NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958774432|ref|XP_038965094|]
View 

2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial isoform X1 [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 57-172 4.74e-43

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 cd05369:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 249  Bit Score: 144.65  E-value: 4.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASR--------------------------------------------- 91
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRkpevleaaaeeissatggrahpiqcdvrdpeaveaavdetlkefg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432     --------------------------------------------------------------------------------
Cdd:cd05369    81 kidilinnaagnflapaeslspngfktvididlngtfnttkavgkrlieakhggsilnisatyaytgspfqvhsaaakag 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  92 ------SLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:cd05369   161 vdaltrSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTT 240


                  ....*..
gi 1958774432 166 IRFDGGE 172
Cdd:cd05369   241 LVVDGGQ 247
 
Name Accession Description Interval E-value
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 57-172 4.74e-43

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: 144.65  E-value: 4.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASR--------------------------------------------- 91
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRkpevleaaaeeissatggrahpiqcdvrdpeaveaavdetlkefg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432     --------------------------------------------------------------------------------
Cdd:cd05369    81 kidilinnaagnflapaeslspngfktvididlngtfnttkavgkrlieakhggsilnisatyaytgspfqvhsaaakag 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  92 ------SLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:cd05369   161 vdaltrSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTT 240


                  ....*..
gi 1958774432 166 IRFDGGE 172
Cdd:cd05369   241 LVVDGGQ 247
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 79-171 3.21e-27

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: 103.28  E-value: 3.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  79 LSSLGAQCVIA---------------SRSLAAEWGRYGMRFNIIQPGPIKTkGAFSRLDPTGKFEKDMIERIPCGRLGTV 143
Cdd:pfam13561 128 LSSIGAERVVPnynaygaakaalealTRYLAVELGPRGIRVNAISPGPIKT-LAASGIPGFDELLAAAEARAPLGRLGTP 206

                          90       100
                  ....*....|....*....|....*...
gi 1958774432 144 EELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:pfam13561 207 EEVANAAAFLASDLASYITGQVLYVDGG 234
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 90-172 2.06e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 98.98  E-value: 2.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGR-YGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK07677  162 TRTLAVEWGRkYGIRVNAIAPGPIERTGGADKLWESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYINGTCITM 241


                  ....
gi 1958774432 169 DGGE 172
Cdd:PRK07677  242 DGGQ 245
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 90-171 2.81e-25

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: 98.32  E-value: 2.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTkGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:COG1028   166 TRSLALELAPRGIRVNAVAPGPIDT-PMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVD 244


                  ..
gi 1958774432 170 GG 171
Cdd:COG1028   245 GG 246
kduD TIGR01832
2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase ...
 90-171 2.10e-12

2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase (also called 2-keto-3-deoxygluconate oxidoreductase), a member of the family of short-chain-alcohol dehydrogenases (pfam00106). This protein has been characterized in Erwinia chrysanthemi as an enzyme of pectin degradation. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 188170 [Multi-domain]  Cd Length: 248  Bit Score: 64.01  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKG-AFSRLDPtgKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:TIGR01832 164 TKLLANEWAAKGINVNAIAPGYMATNNtQALRADE--DRNAAILERIPAGRWGTPDDIGGPAVFLASSASDYVNGYTLAV 241


                  ...
gi 1958774432 169 DGG 171
Cdd:TIGR01832 242 DGG 244
 
Name Accession Description Interval E-value
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 57-172 4.74e-43

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: 144.65  E-value: 4.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASR--------------------------------------------- 91
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRkpevleaaaeeissatggrahpiqcdvrdpeaveaavdetlkefg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432     --------------------------------------------------------------------------------
Cdd:cd05369    81 kidilinnaagnflapaeslspngfktvididlngtfnttkavgkrlieakhggsilnisatyaytgspfqvhsaaakag 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  92 ------SLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:cd05369   161 vdaltrSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTT 240


                  ....*..
gi 1958774432 166 IRFDGGE 172
Cdd:cd05369   241 LVVDGGQ 247
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 79-171 3.21e-27

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: 103.28  E-value: 3.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  79 LSSLGAQCVIA---------------SRSLAAEWGRYGMRFNIIQPGPIKTkGAFSRLDPTGKFEKDMIERIPCGRLGTV 143
Cdd:pfam13561 128 LSSIGAERVVPnynaygaakaalealTRYLAVELGPRGIRVNAISPGPIKT-LAASGIPGFDELLAAAEARAPLGRLGTP 206

                          90       100
                  ....*....|....*....|....*...
gi 1958774432 144 EELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:pfam13561 207 EEVANAAAFLASDLASYITGQVLYVDGG 234
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 90-172 2.06e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 98.98  E-value: 2.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGR-YGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK07677  162 TRTLAVEWGRkYGIRVNAIAPGPIERTGGADKLWESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYINGTCITM 241


                  ....
gi 1958774432 169 DGGE 172
Cdd:PRK07677  242 DGGQ 245
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 90-171 2.81e-25

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: 98.32  E-value: 2.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTkGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:COG1028   166 TRSLALELAPRGIRVNAVAPGPIDT-PMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVD 244


                  ..
gi 1958774432 170 GG 171
Cdd:COG1028   245 GG 246
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 91-171 6.53e-24

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 95.02  E-value: 6.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDG 170
Cdd:PRK07576  169 RTLALEWGPEGIRVNSIVPGPIAGTEGMARLAPSPELQAAVAQSVPLKRNGTKQDIANAALFLASDMASYITGVVLPVDG 248


                  .
gi 1958774432 171 G 171
Cdd:PRK07576  249 G 249
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 37-171 2.39e-21

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: 88.10  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  37 DAPQSKFFPPI--LKPMLPPNAFQGKVAFITGGGTGLGKAMTTFL--SSLGAQCVIASRSLAAEWGRYGMRFNIIQPGPI 112
Cdd:cd05344   104 EAFDLKLLSVIriVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVlsNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYI 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774432 113 KT--------KGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:cd05344   184 DTervrrlleARAEKEGISVEEAEKEVASQIPLGRVGKPEELAALIAFLASEKASYITGQAILVDGG 250
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 79-171 6.69e-20

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: 84.30  E-value: 6.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  79 LSSLGAQCVI---------------ASRSLAAEWGRYGMRFNIIQPGPIKTKgAFSRLDPTGKFEKDMIERIPCGRLGTV 143
Cdd:COG0623   142 LTYLGAERVVpnynvmgvakaaleaSVRYLAADLGPKGIRVNAISAGPIKTL-AASGIPGFDKLLDYAEERAPLGRNVTI 220

                          90       100
                  ....*....|....*....|....*...
gi 1958774432 144 EELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:COG0623   221 EEVGNAAAFLLSDLASGITGEIIYVDGG 248
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 90-169 7.43e-20

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: 83.87  E-value: 7.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGkfEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:cd05233   157 TRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEA--EKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
89-171 1.95e-19

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 82.90  E-value: 1.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  89 ASRSLAAEWGRYGMRFNIIQPGPIKTkgafSRLDPTGKFEKDMIER-IPCGRLGTVEELANLATFLCSDYASWINGAVIR 167
Cdd:PRK05653  164 FTKALALELASRGITVNAVAPGFIDT----DMTEGLPEEVKAEILKeIPLGRLGQPEEVANAVAFLASDAASYITGQVIP 239


                  ....
gi 1958774432 168 FDGG 171
Cdd:PRK05653  240 VNGG 243
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 90-171 3.70e-19

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: 82.21  E-value: 3.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTkgafsrlDPTGKFEKDMIE----RIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:cd05333   160 TKSLAKELASRGITVNAVAPGFIDT-------DMTDALPEKVKEkilkQIPLGRLGTPEEVANAVAFLASDDASYITGQV 232


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:cd05333   233 LHVNGG 238
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 92-171 1.41e-18

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 80.66  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  92 SLAAEWGRYGMRFNIIQPGPIKTK-GAFSRLDptgkfEKDMIER-IPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK05565  168 ALAKELAPSGIRVNAVAPGAIDTEmWSSFSEE-----DKEGLAEeIPLGRLGKPEEIAKVVLFLASDDASYITGQIITVD 242


                  ..
gi 1958774432 170 GG 171
Cdd:PRK05565  243 GG 244
PRK06484 PRK06484
short chain dehydrogenase; Validated
 90-171 1.83e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 82.59  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAfSRLDPTGKFEKDMI-ERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK06484  425 SRSLACEWAPAGIRVNTVAPGYIETPAV-LALKASGRADFDSIrRRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTV 503


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK06484  504 DGG 506
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 87-171 2.75e-18

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 79.85  E-value: 2.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  87 VIA-SRSLAAEWGRYGMRFNIIQPGPIKTKgAFSRLDPtgKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:PRK05557  162 VIGfTKSLARELASRGITVNAVAPGFIETD-MTDALPE--DVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQT 238


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:PRK05557  239 LHVNGG 244
FabG-like PRK07231
SDR family oxidoreductase;
89-171 2.81e-18

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 79.87  E-value: 2.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  89 ASRSLAAEWGRYGMRFNIIQPGPIKTKGA-FSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIR 167
Cdd:PRK07231  164 LTKALAAELGPDKIRVNAVAPVVVETGLLeAFMGEPTPENRAKFLATIPLGRLGTPEDIANAALFLASDEASWITGVTLV 243


                  ....
gi 1958774432 168 FDGG 171
Cdd:PRK07231  244 VDGG 247
PRK07774 PRK07774
SDR family oxidoreductase;
62-172 3.00e-18

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 79.79  E-value: 3.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  62 AFITGGGTGLGKAMttfLSSLGAQcviasrsLAAEWGRYGMRFNIIQPGPIKTKgAFSRLDPtGKFEKDMIERIPCGRLG 141
Cdd:PRK07774  148 AWLYSNFYGLAKVG---LNGLTQQ-------LARELGGMNIRVNAIAPGPIDTE-ATRTVTP-KEFVADMVKGIPLSRMG 215

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958774432 142 TVEELANLATFLCSDYASWINGAVIRFDGGE 172
Cdd:PRK07774  216 TPEDLVGMCLFLLSDEASWITGQIFNVDGGQ 246
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 61-171 3.74e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 79.61  E-value: 3.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  61 VAFITGGGTGLGKAMTT--FLSSLGAqcVIA-SRSLAAEWGRYGMRFNIIQPG--PIK-TKGAFSRLdptgkfEKDMIER 134
Cdd:PRK08213  147 VASVAGLGGNPPEVMDTiaYNTSKGA--VINfTRALAAEWGPHGIRVNAIAPGffPTKmTRGTLERL------GEDLLAH 218

