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Conserved domains on  [gi|2462575256|ref|XP_054198979|]
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peroxisomal trans-2-enoyl-CoA reductase isoform X1 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 35-161 5.49e-61

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: 189.72  E-value: 5.49e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlppTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISS----ATGGRAHPIQCDVRDPEAVEAAVDETL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05369    77 KEFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAV 123
 
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 ...
 35-161 5.49e-61

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: 189.72  E-value: 5.49e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlppTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISS----ATGGRAHPIQCDVRDPEAVEAAVDETL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05369    77 KEFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAV 123
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 35-161 1.18e-40

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: 137.61  E-value: 1.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:COG1028     4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRA-----AGGRALAVAADVTDEAAVEALVAAAV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:COG1028    79 AAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAA 125
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 37-161 9.71e-36

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 125.18  E-value: 9.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK07677    1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQF-----PGQVLTVQMDVRNPEDVQKMVEQIDEK 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07677   76 FGRIDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAV 120
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 38-161 1.10e-34

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 120.80  E-value: 1.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL-----GGKALFIQGDVTDRAQVKALVEQAVERL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 118 GKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:pfam00106  76 GRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAV 119
SDR_dihy_bifunc NF012208
bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family ...
 40-160 8.12e-18

bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family are SDR family oxidoreductases, unrelated to previously known families of dihydrofolate reductase (DHFR), one of which was demonstrated to be a bifunctional dihydropteridine reductase/dihydrofolate reductase. The DHFR activity can give a heterologously expressed protein the ability to confer resistance to trimethoprim, an inhibitor of most forms of DHFR.


Pssm-ID: 411089 [Multi-domain]  Cd Length: 233  Bit Score: 77.65  E-value: 8.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRKlerlkSAADELQ-ANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:NF012208    1 ALVTGSARGIGRAIALALAREGFDVAVHYRR-----SAEAAEQtAQEAEALGVKAITLQADLTDPEQARSLVEEAAEALG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 119 KINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:NF012208   76 GLSVLVNNVGNYLHKPLLETTDEEWHEMLDSNLNATFYVTQA 117
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 39-128 1.43e-06

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 46.83  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLEL----GSNVVIASRKLERLKSAADELQANLPptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERS---GLRVVRVSLDLGAEAGLEQLLKALR 78

                          90
                  ....*....|....*...
gi 2462575256 115 DTFGKINF----LVNNGG 128
Cdd:TIGR01500  79 ELPRPKGLqrllLINNAG 96
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 41-164 6.64e-05

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 41.31  E-value: 6.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256   41 IVTGGATGIGKAIVKELLELG-SNVVIASR---KLERLKSAADELQANLpptkqARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGaRRLVLLSRsgpDAPGAAALLAELEAAG-----ARVTVVACDVADRDALAAVLAAIPAV 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462575256  117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVDQL 164
Cdd:smart00822  79 EGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADL 126
 
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 ...
 35-161 5.49e-61

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: 189.72  E-value: 5.49e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlppTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISS----ATGGRAHPIQCDVRDPEAVEAAVDETL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05369    77 KEFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAV 123
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 35-161 1.18e-40

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: 137.61  E-value: 1.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:COG1028     4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRA-----AGGRALAVAADVTDEAAVEALVAAAV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:COG1028    79 AAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAA 125
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 40-161 1.06e-37

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 129.71  E-value: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptkQARVIPIQCNIRNEEEVNNLVKSTLDTFGK 119
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEAL------GGNAVAVQADVSDEEDVEALVEEALEEFGR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 120 INFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05233    75 LDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAA 116
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 36-161 7.97e-36

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 124.91  E-value: 7.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptkqaRVIPIQCNIRNEEEVNNLVKSTLD 115
Cdd:COG4221     4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGG--------RALAVPLDVTDEAAVEAAVAAAVA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 116 TFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:COG4221    76 EFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAA 121
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 37-161 9.71e-36

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 125.18  E-value: 9.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK07677    1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQF-----PGQVLTVQMDVRNPEDVQKMVEQIDEK 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07677   76 FGRIDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAV 120
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 38-161 1.10e-34

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 120.80  E-value: 1.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL-----GGKALFIQGDVTDRAQVKALVEQAVERL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 118 GKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:pfam00106  76 GRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAV 119
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
34-161 1.78e-34

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 121.42  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  34 LLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLpptkqARVIPIQCNIRNEEEVNNLVKST 113
Cdd:PRK05653    2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAG-----GEARVLVFDVSDEAAVRALIEAA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 114 LDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK05653   77 VEAFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAA 124
PRK07326 PRK07326
SDR family oxidoreductase;
35-164 1.82e-34

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 121.27  E-value: 1.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQanlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK07326    4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELN------NKGNVLGLAADVRDEADVQRAVDAIV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCK-AVDQL 164
Cdd:PRK07326   78 AAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKaAVPAL 128
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
35-161 5.45e-31

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 112.66  E-value: 5.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:COG0300     3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRA-----AGARVEVVALDVTDPDAVAALAEAVL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:COG0300    78 ARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRAL 124
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 35-161 1.30e-29

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 109.13  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRkleRLKSAADELQANLpptKQA--RVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK05557    3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYA---SSEAGAEALVAEI---GALggKALAVQGDVSDAESVERAVDE 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462575256 113 TLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK05557   77 AKAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAV 125
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-161 1.37e-29

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 108.78  E-value: 1.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRK-LERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKST 113
Cdd:PRK05565    3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDInEEAAQELLEEIKEE-----GGDAIAVKADVSSEEDVENLVEQI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 114 LDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK05565   78 VEKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYA 125
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 35-161 2.04e-29

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: 108.60  E-value: 2.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05347     3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEK-----EGVEATAFTCDVSDEEAIKAAVEAIE 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05347    78 EDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAV 124
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 38-161 9.49e-29

