E-value: 3.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE---------------------VSQMVA--- 56
Cdd:cd08933    3 SGLRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESElnragpgsckfvpcdvtkeedIKTLISvtv 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 ------------------------------RDMIN-----------------RGVPGSIVNVSSMVAHVTFPNLITYSST 89
Cdd:cd08933   83 erfgridclvnnagwhpphqttdetsaqefRDLLNlnlisyflaskyalphlRKSQGNIINLSSLVGSIGQKQAAPYVAT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  90 KGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSA---DPEFA-RKLKERHPLRKFAEVEDVVNSILFLLSDRSA 165
Cdd:cd08933  163 KGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAqtpDTLATiKEGELAQLLGRMGTEAESGLAALFLAAEATF 242

                 ..
gi 568971391 166 ST 167
Cdd:cd08933  243 CT 244
PRK05717 PRK05717
SDR family oxidoreductase;
62-177 5.63e-14

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 67.61  E-value: 5.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  62 RGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPhKIRVNSVNPTVVLTDMGKKVSADPEFARKlKERH 141
Cdd:PRK05717 133 RAHNGAIVNLASTRARQSEPDTEAYAASKGGLLALTHALAISLGP-EIRVNAVSPGWIDARDPSQRRAEPLSEAD-HAQH 210
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568971391 142 PLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK05717 211 PAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFVVDGG 246
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
10-177 6.82e-14

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: 67.30  E-value: 6.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTN-------------------------SDLVSLAKEV------------- 51
Cdd:cd05357    3 ALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSeaeaqrlkdelnalrnsavlvqadlSDFAACADLVaaafrafgrcdvl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 ----------------------------------SQMVARdMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLT 97
Cdd:cd05357   83 vnnasafyptplgqgsedawaelfginlkapyllIQAFAR-RLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  98 KAMAMELGPhKIRVNSVNPTVVLtdmgKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRsaSTSGGGILVDAG 177
Cdd:cd05357  162 RSAALELAP-NIRVNGIAPGLIL----LPEDMDAEYRENALRKVPLKRRPSAEEIADAVIFLLDSN--YITGQIIKVDGG 234
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
10-177 8.81e-14

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 67.06  E-value: 8.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKV------------------------VAVTRTNSDLVSLAKEVSQMVAR----DMI- 60
Cdd:PRK08643   5 ALVTGAGQGIGFAIAKRLVEDGFKVaivdyneetaqaaadklskdggkaIAVKADVSDRDQVFAAVRQVVDTfgdlNVVv 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  61 -NRGVP-----------------------------------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTK 98
Cdd:PRK08643  85 nNAGVApttpietiteeqfdkvyninvggviwgiqaaqeafkklghgGKIINATSQAGVVGNPELAVYSSTKFAVRGLTQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  99 AMAMELGPHKIRVNSVNPTVVLTDM--------GKKVSADPEFA-RKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSG 169
Cdd:PRK08643 165 TAARDLASEGITVNAYAPGIVKTPMmfdiahqvGENAGKPDEWGmEQFAKDITLGRLSEPEDVANCVSFLAGPDSDYITG 244

                 ....*...
gi 568971391 170 GGILVDAG 177
Cdd:PRK08643 245 QTIIVDGG 252
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
66-180 1.10e-13

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: 67.09  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKK-VSA-------DPEFARK- 136
Cdd:cd08940  133 GRIINIASVHGLVASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKqISAlaqkngvPQEQAARe 212
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568971391 137 -LKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLA 180
Cdd:cd08940  213 lLLEKQPSKQFVTPEQLGDTAVFLASDAASQITGTAVSVDGGWTA 257
PRK12747 PRK12747
short chain dehydrogenase; Provisional
68-177 1.24e-13

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 66.64  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  68 IVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFA 147
Cdd:PRK12747 140 IINISSAATRISLPDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYATTISAFNRLG 219
                         90       100       110
                 ....*....|....*....|....*....|
gi 568971391 148 EVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK12747 220 EVEDIADTAAFLASPDSRWVTGQLIDVSGG 249
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
44-178 2.56e-13

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 65.91  E-value: 2.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  44 LVSLAKEvsqmvARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM 123
Cdd:PRK08594 126 LTAVARE-----AKKLMTEG--GSIVTLTYLGGERVVQNYNVMGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTLS 198
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568971391 124 GKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK08594 199 AKGVGGFNSILKEIEERAPLRRTTTQEEVGDTAAFLFSDLSRGVTGENIHVDSGY 253
PRK07576 PRK07576
short chain dehydrogenase; Provisional
66-177 3.26e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 65.75  E-value: 3.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNP-TVVLTDMGKKVSADPEFARKLKERHPLR 144
Cdd:PRK07576 137 ASIIQISAPQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPgPIAGTEGMARLAPSPELQAAVAQSVPLK 216
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568971391 145 KFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK07576 217 RNGTKQDIANAALFLASDMASYITGVVLPVDGG 249
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
10-180 3.94e-13

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 65.29  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVV-------AVTRTNSDL-------------VSLAKEVSQMVA------------- 56
Cdd:PRK12429   7 ALVTGAASGIGLEIALALAKEGAKVViadlndeAAAAAAEALqkaggkaigvamdVTDEEAINAGIDyavetfggvdilv 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 -------------------RDMIN-----------RGVP-------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKA 99
Cdd:PRK12429  87 nnagiqhvapiedfptekwKKMIAimldgaflttkAALPimkaqggGRIINMASVHGLVGSAGKAAYVSAKHGLIGLTKV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391 100 MAMELGPHKIRVNSVNPTVVLT--------DMGKKVSADPEFARK--LKERHPLRKFAEVEDVVNSILFLLSDRSASTSG 169
Cdd:PRK12429 167 VALEGATHGVTVNAICPGYVDTplvrkqipDLAKERGISEEEVLEdvLLPLVPQKRFTTVEEIADYALFLASFAAKGVTG 246
                        250
                 ....*....|.
gi 568971391 170 GGILVDAGYLA 180
Cdd:PRK12429 247 QAWVVDGGWTA 257
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
66-174 7.60e-13

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: 64.62  E-value: 7.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM------GKKVsadPEFARKLke 139
Cdd:cd05355  156 SSIINTTSVTAYKGSPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLipssfpEEKV---SEFGSQV-- 230
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568971391 140 rhPLRKFAEVEDVVNSILFLLSDRSASTSG------GGILV 174
Cdd:cd05355  231 --PMGRAGQPAEVAPAYVFLASQDSSYVTGqvlhvnGGEII 269
PRK06701 PRK06701
short chain dehydrogenase; Provisional
65-181 8.79e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 64.67  E-value: 8.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  65 PGS-IVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMgKKVSADPEFARKLKERHPL 143
Cdd:PRK06701 173 QGSaIINTGSITGYEGNETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPL-IPSDFDEEKVSQFGSNTPM 251
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568971391 144 RKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS 181
Cdd:PRK06701 252 QRPGQPEELAPAYVFLASPDSSYITGQMLHVNGGVIVN 289
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
51-177 9.94e-13

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 64.44  E-value: 9.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGvPGSIVNVSS----MVAHvtfPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKK 126
Cdd:PRK08226 120 VTKAVLPEMIARK-DGRIVMMSSvtgdMVAD---PGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAES 195
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568971391 127 VSA-----DPEFA-RKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK08226 196 IARqsnpeDPESVlTEMAKAIPLRRLADPLEVGELAAFLASDESSYLTGTQNVIDGG 252
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
7-177 1.04e-12

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 64.21  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE---------------------VSQMVAR----DMI- 60
Cdd:PRK06200   6 GQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRfgdhvlvvegdvtsyadnqraVDQTVDAfgklDCFv 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  61 -NRGV-----------PGSI---------VNV------------------SSMVAHVT----FPNL--ITYSSTKGAMTM 95
Cdd:PRK06200  86 gNAGIwdyntslvdipAETLdtafdeifnVNVkgyllgakaalpalkasgGSMIFTLSnssfYPGGggPLYTASKHAVVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  96 LTKAMAMELGPHkIRVNSVNPTVVLTDM---------GKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDR-SA 165
Cdd:PRK06200 166 LVRQLAYELAPK-IRVNGVAPGGTVTDLrgpaslgqgETSISDSPGLADMIAAITPLQFAPQPEDHTGPYVLLASRRnSR 244
                        250
                 ....*....|..
gi 568971391 166 STSGGGILVDAG 177
Cdd:PRK06200 245 ALTGVVINADGG 256
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-177 1.07e-12

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 64.28  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLnfSGLRALVTGAGKGIGRDTVKALHASGAKVVA-------------------------VTRTNS------------- 42
Cdd:PRK07067   2 MRL--QGKVALLTGAASGIGEAVAERYLAEGARVVIadikpararlaaleigpaaiavsldVTRQDSidrivaaaverfg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  43 ------------DLVSLAKE------------------VSQMVARDMINRGVPGSIVNVSS--------MVAHvtfpnli 84
Cdd:PRK07067  80 gidilfnnaalfDMAPILDIsrdsydrlfavnvkglffLMQAVARHMVEQGRGGKIINMASqagrrgeaLVSH------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  85 tYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVsaDPEFA-----------RKLKERHPLRKFAEVEDVV 153
Cdd:PRK07067 153 -YCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQV--DALFAryenrppgekkRLVGEAVPLGRMGVPDDLT 229
                        250       260
                 ....*....|....*....|....
gi 568971391 154 NSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK07067 230 GMALFLASADADYIVAQTYNVDGG 253
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
1-169 1.23e-12

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 64.20  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRtnSDLVS-LAKEVSQMVAR---------------------- 57
Cdd:PRK12823   2 MNQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDR--SELVHeVAAELRAAGGEalaltadletyagaqaamaaav 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 --------------------------------------------------DMINRGvPGSIVNVSSMVAHVTfpNLITYS 87
Cdd:PRK12823  80 eafgridvlinnvggtiwakpfeeyeeeqieaeirrslfptlwccravlpHMLAQG-GGAIVNVSSIATRGI--NRVPYS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  88 STKGAMTMLTKAMAMELGPHKIRVNSVNP--TVVLTDMGKKVSADP---------EFARKLKERHPLRKFAEVEDVVNSI 156
Cdd:PRK12823 157 AAKGGVNALTASLAFEYAEHGIRVNAVAPggTEAPPRRVPRNAAPQseqekawyqQIVDQTLDSSLMKRYGTIDEQVAAI 236
                        250
                 ....*....|...
gi 568971391 157 LFLLSDRSASTSG 169
Cdd:PRK12823 237 LFLASDEASYITG 249
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
5-179 1.61e-12