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958774432 135 IPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK08213  219 TPLGRLGDDEDLKGAALLLASDASKHITGQILAVDGG 255
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 91-171 7.24e-18

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: 78.55  E-value: 7.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKfEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDG 170
Cdd:cd05359   160 RYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDL-LEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDG 238


                  .
gi 1958774432 171 G 171
Cdd:cd05359   239 G 239
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 90-171 4.88e-17

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: 76.63  E-value: 4.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTK-GAFSRLDPtgKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:cd05347   165 TKALATEWARHGIQVNAIAPGYFATEmTEAVVADP--EFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQIIFV 242


                  ...
gi 1958774432 169 DGG 171
Cdd:cd05347   243 DGG 245
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 89-174 8.62e-16

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 72.98  E-value: 8.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  89 ASRSLAAEWGRYGMRFNIIQPGPIKTkgafSRLDPTGKFEKDMIE-RIPCGRLGTVEELANLATFLCSDYASWINGAVIR 167
Cdd:PRK12825  166 LTKALARELAEYGITVNMVAPGDIDT----DMKEATIEEAREAKDaETPLGRSGTPEDIARAVAFLCSDASDYITGQVIE 241


                  ....*..
gi 1958774432 168 FDGGEEV 174
Cdd:PRK12825  242 VTGGVDV 248
PRK09242 PRK09242
SDR family oxidoreductase;
59-171 1.91e-15

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 72.47  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  59 GKVAFITGGGTGLGKAMTTflsslgAQCVIASRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKdMIERIPCG 138
Cdd:PRK09242  146 GSVSGLTHVRSGAPYGMTK------AALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYEQ-VIERTPMR 218

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958774432 139 RLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK09242  219 RVGEPEEVAAAVAFLCMPAASYITGQCIAVDGG 251
PRK06484 PRK06484
short chain dehydrogenase; Validated
 90-175 2.67e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 73.34  E-value: 2.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKgAFSRLDPTGKFEKDMI-ERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK06484  165 TRSLACEWAAKGIRVNAVLPGYVRTQ-MVAELERAGKLDPSAVrSRIPLGRLGRPEEIAEAVFFLASDQASYITGSTLVV 243


                  ....*..
gi 1958774432 169 DGGEEVF 175
Cdd:PRK06484  244 DGGWTVY 250
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 91-171 3.29e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 71.97  E-value: 3.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLD-PTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK06940  181 MAEAVKWGERGARINSISPGIISTPLAQDELNgPRGDGYRNMFAKSPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVD 260


                  ..
gi 1958774432 170 GG 171
Cdd:PRK06940  261 GG 262
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 66-172 4.73e-15

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: 71.40  E-value: 4.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  66 GGGTGLGKAMTTFLSSLGAqcVIASRSLAAEWGRYGMRFNIIQPGPIKT---KGAFSRLDPTG--KFEKDMIERIPCGRL 140
Cdd:cd05330   144 GGIRGVGNQSGYAAAKHGV--VGLTRNSAVEYGQYGIRINAIAPGAILTpmvEGSLKQLGPENpeEAGEEFVSVNPMKRF 221

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958774432 141 GTVEELANLATFLCSDYASWINGAVIRFDGGE 172
Cdd:cd05330   222 GEPEEVAAVVAFLLSDDAGYVNAAVVPIDGGQ 253
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 90-171 5.37e-15

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: 70.94  E-value: 5.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKdMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:cd05329   167 TRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDK-VIERTPLKRFGEPEEVAALVAFLCMPAASYITGQIIAVD 245


                  ..
gi 1958774432 170 GG 171
Cdd:cd05329   246 GG 247
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 50-173 6.34e-15

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 70.86  E-value: 6.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  50 PMLPPNAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAAEWGRYGMRFNIIQPGPIKTKG--------AFSRL 121
Cdd:PRK12829  131 PLLKASGHGGVIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRmrrviearAQQLG 210

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958774432 122 DPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGGEE 173
Cdd:PRK12829  211 IGLDEMEQEYLEKISLGRMVEPEDIAATALFLASPAARYITGQAISVDGNVE 262
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
89-171 6.35e-15

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 70.74  E-value: 6.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  89 ASRSLAAEWGRYGMRFNIIQPGPIKTKGAfSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK07533  172 SVRYLAAELGPKGIRVHAISPGPLKTRAA-SGIDDFDALLEDAAERAPLRRLVDIDDVGAVAAFLASDAARRLTGNTLYI 250


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK07533  251 DGG 253
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 87-171 6.49e-15

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: 70.99  E-value: 6.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  87 VIASRSLAAEWG-RYGMRFNIIQPGPIKTK--GAFsRLDPTGKFEKDMIeRIPCGRLGTVEELANLATFLCSDYASWING 163
Cdd:cd05328   159 TVWTRRRAATWLyGAGVRVNTVAPGPVETPilQAF-LQDPRGGESVDAF-VTPMGRRAEPDEIAPVIAFLASDAASWING 236


                  ....*...
gi 1958774432 164 AVIRFDGG 171
Cdd:cd05328   237 ANLFVDGG 244
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 75-171 1.19e-14

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 70.26  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  75 MTTFLSSLGAQCVIaSRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPtgKFEKDMIERIPCGRLGTVEELANLATFLC 154
Cdd:PRK06113  156 MTSYASSKAAASHL-VRNMAFDLGEKNIRVNGIAPGAILTDALKSVITP--EIEQKMLQHTPIRRLGQPQDIANAALFLC 232

                          90
                  ....*....|....*..
gi 1958774432 155 SDYASWINGAVIRFDGG 171
Cdd:PRK06113  233 SPAASWVSGQILTVSGG 249
PRK07577 PRK07577
SDR family oxidoreductase;
21-171 1.78e-14

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 69.37  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  21 PQRFFSFGTKTLYQSID-----APQ-SKFFPPILKpmlppNAFQGKVAFITGGGTgLGKAMTTFLSSLGAQCVIASRSLA 94
Cdd:PRK07577   81 PQPLGKIDLAALQDVYDlnvraAVQvTQAFLEGMK-----LREQGRIVNICSRAI-FGALDRTSYSAAKSALVGCTRTWA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774432  95 AEWGRYGMRFNIIQPGPIKTKgAFSRLDPTG-KFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK07577  155 LELAEYGITVNAVAPGPIETE-LFRQTRPVGsEEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDGG 231
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 91-171 2.21e-14

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: 69.33  E-value: 2.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKT---KGAFSrlDPTGkfEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIR 167
Cdd:cd05358   166 KTLAQEYAPKGIRVNAIAPGAINTpinAEAWD--DPEQ--RADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGTTLF 241


                  ....
gi 1958774432 168 FDGG 171
Cdd:cd05358   242 VDGG 245
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 78-171 3.33e-14

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: 68.65  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  78 FLSSLGAQCVIA-SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFE---KDMIERIPCGRLGTVEELANLATFL 153
Cdd:cd05368   141 FVYSTTKAAVIGlTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPEealKAFAARQPLGRLATPEEVAALAVYL 220

                          90
                  ....*....|....*...
gi 1958774432 154 CSDYASWINGAVIRFDGG 171
Cdd:cd05368   221 ASDESAYVTGTAVVIDGG 238
PRK12826 PRK12826
SDR family oxidoreductase;
91-172 4.00e-14

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 68.79  E-value: 4.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDptGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDG 170
Cdd:PRK12826  168 RALALELAARNITVNSVHPGGVDTPMAGNLGD--AQWAEAIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQTLPVDG 245


                  ..
gi 1958774432 171 GE 172
Cdd:PRK12826  246 GA 247
PRK08589 PRK08589
SDR family oxidoreductase;
90-171 4.56e-14

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 68.65  E-value: 4.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKT----KGAFSRLDPTGKFEKDMIERI-PCGRLGTVEELANLATFLCSDYASWINGA 164
Cdd:PRK08589  165 TKSIAIEYGRDGIRANAIAPGTIETplvdKLTGTSEDEAGKTFRENQKWMtPLGRLGKPEEVAKLVVFLASDDSSFITGE 244


                  ....*..
gi 1958774432 165 VIRFDGG 171
Cdd:PRK08589  245 TIRIDGG 251
PRK06172 PRK06172
SDR family oxidoreductase;
48-171 6.37e-14

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 68.24  E-value: 6.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  48 LKPMLPPNAFQGKVAFI-TGGGTGLGKA--MTTFLSSLGAqcVIA-SRSLAAEWGRYGMRFNIIQPGPIKTKgAFSRLDP 123
Cdd:PRK06172  124 MKYQIPLMLAQGGGAIVnTASVAGLGAApkMSIYAASKHA--VIGlTKSAAIEYAKKGIRVNAVCPAVIDTD-MFRRAYE 200

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958774432 124 TGKFEKDMIERI-PCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK06172  201 ADPRKAEFAAAMhPVGRIGKVEEVASAVLYLCSDGASFTTGHALMVDGG 249
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 79-171 8.93e-14

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: 67.61  E-value: 8.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  79 LSSLGAQCVIAS---------------RSLAAEWGRYGMRFNIIQPGPIKTKGAFSrldptGKFEKDMIE----RIPCGR 139
Cdd:cd05372   139 LSYLGSERVVPGynvmgvakaalessvRYLAYELGRKGIRVNAISAGPIKTLAASG-----ITGFDKMLEyseqRAPLGR 213

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958774432 140 LGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:cd05372   214 NVTAEEVGNTAAFLLSDLSSGITGEIIYVDGG 245
PRK06500 PRK06500
SDR family oxidoreductase;
90-171 9.41e-14

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 67.67  E-value: 9.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKgAFSRLDPTGKFEKDMIERI----PCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:PRK06500  161 AKTLSGELLPRGIRVNAVSPGPVQTP-LYGKLGLPEATLDAVAAQIqalvPLGRFGTPEEIAKAVLYLASDESAFIVGSE 239


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:PRK06500  240 IIVDGG 245
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 90-171 1.01e-13

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: 67.30  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTG-KFEKDMIeriPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:cd05362   162 TRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAvEGYAKMS---PLGRLGEPEDIAPVVAFLASPDGRWVNGQVIRA 238


                  ...
gi 1958774432 169 DGG 171
Cdd:cd05362   239 NGG 241
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 91-171 1.09e-13

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: 67.21  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPtgKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDG 170
Cdd:cd05365   161 RNLAFDLGPKGIRVNAVAPGAVKTDALASVLTP--EIERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSG 238


                  .
gi 1958774432 171 G 171
Cdd:cd05365   239 G 239
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
90-171 1.25e-13