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: 106.48  E-value: 9.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKA-----LGGNAAALEADVSDREAVEALVEKVEAEF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 118 GKINFLVNNGG----GQFLspaeHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05333    76 GPVDILVNNAGitrdNLLM----RMSEEDWDAVINVNLTGVFNVTQAV 119
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 35-161 9.74e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 107.05  E-value: 9.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLpptkqarvIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK06841   13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNA--------KGLVCDVSDSQSVEAAVAAVI 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06841   85 SAFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAV 131
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 35-161 1.03e-27

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 104.26  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK08213   10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEA-----LGIDALWIAADVADEADIERLAEETL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK08213   85 ERFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAV 131
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 37-161 1.16e-27

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 103.89  E-value: 1.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLpptkqARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGG-----AGVLAVVADLTDPEDIDRLVEKAGDA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05344    76 FGRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAV 120
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
24-160 3.90e-27

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 106.85  E-value: 3.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  24 AKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQanlpptKQARVIPIQCNIRNE 103
Cdd:PRK08324  409 AKLQRMPKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELG------GPDRALGVACDVTDE 482

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575256 104 EEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK08324  483 AAVQAAFEEAALAFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVARE 539
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 34-161 1.24e-26

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 101.50  E-value: 1.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  34 LLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKST 113
Cdd:PRK12429    1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQK-----AGGKAIGVAMDVTDEEAINAGIDYA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 114 LDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12429   76 VETFGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAA 123
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-161 1.80e-26

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 100.71  E-value: 1.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLErlkSAADELQANLPPTKQaRVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK12825    2 GSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDE---EAAEELVEAVEALGR-RAQAVQADVTDKAALEAAVAA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462575256 113 TLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12825   78 AVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAV 126
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 35-161 1.91e-26

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: 100.69  E-value: 1.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEA-----EGGKALVLELDVTDEQQVDAAVERTV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd08934    76 EALGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAA 122
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 37-161 4.64e-26

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: 99.63  E-value: 4.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQaRVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASGQ-KVSYISADLSDYEEVEQAFAQAVEK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd08939    80 GGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAV 124
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 35-160 6.84e-26

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: 99.38  E-value: 6.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLerlKSAADELQANLpptKQARV--IPIQCNIRNEEEVNNLVKS 112
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSK---EDAAEEVVEEI---KAVGGkaIAVQADVSKEEDVVALFQS 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 113 TLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd05358    75 AIKEFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCARE 122
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 35-160 2.44e-25

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 98.26  E-value: 2.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLER-LKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKST 113
Cdd:PRK08936    5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEeANDVAEEIKKA-----GGEAIAVKGDVTVESDVVNLIQTA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 114 LDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK08936   80 VKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSRE 126
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 35-160 3.17e-25

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: 97.46  E-value: 3.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLER------------LKSAADELQAnlpptKQARVIPIQCNIRN 102
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEgdngsakslpgtIEETAEEIEA-----AGGQALPIVVDVRD 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462575256 103 EEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd05338    76 EDQVRALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQA 133
PRK12826 PRK12826
SDR family oxidoreductase;
35-161 3.86e-25

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 97.29  E-value: 3.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkqaRVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK12826    4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGG-----KARARQVDVRDRAALKAAVAAGV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12826   79 EDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAA 125
FabG-like PRK07231
SDR family oxidoreductase;
34-161 5.01e-25

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 97.21  E-value: 5.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  34 LLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptkQARVIPIQCNIRNEEEVNNLVKST 113
Cdd:PRK07231    2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA------GGRAIAVAADVSDEADVEAAVAAA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462575256 114 LDTFGKINFLVNNGG-----GQFL--SPAEhisskgWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07231   76 LERFGSVDILVNNAGtthrnGPLLdvDEAE------FDRIFAVNVKSPYLWTQAA 124
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 39-161 3.15e-24

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: 94.99  E-value: 3.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLpptkqarvIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:cd05374     2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNL--------EVLELDVTDEESIKAAVKEVIERFG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 119 KINFLVNNGG-GQFlSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05374    74 RIDVLVNNAGyGLF-GPLEETSIEEVRELFEVNVFGPLRVTRAF 116
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 38-161 3.40e-23

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


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 92.34  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkqARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:cd05346     1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFP----VKVLPLQLDVSDRESIEAALENLPEEF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 118 GKINFLVNNGG---GqfLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05346    77 RDIDILVNNAGlalG--LDPAQEADLEDWETMIDTNVKGLLNVTRLI 121
PRK07831 PRK07831
SDR family oxidoreductase;
33-160 3.76e-23

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 92.40  E-value: 3.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGA-TGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPtkqARVIPIQCNIRNEEEVNNLVK 111
Cdd:PRK07831   13 GLLAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGL---GRVEAVVCDVTSEAQVDALID 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 112 STLDTFGKINFLVNNG--GGQflSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK07831   90 AAVERLGRLDVLVNNAglGGQ--TPVVDMTDDEWSRVLDVTLTGTFRATRA 138
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 48-161 4.74e-23

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: 91.72  E-value: 4.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  48 GIGKAIVKELLELGSNVVIASRKlERLKSAADELQANLPptkqARVIPiqCNIRNEEEVNNLVKSTLDTFGKINFLVNNG 127
Cdd:pfam13561   7 GIGWAIARALAEEGAEVVLTDLN-EALAKRVEELAEELG----AAVLP--CDVTDEEQVEALVAAAVEKFGRLDILVNNA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462575256 128 G--GQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:pfam13561  80 GfaPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAA 115
PRK06398 PRK06398
aldose dehydrogenase; Validated
 35-161 5.05e-23

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 92.20  E-value: 5.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERlksaadelqanlpptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK06398    4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS----------------YNDVDYFKVDVSNKEQVIKGIDYVI 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06398   68 SKYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYT 114
PRK07063 PRK07063
SDR family oxidoreductase;
32-161 5.63e-23

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 92.04  E-value: 5.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  32 PGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPtkqARVIPIQCNIRNEEEVNNLVK 111
Cdd:PRK07063    2 MNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAG---ARVLAVPADVTDAASVAAAVA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 112 STLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07063   79 AAEEAFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAV 128
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 35-161 9.73e-23

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 91.50  E-value: 9.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK13394    5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKA-----GGKAIGVAMDVTNEDAVNAGIDKVA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK13394   80 ERFGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAA 126
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 32-161 1.24e-22