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: 63.70  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRtnSDLV-SLAKEVSQMVAR-------------------------- 57
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDR--SELVhEVLAEILAAGDAahvhtadletyagaqgvvraaverfg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 ----------------------------------------------DMINRGvPGSIVNVSSMVahVTFPNLITYSSTKG 91
Cdd:cd08937   80 rvdvlinnvggtiwakpyehyeeeqieaeirrslfptlwccravlpHMLERQ-QGVIVNVSSIA--TRGIYRIPYSAAKG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  92 AMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKV-------SADPEFARKL----KERHPLRKFAEVEDVVNSILFLL 160
Cdd:cd08937  157 GVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPrnaapmsEQEKVWYQRIvdqtLDSSLMGRYGTIDEQVRAILFLA 236
                        250
                 ....*....|....*....
gi 568971391 161 SDRSASTSGGGILVDAGYL 179
Cdd:cd08937  237 SDEASYITGTVLPVGGGDL 255
PLN02253 PLN02253
xanthoxin dehydrogenase
56-181 1.66e-12

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 64.07  E-value: 1.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  56 ARDMI--NRGVPGSIVNVSSMVAHVTfPNliTYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGkkVSADPEF 133
Cdd:PLN02253 139 ARIMIplKKGSIVSLCSVASAIGGLG-PH--AYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALA--LAHLPED 213
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568971391 134 ARKLKERHPLRKFA-----------EVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS 181
Cdd:PLN02253 214 ERTEDALAGFRAFAgknanlkgvelTVDDVANAVLFLASDEARYISGLNLMIDGGFTCT 272
PRK07062 PRK07062
SDR family oxidoreductase;
56-178 1.77e-12

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 63.52  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  56 ARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVnpTVVLTDMGK-----KVSAD 130
Cdd:PRK07062 129 FLPLLRASAAASIVCVNSLLALQPEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSI--LLGLVESGQwrrryEARAD 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568971391 131 P---------EFARKlkeRH-PLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK07062 207 PgqsweawtaALARK---KGiPLGRLGRPDEAARALFFLASPLSSYTTGSHIDVSGGF 261
PRK06125 PRK06125
short chain dehydrogenase; Provisional
1-177 1.93e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 63.52  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEV----------------------------- 51
Cdd:PRK06125   1 MDLHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLraahgvdvavhaldlsspeareqlaaeag 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 ---------------------------------------SQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGA 92
Cdd:PRK06125  81 didilvnnagaipggglddvddaawragwelkvfgyidlTRLAYPRMKARG-SGVIVNVIGAAGENPDADYICGSAGNAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  93 MTMLTKAMAMELGPHKIRVNSVNPTVVLTDM--------GKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRS 164
Cdd:PRK06125 160 LMAFTRALGGKSLDDGVRVVGVNPGPVATDRmltllkgrARAELGDESRWQELLAGLPLGRPATPEEVADLVAFLASPRS 239
                        250
                 ....*....|...
gi 568971391 165 ASTSGGGILVDAG 177
Cdd:PRK06125 240 GYTSGTVVTVDGG 252
PRK09186 PRK09186
flagellin modification protein A; Provisional
51-178 1.96e-12

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 63.47  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGVpGSIVNVSSmVAHVTFPNLITYSSTkgAMTM-------------LTKAMAMELGPHKIRVNSVNPT 117
Cdd:PRK09186 124 FSQQFAKYFKKQGG-GNLVNISS-IYGVVAPKFEIYEGT--SMTSpveyaaikagiihLTKYLAKYFKDSNIRVNCVSPG 199
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971391 118 VVLTdmgkkvSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK09186 200 GILD------NQPEAFLNAYKKCCNGKGMLDPDDICGTLVFLLSDQSKYITGQNIIVDDGF 254
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-152 2.47e-12

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 62.78  E-value: 2.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQM-------------------------- 54
Cdd:PRK07666   1 MAQSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYgvkvviatadvsdyeevtaaieqlkn 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  55 -----------------------------------------VAR----DMINRGvPGSIVNVSSMVAHVTFPNLITYSST 89
Cdd:PRK07666  81 elgsidilinnagiskfgkfleldpaewekiiqvnlmgvyyATRavlpSMIERQ-SGDIINISSTAGQKGAAVTSAYSAS 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971391  90 KGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVsadpefarKLKERHPlRKFAEVEDV 152
Cdd:PRK07666 160 KFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDL--------GLTDGNP-DKVMQPEDL 213
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
10-125 2.69e-12

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 63.01  E-value: 2.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE--------------------------------------- 50
Cdd:cd05356    4 AVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEieekygvetktiaadfsagddiyeriekelegldigilv 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 ---------------VSQMVARDMINRGV-----------P-------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLT 97
Cdd:cd05356   84 nnvgishsipeyfleTPEDELQDIINVNVmatlkmtrlilPgmvkrkkGAIVNISSFAGLIPTPLLATYSASKAFLDFFS 163
                        170       180
                 ....*....|....*....|....*...
gi 568971391  98 KAMAMELGPHKIRVNSVNPTVVLTDMGK 125
Cdd:cd05356  164 RALYEEYKSQGIDVQSLLPYLVATKMSK 191
PRK06057 PRK06057
short chain dehydrogenase; Provisional
5-177 3.10e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 62.83  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQMVAR--------------------------- 57
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLFVPtdvtdedavnalfdtaaetygsvdiaf 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 ----------DMI-NRGVP-----------------------------GSIVNVSSMVAHV-TFPNLITYSSTKGAMTML 96
Cdd:PRK06057  85 nnagisppedDSIlNTGLDawqrvqdvnltsvylcckaalphmvrqgkGSIINTASFVAVMgSATSQISYTASKGGVLAM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  97 TKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSA-DPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVD 175
Cdd:PRK06057 165 SRELGVQFARQGIRVNALCPGPVNTPLLQELFAkDPERAARRLVHVPMGRFAEPEEIAAAVAFLASDDASFITASTFLVD 244

                 ..
gi 568971391 176 AG 177
Cdd:PRK06057 245 GG 246
PRK07825 PRK07825
short chain dehydrogenase; Provisional
12-123 3.92e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 62.65  E-value: 3.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  12 VTGAGKGIGRDTVKALHASGAKVVA------------------------VTRTNSDLVSLAK------------------ 49
Cdd:PRK07825  10 ITGGARGIGLATARALAALGARVAIgdldealaketaaelglvvggpldVTDPASFAAFLDAveadlgpidvlvnnagvm 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  50 -----------------EV--------SQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMEL 104
Cdd:PRK07825  90 pvgpfldepdavtrrilDVnvygvilgSKLAAPRMVPRG-RGHVVNVASLAGKIPVPGMATYCASKHAVVGFTDAARLEL 168
                        170
                 ....*....|....*....
gi 568971391 105 GPHKIRVNSVNPTVVLTDM 123
Cdd:PRK07825 169 RGTGVHVSVVLPSFVNTEL 187
PRK08264 PRK08264
SDR family oxidoreductase;
4-132 4.38e-12

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 62.21  E-value: 4.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGA-KVVAVTR-------------------TNSDLVSLAKEVSQMVA------- 56
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGAaKVYAAARdpesvtdlgprvvplqldvTDPASVAAAAEAASDVTilvnnag 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 -----------------RDM-----------------INRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAM 102
Cdd:PRK08264  83 ifrtgslllegdedalrAEMetnyfgplamarafapvLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWSLTQALRA 162
                        170       180       190
                 ....*....|....*....|....*....|
gi 568971391 103 ELGPHKIRVNSVNPTVVLTDMGKKVSADPE 132
Cdd:PRK08264 163 ELAPQGTRVLGVHPGPIDTDMAAGLDAPKA 192
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
48-177 4.95e-12

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 62.48  E-value: 4.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  48 AKEVSQMvardMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVL-TDMGKk 126
Cdd:cd05322  119 AREFSKL----MIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLGNLLkSPMFQ- 193
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971391 127 vSADPEFARKL-----------KERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd05322  194 -SLLPQYAKKLgikeseveqyyIDKVPLKRGCDYQDVLNMLLFYASPKASYCTGQSINITGG 254
PRK08416 PRK08416
enoyl-ACP reductase;
52-177 5.74e-12

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 62.10  E-value: 5.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 SQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADP 131
Cdd:PRK08416 132 AQEAAKRMEKVG-GGSIISLSSTGNLVYIENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNYE 210
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568971391 132 EFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK08416 211 EVKAKTEELSPLNRMGQPEDLAGACLFLCSEKASWLTGQTIVVDGG 256
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
5-161 8.02e-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: 61.76  E-value: 8.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEV------------------SQMVA---------- 56
Cdd:cd05343    4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECqsagyptlfpyqcdlsneEQILSmfsairtqhq 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 -------------------------RDMIN-------------------RGVP-GSIVNVSSMVAHVTFPNLIT--YSST 89
Cdd:cd05343   84 gvdvcinnaglarpepllsgktegwKEMFDvnvlalsictreayqsmkeRNVDdGHIININSMSGHRVPPVSVFhfYAAT 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568971391  90 KGAMTMLTKAMAMELGPHK--IRVNSVNPTVVLTDMGKKVS-ADPEFARKLKERHPLRKfaeVEDVVNSILFLLS 161
Cdd:cd05343  164 KHAVTALTEGLRQELREAKthIRATSISPGLVETEFAFKLHdNDPEKAAATYESIPCLK---PEDVANAVLYVLS 235
PRK12937 PRK12937
short chain dehydrogenase; Provisional
55-178 1.07e-11

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 61.30  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  55 VARDMINR-GVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM---GKkvsaD 130
Cdd:PRK12937 121 VLREAARHlGQGGRIINLSTSVIALPLPGYGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATELffnGK----S 196
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568971391 131 PEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK12937 197 AEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQVLRVNGGF 244
PRK05855 PRK05855
SDR family oxidoreductase;
5-122 1.15e-11

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 62.31  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRtnsDLVS------------------------------LAKEV--- 51
Cdd:PRK05855 313 FSGKLVVVTGAGSGIGRETALAFAREGAEVVASDI---DEAAaertaeliraagavahayrvdvsdadameaFAEWVrae 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 -----------------------------------------SQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTK 90
Cdd:PRK05855 390 hgvpdivvnnagigmaggfldtsaedwdrvldvnlwgvihgCRLFGRQMVERGTGGHIVNVASAAAYAPSRSLPAYATSK 469
                        170       180       190
                 ....*....|....*....|....*....|..
gi 568971391  91 GAMTMLTKAMAMELGPHKIRVNSVNPTVVLTD 122
Cdd:PRK05855 470 AAVLMLSECLRAELAAAGIGVTAICPGFVDTN 501
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
9-181 1.38e-11