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 67.10  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAfsrldptGKFEKDMIER----IPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:PRK12824  163 TKALASEGARYGITVNCIAPGYIATPMV-------EQMGPEVLQSivnqIPMKRLGTPEEIAAAVAFLVSEAAGFITGET 235


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:PRK12824  236 ISINGG 241
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 70-171 1.47e-13

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 67.12  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  70 GLGKAM--TTFLSSLGAQCVIASRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDP--TGKFEKDMIERIPCGRLGTVEE 145
Cdd:PRK06463  141 GIGTAAegTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQeeAEKLRELFRNKTVLKTTGKPED 220

                          90       100
                  ....*....|....*....|....*.
gi 1958774432 146 LANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK06463  221 IANIVLFLASDDARYITGQVIVADGG 246
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 87-171 1.96e-13

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 66.53  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  87 VIA-SRSLAAEWGRYGMRFNIIQPGPIKTKgAFSRLdPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:PRK12939  163 VIGmTRSLARELGGRGITVNAIAPGLTATE-ATAYV-PADERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQL 240


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:PRK12939  241 LPVNGG 246
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
90-171 3.07e-13

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 66.30  E-value: 3.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKG-AFSRLDPtgKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK06935  174 TKAFANELAAYNIQVNAIAPGYIKTANtAPIRADK--NRNDEILKRIPAGRWGEPDDLMGAAVFLASRASDYVNGHILAV 251


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK06935  252 DGG 254
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 23-171 4.30e-13

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: 65.87  E-value: 4.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  23 RFFSFGTKTLYQSIDApqskfFPPILKPmlppnafQGKVAFITGGGTGLG---KAMTTFLSSLGAQCViASRSLAAEWGR 99
Cdd:cd05345   106 RVFAVNVKSIYLSAQA-----LVPHMEE-------QGGGVIINIASTAGLrprPGLTWYNASKGWVVT-ATKAMAVELAP 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774432 100 YGMRFNIIQPGPIKTKGAFSRLDP-TGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:cd05345   173 RNIRVNCLCPVAGETPLLSMFMGEdTPENRAKFRATIPLGRLSTPDDIANAALYLASDEASFITGVALEVDGG 245
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 90-171 4.53e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 65.84  E-value: 4.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKT---KGAFSrldptGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVI 166
Cdd:PRK06841  172 TKVLALEWGPYGITVNAISPTVVLTelgKKAWA-----GEKGERAKKLIPAGRFAYPEEIAAAALFLASDAAAMITGENL 246


                  ....*
gi 1958774432 167 RFDGG 171
Cdd:PRK06841  247 VIDGG 251
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 91-171 8.89e-13

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 65.26  E-value: 8.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIER--------IPCGRLGTVEELANLATFLCSDYASWIN 162
Cdd:PRK08339  169 RTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDRAKREGKSVEEalqeyakpIPLGRLGEPEEIGYLVAFLASDLGSYIN 248


                  ....*....
gi 1958774432 163 GAVIRFDGG 171
Cdd:PRK08339  249 GAMIPVDGG 257
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 90-171 1.49e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 64.40  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTK-GAFSRLDPtgKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK07523  170 TKGMATDWAKHGLQCNAIAPGYFDTPlNAALVADP--EFSAWLEKRTPAGRWGKVEELVGACVFLASDASSFVNGHVLYV 247


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK07523  248 DGG 250
kduD TIGR01832
2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase ...
 90-171 2.10e-12

2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase (also called 2-keto-3-deoxygluconate oxidoreductase), a member of the family of short-chain-alcohol dehydrogenases (pfam00106). This protein has been characterized in Erwinia chrysanthemi as an enzyme of pectin degradation. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 188170 [Multi-domain]  Cd Length: 248  Bit Score: 64.01  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKG-AFSRLDPtgKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:TIGR01832 164 TKLLANEWAAKGINVNAIAPGYMATNNtQALRADE--DRNAAILERIPAGRWGTPDDIGGPAVFLASSASDYVNGYTLAV 241


                  ...
gi 1958774432 169 DGG 171
Cdd:TIGR01832 242 DGG 244
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 93-172 2.40e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 64.05  E-value: 2.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  93 LAA-EWGRYGMRFNIIQPGPIKTKGAFSRLDpTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK05875  172 LAAdELGPSWVRVNSIRPGLIRTDLVAPITE-SPELSADYRACTPLPRVGEVEDVANLAMFLLSDAASWITGQVINVDGG 250


                  .
gi 1958774432 172 E 172
Cdd:PRK05875  251 H 251
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 90-171 3.50e-12

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


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 63.20  E-value: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTkGAFSRL----DPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:cd05364   165 TRCTALELAPKGVRVNSVSPGVIVT-GFHRRMgmpeEQYIKFLSRAKETHPLGRPGTVDEVAEAIAFLASDASSFITGQL 243


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:cd05364   244 LPVDGG 249
PRK06124 PRK06124
SDR family oxidoreductase;
91-171 6.69e-12

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 62.42  E-value: 6.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTK-GAFSRLDPTgkFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK06124  172 RALAAEFGPHGITSNAIAPGYFATEtNAAMAADPA--VGPWLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGHVLAVD 249


                  ..
gi 1958774432 170 GG 171
Cdd:PRK06124  250 GG 251
PRK08416 PRK08416
enoyl-ACP reductase;
91-171 7.66e-12

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 62.48  E-value: 7.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKG--AFSRLDptgKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK08416  177 KYAATELGEKNIRVNAVSGGPIDTDAlkAFTNYE---EVKAKTEELSPLNRMGQPEDLAGACLFLCSEKASWLTGQTIVV 253


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK08416  254 DGG 256
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 89-171 8.93e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 62.04  E-value: 8.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  89 ASRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKdMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK07060  160 ITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSGP-MLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLPV 238


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK07060  239 DGG 241
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 90-171 2.34e-11

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: 60.97  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKT-------KGAFSRLDPTGkfEKDMIERIPcGRLGTVEELANLATFLCSDYASWIN 162
Cdd:cd08944   161 TRTLAAELRHAGIRCNALAPGLIDTplllaklAGFEGALGPGG--FHLLIHQLQ-GRLGRPEDVAAAVVFLLSDDASFIT 237


                  ....*....
gi 1958774432 163 GAVIRFDGG 171
Cdd:cd08944   238 GQVLCVDGG 246
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
90-171 3.16e-11

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 60.66  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAfSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK08993  169 TRLMANEWAKHNINVNAIAPGYMATNNT-QQLRADEQRSAEILDRIPAGRWGLPSDLMGPVVFLASSASDYINGYTIAVD 247


                  ..
gi 1958774432 170 GG 171
Cdd:PRK08993  248 GG 249
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 90-172 3.56e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 60.69  E-value: 3.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLD----------PTGKFE-KDMIERIPCGRLGTVEELANLATFLCSDYA 158
Cdd:PRK06523  163 SKSLSKEVAPKGVRVNTVSPGWIETEAAVALAErlaeaagtdyEGAKQIiMDSLGGIPLGRPAEPEEVAELIAFLASDRA 242

                          90
                  ....*....|....
gi 1958774432 159 SWINGAVIRFDGGE 172
Cdd:PRK06523  243 ASITGTEYVIDGGT 256
PRK06138 PRK06138
SDR family oxidoreductase;
72-171 3.65e-11

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 60.55  E-value: 3.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  72 GKAMTTFLSSLGAqcvIAS--RSLAAEWGRYGMRFNIIQPGPIKT---KGAFSRLDPTGKFEKDMIERIPCGRLGTVEEL 146
Cdd:PRK06138  147 GRGRAAYVASKGA---IASltRAMALDHATDGIRVNAVAPGTIDTpyfRRIFARHADPEALREALRARHPMNRFGTAEEV 223

                          90       100
                  ....*....|....*....|....*
gi 1958774432 147 ANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK06138  224 AQAALFLASDESSFATGTTLVVDGG 248
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 46-171 4.61e-11

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 60.12  E-value: 4.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  46 PILKPMLPPNAFqGKVAFI--TGGGTGLGKAMTTFLSSLGAqcVIASRSLAAEWGRYGMRFNIIQPGPIKTKGAfSRLDP 123
Cdd:PRK12827  128 AALPPMIRARRG-GRIVNIasVAGVRGNRGQVNYAASKAGL--IGLTKTLANELAPRGITVNAVAPGAINTPMA-DNAAP 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958774432 124 TGKFEKDMieriPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK12827  204 TEHLLNPV----PVQRLGEPDEVAALVAFLVSDAASYVTGQVIPVDGG 247
PRK07856 PRK07856
SDR family oxidoreductase;
89-177 4.69e-11

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 59.95  E-value: 4.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  89 ASRSLAAEWGRyGMRFNIIQPGPIKTKGAFSRL-DPTGKfekDMIER-IPCGRLGTVEELANLATFLCSDYASWINGAVI 166
Cdd:PRK07856  158 LTRSLAVEWAP-KVRVNAVVVGLVRTEQSELHYgDAEGI---AAVAAtVPLGRLATPADIAWACLFLASDLASYVSGANL 233

                          90
                  ....*....|...
gi 1958774432 167 RFDGGEE--VFLS 177
Cdd:PRK07856  234 EVHGGGErpAFLA 246
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
90-171 7.13e-11

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 59.81  E-value: 7.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRL------DPTGKFEkDMIERIPCGRLGTVEELANLATFLCSDYASWING 163
Cdd:PRK08226  166 TKSLAVEYAQSGIRVNAICPGYVRTPMAESIArqsnpeDPESVLT-EMAKAIPLRRLADPLEVGELAAFLASDESSYLTG 244


                  ....*...
gi 1958774432 164 AVIRFDGG 171
Cdd:PRK08226  245 TQNVIDGG 252
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 59-171 7.50e-11

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 59.70  E-value: 7.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  59 GKVAFITGGGTgLGkAMTTFLSSLGAQCVIAS--RSLAAEWGRYGMRFNIIQPGPIKTKGAfsrldpTGKFEKDMIERIP 136
Cdd:PRK12748  147 GRIINLTSGQS-LG-PMPDELAYAATKGAIEAftKSLAPELAEKGITVNAVNPGPTDTGWI------TEELKHHLVPKFP 218

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958774432 137 CGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK12748  219 QGRVGEPVDAARLIAFLVSEEAKWITGQVIHSEGG 253
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
91-171 8.32e-11