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 90.80  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  32 PGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVK 111
Cdd:PRK12939    2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEA-----AGGRAHAIAADLADPASVQRFFD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 112 STLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12939   77 AAAAALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAA 126
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 37-164 1.28e-22

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 90.86  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlppTKQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK12384    2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAE---YGEGMAYGFGADATSEQSVLALSRGVDEI 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVDQL 164
Cdd:PRK12384   79 FGRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRL 126
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 35-161 2.22e-22

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: 90.13  E-value: 2.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQanlpptKQARVIpiQCNIRNEEEVNNLVKSTL 114
Cdd:cd05341     3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELG------DAARFF--HLDVTDEDGWTAVVDTAR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05341    75 EAFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAV 121
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 40-158 3.03e-22

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 89.10  E-value: 3.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkqarVIPIQCNIRNEEEVNNLVKSTLDTFGK 119
Cdd:cd08929     3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEG--------VLGLAGDVRDEADVRRAVDAMEEAFGG 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462575256 120 INFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMC 158
Cdd:cd08929    75 LDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCI 113
PRK07062 PRK07062
SDR family oxidoreductase;
35-160 3.99e-22

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 89.72  E-value: 3.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK07062    6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFP---GARLLAARCDVLDEADVAAFAAAVE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK07062   83 ARFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRA 128
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
35-161 6.20e-22

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 89.02  E-value: 6.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlerlkSAADELQaNLPPTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK06935   13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHG-----TNWDETR-RLIEKEGRKVTFVQVDLTKPESAEKVVKEAL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06935   87 EEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAV 133
PRK08278 PRK08278
SDR family oxidoreductase;
35-160 7.76e-22

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 89.19  E-value: 7.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASR------KLE-RLKSAADELQAnlpptKQARVIPIQCNIRNEEEVN 107
Cdd:PRK08278    4 LSGKTLFITGASRGIGLAIALRAARDGANIVIAAKtaephpKLPgTIHTAAEEIEA-----AGGQALPLVGDVRDEDQVA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462575256 108 NLVKSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK08278   79 AAVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQA 131
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 35-161 1.24e-21

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 88.53  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASrklerLKSAADELQanlpptkqaRVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK06171    7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNAD-----IHGGDGQHE---------NYQFVPTDVSSAEEVNHTVAEII 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 115 DTFGKINFLVNNGG--------------GQFlspaeHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06171   73 EKFGRIDGLVNNAGiniprllvdekdpaGKY-----ELNEAAFDKMFNINQKGVFLMSQAV 128
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 36-159 2.02e-21

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: 87.98  E-value: 2.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPtkQARVIPiqCNIRNEEEVNNLVKSTLD 115
Cdd:cd08933     8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPG--SCKFVP--CDVTKEEDIKTLISVTVE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 116 TFGKINFLVNNGGGQ-FLSPAEHISSKGWHAVLETNLTGTFYMCK 159
Cdd:cd08933    84 RFGRIDCLVNNAGWHpPHQTTDETSAQEFRDLLNLNLISYFLASK 128
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 32-161 2.66e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 87.48  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  32 PGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQanlpptkqarVIPIQCNIRNEEEVNNLVK 111
Cdd:PRK06057    2 SQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVG----------GLFVPTDVTDEDAVNALFD 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462575256 112 STLDTFGKINFLVNNGGgqfLSPAEH--ISSKG---WHAVLETNLTGTFYMCKAV 161
Cdd:PRK06057   72 TAAETYGSVDIAFNNAG---ISPPEDdsILNTGldaWQRVQDVNLTSVYLCCKAA 123
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 35-161 2.87e-21

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: 87.39  E-value: 2.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkqARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05352     6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYG----VKTKAYKCDVSSQESVEKTFKQIQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05352    82 KDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAA 128
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 36-161 3.45e-21

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: 87.00  E-value: 3.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlppTKQARVIPIQCNIRNEEEVNNLVKSTLD 115
Cdd:cd08930     1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTN----LYKNRVIALELDITSKESIKELIESYLE 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462575256 116 TFGKINFLVNNGGGQF---LSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd08930    77 KFGRIDILINNAYPSPkvwGSRFEEFPYEQWNEVLNVNLGGAFLCSQAF 125
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 35-161 7.10e-21

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: 86.17  E-value: 7.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVI--ASRKlERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKS 112
Cdd:cd05362     1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVnyASSK-AAAEEVVAEIEAA-----GGKAIAVQADVSDPSQVARLFDA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462575256 113 TLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05362    75 AEKAFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEA 123
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 35-160 1.08e-20

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: 85.60  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLksaaDELQANLPptkqaRVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:COG3967     3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKL----EEAAAANP-----GLHTIVLDVADPASIAALAEQVT 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 115 DTFGKINFLVNNGGGQflsPAEHISSKGWH-----AVLETNLTGTFYMCKA 160
Cdd:COG3967    74 AEFPDLNVLINNAGIM---RAEDLLDEAEDladaeREITTNLLGPIRLTAA 121
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 37-158 1.19e-20

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: 85.74  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlppTKQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd05327     1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKE---TGNAKVEVIQLDLSSLASVRQFAEEFLAR 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 117 FGKINFLVNNGGGqfLSPAEHISSKGWHAVLETNLTGTFYMC 158
Cdd:cd05327    78 FPRLDILINNAGI--MAPPRRLTKDGFELQFAVNYLGHFLLT 117
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 28-129 1.33e-20

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 85.67  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  28 SYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQanlppTKQARVIPIQCNIRNEEEVN 107
Cdd:PRK06113    2 FNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQ-----QLGGQAFACRCDITSEQELS 76

                          90       100
                  ....*....|....*....|..
gi 2462575256 108 NLVKSTLDTFGKINFLVNNGGG 129
Cdd:PRK06113   77 ALADFALSKLGKVDILVNNAGG 98
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 37-155 1.64e-20