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: 60.97  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   9 RALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLV-------SLAKEVSQMVARDMI-------NRGVPG-------- 66
Cdd:cd05328    1 TIVITGAASGIGAATAELLEDAGHTVIGIDLREADVIadlstpeGRAAAIADVLARCSGvldglvnCAGVGGttvaglvl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  67 ------------------------SIVNVSSMVA---------------------------HVTFPNLITYSSTKGAMTM 95
Cdd:cd05328   81 kvnyfglralmeallprlrkghgpAAVVVSSIAGagwaqdklelakalaagtearavalaeHAGQPGYLAYAGSKEALTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  96 LTKAMAME-LGPHKIRVNSVNPTVVLTDMGKKVSADPEF-ARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGIL 173
Cdd:cd05328  161 WTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRGgESVDAFVTPMGRRAEPDEIAPVIAFLASDAASWINGANLF 240

                 ....*...
gi 568971391 174 VDAGYLAS 181
Cdd:cd05328  241 VDGGLDAS 248
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
44-178 1.41e-11

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 61.27  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  44 LVSLAKEvsqmvARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM 123
Cdd:PRK07370 126 LAPLCKA-----AKPLMSEG--GSIVTLTYLGGVRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLA 198
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568971391 124 GKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK07370 199 SSAVGGILDMIHHVEEKAPLRRTVTQTEVGNTAAFLLSDLASGITGQTIYVDAGY 253
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-179 1.73e-11

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 60.36  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRT----------------NSDLVSLAKEVSQM------------- 54
Cdd:PRK06550   2 EFMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQdkpdlsgnfhflqldlSDDLEPLFDWVPSVdilcntagilddy 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  55 ----------------------------VARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGP 106
Cdd:PRK06550  82 kplldtsleewqhifdtnltstflltraYLPQMLERK-SGIIINMCSIASFVAGGGGAAYTASKHALAGFTKQLALDYAK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971391 107 HKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYL 179
Cdd:PRK06550 161 DGIQVFGIAPGAVKTPMTAADFEPGGLADWVARETPIKRWAEPEEVAELTLFLASGKADYMQGTIVPIDGGWT 233
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
10-126 1.85e-11

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: 60.33  E-value: 1.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEV-------------------SQMVARDMI---------- 60
Cdd:cd05324    3 ALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKlraeglsvrfhqldvtddaSIEAAADFVeekyggldil 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  61 --NRGV----------------------------------P-------GSIVNVSSMVAHVTFPnlitYSSTKGAMTMLT 97
Cdd:cd05324   83 vnNAGIafkgfddstptreqaretmktnffgtvdvtqallPllkkspaGRIVNVSSGLGSLTSA----YGVSKAALNALT 158
                        170       180
                 ....*....|....*....|....*....
gi 568971391  98 KAMAMELGPHKIRVNSVNPTVVLTDMGKK 126
Cdd:cd05324  159 RILAKELKETGIKVNACCPGWVKTDMGGG 187
PRK09291 PRK09291
SDR family oxidoreductase;
50-121 3.29e-11

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 60.01  E-value: 3.29e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971391  50 EVSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLT 121
Cdd:PRK09291 110 ELTQGFVRKMVARG-KGKVVFTSSMAGLITGPFTGAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
66-178 3.74e-11

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 59.70  E-value: 3.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVvlTDMGkkvSADPEFARKLKERHPLRK 145
Cdd:PRK12748 147 GRIINLTSGQSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGP--TDTG---WITEELKHHLVPKFPQGR 221
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568971391 146 FAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK12748 222 VGEPVDAARLIAFLVSEEAKWITGQVIHSEGGF 254
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
48-177 4.66e-11

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 59.66  E-value: 4.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  48 AKEVSqmvaRDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVL-TDMGKk 126
Cdd:PRK12384 120 AREFS----RLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLGNLLkSPMFQ- 194
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971391 127 vSADPEFARKL-------KERH----PLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK12384 195 -SLLPQYAKKLgikpdevEQYYidkvPLKRGCDYQDVLNMLLFYASPKASYCTGQSINVTGG 255
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
59-178 4.67e-11

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 59.80  E-value: 4.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 MINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVvlTDMGkkvSADPEFARKLK 138
Cdd:PRK12859 141 GFDKKSGGRIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGP--TDTG---WMTEEIKQGLL 215
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568971391 139 ERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK12859 216 PMFPFGRIGEPKDAARLIKFLASEEAEWITGQIIHSEGGF 255
PRK07831 PRK07831
SDR family oxidoreductase;
57-169 4.68e-11

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 59.66  E-value: 4.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 RDMINRGVPGSIVNVSSMV--------AHvtfpnlitYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVS 128
Cdd:PRK07831 141 RYMRARGHGGVIVNNASVLgwraqhgqAH--------YAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKVT 212
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568971391 129 ADpEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSG 169
Cdd:PRK07831 213 SA-ELLDELAAREAFGRAAEPWEVANVIAFLASDYSSYLTG 252
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
18-177 4.79e-11

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 59.64  E-value: 4.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  18 GIGRDTV--KALHASGAKVVavtrtNSDLVSLAKeVSQMVARDMINRGVpGSIVNVSSMVAHVTFPNLITYSSTKGAMTM 95
Cdd:PRK12938  90 GITRDVVfrKMTREDWTAVI-----DTNLTSLFN-VTKQVIDGMVERGW-GRIINISSVNGQKGQFGQTNYSTAKAGIHG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  96 LTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSadPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVD 175
Cdd:PRK12938 163 FTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIR--PDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGADFSLN 240

                 ..
gi 568971391 176 AG 177
Cdd:PRK12938 241 GG 242
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
62-178 6.43e-11

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: 59.17  E-value: 6.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   62 RGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVL--TDMGKKVSADpeFARKLke 139
Cdd:TIGR02685 149 RSTNLSIVNLCDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLlpDAMPFEVQED--YRRKV-- 224
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568971391  140 rhPL-RKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:TIGR02685 225 --PLgQREASAEQIADVVIFLVSPKAKYITGTCIKVDGGL 262
PRK12746 PRK12746
SDR family oxidoreductase;
66-178 1.19e-10

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 58.51  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRK 145
Cdd:PRK12746 140 GRVINISSAEVRLGFTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRNFATNSSVFGR 219
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568971391 146 FAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK12746 220 IGQVEDIADAVAFLASSDSRWVTGQIIDVSGGF 252
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
10-177 1.53e-10

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: 58.08  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNS---------------------------DLVSLAKEVSQMVAR-DM-- 59
Cdd:cd05323    3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENpgaaaelqainpkvkatfvqcdvtsweQLAAAFKKAIEKFGRvDIli 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  60 --------------------------IN-------------------RGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMT 94
Cdd:cd05323   83 nnagildeksylfagklpppwektidVNltgvinttylalhymdknkGGKGGVIVNIGSVAGLYPAPQFPVYSASKHGVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  95 MLTKAMAMELgPHK--IRVNSVNPTVVLTDMgkkvsaDPEFARKLKERHPLRKFAEVEDVVNSILFLLSDrsASTSGGGI 172
Cdd:cd05323  163 GFTRSLADLL-EYKtgVRVNAICPGFTNTPL------LPDLVAKEAEMLPSAPTQSPEVVAKAIVYLIED--DEKNGAIW 233

                 ....*
gi 568971391 173 LVDAG 177
Cdd:cd05323  234 IVDGG 238
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
11-160 3.16e-10

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 57.30  E-value: 3.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  11 LVTGAGKGIGRDTVKALHASG--AKVVAVTRTNSDLVSLAKE-------------------VSQMVA------------- 56
Cdd:cd05367    3 ILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEElrpglrvttvkadlsdaagVEQLLEairkldgerdlli 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 ---------------------------------------RDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLT 97
Cdd:cd05367   83 nnagslgpvskiefidldelqkyfdlnltspvcltstllRAFKKRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDMFF 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568971391  98 KAMAMELgpHKIRVNSVNPTVVLTDMGKKV---SADPEFARKLKERHPLRKFAEVEDVVNSILFLL 160
Cdd:cd05367  163 RVLAAEE--PDVRVLSYAPGVVDTDMQREIretSADPETRSRFRSLKEKGELLDPEQSAEKLANLL 226
PRK07454 PRK07454
SDR family oxidoreductase;
1-121 4.54e-10

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 56.51  E-value: 4.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSgLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQM--------------------VARDMI 60
Cdd:PRK07454   1 MSLNSM-PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTgvkaaaysidlsnpeaiapgIAELLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  61 NRGVP--------------------------------------------------GSIVNVSSMVAHVTFPNLITYSSTK 90
Cdd:PRK07454  80 QFGCPdvlinnagmaytgpllemplsdwqwviqlnltsvfqccsavlpgmrarggGLIINVSSIAARNAFPQWGAYCVSK 159
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568971391  91 GAMTMLTKAMAMELGPHKIRVNSVNPTVVLT 121
Cdd:PRK07454 160 AALAAFTKCLAEEERSHGIRVCTITLGAVNT 190
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
66-177 4.71e-10

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: 56.76  E-value: 4.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM--GKKVSADPEFARKLKER--- 140
Cdd:cd05330  135 GMIVNTASVGGIRGVGNQSGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMveGSLKQLGPENPEEAGEEfvs 214
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568971391 141 -HPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd05330  215 vNPMKRFGEPEEVAAVVAFLLSDDAGYVNAAVVPIDGG 252
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
10-177 5.62e-10

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: 56.59  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE---------------------VSQMVAR----------- 57
Cdd:cd05348    7 ALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADfgdavvgvegdvrsladneraVARCVERfgkldcfigna 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 ----------------------DMINRGVPGSIVNVS-----------SMVAHVT----FPNL--ITYSSTKGAMTMLTK 98
Cdd:cd05348   87 giwdystslvdipeekldeafdELFHINVKGYILGAKaalpalyategSVIFTVSnagfYPGGggPLYTASKHAVVGLVK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  99 AMAMELGPHkIRVNSVNPTVVLTD--------MGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGG 170
Cdd:cd05348  167 QLAYELAPH-IRVNGVAPGGMVTDlrgpaslgQGETSISTPPLDDMLKSILPLGFAPEPEDYTGAYVFLASRGDNRPATG 245

                 ....*...
gi 568971391 171 GIL-VDAG 177
Cdd:cd05348  246 TVInYDGG 253
PRK07677 PRK07677
short chain dehydrogenase; Provisional
51-177 5.67e-10

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 56.61  E-value: 5.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELG-PHKIRVNSVNP-TVVLTDMGKKVS 128
Cdd:PRK07677 116 CSQAVGKYWIEKGIKGNIINMVATYAWDAGPGVIHSAAAKAGVLAMTRTLAVEWGrKYGIRVNAIAPgPIERTGGADKLW 195
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568971391 129 ADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK07677 196 ESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYINGTCITMDGG 244
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
1-180 6.43e-10