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 59.24  E-value: 8.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTK--GAFSRLDPTGKFEKDMIeriPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK12428  150 RQAQPWFGARGIRVNCVAPGPVFTPilGDFRSMLGQERVDSDAK---RMGRPATADEQAAVLVFLCSDAARWINGVNLPV 226


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK12428  227 DGG 229
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 84-171 9.99e-11

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: 59.27  E-value: 9.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  84 AQCVIASRSLAAEWGRYGMRFNIIQPGPIKTkgafsrlDPTGKFEKDMIER----IPCGRLGTVEELANLATFLCSDYAS 159
Cdd:cd05352   165 AAVIHLAKSLAVEWAKYFIRVNSISPGYIDT-------DLTDFVDKELRKKwesyIPLKRIALPEELVGAYLYLASDASS 237

                          90
                  ....*....|..
gi 1958774432 160 WINGAVIRFDGG 171
Cdd:cd05352   238 YTTGSDLIIDGG 249
PRK07074 PRK07074
SDR family oxidoreductase;
90-171 1.06e-10

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 59.01  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK07074  159 TKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAANPQVFEELKKWYPLQDFATPDDVANAVLFLASPAARAITGVCLPVD 238


                  ..
gi 1958774432 170 GG 171
Cdd:PRK07074  239 GG 240
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 75-171 1.15e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 59.31  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  75 MTTFLSSLGAQCVIA-----------SRSLAAEWGRYGMRFNIIQPG--------PIKTKGAFSRLDPtgkFEKDMIERI 135
Cdd:PRK07097  144 ICSMMSELGRETVSAyaaakgglkmlTKNIASEYGEANIQCNGIGPGyiatpqtaPLRELQADGSRHP---FDQFIIAKT 220

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958774432 136 PCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK07097  221 PAARWGDPEDLAGPAVFLASDASNFVNGHILYVDGG 256
PRK06949 PRK06949
SDR family oxidoreductase;
79-171 1.23e-10

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 59.01  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  79 LSSLGAQC------VIASRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKfeKDMIERIPCGRLGTVEELANLATF 152
Cdd:PRK06949  160 LPQIGLYCmskaavVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQG--QKLVSMLPRKRVGKPEDLDGLLLL 237

                          90
                  ....*....|....*....
gi 1958774432 153 LCSDYASWINGAVIRFDGG 171
Cdd:PRK06949  238 LAADESQFINGAIISADDG 256
PRK06114 PRK06114
SDR family oxidoreductase;
90-171 1.52e-10

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 58.64  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPG----PIKTKGAFSRLdpTGKFEkdmiERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:PRK06114  171 SKSLAMEWVGRGIRVNSISPGytatPMNTRPEMVHQ--TKLFE----EQTPMQRMAKVDEMVGPAVFLLSDAASFCTGVD 244


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:PRK06114  245 LLVDGG 250
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 90-171 1.74e-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: 58.65  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTK-GAFSRLDPTGKfeKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:cd08942   170 TRKLAKELAGEHITVNAIAPGRFPSKmTAFLLNDPAAL--EAEEKSIPLGRWGRPEDMAGLAIMLASRAGAYLTGAVIPV 247


                  ...
gi 1958774432 169 DGG 171
Cdd:cd08942   248 DGG 250
PRK07063 PRK07063
SDR family oxidoreductase;
90-174 2.10e-10

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 58.52  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLD--PTGKFEKDMIERI-PCGRLGTVEELANLATFLCSDYASWINGAVI 166
Cdd:PRK07063  169 TRALGIEYAARNVRVNAIAPGYIETQLTEDWWNaqPDPAAARAETLALqPMKRIGRPEEVAMTAVFLASDEAPFINATCI 248


                  ....*...
gi 1958774432 167 RFDGGEEV 174
Cdd:PRK07063  249 TIDGGRSV 256
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
90-171 2.36e-10

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 57.99  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTkgafsrlDPTGKFEKD------MIERIPCGRLGTVEELANLATFLCSDYASWING 163
Cdd:PRK12481  167 TRALATELSQYNINVNAIAPGYMAT-------DNTAALRADtarneaILERIPASRWGTPDDLAGPAIFLSSSASDYVTG 239


                  ....*...
gi 1958774432 164 AVIRFDGG 171
Cdd:PRK12481  240 YTLAVDGG 247
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
91-174 3.20e-10

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 58.06  E-value: 3.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAfSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDG 170
Cdd:PRK08690  172 RFTAACLGKEGIRCNGISAGPIKTLAA-SGIADFGKLLGHVAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDG 250


                  ....
gi 1958774432 171 GEEV 174
Cdd:PRK08690  251 GYSI 254
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
44-171 3.84e-10

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 57.52  E-value: 3.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  44 FPPILK---PMLPPNA------FQGKVAFITGGGT-GLGKAmttflsSLGAqcviASRSLAAEWGRYGMRFNIIQPGPIK 113
Cdd:PRK06997  124 FPALAKaalPMLSDDAslltlsYLGAERVVPNYNTmGLAKA------SLEA----SVRYLAVSLGPKGIRANGISAGPIK 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774432 114 TKGAfSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK06997  194 TLAA-SGIKDFGKILDFVESNAPLRRNVTIEEVGNVAAFLLSDLASGVTGEITHVDSG 250
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 91-171 4.07e-10

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: 57.34  E-value: 4.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAFSrldptgkFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDG 170
Cdd:cd08930   177 KYLAKYYADTGIRVNAISPGGILNNQPSE-------FLEKYTKKCPLKRMLNPEDLRGAIIFLLSDASSYVTGQNLVIDG 249


                  .
gi 1958774432 171 G 171
Cdd:cd08930   250 G 250
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
91-174 5.58e-10

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 57.03  E-value: 5.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAfsrlDPTGKFeKDMI----ERIPCGRLGTVEELANLATFLCSDYASWINGAVI 166
Cdd:PRK07370  173 RYLAAELGPKNIRVNAISAGPIRTLAS----SAVGGI-LDMIhhveEKAPLRRTVTQTEVGNTAAFLLSDLASGITGQTI 247


                  ....*...
gi 1958774432 167 RFDGGEEV 174
Cdd:PRK07370  248 YVDAGYCI 255
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 90-171 5.76e-10

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 57.10  E-value: 5.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTkGAFSRldptgKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK12859  179 TSSLAAEVAHLGITVNAINPGPTDT-GWMTE-----EIKQGLLPMFPFGRIGEPKDAARLIKFLASEEAEWITGQIIHSE 252


                  ..
gi 1958774432 170 GG 171
Cdd:PRK12859  253 GG 254
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 90-171 6.36e-10

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: 57.08  E-value: 6.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPtgkfEKDMIERI------PCGRLGTVEELANLATFLCSDYASWING 163
Cdd:cd05326   164 TRSAATELGEHGIRVNCVSPYGVATPLLTAGFGV----EDEAIEEAvrgaanLKGTALRPEDIAAAVLYLASDDSRYVSG 239


                  ....*...
gi 1958774432 164 AVIRFDGG 171
Cdd:cd05326   240 QNLVVDGG 247
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 52-171 6.93e-10

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: 57.08  E-value: 6.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  52 LPPNAFqGKVAFITGGGTGLGKA-MTTFlSSL-------GAQCVIA--SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRL 121
Cdd:cd08935   133 LPSQVF-GKDMLEQKGGSIINISsMNAF-SPLtkvpaysAAKAAVSnfTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLL 210

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958774432 122 -DPTGKFE---KDMIERIPCGRLGTVEELANLATFLCSD-YASWINGAVIRFDGG 171
Cdd:cd08935   211 iNPDGSYTdrsNKILGRTPMGRFGKPEELLGALLFLASEkASSFVTGVVIPVDGG 265
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 76-171 8.11e-10

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 56.71  E-value: 8.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  76 TTFLSSLGAQCVIaSRSLAAEWGRYGMRFNIIQPGPIKTK-GAFSRLDPtgKFEKDMIERIPCGRLGTVEELANLATFLC 154
Cdd:cd05351   147 TVYCSTKAALDML-TKVMALELGPHKIRVNSVNPTVVMTDmGRDNWSDP--EKAKKMLNRIPLGKFAEVEDVVNAILFLL 223

                          90
                  ....*....|....*..
gi 1958774432 155 SDYASWINGAVIRFDGG 171
Cdd:cd05351   224 SDKSSMTTGSTLPVDGG 240
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 63-171 1.16e-09

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 56.12  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  63 FITGGGtglGKAMTTflsslgAQCVIA--SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPtGKFEKDMIERIPCGRL 140
Cdd:PRK06550  131 FVAGGG---GAAYTA------SKHALAgfTKQLALDYAKDGIQVFGIAPGAVKTPMTAADFEP-GGLADWVARETPIKRW 200

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958774432 141 GTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK06550  201 AEPEEVAELTLFLASGKADYMQGTIVPIDGG 231
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 93-171 1.27e-09

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 55.90  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  93 LAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPtgkfekDMIERI----PCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK12937  167 LANELRGRGITVNAVAPGPVATELFFNGKSA------EQIDQLaglaPLERLGTPEEIAAAVAFLAGPDGAWVNGQVLRV 240


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK12937  241 NGG 243
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 59-171 1.37e-09

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: 56.05  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  59 GKVAFITGGgTGLG--KAMTTFLSSLGAQCVIASrSLAAEWGRYGMRFNIIQPGPIKTKGAFsrldPTGKFE-----KDM 131
Cdd:cd05361   125 GSIIFITSA-VPKKplAYNSLYGPARAAAVALAE-SLAKELSRDNILVYAIGPNFFNSPTYF----PTSDWEnnpelRER 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958774432 132 IER-IPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:cd05361   199 VKRdVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFAGG 239
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
91-171 1.57e-09

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 55.89  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKT---KGafsrldpTGKFE---KDMIERIPCGRLGTVEELANLATFLCSDYASWINGA 164
Cdd:PRK08594  173 KYLANDLGKDGIRVNAISAGPIRTlsaKG-------VGGFNsilKEIEERAPLRRTTTQEEVGDTAAFLFSDLSRGVTGE 245


                  ....*..
gi 1958774432 165 VIRFDGG 171
Cdd:PRK08594  246 NIHVDSG 252
PRK08340 PRK08340
SDR family oxidoreductase;
90-170 2.04e-09

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 55.58  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRL---------DPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASW 160
Cdd:PRK08340  162 AKGVSRTYGGKGIRAYTVLLGSFDTPGARENLariaeergvSFEETWEREVLERTPLKRTGRWEELGSLIAFLLSENAEY 241

                          90
                  ....*....|
gi 1958774432 161 INGAVIRFDG 170
Cdd:PRK08340  242 MLGSTIVFDG 251
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
79-171 2.78e-09