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: 85.14  E-value: 1.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptkQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd08943     1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQG------GPRALGVQCDVTSEAQVQSAFEQAVLE 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTF 155
Cdd:cd08943    75 FGGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHF 113
PRK09242 PRK09242
SDR family oxidoreductase;
35-160 2.24e-20

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 84.80  E-value: 2.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK09242    7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFP---EREVHGLAADVSDDEDRRAILDWVE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK09242   84 DHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRY 129
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-161 2.42e-20

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 84.36  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK07666    5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEA-----YGVKVVIATADVSDYEEVTAAIEQLK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462575256 115 DTFGKINFLVNNGG-GQF-----LSPAEhisskgWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07666   80 NELGSIDILINNAGiSKFgkfleLDPAE------WEKIIQVNLMGVYYATRAV 126
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 37-159 2.52e-20

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: 84.65  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAAdelqanlppTKQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd05371     2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVA---------KLGDNCRFVPVDVTSEKDVKAALALAKAK 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462575256 117 FGKINFLVN-----------NGGGQFLSPAEHisskgWHAVLETNLTGTFYMCK 159
Cdd:cd05371    73 FGRLDIVVNcagiavaaktyNKKGQQPHSLEL-----FQRVINVNLIGTFNVIR 121
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 35-159 3.55e-20

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: 84.43  E-value: 3.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05326     2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAEL-------GDPDISFVHCDVTVEADVRAAVDTAV 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGG--GQFLSPAEHISSKGWHAVLETNLTGTFYMCK 159
Cdd:cd05326    75 ARFGRLDIMFNNAGvlGAPCYSILETSLEEFERVLDVNVYGAFLGTK 121
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 35-161 4.08e-20

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 84.34  E-value: 4.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLErlksAADELQANLPptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK12829    9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEA----ALAATAARLP---GAKVTATVADVADPAQVERVFDTAV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPA-EHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12829   82 ERFGGLDVLVNNAGIAGPTGGiDEITPEQWEQTLAVNLNGQFYFARAA 129
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 36-161 6.27e-20

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 83.74  E-value: 6.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTLD 115
Cdd:cd08945     2 DSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELRE-----AGVEADGRTCDVRSVPEIEALVAAAVA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 116 TFGKINFLVNN----GGGQFLSPAEHIsskgWHAVLETNLTGTFYMCKAV 161
Cdd:cd08945    77 RYGPIDVLVNNagrsGGGATAELADEL----WLDVVETNLTGVFRVTKEV 122
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 39-156 8.03e-20

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 83.12  E-value: 8.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRKLErlKSAADELQANLPPTKqarVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:cd05323     2 VAIITGGASGIGLATAKLLLKKGAKVAILDRNEN--PGAAAELQAINPKVK---ATFVQCDVTSWEQLAAAFKKAIEKFG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462575256 119 KINFLVNNGGGqFLSPAEHISSKG---WHAVLETNLTGTFY 156
Cdd:cd05323    77 RVDILINNAGI-LDEKSYLFAGKLpppWEKTIDVNLTGVIN 116
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
35-161 1.20e-19

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 83.15  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkqarVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK07067    4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPA--------AIAVSLDVTRQDSIDRIVAAAV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07067   76 ERFGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAV 122
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 40-161 1.84e-19

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: 82.40  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRK-LERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVINYRKsKDAAAEVAAEIEE-----LGGKAVVVRADVSQPQDVEEMFAAVKERFG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462575256 119 KINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05359    76 RLDVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQA 118
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 35-161 2.27e-19

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: 82.25  E-value: 2.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqANLPPTKqARVIPIqcNIRNEEEVNNLVKSTL 114
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSEC-LELGAPS-PHVVPL--DMSDLEDAEQVVEEAL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05332    77 KLFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAA 123
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
34-150 2.56e-19

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 82.07  E-value: 2.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  34 LLQGQVAIVTGGATGIGKAIVKELLELGSNVVIasrKLERLKSAADELQANLPpTKQARVIPIQCNIRNEEEVNNLVKST 113
Cdd:PRK08063    1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAV---NYARSRKAAEETAEEIE-ALGRKALAVKANVGDVEKIKEMFAQI 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462575256 114 LDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETN 150
Cdd:PRK08063   77 DEEFGRLDVFVNNAASGVLRPAMELEESHWDWTMNIN 113
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 35-154 3.36e-19

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 81.79  E-value: 3.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTkqarVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05343     4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPT----LFPYQCDLSNEEQILSMFSAIR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGT 154
Cdd:cd05343    80 TQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLAL 119
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 35-161 3.95e-19

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 81.59  E-value: 3.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanlpptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK08265    4 LAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASL--------GERARFIATDITDDAAIERAVATVV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNgGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK08265   76 ARFGRVDILVNL-ACTYLDDGLASSRADWLAALDVNLVSAAMLAQAA 121
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 39-129 4.62e-19

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: 81.08  E-value: 4.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQA-----GGQAIGLECNVTSEQDLEAVVKATVSQFG 75

                          90
                  ....*....|.
gi 2462575256 119 KINFLVNNGGG 129
Cdd:cd05365    76 GITILVNNAGG 86
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 35-159 4.72e-19

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: 81.34  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanlpPTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05329     4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEW-----REKGFKVEGSVCDVSSRSERQELMDTVA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTF-GKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCK 159
Cdd:cd05329    79 SHFgGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSR 124
PRK06194 PRK06194
hypothetical protein; Provisional
 35-156 5.43e-19

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 81.60  E-value: 5.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK06194    4 FAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRA-----QGAEVLGVRTDVSDAAQVEALADAAL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 115 DTFGKINFLVNN---GGGQFLspAEHiSSKGWHAVLETNLTGTFY 156
Cdd:PRK06194   79 ERFGAVHLLFNNagvGAGGLV--WEN-SLADWEWVLGVNLWGVIH 120
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 33-161 1.47e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 80.00  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK07890    1 MLLKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDD-----LGRRALAVPTDITDEDQCANLVAL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 113 TLDTFGKINFLVNNGGG-QFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07890   76 ALERFGRVDALVNNAFRvPSMKPLADADFAHWRAVIELNVLGTLRLTQAF 125
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 35-161 1.77e-18