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 56.44  E-value: 6.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQ-----------MVARDMINRGVP---- 65
Cdd:PRK13394   1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKaggkaigvamdVTNEDAVNAGIDkvae 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 --------------------------------------------------------GSIVNVSSMVAHVTFPNLITYSST 89
Cdd:PRK13394  81 rfgsvdilvsnagiqivnpienysfadwkkmqaihvdgaflttkaalkhmykddrgGVVIYMGSVHSHEASPLKSAYVTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  90 KGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKK----------VSADPEFARKLKERHPLRKFAEVEDVVNSILFL 159
Cdd:PRK13394 161 KHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKqipeqakelgISEEEVVKKVMLGKTVDGVFTTVEDVAQTVLFL 240
                        250       260
                 ....*....|....*....|.
gi 568971391 160 LSDRSASTSGGGILVDAGYLA 180
Cdd:PRK13394 241 SSFPSAALTGQSFVVSHGWFM 261
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
51-177 6.57e-10

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 56.25  E-value: 6.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGVpGSIVNVSSMVahvtFPNLIT----YSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKK 126
Cdd:PRK08642 125 TIQAALPGMREQGF-GRIINIGTNL----FQNPVVpyhdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASA 199
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568971391 127 VSADPEFARkLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK08642 200 ATPDEVFDL-IAATTPLRKVTTPQEFADAVLFFASPWARAVTGQNLVVDGG 249
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
53-177 6.98e-10

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: 56.47  E-value: 6.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  53 QMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVsaDPE 132
Cdd:cd05363  117 QAVARAMIAQGRGGKIINMASQAGRRGEALVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGV--DAK 194
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568971391 133 FA-----------RKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd05363  195 FAryenrprgekkRLVGEAVPFGRMGRAEDLTGMAIFLASTDADYIVAQTYNVDGG 250
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
65-177 8.56e-10

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: 55.95  E-value: 8.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  65 PGSIVNVSSmVAHVTFPNL--ITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHP 142
Cdd:cd08942  137 PARVINIGS-IAGIVVSGLenYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNDPAALEAEEKSIP 215
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568971391 143 LRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:cd08942  216 LGRWGRPEDMAGLAIMLASRAGAYLTGAVIPVDGG 250
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
1-131 1.09e-09

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: 55.55  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLnfSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDL----------------VSLAKEVSQMVAR------- 57
Cdd:COG3967    1 MKL--TGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLeeaaaanpglhtivldVADPASIAALAEQvtaefpd 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 -DMI--NRGV-----------------------------------------PGS-IVNVSSMVAHVTFPNLITYSSTKGA 92
Cdd:COG3967   79 lNVLinNAGImraedlldeaedladaereittnllgpirltaaflphlkaqPEAaIVNVSSGLAFVPLAVTPTYSATKAA 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568971391  93 MTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADP 131
Cdd:COG3967  159 LHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDP 197
PRK09134 PRK09134
SDR family oxidoreductase;
9-177 1.79e-09

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 55.32  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   9 RALVTGAGKGIGR-------------------------DTVKALHASGAKVVAVtrtNSDLVSLAkEVSQMVARDMINRG 63
Cdd:PRK09134  11 AALVTGAARRIGRaialdlaahgfdvavhynrsrdeaeALAAEIRALGRRAVAL---QADLADEA-EVRALVARASAALG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  64 VPGSIVNVSS------------------MVAHVTFP--------------------NLI------------TYSSTKGAM 93
Cdd:PRK09134  87 PITLLVNNASlfeydsaasftraswdrhMATNLRAPfvlaqafaralpadarglvvNMIdqrvwnlnpdflSYTLSKAAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  94 TMLTKAMAMELGPhKIRVNSVNPTVVLTDMGKkvsADPEFARKLkERHPLRKFAEVEDVVNSILFLLSDRsaSTSGGGIL 173
Cdd:PRK09134 167 WTATRTLAQALAP-RIRVNAIGPGPTLPSGRQ---SPEDFARQH-AATPLGRGSTPEEIAAAVRYLLDAP--SVTGQMIA 239

                 ....
gi 568971391 174 VDAG 177
Cdd:PRK09134 240 VDGG 243
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
66-178 2.53e-09

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 54.56  E-value: 2.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTdmgKKVSADPEFARKL---KERHP 142
Cdd:PRK07533 142 GSLLTMSYYGAEKVVENYNLMGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKT---RAASGIDDFDALLedaAERAP 218
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568971391 143 LRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK07533 219 LRRLVDIDDVGAVAAFLASDAARRLTGNTLYIDGGY 254
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
66-178 2.94e-09

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 54.75  E-value: 2.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVN--SVNPTVVLTDMGkkvSADPEFARKLKERH-P 142
Cdd:PRK08415 137 ASVLTLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNaiSAGPIKTLAASG---IGDFRMILKWNEINaP 213
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568971391 143 LRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK08415 214 LKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVDAGY 249
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
10-132 3.01e-09

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 54.34  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGA-KVVAVTRTNSDLVSL---------------------------AKEV---------- 51
Cdd:cd05354    6 VLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLvakygdkvvplrldvtdpesikaaaaqAKDVdvvinnagvl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 ---SQMVARDM------------------------INRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMEL 104
Cdd:cd05354   86 kpaTLLEEGALealkqemdvnvfgllrlaqafapvLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSLTQGLRAEL 165
                        170       180
                 ....*....|....*....|....*...
gi 568971391 105 GPHKIRVNSVNPTVVLTDMGKKVSADPE 132
Cdd:cd05354  166 AAQGTLVLSVHPGPIDTRMAAGAGGPKE 193
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
62-149 3.23e-09

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 53.99  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  62 RGVPGS-IVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKER 140
Cdd:cd08931  123 KATPGArVINTASSSAIYGQPDLAVYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAAPKKGLGRV 202

                 ....*....
gi 568971391 141 HPLRKFAEV 149
Cdd:cd08931  203 LPVSDVAKV 211
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
3-169 3.79e-09

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 54.25  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   3 LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDL-----------VSLAKEV-------------------- 51
Cdd:PRK06171   5 LNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGqhenyqfvptdVSSAEEVnhtvaeiiekfgridglvnn 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 ----------------------------------------SQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKG 91
Cdd:PRK06171  85 aginiprllvdekdpagkyelneaafdkmfninqkgvflmSQAVARQMVKQH-DGVIVNMSSEAGLEGSEGQSCYAATKA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  92 AMTMLTKAMAMELGPHKIRVNSVNPTVV-LTDM-------------GKKVSADPEFARKlKERHPLR---KFAEVEDVVN 154
Cdd:PRK06171 164 ALNSFTRSWAKELGKHNIRVVGVAPGILeATGLrtpeyeealaytrGITVEQLRAGYTK-TSTIPLGrsgKLSEVADLVC 242
                        250
                 ....*....|....*
gi 568971391 155 silFLLSDRSASTSG 169
Cdd:PRK06171 243 ---YLLSDRASYITG 254
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
10-140 6.08e-09

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: 53.45  E-value: 6.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASG-AKVVAVTRTNS--------------------DLVSLAKEVSQMVA------------ 56
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSaatelaalgashsrlhilelDVTDEIAESAEAVAerlgdagldvli 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 --------------------------------------RDMINRGVPGSIVNVSSMVAHVTFPNL---ITYSSTKGAMTM 95
Cdd:cd05325   81 nnagilhsygpasevdsedllevfqvnvlgpllltqafLPLLLKGARAKIINISSRVGSIGDNTSggwYSYRASKAALNM 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568971391  96 LTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSA-----DPEF-ARKLKER 140
Cdd:cd05325  161 LTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKnkgpiTPEEsVAGLLKV 211
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
46-178 6.15e-09

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 53.67  E-value: 6.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  46 SLAKEVSQMVARDminrgvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVN--SVNPTVVLTDM 123
Cdd:PRK06997 126 ALAKAALPMLSDD-------ASLLTLSYLGAERVVPNYNTMGLAKASLEASVRYLAVSLGPKGIRANgiSAGPIKTLAAS 198
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568971391 124 GKKvsadpEFARKLK---ERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK06997 199 GIK-----DFGKILDfveSNAPLRRNVTIEEVGNVAAFLLSDLASGVTGEITHVDSGF 251
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
50-178 6.48e-09

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 53.60  E-value: 6.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  50 EVSQMVARDMINrgvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVsA 129
Cdd:PRK06505 126 EIAKRAAKLMPD---GGSMLTLTYGGSTRVMPNYNVMGVAKAALEASVRYLAADYGPQGIRVNAISAGPVRTLAGAGI-G 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568971391 130 DPEFARKLKERH-PLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK06505 202 DARAIFSYQQRNsPLRRTVTIDEVGGSALYLLSDLSSGVTGEIHFVDSGY 251
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
10-161 8.20e-09

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: 52.58  E-value: 8.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSD----------LVSLAKEV---------------------------- 51
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDyqvditdeasIKALFEKVghfdaivstagdaefaplaeltdadfqr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  52 ---SQM--------VARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELgPHKIRVNSVNPTVVL 120
Cdd:cd11731   81 glnSKLlgqinlvrHGLPYLNDG--GSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAIEL-PRGIRINAVSPGVVE 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568971391 121 TDMGKKVSADPEFARklkerhplrkfAEVEDVVNSILFLLS 161
Cdd:cd11731  158 ESLEAYGDFFPGFEP-----------VPAEDVAKAYVRSVE 187
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
56-178 8.33e-09

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 53.43  E-value: 8.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  56 ARDMInRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFAR 135
Cdd:PRK08690 131 ARPMM-RGRNSAIVALSYLGAVRAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIADFGKLLG 209
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568971391 136 KLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK08690 210 HVAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDGGY 252
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
4-161 9.17e-09

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


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 53.05  E-value: 9.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDtvKALHASGAKVVAVTRTN-SDLVSlakeVSQMVARDMINRGvPGSIVNVSSMVAHVTFPN 82
Cdd:cd05346   75 EFRDIDILVNNAGLALGLD--PAQEADLEDWETMIDTNvKGLLN----VTRLILPIMIARN-QGHIINLGSIAGRYPYAG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  83 LITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGK-KVSADPEFARKLKER-HPLRKfaevEDVVNSILFLL 160
Cdd:cd05346  148 GNVYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLvRFHGDKEKADKVYEGvEPLTP----EDIAETILWVA 223

                 .
gi 568971391 161 S 161
Cdd:cd05346  224 S 224
PRK07041 PRK07041
SDR family oxidoreductase;
66-177 1.11e-08