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 55.11  E-value: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  79 LSSLGAQCVIA---------------SRSLAAEWGRYGMRFNIIQPGPIKTKgAFSRLDPTGKFEKDMIERIPCGRLGTV 143
Cdd:PRK08063  139 LSSLGSIRYLEnyttvgvskaalealTRYLAVELAPKGIAVNAVSGGAVDTD-ALKHFPNREELLEDARAKTPAGRMVEP 217

                          90       100
                  ....*....|....*....|....*...
gi 1958774432 144 EELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK08063  218 EDVANAVLFLCSPEADMIRGQTIIVDGG 245
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 90-171 3.37e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 54.74  E-value: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTkgafsrldPTGK--FEKDMiER-------IPCGRLGTVEELANLATFLCSDYASW 160
Cdd:PRK06057  165 SRELGVQFARQGIRVNALCPGPVNT--------PLLQelFAKDP-ERaarrlvhVPMGRFAEPEEIAAAVAFLASDDASF 235

                          90
                  ....*....|.
gi 1958774432 161 INGAVIRFDGG 171
Cdd:PRK06057  236 ITASTFLVDGG 246
PRK05867 PRK05867
SDR family oxidoreductase;
84-171 4.12e-09

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 54.66  E-value: 4.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  84 AQCVIASRSLAAEWGRYGMRFNIIQPGPIKTKgafsRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWING 163
Cdd:PRK05867  166 AAVIHLTKAMAVELAPHKIRVNSVSPGYILTE----LVEPYTEYQPLWEPKIPLGRLGRPEELAGLYLYLASEASSYMTG 241


                  ....*...
gi 1958774432 164 AVIRFDGG 171
Cdd:PRK05867  242 SDIVIDGG 249
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 90-171 4.92e-09

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: 54.47  E-value: 4.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKgaFSRLDPTGK-FEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:cd08936   171 TKNLAPELAPRNIRVNCLAPGLIKTS--FSSALWMDKaVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASYITGETVVV 248


                  ...
gi 1958774432 169 DGG 171
Cdd:cd08936   249 GGG 251
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 92-172 1.33e-08

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 53.30  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  92 SLAAEWGRYGMRFNIIQPGPIKTK--------GAFSRLDPT--GKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWI 161
Cdd:cd08937   164 SLAFEHARDGIRVNAVAPGGTEAPprkiprnaAPMSEQEKVwyQRIVDQTLDSSLMGRYGTIDEQVRAILFLASDEASYI 243

                          90
                  ....*....|.
gi 1958774432 162 NGAVIRFDGGE 172
Cdd:cd08937   244 TGTVLPVGGGD 254
PRK07984 PRK07984
enoyl-ACP reductase FabI;
70-171 1.45e-08

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 52.98  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  70 GLGKAmttflsSLGAQCviasRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDptgkFEKdMIER----IPCGRLGTVEE 145
Cdd:PRK07984  160 GLAKA------SLEANV----RYMANAMGPEGVRVNAISAGPIRTLAASGIKD----FRK-MLAHceavTPIRRTVTIED 224

                          90       100
                  ....*....|....*....|....*.
gi 1958774432 146 LANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK07984  225 VGNSAAFLCSDLSAGISGEVVHVDGG 250
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 87-171 1.52e-08

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: 52.97  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  87 VIASRSLAAEWGRYgMRFNIIQPGPIKTKGAFSRldPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVI 166
Cdd:cd09761   154 VALTHALAMSLGPD-IRVNCISPGWINTTEQQEF--TAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETF 230


                  ....*
gi 1958774432 167 RFDGG 171
Cdd:cd09761   231 IVDGG 235
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 94-171 2.61e-08

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 52.27  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  94 AAEWGRYGMRFNIIQPGPIKTkgafsrlDPTGKFEKDMIER----IPCGRLGTVEELANLATF-LCSDYaswINGAVIRF 168
Cdd:PRK08217  178 AKELARYGIRVAAIAPGVIET-------EMTAAMKPEALERlekmIPVGRLGEPEEIAHTVRFiIENDY---VTGRVLEI 247


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK08217  248 DGG 250
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 90-171 3.58e-08

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 52.01  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAfSRLDPTGKFekDMIER-IPCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK08642  170 TRNLAAELGPYGITVNMVSGGLLRTTDA-SAATPDEVF--DLIAAtTPLRKVTTPQEFADAVLFFASPWARAVTGQNLVV 246


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK08642  247 DGG 249
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 90-172 3.64e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 51.97  E-value: 3.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKT-------KG-AFSRLDPTGKFEKDMiERIPCGRLGTVEELANLATFLCSDYASWI 161
Cdd:PRK06125  164 TRALGGKSLDDGVRVVGVNPGPVATdrmltllKGrARAELGDESRWQELL-AGLPLGRPATPEEVADLVAFLASPRSGYT 242

                          90
                  ....*....|.
gi 1958774432 162 NGAVIRFDGGE 172
Cdd:PRK06125  243 SGTVVTVDGGI 253
PRK07035 PRK07035
SDR family oxidoreductase;
90-171 3.78e-08

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 51.94  E-value: 3.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAfSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK07035  169 TKAFAKECAPFGIRVNALLPGLTDTKFA-SALFKNDAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTGECLNVD 247


                  ..
gi 1958774432 170 GG 171
Cdd:PRK07035  248 GG 249
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
 70-171 4.27e-08

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 52.08  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  70 GLGKAMttflSSLGAQCVIASRSLAAEWGR-YGMRFNIIQPGPIKTKGAfsrlDPTGkFEKDMIE----RIPCGRLGTVE 144
Cdd:PLN02730  188 GYGGGM----SSAKAALESDTRVLAFEAGRkYKIRVNTISAGPLGSRAA----KAIG-FIDDMIEysyaNAPLQKELTAD 258

                          90       100
                  ....*....|....*....|....*..
gi 1958774432 145 ELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PLN02730  259 EVGNAAAFLASPLASAITGATIYVDNG 285
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 93-171 4.58e-08

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 51.82  E-value: 4.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  93 LAAEWGRYGMRFNIIQPGPIKTKGAFSRL-DPTGKFE---KDMIERIPCGRLGTVEELANLATFLCSD-YASWINGAVIR 167
Cdd:PRK08277  188 LAVHFAKVGIRVNAIAPGFFLTEQNRALLfNEDGSLTeraNKILAHTPMGRFGKPEELLGTLLWLADEkASSFVTGVVLP 267


                  ....
gi 1958774432 168 FDGG 171
Cdd:PRK08277  268 VDGG 271
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 90-171 5.65e-08

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 51.43  E-value: 5.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKT---------KGAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASW 160
Cdd:PRK12429  164 TKVVALEGATHGVTVNAICPGYVDTplvrkqipdLAKERGISEEEVLEDVLLPLVPQKRFTTVEEIADYALFLASFAAKG 243

                          90
                  ....*....|.
gi 1958774432 161 INGAVIRFDGG 171
Cdd:PRK12429  244 VTGQAWVVDGG 254
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
91-171 5.96e-08

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 51.26  E-value: 5.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTkgafsrLDPTG-KFEKDMI----ERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:PRK06079  169 RYLARDLGKKGIRVNAISAGAVKT------LAVTGiKGHKDLLkesdSRTVDGVGVTIEEVGNTAAFLLSDLSTGVTGDI 242


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:PRK06079  243 IYVDKG 248
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 89-172 7.24e-08

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 51.11  E-value: 7.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  89 ASRSLAAEWGRYGMRFNIIQPGPI---KTKGAFSRLDPT-GKFEKDMIE----RIPCGRLGTVEELANLATFLCSDYASW 160
Cdd:PRK07890  164 ASQSLATELGPQGIRVNSVAPGYIwgdPLKGYFRHQAGKyGVTVEQIYAetaaNSDLKRLPTDDEVASAVLFLASDLARA 243

                          90
                  ....*....|..
gi 1958774432 161 INGAVIRFDGGE 172
Cdd:PRK07890  244 ITGQTLDVNCGE 255
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 90-171 1.24e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 50.39  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGpiktkGAFSR-LDPTGKFEKDMIERI-----PCGRLGTVEELANLATFLCSDYASWING 163
Cdd:PRK08265  161 TRSMAMDLAPDGIRVNSVSPG-----WTWSRvMDELSGGDRAKADRVaapfhLLGRVGDPEEVAQVVAFLCSDAASFVTG 235


                  ....*...
gi 1958774432 164 AVIRFDGG 171
Cdd:PRK08265  236 ADYAVDGG 243
PRK06947 PRK06947
SDR family oxidoreductase;
93-171 1.57e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 50.19  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  93 LAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPtgkfekDMIERI----PCGRLGTVEELANLATFLCSDYASWINGAVIRF 168
Cdd:PRK06947  171 LAKELGPHGVRVNAVRPGLIETEIHASGGQP------GRAARLgaqtPLGRAGEADEVAETIVWLLSDAASYVTGALLDV 244


                  ...
gi 1958774432 169 DGG 171
Cdd:PRK06947  245 GGG 247
PRK12743 PRK12743
SDR family oxidoreductase;
91-171 2.02e-07

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 49.65  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTkgAFSRLDPTGKFEKDMiERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDG 170
Cdd:PRK12743  165 KAMALELVEHGILVNAVAPGAIAT--PMNGMDDSDVKPDSR-PGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSLIVDG 241


                  .
gi 1958774432 171 G 171
Cdd:PRK12743  242 G 242
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 88-171 2.18e-07

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: 49.69  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  88 IASRSLAAEWG--RYGMRFNIIQPGPIKTKGAFSRLDPTGkfEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:cd05341   160 GLTKSAALECAtqGYGIRVNSVHPGYIYTPMTDELLIAQG--EMGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVTGSE 237


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:cd05341   238 LVVDGG 243
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 72-171 3.48e-07

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: 49.15  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  72 GKAMTTFLSSLGAQCVIASRSLAAEWGRYGMRFNIIQPGPIKTK------GAFSRLD--PTGKFEKDMIERIPCGRLGTV 143
Cdd:cd05363   143 GEALVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEhwdgvdAKFARYEnrPRGEKKRLVGEAVPFGRMGRA 222

                          90       100
                  ....*....|....*....|....*...
gi 1958774432 144 EELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:cd05363   223 EDLTGMAIFLASTDADYIVAQTYNVDGG 250
PRK06123 PRK06123
SDR family oxidoreductase;
90-171 3.49e-07