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: 79.76  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQARVIPiqCNIRNEEEVNNLVKSTL 114
Cdd:cd05364     1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKILLVV--ADLTEEEGQDRIISTTL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05364    79 AKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLA 125
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 28-161 2.05e-18

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: 80.03  E-value: 2.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  28 SYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKsaADElqanlppTKQA------RVIPIQCNIR 101
Cdd:cd05355    17 SYKGSGKLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDD--AEE-------TKKLieeegrKCLLIPGDLG 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 102 NEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPA-EHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05355    88 DESFCRDLVKEVVKEFGKLDILVNNAAYQHPQESiEDITTEQLEKTFRTNIFSMFYLTKAA 148
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 29-164 2.39e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 80.08  E-value: 2.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  29 YLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASrkLERLKSAADelqanlppTKQA------RVIPIQCNIRN 102
Cdd:PRK06701   38 YKGSGKLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVY--LDEHEDANE--------TKQRvekegvKCLLIPGDVSD 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462575256 103 EEEVNNLVKSTLDTFGKINFLVNNGGGQF-LSPAEHISSKGWHAVLETNLTGTFYMCK-AVDQL 164
Cdd:PRK06701  108 EAFCKDAVEETVRELGRLDILVNNAAFQYpQQSLEDITAEQLDKTFKTNIYSYFHMTKaALPHL 171
PRK05867 PRK05867
SDR family oxidoreductase;
35-160 2.54e-18

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 79.31  E-value: 2.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK05867    7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTS-----GGKVVPVCCDVSQHQQVTSMLDQVT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK05867   82 AELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQA 127
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 37-161 2.70e-18

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: 79.41  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIAS-RKLERLKSAADELQAnlppTKQARVIPIQCNIRNEEEVNNLVKSTLD 115
Cdd:cd08940     2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGfGDAAEIEAVRAGLAA----KHGVKVLYHGADLSKPAAIEDMVAYAQR 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 116 TFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd08940    78 QFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLA 123
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 35-160 4.16e-18

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 78.84  E-value: 4.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkqaRVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK07576    7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGP-----EGLGVSADVRDYAAVEAAFAQIA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK07576   82 DEFGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKA 127
PRK07814 PRK07814
SDR family oxidoreductase;
35-134 6.58e-18

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 78.67  E-value: 6.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlppTKQARVIPiqCNIRNEEEVNNLVKSTL 114
Cdd:PRK07814    8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAA---GRRAHVVA--ADLAHPEATAGLAGQAV 82

                          90       100
                  ....*....|....*....|
gi 2462575256 115 DTFGKINFLVNNGGGQFLSP 134
Cdd:PRK07814   83 EAFGRLDIVVNNVGGTMPNP 102
SDR_dihy_bifunc NF012208
bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family ...
 40-160 8.12e-18

bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family are SDR family oxidoreductases, unrelated to previously known families of dihydrofolate reductase (DHFR), one of which was demonstrated to be a bifunctional dihydropteridine reductase/dihydrofolate reductase. The DHFR activity can give a heterologously expressed protein the ability to confer resistance to trimethoprim, an inhibitor of most forms of DHFR.


Pssm-ID: 411089 [Multi-domain]  Cd Length: 233  Bit Score: 77.65  E-value: 8.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRKlerlkSAADELQ-ANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:NF012208    1 ALVTGSARGIGRAIALALAREGFDVAVHYRR-----SAEAAEQtAQEAEALGVKAITLQADLTDPEQARSLVEEAAEALG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 119 KINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:NF012208   76 GLSVLVNNVGNYLHKPLLETTDEEWHEMLDSNLNATFYVTQA 117
PLN02253 PLN02253
xanthoxin dehydrogenase
 20-155 8.67e-18

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 78.33  E-value: 8.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  20 MASWAKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlerlksaaDELQANLPPT--KQARVIPIQ 97
Cdd:PLN02253    1 MATASSSASSLPSQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQ--------DDLGQNVCDSlgGEPNVCFFH 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  98 CNIRNEEEVNNLVKSTLDTFGKINFLVNNGG--GQFLSPAEHISSKGWHAVLETNLTGTF 155
Cdd:PLN02253   73 CDVTVEDDVSRAVDFTVDKFGTLDIMVNNAGltGPPCPDIRNVELSEFEKVFDVNVKGVF 132
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-156 1.51e-17

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 77.52  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIasrKLERLKSAADELqanlpptKQARVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK06463    3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVAV---LYNSAENEAKEL-------REKGVFTIKCDVGNRDQVKKSKEV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 113 TLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFY 156
Cdd:PRK06463   73 VEKEFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIY 116
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 36-161 1.56e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 77.64  E-value: 1.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSaadelqanlpptkQARVIPIQCNIRNEEEVNNLVKSTLD 115
Cdd:PRK06179    3 NSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAP-------------IPGVELLELDVTDDASVQAAVDEVIA 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 116 TFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06179   70 RAGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAV 115
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-155 1.86e-17

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 76.92  E-value: 1.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK08217    3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGA-----LGTEVRGYAANVTDEEDVEATFAQIA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 115 DTFGKINFLVNNGG----GQFLSPAEH-ISSK----GWHAVLETNLTGTF 155
Cdd:PRK08217   78 EDFGQLNGLINNAGilrdGLLVKAKDGkVTSKmsleQFQSVIDVNLTGVF 127
PRK07201 PRK07201
SDR family oxidoreductase;
33-128 1.91e-17

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 78.84  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK07201  367 GPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRA-----KGGTAHAYTCDLTDSAAVDHTVKD 441

                          90
                  ....*....|....*.
gi 2462575256 113 TLDTFGKINFLVNNGG 128
Cdd:PRK07201  442 ILAEHGHVDYLVNNAG 457
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 35-161 1.91e-17

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 76.97  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIasrKLERLKSAADELQANLpPTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK12935    4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAENLVNEL-GKEGHDVYAVQADVSKVEDANRLVEEAV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12935   80 NHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAV 126
PRK07035 PRK07035
SDR family oxidoreductase;
35-164 2.70e-17