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 52.73  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPhkIRVNSVNPTVVLTDMGKKVSADPEFAR--KLKERHPL 143
Cdd:PRK07041 117 GSLTFVSGFAAVRPSASGVLQGAINAALEALARGLALELAP--VRVNTVSPGLVDTPLWSKLAGDAREAMfaAAAERLPA 194
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568971391 144 RKFAEVEDVVNSILFLLSdrSASTSGGGILVDAG 177
Cdd:PRK07041 195 RRVGQPEDVANAILFLAA--NGFTTGSTVLVDGG 226
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
10-145 1.51e-08

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: 52.26  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE--------------------------------------- 50
Cdd:cd08939    4 VLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEieaeanasgqkvsyisadlsdyeeveqafaqavekggpp 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 ------------------------------------VSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMT 94
Cdd:cd08939   84 dlvvncagisipglfedltaeefergmdvnyfgslnVAHAVLPLMKEQR-PGHIVFVSSQAALVGIYGYSAYCPSKFALR 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568971391  95 MLTKAMAMELGPHKIRVNSVNPTVVLTdmgkkvsadPEFARKLKERHPLRK 145
Cdd:cd08939  163 GLAESLRQELKPYNIRVSVVYPPDTDT---------PGFEEENKTKPEETK 204
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
10-169 3.06e-08

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: 51.21  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSL----------------AKEVSQMV--ARDM------------ 59
Cdd:cd08932    3 ALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALsasggdveavpydardPEDARALVdaLRDRfgridvlvhnag 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  60 --------------------INRGVP----------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAME 103
Cdd:cd08932   83 igrpttlregsdaeleahfsINVIAPaeltrallpalreagsGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHALRQE 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568971391 104 LGPHKIRVNSVNPTVVLTDMGKKVSADPEFarklkerhPLRKFAEVEDVVNSILFLLSDRSASTSG 169
Cdd:cd08932  163 GWDHGVRVSAVCPGFVDTPMAQGLTLVGAF--------PPEEMIQPKDIANLVRMVIELPENITSV 220
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
66-162 3.63e-08

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 51.54  E-value: 3.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMgkkVSADPEFAR-KLKERHPLR 144
Cdd:PRK12935 136 GRIISISSIIGQAGGFGQTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEM---VAEVPEEVRqKIVAKIPKK 212
                         90
                 ....*....|....*...
gi 568971391 145 KFAEVEDVVNSILFLLSD 162
Cdd:PRK12935 213 RFGQADEIAKGVVYLCRD 230
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
7-127 4.34e-08

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: 51.46  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTN--------------------------SDLVSLAKEVSQMVAR--- 57
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEekgeeaaaeikketgnakveviqldlSSLASVRQFAEEFLARfpr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 -DMI--NRGV--------------------------------------PGSIVNVSS---MVAHVTFPNLI--------- 84
Cdd:cd05327   81 lDILinNAGImapprrltkdgfelqfavnylghflltnlllpvlkasaPSRIVNVSSiahRAGPIDFNDLDlennkeysp 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568971391  85 --TYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKV 127
Cdd:cd05327  161 ykAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRN 205
PRK07984 PRK07984
enoyl-ACP reductase FabI;
31-178 4.70e-08

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 51.06  E-value: 4.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  31 GAKVVAVTR---------TNSDLVSLAKEvsqmvARDMINrgvPGS-IVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAM 100
Cdd:PRK07984 102 GDYVNAVTRegfkiahdiSSYSFVAMAKA-----CRSMLN---PGSaLLTLSYLGAERAIPNYNVMGLAKASLEANVRYM 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391 101 AMELGPHKIRVNSVN--PTVVLTDMGKKvsadpEFARKL---KERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVD 175
Cdd:PRK07984 174 ANAMGPEGVRVNAISagPIRTLAASGIK-----DFRKMLahcEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVD 248

                 ...
gi 568971391 176 AGY 178
Cdd:PRK07984 249 GGF 251
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
7-129 6.08e-08

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: 50.75  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAK----------------EVSQMVAR------------- 57
Cdd:cd05371    2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKlgdncrfvpvdvtsekDVKAALALakakfgrldivvn 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 ---------------------DMINR----------------------------GVPGSIVNVSSMVAHVTFPNLITYSS 88
Cdd:cd05371   82 cagiavaaktynkkgqqphslELFQRvinvnligtfnvirlaagamgknepdqgGERGVIINTASVAAFEGQIGQAAYSA 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568971391  89 TKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSA 129
Cdd:cd05371  162 SKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPE 202
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
55-160 7.53e-08

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 50.34  E-value: 7.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  55 VARDMINRGVPGSIVNVSSmVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKkvSADPEFA 134
Cdd:PRK08217 133 AAAKMIESGSKGVIINISS-IARAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTA--AMKPEAL 209
                         90       100
                 ....*....|....*....|....*.
gi 568971391 135 RKLKERHPLRKFAEVEDVVNSILFLL 160
Cdd:PRK08217 210 ERLEKMIPVGRLGEPEEIAHTVRFII 235
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
10-160 8.10e-08

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: 49.82  E-value: 8.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGA-KVVAVTRT-----------NSDLVSLAKEVSQMVARDMI--------------NRG 63
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSpKVLVVSRRdvvvhnaaildDGRLIDLTGSRIERAIRANVvgtrrlleaarelmKAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  64 VPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFarKLKERHPL 143
Cdd:cd02266   81 RLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEE--ILGNRRHG 158
                        170
                 ....*....|....*..
gi 568971391 144 RKFAEVEDVVNSILFLL 160
Cdd:cd02266  159 VRTMPPEEVARALLNAL 175
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
10-128 8.97e-08

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: 50.32  E-value: 8.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVV--------AVTRTN-------------------SDLVSLAKEVSQMV------- 55
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVildinekgAEETANnvrkaggkvhyykcdvskrEEVYEAAKKIKKEVgdvtili 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  56 -------------------------------------ARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTK 98
Cdd:cd05339   82 nnagvvsgkkllelpdeeiektfevntlahfwttkafLPDMLERN-HGHIVTIASVAGLISPAGLADYCASKAAAVGFHE 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 568971391  99 AMAMEL---GPHKIRVNSVNPTVVLTDMGKKVS 128
Cdd:cd05339  161 SLRLELkayGKPGIKTTLVCPYFINTGMFQGVK 193
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
3-177 9.16e-08

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 50.30  E-value: 9.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   3 LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQMVA--------RDMI-------------- 60
Cdd:PRK12936   2 FDLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKifpanlsdRDEVkalgqkaeadlegv 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  61 -----NRGVP----------------------------------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTM 95
Cdd:PRK12936  82 dilvnNAGITkdglfvrmsdedwdsvlevnltatfrltrelthpmmrrryGRIINITSVVGVTGNPGQANYCASKAGMIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  96 LTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEfaRKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVD 175
Cdd:PRK12936 162 FSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQK--EAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTIHVN 239

                 ..
gi 568971391 176 AG 177
Cdd:PRK12936 240 GG 241
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
7-158 1.01e-07

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: 50.23  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVS---------------QMVARDMINRGVP------ 65
Cdd:cd08934    3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEaeggkalvleldvtdEQQVDAAVERTVEalgrld 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 -------------------------------------------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTML 96
Cdd:cd08934   83 ilvnnagimllgpvedadttdwtrmidtnllglmytthaalphhllrnkGTIVNISSVAGRVAVRNSAVYNATKFGVNAF 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568971391  97 TKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPE---FARKLKERHPLrkfaEVEDVVNSILF 158
Cdd:cd08934  163 SEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITkeaYEERISTIRKL----QAEDIAAAVRY 223
PRK06128 PRK06128
SDR family oxidoreductase;
7-121 1.07e-07

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 50.24  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   7 GLRALVTGAGKGIGRDTVKALhaSGAKVVAVTRTNsdlvslakeVSQM--VARDMINRGVPG-SIVNVSSMVAHVTFPNL 83
Cdd:PRK06128 134 GLDILVNIAGKQTAVKDIADI--TTEQFDATFKTN---------VYAMfwLCKAAIPHLPPGaSIINTGSIQSYQPSPTL 202
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568971391  84 ITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLT 121
Cdd:PRK06128 203 LDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWT 240
PRK08263 PRK08263
short chain dehydrogenase; Provisional
11-141 1.94e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 49.27  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  11 LVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAK----------------------------------------- 49
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEkygdrllplaldvtdraavfaavetavehfgrldivvnnag 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  50 --------EVSQMVARDMINRGVPGS------------------IVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAME 103
Cdd:PRK08263  87 yglfgmieEVTESEARAQIDTNFFGAlwvtqavlpylreqrsghIIQISSIGGISAFPMSGIYHASKWALEGMSEALAQE 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568971391 104 LGPHKIRVNSVNPTVVLTDMG----KKVSADPEFARkLKERH 141
Cdd:PRK08263 167 VAEFGIKVTLVEPGGYSTDWAgtsaKRATPLDAYDT-LREEL 207
PRK07985 PRK07985
SDR family oxidoreductase;
67-165 1.95e-07

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 49.61  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  67 SIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM----GKKVSADPEFARKLkerhP 142
Cdd:PRK07985 180 SIITTSSIQAYQPSPHLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALqisgGQTQDKIPQFGQQT----P 255
                         90       100
                 ....*....|....*....|...
gi 568971391 143 LRKFAEVEDVVNSILFLLSDRSA 165
Cdd:PRK07985 256 MKRAGQPAELAPVYVYLASQESS 278
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
56-178 2.58e-07

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 48.98  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  56 ARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVN--PTVVLTDMGkkvSADPEF 133
Cdd:PRK08159 134 AEKLMTDG--GSILTLTYYGAEKVMPHYNVMGVAKAALEASVKYLAVDLGPKNIRVNAISagPIKTLAASG---IGDFRY 208
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568971391 134 ARKLKERH-PLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK08159 209 ILKWNEYNaPLRRTVTIEEVGDSALYLLSDLSRGVTGEVHHVDSGY 254
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
10-178 2.72e-07

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


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 48.86  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   10 ALVTGAGKGIGRDTVKALHASGAKVVAVTR------------TNSDLVSLAKEVSQMVA------RD------------- 58
Cdd:TIGR04504   4 ALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpavgyplaTRAELDAVAAACPDQVLpviadvRDpaalaaavalave 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   59 --------------------------------------------------MINRGVPGS--IVNVSSMVAHVTFPNLITY 86
Cdd:TIGR04504  84 rwgrldaavaaagviaggrplwettdaeldllldvnlrgvwnlaraavpaMLARPDPRGgrFVAVASAAATRGLPHLAAY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   87 SSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKK------VSADPEFARklkeRHPLRKFAEVEDVVNSILFLL 160
Cdd:TIGR04504 164 CAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAAtarlygLTDVEEFAG----HQLLGRLLEPEEVAAAVAWLC 239
                         250
                  ....*....|....*...
gi 568971391  161 SDRSASTSGGGILVDAGY 178
Cdd:TIGR04504 240 SPASSAVTGSVVHADGGF 257
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
51-179 3.82e-07