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 49.01  E-value: 3.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEwgryGMRFNIIQPGPIKTKGAFSRLDPtGKFEKdMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK06123  172 AKEVAAE----GIRVNAVRPGVIYTEIHASGGEP-GRVDR-VKAGIPMGRGGTAEEVARAILWLLSDEASYTTGTFIDVS 245


                  ..
gi 1958774432 170 GG 171
Cdd:PRK06123  246 GG 247
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 50-171 4.41e-07

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 48.60  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  50 PMLPPnafqGKVAFITGGGTGLGKAMTTFLSSLGAQCVIA--SRSLAAEWGRYGMRFNIIQPGPIktkgafsrldpTGKF 127
Cdd:PRK05786  123 RFLKE----GSSIVLVSSMSGIYKASPDQLSYAVAKAGLAkaVEILASELLGRGIRVNGIAPTTI-----------SGDF 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958774432 128 EKDMIERIPcGRLGTV----EELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK05786  188 EPERNWKKL-RKLGDDmappEDFAKVIIWLLTDEADWVDGVVIPVDGG 234
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
48-95 8.73e-07

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 48.69  E-value: 8.73e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958774432  48 LKPMLPPNAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:PRK08324  411 LQRMPKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEA 458
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 131-171 1.09e-06

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: 47.83  E-value: 1.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958774432 131 MIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:cd08940   214 LLEKQPSKQFVTPEQLGDTAVFLASDAASQITGTAVSVDGG 254
PRK12742 PRK12742
SDR family oxidoreductase;
91-171 1.30e-06

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 47.44  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKgafsrLDPTGKFEKDMIER-IPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK12742  158 RGLARDFGPRGITINVVQPGPIDTD-----ANPANGPMKDMMHSfMAIKRHGRPEEVAGMVAWLAGPEASFVTGAMHTID 232


                  ..
gi 1958774432 170 GG 171
Cdd:PRK12742  233 GA 234
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 90-171 1.34e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 47.72  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKgafsrLDPTGKFEKDMIE---RIPCGRLGTVEELANLATFLCSDYASWINGAVI 166
Cdd:PRK06701  206 TRSLAQSLVQKGIRVNAVAPGPIWTP-----LIPSDFDEEKVSQfgsNTPMQRPGQPEELAPAYVFLASPDSSYITGQML 280


                  ....*
gi 1958774432 167 RFDGG 171
Cdd:PRK06701  281 HVNGG 285
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 90-175 1.45e-06

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: 47.29  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKgafsrLDPTGKFEKDMIE---RIPCGRLGTVEELANLATFLCSDYASWINGAVI 166
Cdd:cd05355   187 TRGLSLQLAEKGIRVNAVAPGPIWTP-----LIPSSFPEEKVSEfgsQVPMGRAGQPAEVAPAYVFLASQDSSYVTGQVL 261


                  ....*....
gi 1958774432 167 RFDGGEEVF 175
Cdd:cd05355   262 HVNGGEIIN 270
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 90-171 2.08e-06

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 46.84  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGpiktkgaFSRLDPTGKFE--KDMIERIPCG-RLGTVEELANLATFLCSDYASWINGAVI 166
Cdd:TIGR02685 184 TRSAALELAPLQIRVNGVAPG-------LSLLPDAMPFEvqEDYRRKVPLGqREASAEQIADVVIFLVSPKAKYITGTCI 256


                  ....*
gi 1958774432 167 RFDGG 171
Cdd:TIGR02685 257 KVDGG 261
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 58-98 2.08e-06

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: 46.71  E-value: 2.08e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958774432  58 QGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS------LAAEWG 98
Cdd:COG4221     4 KGKVALITGASSGIGAATARALAAAGARVVLAARRaerleaLAAELG 50
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 90-171 2.95e-06

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: 46.22  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKF-----EKDMIE---RIPCGRLGTVEELANLATFLCSDYASWI 161
Cdd:cd05366   164 TQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEIagkpeGEGFAEfssSIPLGRLSEPEDVAGLVSFLASEDSDYI 243

                          90
                  ....*....|
gi 1958774432 162 NGAVIRFDGG 171
Cdd:cd05366   244 TGQTILVDGG 253
PLN02253 PLN02253
xanthoxin dehydrogenase
 83-171 2.96e-06

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 46.35  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  83 GAQCVIA--SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIE-RIPCGRLG-------TVEELANLATF 152
Cdd:PLN02253  170 GSKHAVLglTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTEDALAGfRAFAGKNAnlkgvelTVDDVANAVLF 249

                          90
                  ....*....|....*....
gi 1958774432 153 LCSDYASWINGAVIRFDGG 171
Cdd:PLN02253  250 LASDEARYISGLNLMIDGG 268
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 58-171 3.51e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 46.29  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  58 QGKVAFITGGGTGLGK-AMTTFLSSLGAQCVIaSRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDpTGKFEKDMIERIP 136
Cdd:PRK08085  137 AGKIINICSMQSELGRdTITPYAASKGAVKML-TRGMCVELARHNIQVNGIAPGYFKTEMTKALVE-DEAFTAWLCKRTP 214

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958774432 137 CGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK08085  215 AARWGDPQELIGAAVFLSSKASDFVNGHLLFVDGG 249
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 91-171 4.26e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 46.08  E-value: 4.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKgAFSRLDPTGKFeKDMIERI-PCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK07478  169 QVLAAEYGAQGIRVNALLPGGTDTP-MGRAMGDTPEA-LAFVAGLhALKRMAQPEEIAQAALFLASDAASFVTGTALLVD 246


                  ..
gi 1958774432 170 GG 171
Cdd:PRK07478  247 GG 248
PRK07985 PRK07985
SDR family oxidoreductase;
90-174 4.45e-06

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 46.14  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKgafsrLDPTGKFEKDMI----ERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:PRK07985  210 SRGLAKQVAEKGIRVNIVAPGPIWTA-----LQISGGQTQDKIpqfgQQTPMKRAGQPAELAPVYVYLASQESSYVTAEV 284


                  ....*....
gi 1958774432 166 IRFDGGEEV 174
Cdd:PRK07985  285 HGVCGGEHL 293
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 90-174 4.60e-06

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: 45.99  E-value: 4.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKT----KGAFSRLDPTGKFEKDMIERiPCGRLGTVEELANLATFLCSDyASWINGAV 165
Cdd:cd08933   170 TKALAVDESRYGVRVNCISPGNIWTplweELAAQTPDTLATIKEGELAQ-LLGRMGTEAESGLAALFLAAE-ATFCTGID 247


                  ....*....
gi 1958774432 166 IRFDGGEEV 174
Cdd:cd08933   248 LLLSGGAEL 256
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
70-176 5.62e-06

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 45.99  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  70 GLGKAMTTFLSslgaqcviasRSLAAEWGRYGMRFNIIQPGPIktkgaFSRldpTGKFEKDMIER------IPCGRLG-- 141
Cdd:PRK08324  572 GAAKAAELHLV----------RQLALELGPDGIRVNGVNPDAV-----VRG---SGIWTGEWIEAraaaygLSEEELEef 633

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958774432 142 -----------TVEELANLATFLCSDYASWINGAVIRFDGG-EEVFL 176
Cdd:PRK08324  634 yrarnllkrevTPEDVAEAVVFLASGLLSKTTGAIITVDGGnAAAFL 680
PRK06398 PRK06398
aldose dehydrogenase; Validated
 136-171 6.61e-06

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 45.21  E-value: 6.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958774432 136 PCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK06398  208 PMKRVGKPEEVAYVVAFLASDLASFITGECVTVDGG 243
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
91-171 8.01e-06

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 45.12  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAFSrldpTGKFEkdMIER-----IPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:PRK08415  169 RYLAVDLGKKGIRVNAISAGPIKTLAASG----IGDFR--MILKwneinAPLKKNVSIEEVGNSGMYLLSDLSSGVTGEI 242


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:PRK08415  243 HYVDAG 248
PRK08628 PRK08628
SDR family oxidoreductase;
60-171 1.02e-05

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 44.95  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  60 KVAfITG-GGTglgkamTTFLSSLGAQCVIaSRSLAAEWGRYGMRFNIIQPG----P-----IKTKGafsrlDPTGKFEK 129
Cdd:PRK08628  141 KTA-LTGqGGT------SGYAAAKGAQLAL-TREWAVALAKDGVRVNAVIPAevmtPlyenwIATFD-----DPEAKLAA 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958774432 130 dMIERIPCG-RLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK08628  208 -ITAKIPLGhRMTTAEEIADTAVFLLSERSSHTTGQWLFVDGG 249
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
 70-171 1.23e-05

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 44.81  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  70 GLGKAMttflSSLGAQCVIASRSLAAEWGR-YGMRFNIIQPGPIKtkgafSRLDPTGKFEKDMI----ERIPCGRLGTVE 144
Cdd:PRK06300  187 GYGGGM----SSAKAALESDTKVLAWEAGRrWGIRVNTISAGPLA-----SRAGKAIGFIERMVdyyqDWAPLPEPMEAE 257

                          90       100
                  ....*....|....*....|....*..
gi 1958774432 145 ELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK06300  258 QVGAAAAFLVSPLASAITGETLYVDHG 284
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
87-171 1.77e-05

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 44.25  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  87 VI-ASRSLAAEWGRYGMRFNIIQPGPIKTK------GAFSRLD--PTGKFEKDMIERIPCGRLGTVEELANLATFLCSDY 157
Cdd:PRK07067  160 VIsYTQSAALALIRHGINVNAIAPGVVDTPmwdqvdALFARYEnrPPGEKKRLVGEAVPLGRMGVPDDLTGMALFLASAD 239

                          90
                  ....*....|....
gi 1958774432 158 ASWINGAVIRFDGG 171
Cdd:PRK07067  240 ADYIVAQTYNVDGG 253
PRK06949 PRK06949
SDR family oxidoreductase;
57-93 1.80e-05

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 43.98  E-value: 1.80e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSL 93
Cdd:PRK06949    7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRV 43
PRK06128 PRK06128
SDR family oxidoreductase;
50-171 1.85e-05

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 44.08  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  50 PMLPPNAfqgkvAFITGGGTGLGKAMTTFL--SSLGAQCVIASRSLAAEWGRYGMRFNIIQPGPIKTKgafsrLDPTGKF 127
Cdd:PRK06128  179 PHLPPGA-----SIINTGSIQSYQPSPTLLdyASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTP-----LQPSGGQ 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958774432 128 EKDMIERI----PCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK06128  249 PPEKIPDFgsetPMKRPGQPVEMAPLYVLLASQESSYVTGEVFGVTGG 296
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 60-108 2.65e-05