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 76.59  E-value: 2.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK07035    6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVA-----AGGKAEALACHIGEMEQIDALFAHIR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 115 DTFGKINFLVNNGGGQ-FLSPAEHISSKGWHAVLETNLTGTFYMCKAVDQL 164
Cdd:PRK07035   81 ERHGRLDILVNNAAANpYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKL 131
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 35-160 2.76e-17

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: 76.19  E-value: 2.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLksaaDELQANLPPTKQarvipIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05370     3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERL----AEAKKELPNIHT-----IVLDVGDAESVEALAEALL 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 115 DTFGKINFLVNNGGGQ----FLSPAEHisSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd05370    74 SEYPNLDILINNAGIQrpidLRDPASD--LDKADTEIDTNLIGPIRLIKA 121
PRK07774 PRK07774
SDR family oxidoreductase;
33-161 4.63e-17

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 75.94  E-value: 4.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK07774    2 GRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVA-----DGGTAIAVQVDVSDPDSAKAMADA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462575256 113 TLDTFGKINFLVNNG---GGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07774   77 TVSAFGGIDYLVNNAaiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAV 128
PRK07856 PRK07856
SDR family oxidoreductase;
35-160 4.88e-17

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 75.74  E-value: 4.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlerlksaadelQANLPPTKQARVIPiqCNIRNEEEVNNLVKSTL 114
Cdd:PRK07856    4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR-----------APETVDGRPAEFHA--ADVRDPDQVAALVDAIV 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK07856   71 ERHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQA 116
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 35-161 5.93e-17

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: 76.02  E-value: 5.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05330     1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAP---DAEVLLIKADVSDEAQVEAYVDATV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462575256 115 DTFGKINFLVNNGG--GQfLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05330    78 EQFGRIDGFFNNAGieGK-QNLTEDFGADEFDKVVSINLRGVFYGLEKV 125
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 35-156 7.01e-17

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 75.71  E-value: 7.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK08277    8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAA-----GGEALAVKADVLDKESLEQARQQIL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGG------------QFLSPAEHI---SSKGWHAVLETNLTGTFY 156
Cdd:PRK08277   83 EDFGPCDILINGAGGnhpkattdnefhELIEPTKTFfdlDEEGFEFVFDLNLLGTLL 139
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-161 9.31e-17

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 75.13  E-value: 9.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRkleRLKSAADELQANLPPtkqaRVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK08642    3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYH---QSEDAAEALADELGD----RAIALQADVTDREQVQAMFATAT 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462575256 115 DTFGK-INFLVNNGGGQFL------SPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK08642   76 EHFGKpITTVVNNALADFSfdgdarKKADDITWEDFQQQLEGSVKGALNTIQAA 129
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 37-160 1.01e-16

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: 75.11  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLER-LKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTLD 115
Cdd:cd05366     2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEaAKSTIQEISE-----AGYNAVAVGADVTDKDDVEALIDQAVE 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 116 TFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd05366    77 KFGSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQA 121
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 33-160 1.01e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 74.97  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK07478    2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRA-----EGGEAVALAGDVRDEAYAKALVAL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 113 TLDTFGKINFLVNNGG--GQfLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK07478   77 AVERFGGLDIAFNNAGtlGE-MGPVAEMSLEGWRETLATNLTSAFLGAKH 125
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 35-159 1.07e-16

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: 74.83  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLErlksAADELQANLPPTKQArvipIQCNIRNEEEVNNLVKSTL 114
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGG----AAQAVVAQIAGGALA----LRVDVTDEQQVAALFERAV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPA-EHISSKGWHAVLETNLTGTFYMCK 159
Cdd:cd08944    73 EEFGGLDLLVNNAGAMHLTPAiIDTDLAVWDQTMAINLRGTFLCCR 118
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 35-159 1.27e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 75.22  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnLPPTKQARVIPiqCNIRNEEEVNNLVKSTL 114
Cdd:PRK05875    5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEA-LKGAGAVRYEP--ADVTDEDQVARAVDAAT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGG-QFLSPAEHISSKGWHAVLETNLTGTFYMCK 159
Cdd:PRK05875   82 AWHGRLHGVVHCAGGsETIGPITQIDSDAWRRTVDLNVNGTMYVLK 127
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
37-163 1.38e-16

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 74.76  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK08643    2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKD-----GGKAIAVKADVSDRDQVFAAVRQVVDT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFY-MCKAVDQ 163
Cdd:PRK08643   77 FGDLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWgIQAAQEA 124
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 35-161 1.41e-16

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: 74.73  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLpptkqarvIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05345     3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAA--------IAIQADVTKRADVEAMVEAAL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 115 DTFGKINFLVNNGGGQFLS-PAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05345    75 SKFGRLDILVNNAGITHRNkPMLEVDEEEFDRVFAVNVKSIYLSAQAL 122
PRK06138 PRK06138
SDR family oxidoreductase;
35-161 1.72e-16

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 74.42  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLErlksAADELQANLPPTKQARVipIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK06138    3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAE----AAERVAAAIAAGGRAFA--RQGDVGSAEAVEALVDFVA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06138   77 ARWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYA 123
PRK06181 PRK06181
SDR family oxidoreductase;
37-160 1.84e-16

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 74.63  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPtkqARVIPiqCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK06181    1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGE---ALVVP--TDVSDAEACERLIEAAVAR 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGW-HAVLETNLTGTFYMCKA 160
Cdd:PRK06181   76 FGGIDILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHA 120
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 35-161 2.40e-16

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: 74.10  E-value: 2.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd08937     2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEILAA-----GDAAHVHTADLETYAGAQGVVRAAV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 115 DTFGKINFLVNN-GGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd08937    76 ERFGRVDVLINNvGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAV 123
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 35-163 2.78e-16

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: 73.81  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkqarVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPA--------ACAISLDVTDQASIDRCVAALV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVDQ 163
Cdd:cd05363    73 DRWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVAR 121
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 35-160 3.55e-16

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: 73.67  E-value: 3.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanlppTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd08942     4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEEL------SAYGECIAIPADLSSEEGIEALVARVA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd08942    78 ERSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQA 123
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
33-161 3.58e-16