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: 48.34  E-value: 3.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARdminRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSV------NPTVVLTDMG 124
Cdd:cd05361  116 IAQMKKA----GG--GSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIgpnffnSPTYFPTSDW 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568971391 125 KKvsaDPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYL 179
Cdd:cd05361  190 EN---NPELRERVKRDVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFAGGYL 241
PRK08339 PRK08339
short chain dehydrogenase; Provisional
66-181 4.86e-07

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 48.31  E-value: 4.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSAD---------PEFARK 136
Cdd:PRK08339 137 GRIIYSTSVAIKEPIPNIALSNVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDrakregksvEEALQE 216
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568971391 137 LKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS 181
Cdd:PRK08339 217 YAKPIPLGRLGEPEEIGYLVAFLASDLGSYINGAMIPVDGGRLNS 261
PRK08267 PRK08267
SDR family oxidoreductase;
62-130 5.18e-07

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 48.01  E-value: 5.18e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  62 RGVPGS-IVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSAD 130
Cdd:PRK08267 124 KATPGArVINTSSASAIYGQPGLAVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNE 193
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
37-177 6.99e-07

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 47.79  E-value: 6.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  37 VTRTNSDLVSLAKEVSQM-------VARDMINRgvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKI 109
Cdd:PRK06079 103 VTDTSRDGYALAQDISAYsliavakYARPLLNP--GASIVTLTYFGSERAIPNYNVMGIAKAALESSVRYLARDLGKKGI 180
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568971391 110 RVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK06079 181 RVNAISAGAVKTLAVTGIKGHKDLLKESDSRTVDGVGVTIEEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
PRK06180 PRK06180
short chain dehydrogenase; Provisional
66-122 7.81e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 47.60  E-value: 7.81e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTD 122
Cdd:PRK06180 130 GHIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPGSFRTD 186
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
44-178 7.83e-07

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 47.69  E-value: 7.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  44 LVSLAKEvsqmvARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDM 123
Cdd:PRK06603 125 LLELSRS-----AEALMHDG--GSIVTLTYYGAEKVIPNYNVMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLA 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568971391 124 GkkvSADPEFARKLKER---HPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK06603 198 S---SAIGDFSTMLKSHaatAPLKRNTTQEDVGGAAVYLFSELSKGVTGEIHYVDCGY 252
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
11-177 8.29e-07

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: 47.53  E-value: 8.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  11 LVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSlaKEVsqMVARDMINRGVpGSIVNVSSMVAHVTFPNLITYSSTK 90
Cdd:cd08945   84 LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVT--KEV--LKAGGMLERGT-GRIINIASTGGKQGVVHAAPYSASK 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  91 GAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSA---------DPEFARKLKERHPLRKFAEVEDVVNSILFLLS 161
Cdd:cd08945  159 HGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVREhyadiwevsTEEAFDRITARVPLGRYVTPEEVAGMVAYLIG 238
                        170
                 ....*....|....*.
gi 568971391 162 DRSASTSGGGILVDAG 177
Cdd:cd08945  239 DGAAAVTAQALNVCGG 254
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-177 1.12e-06

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 47.06  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQ-----MVARD--------------------- 58
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKygnihYVVGDvsstesarnviekaakvlnai 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 -----------------------MINRGV---------------PGS-IVNVSSMV-AHVTFPNLITYSSTKGAMTMLTK 98
Cdd:PRK05786  83 dglvvtvggyvedtveefsgleeMLTNHIkiplyavnaslrflkEGSsIVLVSSMSgIYKASPDQLSYAVAKAGLAKAVE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  99 AMAMELGPHKIRVNSVNPTVVLTDMgkkvsaDPEfaRKLKERHPLRKF-AEVEDVVNSILFLLSDRSASTSGGGILVDAG 177
Cdd:PRK05786 163 ILASELLGRGIRVNGIAPTTISGDF------EPE--RNWKKLRKLGDDmAPPEDFAKVIIWLLTDEADWVDGVVIPVDGG 234
PRK07326 PRK07326
SDR family oxidoreductase;
4-161 1.19e-06

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 46.93  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE-----------------------VSQMVA---- 56
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAElnnkgnvlglaadvrdeadvqraVDAIVAafgg 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  57 ------------------------RDMIN-----------RGVP------GSIVNVSSMVAHVTFPNLITYSSTKGAMTM 95
Cdd:PRK07326  83 ldvlianagvghfapveeltpeewRLVIDtnltgafytikAAVPalkrggGYIINISSLAGTNFFAGGAAYNASKFGLVG 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568971391  96 LTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADpEFARKLKErhplrkfaevEDVVNSILFLLS 161
Cdd:PRK07326 163 FSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPSE-KDAWKIQP----------EDIAQLVLDLLK 217
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
51-136 1.91e-06

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: 46.62  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  51 VSQMVARDMINRGVpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNP-TVVLTDMGKKVS- 128
Cdd:cd05338  130 LSQAALPHMVKAGQ-GHILNISPPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPsTAIETPAATELSg 208

                 ....*....
gi 568971391 129 -ADPEFARK 136
Cdd:cd05338  209 gSDPARARS 217
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
10-161 3.91e-06

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: 45.58  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDL-----------------VSLAKEVSQMVAR--------------- 57
Cdd:cd08929    3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLaaaaaqelegvlglagdVRDEADVRRAVDAmeeafggldalvnna 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 --------------------DMINRGVP---------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAM 102
Cdd:cd08929   83 gvgvmkpveeltpeewrlvlDTNLTGAFycihkaapallrrggGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAAML 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568971391 103 ELGPHKIRVNSVNPTVVLTDMGKkvSADPEFArKLKErhplrkfaevEDVVNSILFLLS 161
Cdd:cd08929  163 DLREANIRVVNVMPGSVDTGFAG--SPEGQAW-KLAP----------EDVAQAVLFALE 208
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
58-181 4.31e-06

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 45.38  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 DMINRGvpGSIVNVSS---------------MVAHVTFPNLIT------------YSSTKGAMTMLTKAMAME-LGPHKI 109
Cdd:PRK12428  84 PRMAPG--GAIVNVASlagaewpqrlelhkaLAATASFDEGAAwlaahpvalatgYQLSKEALILWTMRQAQPwFGARGI 161
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971391 110 RVNSVNPTVVLTDM-GKKVSADPEfARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS 181
Cdd:PRK12428 162 RVNCVAPGPVFTPIlGDFRSMLGQ-ERVDSDAKRMGRPATADEQAAVLVFLCSDAARWINGVNLPVDGGLAAT 233
PRK09072 PRK09072
SDR family oxidoreductase;
1-123 5.28e-06

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 45.32  E-value: 5.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLnfSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVS-----QMVARD----------------- 58
Cdd:PRK09072   1 MDL--KDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPypgrhRWVVADltseagreavlararem 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 ------------------------------MINRGVP----------------GSIVNVSSMVAHVTFPNLITYSSTKGA 92
Cdd:PRK09072  79 gginvlinnagvnhfalledqdpeaierllALNLTAPmqltrallpllraqpsAMVVNVGSTFGSIGYPGYASYCASKFA 158
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568971391  93 MTMLTKAMAMELGPHKIRVNSVNPTVVLTDM 123
Cdd:PRK09072 159 LRGFSEALRRELADTGVRVLYLAPRATRTAM 189
PRK05872 PRK05872
short chain dehydrogenase; Provisional
10-167 6.68e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 44.96  E-value: 6.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNS-----------------------DLVSLAKEVSQMVAR----DMI-- 60
Cdd:PRK05872  12 VVVTGAARGIGAELARRLHARGAKLALVDLEEAelaalaaelggddrvltvvadvtDLAAMQAAAEEAVERfggiDVVva 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  61 NRGV--PGSI-------------VNV--SSMVAHVTFPNLIT----------------------YSSTKGAMTMLTKAMA 101
Cdd:PRK05872  92 NAGIasGGSVaqvdpdafrrvidVNLlgVFHTVRATLPALIErrgyvlqvsslaafaaapgmaaYCASKAGVEAFANALR 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568971391 102 MELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKER--HPLRKFAEVEDVVNSILFLLSDRSAST 167
Cdd:PRK05872 172 LEVAHHGVTVGSAYLSWIDTDLVRDADADLPAFRELRARlpWPLRRTTSVEKCAAAFVDGIERRARRV 239
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
5-50 8.14e-06

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 45.29  E-value: 8.14e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE 50
Cdd:COG3347  423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAE 468
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
4-129 9.34e-06

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: 44.22  E-value: 9.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   4 NFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQMVARDM------------------------ 59
Cdd:cd05370    2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNIHTIVLdvgdaesvealaeallseypnldi 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  60 ----------------------------INRGVP----------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTM 95
Cdd:cd05370   82 linnagiqrpidlrdpasdldkadteidTNLIGPirlikaflphlkkqpeATIVNVSSGLAFVPMAANPVYCATKAALHS 161
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568971391  96 LTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSA 129
Cdd:cd05370  162 YTLALRHQLKDTGVEVVEIVPPAVDTELHEERRN 195
KR_fFAS_SDR_c_like cd08950
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like ...
3-42 1.68e-05

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like SDRs; KR domain of fungal-type fatty acid synthase (FAS), type I. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member, is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the Classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187653 [Multi-domain]  Cd Length: 259  Bit Score: 43.72  E-value: 1.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568971391   3 LNFSGLRALVTGAGKG-IGRDTVKALHASGAKVVAVTRTNS 42
Cdd:cd08950    3 LSFAGKVALVTGAGPGsIGAEVVAGLLAGGATVIVTTSRFS 43
PRK08177 PRK08177
SDR family oxidoreductase;
10-124 1.98e-05

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 43.48  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSL------------------------------------------ 47
Cdd:PRK08177   4 ALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALqalpgvhiekldmndpasldqllqrlqgqrfdllfvnagisg 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  48 ----------AKEVSQM----------VARDMINRGVPGS--IVNVSSMVAHVTFP---NLITYSSTKGAMTMLTKAMAM 102
Cdd:PRK08177  84 pahqsaadatAAEIGQLfltnaiapirLARRLLGQVRPGQgvLAFMSSQLGSVELPdggEMPLYKASKAALNSMTRSFVA 163
                        170       180
                 ....*....|....*....|..
gi 568971391 103 ELGPHKIRVNSVNPTVVLTDMG 124
Cdd:PRK08177 164 ELGEPTLTVLSMHPGWVKTDMG 185
PRK07201 PRK07201
SDR family oxidoreductase;
11-51 3.03e-05

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 43.40  E-value: 3.03e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568971391  11 LVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEV 51
Cdd:PRK07201 375 LITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEI 415
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
11-169 3.28e-05