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 42.99  E-value: 2.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958774432  60 KVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS------LAAEWGRYGMRFNIIQ 108
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSeekleaVAKELGALGGKALFIQ 55
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 92-171 2.65e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 43.52  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  92 SLAAEWGRYGMRFNIIQPGPIKTKGAFSRL-DPTGKFEKDMIERIpcGRLGTVEELANLATFLCSDYASWINGAVIRFDG 170
Cdd:PRK12747  171 TLAKQLGARGITVNAILPGFIKTDMNAELLsDPMMKQYATTISAF--NRLGEVEDIADTAAFLASPDSRWVTGQLIDVSG 248


                  .
gi 1958774432 171 G 171
Cdd:PRK12747  249 G 249
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 90-171 3.56e-05

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 43.08  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKG----------AFSRldptGKFEKDMIE------RIPCGRLGTVEELANLATFL 153
Cdd:PRK06171  169 TRSWAKELGKHNIRVVGVAPGILEATGlrtpeyeealAYTR----GITVEQLRAgytktsTIPLGRSGKLSEVADLVCYL 244

                          90
                  ....*....|....*...
gi 1958774432 154 CSDYASWINGAVIRFDGG 171
Cdd:PRK06171  245 LSDRASYITGVTTNIAGG 262
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 61-171 3.59e-05

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 43.07  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  61 VAFITGGGTGLGKamtTFLSSLGAQCVIASRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRldPTGKFEKdMIERIPCGRL 140
Cdd:PRK12935  141 ISSIIGQAGGFGQ---TNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEV--PEEVRQK-IVAKIPKKRF 214

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958774432 141 GTVEELANLATFLCSDYAsWINGAVIRFDGG 171
Cdd:PRK12935  215 GQADEIAKGVVYLCRDGA-YITGQQLNINGG 244
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 90-171 3.97e-05

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 42.98  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKgafsrldPTGKF---EKDMI-ERIPCGRLGTVEELANLATFLCSDYASWINGAV 165
Cdd:PRK12936  163 SKSLAQEIATRNVTVNCVAPGFIESA-------MTGKLndkQKEAImGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQT 235


                  ....*.
gi 1958774432 166 IRFDGG 171
Cdd:PRK12936  236 IHVNGG 241
PRK07069 PRK07069
short chain dehydrogenase; Validated
 90-171 4.91e-05

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 42.77  E-value: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGM--RFNIIQPGPIKT---KGAFSRLDPTGKFEKdMIERIPCGRLGTVEELANLATFLCSDYASWINGA 164
Cdd:PRK07069  162 TKSIALDCARRGLdvRCNSIHPTFIRTgivDPIFQRLGEEEATRK-LARGVPLGRLGEPDDVAHAVLYLASDESRFVTGA 240


                  ....*..
gi 1958774432 165 VIRFDGG 171
Cdd:PRK07069  241 ELVIDGG 247
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 70-171 5.51e-05

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: 42.76  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  70 GLGKAMTTFLSslgaqcviasRSLAAEWGRYGMRFNIIQPGPIKTKGAFS-------RLDPTGKFEKDMIERIPCGRLGT 142
Cdd:cd08943   151 SAAKAAEAHLA----------RCLALEGGEDGIRVNTVNPDAVFRGSKIWegvwraaRAKAYGLLEEEYRTRNLLKREVL 220

                          90       100
                  ....*....|....*....|....*....
gi 1958774432 143 VEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:cd08943   221 PEDVAEAVVAMASEDFGKTTGAIVTVDGG 249
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
56-108 6.10e-05

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 42.55  E-value: 6.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774432  56 AFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS------LAAEWGRYGMRFNIIQ 108
Cdd:COG0300     2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDaerleaLAAELRAAGARVEVVA 60
PRK09730 PRK09730
SDR family oxidoreductase;
93-171 6.33e-05

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 42.53  E-value: 6.33e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774432  93 LAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPtGKFEKdMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK09730  170 LSLEVAAQGIRVNCVRPGFIYTEMHASGGEP-GRVDR-VKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTGSFIDLAGG 246
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 90-175 6.40e-05

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 42.33  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPT---------GKFEKDMIERIPCGRLGTVEELANLATFLCSDYASW 160
Cdd:PRK12384  165 TQSLALDLAEYGITVHSLMLGNLLKSPMFQSLLPQyakklgikpDEVEQYYIDKVPLKRGCDYQDVLNMLLFYASPKASY 244

                          90
                  ....*....|....*
gi 1958774432 161 INGAVIRFDGGEEVF 175
Cdd:PRK12384  245 CTGQSINVTGGQVMF 259
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 90-171 7.87e-05

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: 42.07  E-value: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTkgAFSR---LDPTGK------FEKDMIERIPCGRLGTVEELANLATFLCSDYASW 160
Cdd:cd05331   151 SKCLGLELAPYGVRCNVVSPGSTDT--AMQRtlwHDEDGAaqviagVPEQFRLGIPLGKIAQPADIANAVLFLASDQAGH 228

                          90
                  ....*....|.
gi 1958774432 161 INGAVIRFDGG 171
Cdd:cd05331   229 ITMHDLVVDGG 239
PRK07041 PRK07041
SDR family oxidoreductase;
6-171 8.16e-05

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 41.95  E-value: 8.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432   6 RAFFAGVSRL--------PCDPGPQRffSFGTKTLYQSIDapqSKFFPPIL---KPMLPPNafqGKVAFITG-------G 67
Cdd:PRK07041   61 DAFFAEAGPFdhvvitaaDTPGGPVR--ALPLAAAQAAMD---SKFWGAYRvarAARIAPG---GSLTFVSGfaavrpsA 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  68 GTGLGKAMTTFLSSLGaqcviasRSLAAEwgRYGMRFNIIQPGPIKTKgAFSRLDPTGKFEK--DMIERIPCGRLGTVEE 145
Cdd:PRK07041  133 SGVLQGAINAALEALA-------RGLALE--LAPVRVNTVSPGLVDTP-LWSKLAGDAREAMfaAAAERLPARRVGQPED 202

                         170       180
                  ....*....|....*....|....*.
gi 1958774432 146 LANLATFLCSDyaSWINGAVIRFDGG 171
Cdd:PRK07041  203 VANAILFLAAN--GFTTGSTVLVDGG 226
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 90-171 8.70e-05

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 42.19  E-value: 8.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFE---------KDMIERIPCGRLGTVEELANLATFLCSDYASW 160
Cdd:PRK13394  168 ARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEQAKELgiseeevvkKVMLGKTVDGVFTTVEDVAQTVLFLSSFPSAA 247

                          90
                  ....*....|.
gi 1958774432 161 INGAVIRFDGG 171
Cdd:PRK13394  248 LTGQSFVVSHG 258
PRK05717 PRK05717
SDR family oxidoreductase;
102-171 1.04e-04

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 41.80  E-value: 1.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774432 102 MRFNIIQPGPIKTKG-AFSRLDPTGKFEKDmieRIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK05717  179 IRVNAVSPGWIDARDpSQRRAEPLSEADHA---QHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFVVDGG 246
PRK07814 PRK07814
SDR family oxidoreductase;
59-92 1.12e-04

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 41.69  E-value: 1.12e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958774432  59 GKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS 92
Cdd:PRK07814   10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAART 43
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
91-190 1.18e-04

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 41.66  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKdMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDG 170
Cdd:PRK06505  171 RYLAADYGPQGIRVNAISAGPVRTLAGAGIGDARAIFSY-QQRNSPLRRTVTIDEVGGSALYLLSDLSSGVTGEIHFVDS 249

                          90       100
                  ....*....|....*....|
gi 1958774432 171 GEEVFLSGEFNSLKKVTKEE 190
Cdd:PRK06505  250 GYNIVSMPTLEELKSSDEER 269
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 56-95 1.23e-04

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: 41.52  E-value: 1.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958774432  56 AFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:cd05370     2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREER 41
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 93-171 1.52e-04

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: 41.51  E-value: 1.52e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774432  93 LAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIerIPCGRLGTVEELANLATFLCSDyaSWINGAVIRFDGG 171
Cdd:cd05371   173 IARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQV--PFPSRLGDPAEYAHLVQHIIEN--PYLNGEVIRLDGA 247
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
91-174 1.62e-04

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 41.28  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  91 RSLAAEWGRYGMRFNIIQPGPIKTKGAfsrlDPTGKFEKDMI---ERIPCGRLGTVEELANLATFLCSDYASWINGAVIR 167
Cdd:PRK08159  174 KYLAVDLGPKNIRVNAISAGPIKTLAA----SGIGDFRYILKwneYNAPLRRTVTIEEVGDSALYLLSDLSRGVTGEVHH 249


                  ....*..
gi 1958774432 168 FDGGEEV 174
Cdd:PRK08159  250 VDSGYHV 256
PRK06194 PRK06194
hypothetical protein; Provisional
 57-89 1.90e-04

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 41.15  E-value: 1.90e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIA 89
Cdd:PRK06194    4 FAGKVAVITGAASGFGLAFARIGAALGMKLVLA 36
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 57-123 2.01e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 40.85  E-value: 2.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASR------SLAAEWGRYGMRFNIIQPGPIKTkgAFSRLDP 123
Cdd:PRK07060    7 FSGKSVLVTGASSGIGRACAVALAQRGARVVAAARnaaaldRLAGETGCEPLRLDVGDDAAIRA--ALAAAGA 77
PRK07035 PRK07035
SDR family oxidoreductase;
59-95 2.04e-04

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 40.77  E-value: 2.04e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958774432  59 GKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:PRK07035    8 GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDG 44
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 58-95 2.15e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 40.76  E-value: 2.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958774432  58 QGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:PRK08265    5 AGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADN 42
PRK07814 PRK07814
SDR family oxidoreductase;
102-171 2.32e-04

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 40.92  E-value: 2.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432 102 MRFNIIQPGPIKTKgAFSRLDPTGKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK07814  182 IRVNAIAPGSILTS-ALEVVAANDELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKTLEVDGG 250
PRK07063 PRK07063
SDR family oxidoreductase;
54-122 2.73e-04

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 40.42  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  54 PNAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSL------AAEWGRYG-------MRFNIIQPGPI-----KTK 115
Cdd:PRK07063    2 MNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAalaeraAAAIARDVagarvlaVPADVTDAASVaaavaAAE 81


                  ....*..
gi 1958774432 116 GAFSRLD 122
Cdd:PRK07063   82 EAFGPLD 88
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 58-91 3.16e-04