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 73.68  E-value: 3.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIA--SRKLERLksaADELQAnlpptKQARVIPIQCNIRNEEEVNNLV 110
Cdd:PRK08226    2 GKLTGKTALITGALQGIGEGIARVFARHGANLILLdiSPEIEKL---ADELCG-----RGHRCTAVVADVRDPASVAAAI 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 111 KSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK08226   74 KRAKEKEGRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAV 124
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 35-160 3.59e-16

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 73.63  E-value: 3.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLE---RLK----SAADELQAnlpptKQARVIPIQCNIRNEEEVN 107
Cdd:cd09762     1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpKLPgtiyTAAEEIEA-----AGGKALPCIVDIRDEDQVR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462575256 108 NLVKSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd09762    76 AAVEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKA 128
PRK06114 PRK06114
SDR family oxidoreductase;
35-160 7.79e-16

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 72.89  E-value: 7.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLER-LKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKST 113
Cdd:PRK06114    6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAETAEHIEA-----AGRRAIQIAADVTSKADLRAAVART 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 114 LDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK06114   81 EAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQA 127
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 35-163 1.20e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 72.11  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQARVipiqcNIRNEEEVNNLVKSTL 114
Cdd:PRK07523    8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAF-----DVTDHDAVRAAIDAFE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVDQ 163
Cdd:PRK07523   83 AEIGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVAR 131
PRK07074 PRK07074
SDR family oxidoreductase;
38-161 1.35e-15

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 72.11  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptkqARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:PRK07074    3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGD-------ARFVPVACDLTDAASLAAALANAAAER 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 118 GKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07074   76 GPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAV 119
PRK09135 PRK09135
pteridine reductase; Provisional
 36-160 1.35e-15

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 71.88  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRkleRLKSAADELQANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLD 115
Cdd:PRK09135    5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYH---RSAAEADALAAELNALRPGSAAALQADLLDPDALPELVAACVA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 116 TFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK09135   82 AFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQA 126
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 35-161 1.72e-15

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 71.84  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVViasrklerlksAADelqANLPPTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK08220    6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVI-----------GFD---QAFLTQEDYPFATFVLDVSDAAAVAQVCQRLL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK08220   72 AETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAV 118
PRK07454 PRK07454
SDR family oxidoreductase;
34-161 2.09e-15

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 71.53  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  34 LLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKST 113
Cdd:PRK07454    3 LNSMPRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRS-----TGVKAAAYSIDLSNPEAIAPGIAEL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 114 LDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07454   78 LEQFGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAV 125
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 35-160 2.38e-15

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 71.31  E-value: 2.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVI--ASRklerlKSAADELQANLpPTKQARVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK12937    3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVnyAGS-----AAAADELVAEI-EAAGGRAIAVQADVADAAAVTRLFDA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 113 TLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK12937   77 AETAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLRE 124
PRK06124 PRK06124
SDR family oxidoreductase;
28-165 2.55e-15

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 71.28  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  28 SYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVN 107
Cdd:PRK06124    2 SILQRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRA-----AGGAAEALAFDIADEEAVA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462575256 108 NLVKSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVDQLI 165
Cdd:PRK06124   77 AAFARIDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRM 134
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 35-155 2.62e-15

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 72.64  E-value: 2.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlppTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:COG3347   423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGG---YGADAVDATDVDVTAEAAVAAAFGFAG 499

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTF 155
Cdd:COG3347   500 LDIGGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQF 540
PRK06172 PRK06172
SDR family oxidoreductase;
35-155 3.53e-15

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 70.94  E-value: 3.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlerlksaADELQANLPPTKQA--RVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK06172    5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRD-------AAGGEETVALIREAggEALFVACDVTRDAEVKALVEQ 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 113 TLDTFGKINFLVNNGG-GQFLSPAEHISSKGWHAVLETNLTGTF 155
Cdd:PRK06172   78 TIAAYGRLDYAFNNAGiEIEQGRLAEGSEAEFDAIMGVNVKGVW 121
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 39-160 6.12e-15

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 69.96  E-value: 6.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSN-VVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:cd05324     2 VALVTGANRGIGFEIVRQLAKSGPGtVILTARDVERGQAAVEKLRA-----EGLSVRFHQLDVTDDASIEAAADFVEEKY 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 118 GKINFLVNNGG-----GQFLSPAEHIsskgWHAVLETNLTGTFYMCKA 160
Cdd:cd05324    77 GGLDILVNNAGiafkgFDDSTPTREQ----ARETMKTNFFGTVDVTQA 120
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 39-161 7.62e-15

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 69.79  E-value: 7.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLpptkqarvIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:PRK10538    2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNL--------YIAQLDVRNRAAIEEMLASLPAEWR 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 119 KINFLVNNGGGQF-LSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK10538   74 NIDVLVNNAGLALgLEPAHKASVEDWETMIDTNNKGLVYMTRAV 117
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 35-161 1.00e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 69.71  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK07097    8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRE-----LGIEAHGYVCDVTDEDGVQAMVSQIE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07097   83 KEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAV 129
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 38-161 1.11e-14

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 69.61  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIAS-RKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK12745    3 PVALVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELRA-----LGVEVIFFPADVADLSAHEAMLDAAQAA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 117 FGKINFLVNNGG------GQFLSPAEhissKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12745   78 WGRIDCLVNNAGvgvkvrGDLLDLTP----ESFDRVLAINLRGPFFLTQAV 124
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 35-161 1.14e-14

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: 69.49  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd08936     8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQG-----EGLSVTGTVCHVGKAEDRERLVATAV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462575256 115 DTFGKINFLVNNGG-----GQFLSPAEHIsskgWHAVLETNLTGTFYMCKAV 161
Cdd:cd08936    83 NLHGGVDILVSNAAvnpffGNILDSTEEV----WDKILDVNVKATALMTKAV 130
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 33-176 1.79e-14