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: 42.95  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  11 LVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVS-----------------------QMVARD--------- 58
Cdd:cd05340    8 LVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINeeggrqpqwfildlltctsencqQLAQRIavnyprldg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 ------------------------------------------MINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTML 96
Cdd:cd05340   88 vlhnagllgdvcplseqnpqvwqdv*qvnvnatfmltqallpLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFATEGL 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568971391  97 TKAMAMELGPHKIRVNSVNPTVvlTDMGKKVSADP-EFARKLKErhPlrkfaevEDVVNSILFLLSDRSASTSG 169
Cdd:cd05340  168 *QVLADEYQQRNLRVNCINPGG--TRTAMRASAFPtEDPQKLKT--P-------ADIMPLYLWLMGDDSRRKTG 230
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
66-169 5.50e-05

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: 41.93  E-value: 5.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELG--PHKIRVNSVNPTVVLTDMGKKVSADPEFARKLkerhPL 143
Cdd:cd05334  119 GLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENSglPAGSTANAILPVTLDTPANRKAMPDADFSSWT----PL 194
                         90       100
                 ....*....|....*....|....*.
gi 568971391 144 RKFAEVedvvnsILFLLSDRSASTSG 169
Cdd:cd05334  195 EFIAEL------ILFWASGAARPKSG 214
PRK08862 PRK08862
SDR family oxidoreductase;
52-118 6.06e-05

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 42.02  E-value: 6.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971391  52 SQMVARDMINRGVPGSIVNVssmVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTV 118
Cdd:PRK08862 123 GQVAAERMRKRNKKGVIVNV---ISHDDHQDLTGVESSNALVSGFTHSWAKELTPFNIRVGGVVPSI 186
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
10-157 9.96e-05

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 41.59  E-value: 9.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRT-NSDLVSLA-----------------KEVSQ------------------ 53
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVISISRTeNKELTKLAeqynsnltfhsldlqdvHELETnfneilssiqednvssih 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  54 ------MVA---------RDMINR-----------------------GVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTM 95
Cdd:PRK06924  84 linnagMVApikpiekaeSEELITnvhlnllapmiltstfmkhtkdwKVDKRVINISSGAAKNPYFGWSAYCSSKAGLDM 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971391  96 LTKAMAME--LGPHKIRVNSVNPTVVLTDM-------GKKVSADPEFARKLKERHPLRKFAEVEDVVNSIL 157
Cdd:PRK06924 164 FTQTVATEqeEEEYPVKIVAFSPGVMDTNMqaqirssSKEDFTNLDRFITLKEEGKLLSPEYVAKALRNLL 234
PRK12742 PRK12742
SDR family oxidoreductase;
56-180 1.04e-04

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 41.28  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  56 ARDMINRG---VPGSiVNVSSMvahvTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGkkvSADPE 132
Cdd:PRK12742 118 ARQMPEGGriiIIGS-VNGDRM----PVAGMAAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDAN---PANGP 189
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568971391 133 FARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLA 180
Cdd:PRK12742 190 MKDMMHSFMAIKRHGRPEEVAGMVAWLAGPEASFVTGAMHTIDGAFGA 237
PRK07775 PRK07775
SDR family oxidoreductase;
48-174 1.07e-04

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 41.28  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  48 AKEVSQMVARDMINRGvPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKV 127
Cdd:PRK07775 122 ANRLATAVLPGMIERR-RGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWSL 200
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568971391 128 SAD------PEFARKLKERHPlrKFAEVEDVVNSILFLlsdrsASTSGGGILV 174
Cdd:PRK07775 201 PAEvigpmlEDWAKWGQARHD--YFLRASDLARAITFV-----AETPRGAHVV 246
PRK06182 PRK06182
short chain dehydrogenase; Validated
10-124 1.22e-04

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 41.10  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAK--------------EVSQMVARDMINRG------------ 63
Cdd:PRK06182   6 ALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASlgvhplsldvtdeaSIKAAVDTIIAEEGridvlvnnagyg 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  64 -------VP-------------------------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELG 105
Cdd:PRK06182  86 sygaiedVPidearrqfevnlfgaarltqlvlphmraqrsGRIINISSMGGKIYTPLGAWYHATKFALEGFSDALRLEVA 165
                        170
                 ....*....|....*....
gi 568971391 106 PHKIRVNSVNPTVVLTDMG 124
Cdd:PRK06182 166 PFGIDVVVIEPGGIKTEWG 184
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
22-178 1.22e-04

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 41.08  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  22 DTVKALHASGAKvvavtrtnsdLVSLAKevsqmVARDMINRGvpGSIVNVSsMVAHVTFPNLITYSSTKGAMTMLTKAMA 101
Cdd:PRK07889 112 DVATALHVSAYS----------LKSLAK-----ALLPLMNEG--GSIVGLD-FDATVAWPAYDWMGVAKAALESTNRYLA 173
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568971391 102 MELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLR-KFAEVEDVVNSILFLLSDRSASTSGGGILVDAGY 178
Cdd:PRK07889 174 RDLGPRGIRVNLVAAGPIRTLAAKAIPGFELLEEGWDERAPLGwDVKDPTPVARAVVALLSDWFPATTGEIVHVDGGA 251
PRK08251 PRK08251
SDR family oxidoreductase;
66-131 1.41e-04

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 41.07  E-value: 1.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971391  66 GSIVNVSSMVAHVTFP-NLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADP 131
Cdd:PRK08251 133 GHLVLISSVSAVRGLPgVKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAKSTP 199
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
3-47 1.43e-04

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 41.22  E-value: 1.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568971391   3 LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTrTNSDLVSL 47
Cdd:PRK07424 174 LSLKGKTVAVTGASGTLGQALLKELHQQGAKVVALT-SNSDKITL 217
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
66-142 1.60e-04

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 41.11  E-value: 1.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHP 142
Cdd:cd09805  130 GRVVNVSSMGGRVPFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAKKLWERLP 206
PRK06940 PRK06940
short chain dehydrogenase; Provisional
83-181 1.60e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 40.77  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  83 LITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADP--EFARKLKERHPLRKFAEVEDVVNSILFLL 160
Cdd:PRK06940 166 LHAYQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAQDELNGPrgDGYRNMFAKSPAGRPGTPDEIAALAEFLM 245
                         90       100
                 ....*....|....*....|.
gi 568971391 161 SDRSASTSGGGILVDAGYLAS 181
Cdd:PRK06940 246 GPRGSFITGSDFLVDGGATAS 266
PRK07832 PRK07832
SDR family oxidoreductase;
9-127 1.61e-04

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 40.80  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   9 RALVTGAGKGIGRDTVKALHASGAKVVAVTR-------TNSDLVSLAKEVSQMVARD----------------------- 58
Cdd:PRK07832   2 RCFVTGAASGIGRATALRLAAQGAELFLTDRdadglaqTVADARALGGTVPEHRALDisdydavaafaadihaahgsmdv 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 ------------------------------------------MINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTML 96
Cdd:PRK07832  82 vmniagisawgtvdrltheqwrrmvdvnlmgpihvietfvppMVAAGRGGHLVNVSSAAGLVALPWHAAYSASKFGLRGL 161
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568971391  97 TKAMAMELGPHKIRVNSVNPTVVLTDMGKKV 127
Cdd:PRK07832 162 SEVLRFDLARHGIGVSVVVPGAVKTPLVNTV 192
PRK06179 PRK06179
short chain dehydrogenase; Provisional
10-123 1.75e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 40.66  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNS----------------DLVSLAKEVSQMVARD--------------- 58
Cdd:PRK06179   7 ALVTGASSGIGRATAEKLARAGYRVFGTSRNPAraapipgvelleldvtDDASVQAAVDEVIARAgridvlvnnagvgla 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  59 ------------------------MINRGVP-------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPH 107
Cdd:PRK06179  87 gaaeessiaqaqalfdtnvfgilrMTRAVLPhmraqgsGRIINISSVLGFLPAPYMALYAASKHAVEGYSESLDHEVRQF 166
                        170
                 ....*....|....*.
gi 568971391 108 KIRVNSVNPTVVLTDM 123
Cdd:PRK06179 167 GIRVSLVEPAYTKTNF 182
PRK06196 PRK06196
oxidoreductase; Provisional
3-39 1.79e-04

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 40.82  E-value: 1.79e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568971391   3 LNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTR 39
Cdd:PRK06196  22 HDLSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPAR 58
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
5-130 2.32e-04

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: 40.26  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDL---------------------VSLAKEVSQMVAR------ 57
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLeevkseclelgapsphvvpldMSDLEDAEQVVEEalklfg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 --DMI--NRGVP----------------------------------------GSIVNVSSMVAHVTFPNLITYSSTKGAM 93
Cdd:cd05332   81 glDILinNAGISmrslfhdtsidvdrkimevnyfgpvaltkaalphliersqGSIVVVSSIAGKIGVPFRTAYAASKHAL 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568971391  94 TMLTKAMAMELGPHKIRVNSVNPTVVLTDMG-KKVSAD 130
Cdd:cd05332  161 QGFFDSLRAELSEPNISVTVVCPGLIDTNIAmNALSGD 198
PRK05650 PRK05650
SDR family oxidoreductase;
66-156 2.33e-04

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 40.41  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKV-SADPEFAR---KLKERH 141
Cdd:PRK05650 129 GRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLLDSFrGPNPAMKAqvgKLLEKS 208
                         90
                 ....*....|....*
gi 568971391 142 PLRKfaevEDVVNSI 156
Cdd:PRK05650 209 PITA----ADIADYI 219
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-51 2.74e-04

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 40.59  E-value: 2.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVVA--VTRTNSDLVSLAKEV 51
Cdd:PRK08261 210 GKVALVTGAARGIGAAIAEVLARDGAHVVCldVPAAGEALAAVANRV 256
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
4-51 2.88e-04

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 40.48  E-value: 2.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568971391   4 NFSGLRALVTGAGKgIGRDTVKALHASGAKVVAVT-RTNSDLVSLAKEV 51
Cdd:COG0373  179 DLSGKTVLVIGAGE-MGELAARHLAAKGVKRITVAnRTLERAEELAEEF 226
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
5-127 3.05e-04

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: 40.01  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   5 FSGLRALVTGAGKGIGrDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQMVARdmiNRGvpgSIVNVSSMVAHVTFPNLI 84
Cdd:cd05350   73 LGGLDLVIINAGVGKG-TSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAK---GRG---HLVLISSVAALRGLPGAA 145
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568971391  85 TYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKV 127
Cdd:cd05350  146 AYSASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANM 188
PRK06720 PRK06720
hypothetical protein; Provisional
1-63 3.15e-04