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: 40.21  E-value: 3.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958774432  58 QGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASR 91
Cdd:cd08934     2 QGKVALVTGASSGIGEATARALAAEGAAVAIAAR 35
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
92-171 3.21e-04

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 40.38  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  92 SLAAEWGRYGMRFNIIQPGPIKTkgafsrlDPTGKFEKDMIERI----PCGRLGTVEELANLATFLCSDYASWINGAVIR 167
Cdd:PRK12938  166 SLAQEVATKGVTVNTVSPGYIGT-------DMVKAIRPDVLEKIvatiPVRRLGSPDEIGSIVAWLASEESGFSTGADFS 238


                  ....
gi 1958774432 168 FDGG 171
Cdd:PRK12938  239 LNGG 242
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 59-92 3.37e-04

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: 40.29  E-value: 3.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958774432  59 GKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS 92
Cdd:cd05327     1 GKVVVITGANSGIGKETARELAKRGAHVIIACRN 34
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 58-103 3.95e-04

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 40.06  E-value: 3.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958774432  58 QGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS------LAAEWGRYGMR 103
Cdd:PRK07666    6 QGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTeenlkaVAEEVEAYGVK 57
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 134-169 4.08e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 39.99  E-value: 4.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958774432 134 RIPCGRLGTVEELANLATFLCSDYASWINGAVIRFD 169
Cdd:PRK06198  216 TQPFGRLLDPDEVARAVAFLLSDESGLMTGSVIDFD 251
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 57-122 5.61e-04

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 39.60  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVI-------ASRSLAAEWGRYGMRFNIIQPGPIK----------TKGAFS 119
Cdd:PRK12935    4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVInynsskeAAENLVNELGKEGHDVYAVQADVSKvedanrlveeAVNHFG 83


                  ...
gi 1958774432 120 RLD 122
Cdd:PRK12935   84 KVD 86
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 58-92 6.00e-04

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 39.71  E-value: 6.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958774432  58 QGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS 92
Cdd:PRK08936    6 EGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRS 40
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 90-114 6.39e-04

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 39.13  E-value: 6.39e-04
                          10        20
                  ....*....|....*....|....*
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKT 114
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDT 184
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
89-171 6.53e-04

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 39.54  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  89 ASRSLAAEWGRYGMRFNIIQPGPIKTKGAFSrLDPTGKFEKDMIERIPCG-RLGTVEELANLATFLCSDYASWINGAVIR 167
Cdd:PRK07889  168 TNRYLARDLGPRGIRVNLVAAGPIRTLAAKA-IPGFELLEEGWDERAPLGwDVKDPTPVARAVVALLSDWFPATTGEIVH 246


                  ....
gi 1958774432 168 FDGG 171
Cdd:PRK07889  247 VDGG 250
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 59-92 7.29e-04

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: 39.16  E-value: 7.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958774432  59 GKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS 92
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARS 34
PRK12746 PRK12746
SDR family oxidoreductase;
93-171 7.42e-04

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 39.25  E-value: 7.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774432  93 LAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTgKFEKDMIERIPCGRLGTVEELANLATFLCSDYASWINGAVIRFDGG 171
Cdd:PRK12746  174 LAKHLGERGITVNTIMPGYTKTDINAKLLDDP-EIRNFATNSSVFGRIGQVEDIADAVAFLASSDSRWVTGQIIDVSGG 251
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
57-122 7.65e-04

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 39.32  E-value: 7.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVI-------ASRSLAAEWGRYGMRFNIIQPG---PIKTKGAFSRLD 122
Cdd:PRK08063    2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVnyarsrkAAEETAEEIEALGRKALAVKANvgdVEKIKEMFAQID 77
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 57-95 8.46e-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: 39.11  E-value: 8.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREER 39
PRK06196 PRK06196
oxidoreductase; Provisional
 59-95 8.97e-04

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 39.28  E-value: 8.97e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958774432  59 GKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:PRK06196   26 GKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDV 62
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 61-89 9.23e-04

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: 38.76  E-value: 9.23e-04
                          10        20
                  ....*....|....*....|....*....
gi 1958774432  61 VAFITGGGTGLGKAMTTFLSSLGAQCVIA 89
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVIL 29
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 90-171 9.39e-04

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 39.10  E-value: 9.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTkgAFSRL---DPTGkfEKDMI----ER----IPCGRLGTVEELANLATFLCSDYA 158
Cdd:PRK08220  159 AKCVGLELAPYGVRCNVVSPGSTDT--DMQRTlwvDEDG--EQQVIagfpEQfklgIPLGKIARPQEIANAVLFLASDLA 234

                          90
                  ....*....|...
gi 1958774432 159 SWINGAVIRFDGG 171
Cdd:PRK08220  235 SHITLQDIVVDGG 247
PRK06181 PRK06181
SDR family oxidoreductase;
59-101 9.41e-04

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 39.19  E-value: 9.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958774432  59 GKVAFITGGGTGLGKAMTTFLSSLGAQCVIASR------SLAAEWGRYG 101
Cdd:PRK06181    1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARnetrlaSLAQELADHG 49
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 90-172 1.13e-03

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: 38.60  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPT---------GKFEKDMIERIPCGRLGTVEELANLATFLCSDYASW 160
Cdd:cd05322   164 TQSLALDLAEHGITVNSLMLGNLLKSPMFQSLLPQyakklgikeSEVEQYYIDKVPLKRGCDYQDVLNMLLFYASPKASY 243

                          90
                  ....*....|..
gi 1958774432 161 INGAVIRFDGGE 172
Cdd:cd05322   244 CTGQSINITGGQ 255
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 57-88 1.32e-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: 38.46  E-value: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVI 88
Cdd:cd05353     3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVVV 34
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 58-85 1.46e-03

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 38.40  E-value: 1.46e-03
                          10        20
                  ....*....|....*....|....*...
gi 1958774432  58 QGKVAFITGGGTGLGKAMTTFLSSLGAQ 85
Cdd:PRK08217    4 KDKVIVITGGAQGLGRAMAEYLAQKGAK 31
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 51-98 1.68e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 38.41  E-value: 1.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958774432  51 MLPPNAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVI------ASRSLAAEWG 98
Cdd:PRK05872    1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALvdleeaELAALAAELG 54
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 92-171 1.76e-03

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 38.00  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  92 SLAAEWGRYGMRFNIIQPGPIKtkgAFSRLDPTGKFEKDMIERI-------------PCGRLGTVEELANLATFLCSDYA 158
Cdd:PRK12823  168 SLAFEYAEHGIRVNAVAPGGTE---APPRRVPRNAAPQSEQEKAwyqqivdqtldssLMKRYGTIDEQVAAILFLASDEA 244

                          90
                  ....*....|...
gi 1958774432 159 SWINGAVIRFDGG 171
Cdd:PRK12823  245 SYITGTVLPVGGG 257
PLN02253 PLN02253
xanthoxin dehydrogenase
 52-89 1.92e-03

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 38.27  E-value: 1.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958774432  52 LPPNAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIA 89
Cdd:PLN02253   11 LPSQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIV 48
PRK08628 PRK08628
SDR family oxidoreductase;
58-92 2.09e-03

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 38.02  E-value: 2.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958774432  58 QGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS 92
Cdd:PRK08628    6 KDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRS 40
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 59-96 2.10e-03

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: 38.04  E-value: 2.10e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958774432  59 GKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAAE 96
Cdd:cd05371     2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPG 39
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 57-95 2.27e-03

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 37.83  E-value: 2.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:COG3967     3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEK 41
PRK07062 PRK07062
SDR family oxidoreductase;
90-171 2.83e-03

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 37.71  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774432  90 SRSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGKFEKDMIE---------RIPCGRLGTVEELANLATFLCSDYASW 160
Cdd:PRK07062  170 VKSLATELAPKGVRVNSILLGLVESGQWRRRYEARADPGQSWEAwtaalarkkGIPLGRLGRPDEAARALFFLASPLSSY 249

                          90
                  ....*....|.
gi 1958774432 161 INGAVIRFDGG 171
Cdd:PRK07062  250 TTGSHIDVSGG 260
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 57-89 2.88e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 37.40  E-value: 2.88e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIA 89
Cdd:PRK06057    5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVG 37
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 55-94 3.04e-03

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 37.47  E-value: 3.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958774432  55 NAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLA 94
Cdd:PRK12828    3 HSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAA 42
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 59-94 3.09e-03

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 37.45  E-value: 3.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958774432  59 GKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLA 94
Cdd:cd09807     1 GKTVIITGANTGIGKETARELARRGARVIMACRDMA 36
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
58-95 3.19e-03

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 37.31  E-value: 3.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958774432  58 QGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:PRK07067    5 QGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPAR 42
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 57-96 3.40e-03

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: 37.45  E-value: 3.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASR------SLAAE 96
Cdd:cd05351     5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRtqadldSLVRE 50
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 59-95 3.51e-03

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: 37.37  E-value: 3.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958774432  59 GKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:cd05338     3 GKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASE 39
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 58-99 3.58e-03

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: 37.05  E-value: 3.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958774432  58 QGKVAFITGGGTGLGKAMTTFLSSLGAQCVIAS------RSLAAEWGR 99
Cdd:cd05326     3 DGKVAIITGGASGIGEATARLFAKHGARVVIADidddagQAVAAELGD 50
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 50-88 4.80e-03

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 37.07  E-value: 4.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958774432  50 PMLPPNAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVI 88
Cdd:PRK07792    3 RTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVV 41
PRK07326 PRK07326
SDR family oxidoreductase;
55-95 5.46e-03

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 36.53  E-value: 5.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958774432  55 NAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:PRK07326    2 MSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKE 42
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 57-92 6.22e-03

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: 36.74  E-value: 6.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS 92
Cdd:cd08937     2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS 37
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 55-104 6.47e-03

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: 36.59  E-value: 6.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774432  55 NAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIAS------RSLAAEWGRYGMRF 104
Cdd:cd05341     1 NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDildeegQAAAAELGDAARFF 56
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 57-95 7.51e-03

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 36.42  E-value: 7.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958774432  57 FQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRSLAA 95
Cdd:PRK08277    8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEK 46
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 54-96 8.03e-03

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 36.08  E-value: 8.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958774432  54 PNAFQGKVAFITGGGTGLGKAMTTFLSSLGAQCVIASRS-----LAAE 96
Cdd:PRK12823    3 NQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSelvheVAAE 50
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 59-89 9.64e-03

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: 35.83  E-value: 9.64e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958774432  59 GKVAFITGGGTGLGKAMTTFLSSLGAQCVIA 89
Cdd:cd08943     1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVA 31
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH