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Conserved domains on  [gi|446465278|ref|WP_000543132|]
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MULTISPECIES: short-chain dehydrogenase [Bacillus]

Protein Classification

short-chain dehydrogenase( domain architecture ID 10013043)

short-chain dehydrogenase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08309 PRK08309
short chain dehydrogenase; Provisional
 1-175 9.74e-111

short chain dehydrogenase; Provisional


:

Pssm-ID: 236232  Cd Length: 177  Bit Score: 312.84  E-value: 9.74e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   1 MHALVIGGTGMLKKVSMWLCEQGFHVSIIGRDEVKLEYVKRASSAPENITCLPLDYHNNDEVKIAIKGTIERNGPITLVV 80
Cdd:PRK08309   1 MHALVIGGTGMLKRVSLWLCEKGFHVSVIARREVKLENVKRESTTPESITPLPLDYHDDDALKLAIKSTIEKNGPFDLAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278  81 AWIHSSAKYALSLICKEIEFSSETYSLFHILGSKAS--RMNAGKIGGTLCLYHRIILGFILEDTFGRWLTHQEISDGVIN 158
Cdd:PRK08309  81 AWIHSSAKDALSVVCRELDGSSETYRLFHVLGSAASdpRIPSEKIGPARCSYRRVILGFVLEDTYSRWLTHEEISDGVIK 160

                        170
                 ....*....|....*..
gi 446465278 159 GIESNCNEWIVGQIEPW 175
Cdd:PRK08309 161 AIESDADEHVVGTVEPW 177
 
Name Accession Description Interval E-value
PRK08309 PRK08309
short chain dehydrogenase; Provisional
 1-175 9.74e-111

short chain dehydrogenase; Provisional


Pssm-ID: 236232  Cd Length: 177  Bit Score: 312.84  E-value: 9.74e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   1 MHALVIGGTGMLKKVSMWLCEQGFHVSIIGRDEVKLEYVKRASSAPENITCLPLDYHNNDEVKIAIKGTIERNGPITLVV 80
Cdd:PRK08309   1 MHALVIGGTGMLKRVSLWLCEKGFHVSVIARREVKLENVKRESTTPESITPLPLDYHDDDALKLAIKSTIEKNGPFDLAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278  81 AWIHSSAKYALSLICKEIEFSSETYSLFHILGSKAS--RMNAGKIGGTLCLYHRIILGFILEDTFGRWLTHQEISDGVIN 158
Cdd:PRK08309  81 AWIHSSAKDALSVVCRELDGSSETYRLFHVLGSAASdpRIPSEKIGPARCSYRRVILGFVLEDTYSRWLTHEEISDGVIK 160

                        170
                 ....*....|....*..
gi 446465278 159 GIESNCNEWIVGQIEPW 175
Cdd:PRK08309 161 AIESDADEHVVGTVEPW 177
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 2-80 1.03e-07

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: 49.94  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   2 HALVIGGT-GMLKKVSMWLCEQGFHVSIIGRDEVKLEYVK---RASSAPE--NITCLPLDYHNNDEVKIAIKGTIERNGP 75
Cdd:cd08939    3 HVLITGGSsGIGKALAKELVKEGANVIIVARSESKLEEAVeeiEAEANASgqKVSYISADLSDYEEVEQAFAQAVEKGGP 82


                 ....*
gi 446465278  76 ITLVV 80
Cdd:cd08939   83 PDLVV 87
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
2-80 2.60e-05

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 43.32  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   2 HALVIGGTGML-KKVSMWLCEQGFHVSIIGRDEVKLE-YVKRASSAPENITCLPLDYHNNDEVKIAIKGTIERNGPITLV 79
Cdd:COG0300    7 TVLITGASSGIgRALARALAARGARVVLVARDAERLEaLAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPIDVL 86


                 .
gi 446465278  80 V 80
Cdd:COG0300   87 V 87
 
Name Accession Description Interval E-value
PRK08309 PRK08309
short chain dehydrogenase; Provisional
 1-175 9.74e-111

short chain dehydrogenase; Provisional


Pssm-ID: 236232  Cd Length: 177  Bit Score: 312.84  E-value: 9.74e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   1 MHALVIGGTGMLKKVSMWLCEQGFHVSIIGRDEVKLEYVKRASSAPENITCLPLDYHNNDEVKIAIKGTIERNGPITLVV 80
Cdd:PRK08309   1 MHALVIGGTGMLKRVSLWLCEKGFHVSVIARREVKLENVKRESTTPESITPLPLDYHDDDALKLAIKSTIEKNGPFDLAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278  81 AWIHSSAKYALSLICKEIEFSSETYSLFHILGSKAS--RMNAGKIGGTLCLYHRIILGFILEDTFGRWLTHQEISDGVIN 158
Cdd:PRK08309  81 AWIHSSAKDALSVVCRELDGSSETYRLFHVLGSAASdpRIPSEKIGPARCSYRRVILGFVLEDTYSRWLTHEEISDGVIK 160

                        170
                 ....*....|....*..
gi 446465278 159 GIESNCNEWIVGQIEPW 175
Cdd:PRK08309 161 AIESDADEHVVGTVEPW 177
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 2-80 1.03e-07

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: 49.94  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   2 HALVIGGT-GMLKKVSMWLCEQGFHVSIIGRDEVKLEYVK---RASSAPE--NITCLPLDYHNNDEVKIAIKGTIERNGP 75
Cdd:cd08939    3 HVLITGGSsGIGKALAKELVKEGANVIIVARSESKLEEAVeeiEAEANASgqKVSYISADLSDYEEVEQAFAQAVEKGGP 82


                 ....*
gi 446465278  76 ITLVV 80
Cdd:cd08939   83 PDLVV 87
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 4-80 1.00e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 47.37  E-value: 1.00e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446465278   4 LVIGGT-GMLKKVSMWLCEQGFHVSIIGRDEVKLEYVKRASSAPE-NITCLPLDYHNNDEVKIAIKGTIERNGPITLVV 80
Cdd:PRK07677   5 IITGGSsGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPgQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDALI 83
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
2-88 5.02e-06

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 45.15  E-value: 5.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   2 HALVIGGTGML-KKVSMWLCEQGFHVSIIGRDEVKLEYVKRA-SSAPENITCLPLDYHNNDEVKIAIKGTIERNGPITLV 79
Cdd:PRK05653   7 TALVTGASRGIgRAIALRLAADGAKVVIYDSNEEAAEALAAElRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALDIL 86

                         90
                 ....*....|.
gi 446465278  80 V--AWIHSSAK 88
Cdd:PRK05653  87 VnnAGITRDAL 97
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 2-81 7.69e-06

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: 44.50  E-value: 7.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   2 HALVIGG-TGMLKKVSMWLCEQGFHVSIIGRDEVKLEYVKRASSAPENITCLPL--DYHNNDEVKIAIKGTIERNGPITL 78
Cdd:cd05369    5 VAFITGGgTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIqcDVRDPEAVEAAVDETLKEFGKIDI 84


                 ...
gi 446465278  79 VVA 81
Cdd:cd05369   85 LIN 87
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
2-80 2.60e-05

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 43.32  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   2 HALVIGGTGML-KKVSMWLCEQGFHVSIIGRDEVKLE-YVKRASSAPENITCLPLDYHNNDEVKIAIKGTIERNGPITLV 79
Cdd:COG0300    7 TVLITGASSGIgRALARALAARGARVVLVARDAERLEaLAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPIDVL 86


                 .
gi 446465278  80 V 80
Cdd:COG0300   87 V 87
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 21-80 5.18e-05

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 42.22  E-value: 5.18e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278  21 EQGFHVSIIGRDEVKLEyvKRASSAPENITCLPLDYHNNDEVKIAIKGTIERNGPITLVV 80
Cdd:cd05374   22 AQGYRVIATARNPDKLE--SLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLV 79
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 19-81 5.81e-04

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: 39.01  E-value: 5.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446465278  19 LCEQGFHVSIIGRDEVKLEyvKRASSAPENITCLPLDYHNNDEVKIAIKGTIERNGPITLVVA 81
Cdd:COG4221   25 LAAAGARVVLAARRAERLE--ALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVN 85
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 3-80 8.37e-04

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: 38.68  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   3 ALVIGGT-GMLKKVSMWLCEQGFHVSIIGRDEVKL-EYVKRASSAPENITCLPLDYHNNDEVKIAIKGTIERNGPITLVV 80
Cdd:cd05333    3 ALVTGASrGIGRAIALRLAAEGAKVAVTDRSEEAAaETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDILV 82
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 3-128 1.06e-03

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 38.52  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465278   3 ALVIG-GTGMLKKVSMWLCEQGFHVSIIGRDEVKLE--YVKRASSAPENITCLPLDYHNNDEVkIAIKGTIERN-GPITL 78
Cdd:cd05373    2 AAVVGaGDGLGAAIARRFAAEGFSVALAARREAKLEalLVDIIRDAGGSAKAVPTDARDEDEV-IALFDLIEEEiGPLEV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446465278  79 VVawIHSSAKYALSLickeIEFSSETYslfhilgSKASRMNAgkIGGTLC 128
Cdd:cd05373   81 LV--YNAGANVWFPI----LETTPRVF-------EKVWEMAA--FGGFLA 115
PRK09072 PRK09072
SDR family oxidoreductase;
19-80 5.05e-03

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 36.46  E-value: 5.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446465278  19 LCEQGFHVSIIGRDEVKLEYVKRASSAPENITCLPLDYHNNDEVKiAIKGTIERNGPITLVV 80
Cdd:PRK09072  25 LAAAGARLLLVGRNAEKLEALAARLPYPGRHRWVVADLTSEAGRE-AVLARAREMGGINVLI 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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