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 39.57  E-value: 3.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971391   1 MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVaVTRTNsdlvslaKEVSQMVARDMINRG 63
Cdd:PRK06720  10 MKMKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVI-VTDID-------QESGQATVEEITNLG 64
PRK05693 PRK05693
SDR family oxidoreductase;
10-142 3.53e-04

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 39.77  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQMVARD-----------------------MIN----- 61
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAAGFTAVQLDvndgaalarlaeeleaehggldvLINnagyg 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  62 -----------------------------------RGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGP 106
Cdd:PRK05693  84 amgplldggveamrrqfetnvfavvgvtralfpllRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDALRLELAP 163
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568971391 107 HKIRVNSVNPTVVLTDMGKKVSADPEfaRKLKERHP 142
Cdd:PRK05693 164 FGVQVMEVQPGAIASQFASNASREAE--QLLAEQSP 197
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
11-169 3.74e-04

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 39.86  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  11 LVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQMVAR---------------------DMINRGVP---- 65
Cdd:PRK08945  16 LVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPqpaiipldlltatpqnyqqlaDTIEEQFGrldg 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 -------------------------------------------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTML 96
Cdd:PRK08945  96 vlhnagllgelgpmeqqdpevwqdvmqvnvnatfmltqallplllkspaASLVFTSSSVGRQGRANWGAYAVSKFATEGM 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568971391  97 TKAMAMELGPHKIRVNSVNPTVVLTDMgkKVSADP-EFARKLKErhPlrkfaevEDVVNSILFLLSDRSASTSG 169
Cdd:PRK08945 176 MQVLADEYQGTNLRVNCINPGGTRTAM--RASAFPgEDPQKLKT--P-------EDIMPLYLYLMGDDSRRKNG 238
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-48 4.53e-04

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 39.58  E-value: 4.53e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568971391   9 RALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLA 48
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLA 40
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
58-137 6.09e-04

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: 39.37  E-value: 6.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  58 DMINRGVPGSIVNVSSMV---AHVTFPNL---------ITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGK 125
Cdd:cd09807  122 DLLKKSAPSRIVNVSSLAhkaGKINFDDLnseksyntgFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGR 201
                         90
                 ....*....|..
gi 568971391 126 KVSADPEFARKL 137
Cdd:cd09807  202 HTGIHHLFLSTL 213
PRK06181 PRK06181
SDR family oxidoreductase;
10-163 6.86e-04

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 39.19  E-value: 6.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVSQMVA---------------RDMINRGVP--------- 65
Cdd:PRK06181   4 VIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGealvvptdvsdaeacERLIEAAVArfggidilv 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 ----------------------------------------------GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKA 99
Cdd:PRK06181  84 nnagitmwsrfdeltdlsvfervmrvnylgavycthaalphlkasrGQIVVVSSLAGLTGVPTRSGYAASKHALHGFFDS 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971391 100 MAMELGPHKIRVNSVNPTVVLTDMGKKV---SADPEFARKLKErhplRKFAEVEDVVNSILFLLSDR 163
Cdd:PRK06181 164 LRIELADDGVAVTVVCPGFVATDIRKRAldgDGKPLGKSPMQE----SKIMSAEECAEAILPAIARR 226
PRK07023 PRK07023
SDR family oxidoreductase;
68-162 7.18e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 38.84  E-value: 7.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  68 IVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMElGPHKIRVNSVNPTVVLTDMGKKV-SADPE-FA--RKLKERHPL 143
Cdd:PRK07023 132 ILHISSGAARNAYAGWSVYCATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGMQATIrATDEErFPmrERFRELKAS 210
                         90       100
                 ....*....|....*....|
gi 568971391 144 RKFAEVEDVVNSIL-FLLSD 162
Cdd:PRK07023 211 GALSTPEDAARRLIaYLLSD 230
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
87-177 8.16e-04

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 38.99  E-value: 8.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  87 SSTKGAMTMLTKAMAMELG-PHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSA 165
Cdd:PLN02730 194 SSAKAALESDTRVLAFEAGrKYKIRVNTISAGPLGSRAAKAIGFIDDMIEYSYANAPLQKELTADEVGNAAAFLASPLAS 273
                         90
                 ....*....|..
gi 568971391 166 STSGGGILVDAG 177
Cdd:PLN02730 274 AITGATIYVDNG 285
PRK07109 PRK07109
short chain dehydrogenase; Provisional
10-51 9.76e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 38.75  E-value: 9.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEV 51
Cdd:PRK07109  11 VVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEI 52
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
4-59 1.06e-03

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 37.55  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568971391    4 NFSGLRALVTGAGKgIGRDTVKALHASGAKVVAVT-RTNSDLVSLAKEVSQMVARDM 59
Cdd:pfam01488   9 DLKDKKVLLIGAGE-MGELVAKHLLAKGAKEVTIAnRTIERAQELAEKFGGVEALPL 64
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
7-38 1.17e-03

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 38.48  E-value: 1.17e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVVAVT 38
Cdd:PRK13771 163 GETVLVTGAGGGVGIHAIQVAKALGAKVIAVT 194
PRK08340 PRK08340
SDR family oxidoreductase;
66-175 1.20e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 38.25  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSV------------NPTVVLTDMGkkVSADPEF 133
Cdd:PRK08340 131 GVLVYLSSVSVKEPMPPLVLADVTRAGLVQLAKGVSRTYGGKGIRAYTVllgsfdtpgareNLARIAEERG--VSFEETW 208
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568971391 134 ARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVD 175
Cdd:PRK08340 209 EREVLERTPLKRTGRWEELGSLIAFLLSENAEYMLGSTIVFD 250
PRK06197 PRK06197
short chain dehydrogenase; Provisional
6-39 1.21e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 38.47  E-value: 1.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 568971391   6 SGLRALVTGAGKGIGRDTVKALHASGAKVVAVTR 39
Cdd:PRK06197  15 SGRVAVVTGANTGLGYETAAALAAKGAHVVLAVR 48
PRK05866 PRK05866
SDR family oxidoreductase;
6-52 1.47e-03

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 38.18  E-value: 1.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568971391   6 SGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEVS 52
Cdd:PRK05866  39 TGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRIT 85
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
4-55 1.56e-03

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 38.02  E-value: 1.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568971391   4 NFSGLRALVTGAGKgIGRDTVKALHASGAKVVAVT-RTNSDLVSLAKEVSQMV 55
Cdd:cd05213  175 NLKGKKVLVIGAGE-MGELAAKHLAAKGVAEITIAnRTYERAEELAKELGGNA 226
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
12-51 1.62e-03

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: 37.75  E-value: 1.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568971391  12 VTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEV 51
Cdd:cd05360    5 ITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREV 44
PRK06953 PRK06953
SDR family oxidoreductase;
10-47 1.92e-03

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 37.74  E-value: 1.92e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSL 47
Cdd:PRK06953   4 VLIVGASRGIGREFVRQYRADGWRVIATARDAAALAAL 41
PRK07806 PRK07806
SDR family oxidoreductase;
6-42 2.07e-03

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 37.39  E-value: 2.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568971391   6 SGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNS 42
Cdd:PRK07806   5 PGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKA 41
PRK06482 PRK06482
SDR family oxidoreductase;
66-124 2.16e-03

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 37.79  E-value: 2.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMG 124
Cdd:PRK06482 128 GRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFG 186
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
4-51 2.66e-03

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 37.47  E-value: 2.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568971391   4 NFSGLRALVTGAGKgIGRDTVKALHASGAKVVAVT-RTNSDLVSLAKEV 51
Cdd:PRK00045 179 DLSGKKVLVIGAGE-MGELVAKHLAEKGVRKITVAnRTLERAEELAEEF 226
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
3-35 2.77e-03

(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: 37.30  E-value: 2.77e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568971391   3 LNFSGLRALVTGAGKGIGRDTVKALHASGAKVV 35
Cdd:cd05353    1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVV 33
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
7-51 3.16e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240636  Cd Length: 303  Bit Score: 37.24  E-value: 3.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568971391   7 GLRALVTGAGkGIGRDTVKALHASGAKVVAVTRTNSDlVSLAKEV 51
Cdd:cd12159  125 GSTVAIVGAG-GIGRALIPLLAPFGAKVIAVNRSGRP-VEGADET 167
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-169 3.27e-03

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 37.07  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391   1 MKLNFSGLRALVTGAGKGIGR-------------------------DTVKALHASGAKVVAVTRTNSD------LVSLAK 49
Cdd:PRK07792   6 NTTDLSGKVAVVTGAAAGLGRaealglarlgatvvvndvasaldasDVLDEIRAAGAKAVAVAGDISQratadeLVATAV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  50 EVSQM--------VARDMI----------------NRG----------------------VPGSIVNVSS---MVAHVTF 80
Cdd:PRK07792  86 GLGGLdivvnnagITRDRMlfnmsdeewdaviavhLRGhflltrnaaaywrakakaaggpVYGRIVNTSSeagLVGPVGQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971391  81 PNlitYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTvVLTDMGKKVSAD-PEFARklKERHPLrkfaEVEDVVNSILFL 159
Cdd:PRK07792 166 AN---YGAAKAGITALTLSAARALGRYGVRANAICPR-ARTAMTADVFGDaPDVEA--GGIDPL----SPEHVVPLVQFL 235
                        250
                 ....*....|
gi 568971391 160 LSDRSASTSG 169
Cdd:PRK07792 236 ASPAAAEVNG 245
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
10-51 3.81e-03

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: 36.73  E-value: 3.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568971391  10 ALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKEV 51
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEV 42
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
7-40 4.43e-03

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 36.58  E-value: 4.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 568971391   7 GLRALVTGAGKGIGRDTVKALHASGAKVVAVTRT 40
Cdd:cd08270  133 GRRVLVTGASGGVGRFAVQLAALAGAHVVAVVGS 166
PRK06914 PRK06914
SDR family oxidoreductase;
66-116 6.92e-03

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 36.15  E-value: 6.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568971391  66 GSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNP 116
Cdd:PRK06914 133 GKIINISSISGRVGFPGLSPYVSSKYALEGFSESLRLELKPFGIDVALIEP 183
PRK07578 PRK07578
short chain dehydrogenase; Provisional
55-125 7.60e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 35.56  E-value: 7.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971391  55 VARDMINRGvpGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELgPHKIRVNSVNPTVVLTDMGK 125
Cdd:PRK07578  96 IGQHYLNDG--GSFTLTSGILSDEPIPGGASAATVNGALEGFVKAAALEL-PRGIRINVVSPTVLTESLEK 163
PRK05993 PRK05993
SDR family oxidoreductase;
11-50 8.83e-03

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 35.77  E-value: 8.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568971391  11 LVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKE 50
Cdd:PRK05993   8 LITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAE 47
 
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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