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 69.21  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIasrkLERLKSAADELQANLPptkqARVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK06200    2 GWLHGQVALITGGGSGIGRALVERFLAEGARVAV----LERSAEKLASLRQRFG----DHVLVVEGDVTSYADNQRAVDQ 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462575256 113 TLDTFGKINFLVNNGG-GQFLSPAEHIS----SKGWHAVLETNLTGTFYMCKAvdqliwllCLFEMAQT 176
Cdd:PRK06200   74 TVDAFGKLDCFVGNAGiWDYNTSLVDIPaetlDTAFDEIFNVNVKGYLLGAKA--------ALPALKAS 134
PRK06484 PRK06484
short chain dehydrogenase; Validated
 18-160 1.80e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 70.26  E-value: 1.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  18 AGMASWAKGRSYLAPgllQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAAdELQANLPPTKQArvipiq 97
Cdd:PRK06484  253 SGPASTAQAPSPLAE---SPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLA-EALGDEHLSVQA------ 322

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462575256  98 cNIRNEEEVNNLVKSTLDTFGKINFLVNNGG-GQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK06484  323 -DITDEAAVESAFAQIQARWGRLDVLVNNAGiAEVFKPSLEQSAEDFTRVYDVNLSGAFACARA 385
PRK08628 PRK08628
SDR family oxidoreductase;
35-128 2.18e-14

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 68.83  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK08628    5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRS-APDDEFAEELRA-----LQPRAEFVQVDLTDDAQCRDAVEQTV 78

                          90
                  ....*....|....
gi 2462575256 115 DTFGKINFLVNNGG 128
Cdd:PRK08628   79 AKFGRIDGLVNNAG 92
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 39-160 2.52e-14

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 68.16  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADElqanlpptkQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:cd08932     2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS---------GGDVEAVPYDARDPEDARALVDALRDRFG 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 119 KINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd08932    73 RIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRA 114
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 39-161 2.55e-14

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 68.47  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELG--SNVVIASRKLERLKSAADELQANLpptkqaRVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEELRPGL------RVTTVKADLSDAAGVEQLLEAIRKL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 117 FGKINFLVNNGG--GQfLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05367    75 DGERDLLINNAGslGP-VSKIEFIDLDELQKYFDLNLTSPVCLTSTL 120
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 32-161 3.01e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 68.49  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  32 PGLLQGQVAIVTGGATGIGKAIVKELLELG-SNVVIASRKLERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLV 110
Cdd:PRK06198    1 MGRLDGKVALVTGGTQGLGAAIARAFAERGaAGLVICGRNAEKGEAQAAELEAL-----GAKAVFVQADLSDVEDCRRVV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575256 111 KSTLDTFGKINFLVNNGG----GQFL--SPAEhisskgWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06198   76 AAADEAFGRLDALVNAAGltdrGTILdtSPEL------FDRHFAVNVRAPFFLMQEA 126
PRK09186 PRK09186
flagellin modification protein A; Provisional
 34-126 3.99e-14

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 68.09  E-value: 3.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  34 LLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLpptKQARVIPIQCNIRNEEEVNNLVKST 113
Cdd:PRK09186    1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEF---KSKKLSLVELDITDQESLEEFLSKS 77

                          90
                  ....*....|...
gi 2462575256 114 LDTFGKINFLVNN 126
Cdd:PRK09186   78 AEKYGKIDGAVNC 90
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 38-161 4.72e-14

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 67.87  E-value: 4.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRkleRLKSAADELQANLpptkQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNYY---RSTESAEAVAAEA----GERAIAIQADVRDRDQVQAMIEEAKNHF 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 118 GKINFLVNNGGGQFL------SPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05349    74 GPVDTIVNNALIDFPfdpdqrKTFDTIDWEDYQQQLEGAVKGALNLLQAV 123
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
38-161 6.58e-14

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 67.48  E-value: 6.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKlerLKSAADELQaNLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:PRK12824    3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFS---GNDCAKDWF-EEYGFTEDQVRLKELDVTDTEECAEALAEIEEEE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 118 GKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12824   79 GPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPL 122
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 39-161 9.92e-14

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: 66.88  E-value: 9.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIasrkLERLKSAADELQANLPPTkQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVI----LDINEKGAEETANNVRKA-GGKVHYYKCDVSKREEVYEAAKKIKKEVG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462575256 119 KINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05339    76 DVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAF 118
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 35-156 1.05e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 67.64  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK07109    6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRA-----AGGEALAVVADVADAEAVQAAADRAE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFY 156
Cdd:PRK07109   81 EELGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVH 122
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 36-165 1.07e-13

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 67.10  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLpptkQARVIPIQCNIRNEEEVNNLVKSTLD 115
Cdd:cd05322     1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEY----GEKAYGFGADATNEQSVIALSKGVDE 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462575256 116 TFGKINFLVNNGGgqfLSPAEHISS---KGWHAVLETNLTGTFYMCKAVDQLI 165
Cdd:cd05322    77 IFKRVDLLVYSAG---IAKSAKITDfelGDFDRSLQVNLVGYFLCAREFSKLM 126
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 35-165 1.60e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 66.92  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK05872    7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGG------DDRVLTVVADVTDLAAMQAAAEEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA-VDQLI 165
Cdd:PRK05872   81 ERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRAtLPALI 132
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 35-156 1.62e-13

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 66.71  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd08935     3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITA-----LGGRAIALAADVLDRASLERAREEIV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGG---------QFLSPAEH-----ISSKGWHAVLETNLTGTFY 156
Cdd:cd08935    78 AQFGTVDILINGAGGnhpdattdpEHYEPETEqnffdLDEEGWEFVFDLNLNGSFL 133
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 38-160 2.03e-13

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 65.87  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQanlppTKQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:cd05360     1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVR-----ELGGEAIAVVADVADAAQVERAADTAVERF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462575256 118 GKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd05360    76 GRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLA 118
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 35-161 2.53e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 65.90  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPtKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK12827    4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEA-AGGKALGLAFDVRDFAATRAALDAGV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12827   83 EEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAA 129
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 35-163 4.69e-13

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 64.94  E-value: 4.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanlppTKQARVIPiqCNIRNEEEVNNLVKSTL 114
Cdd:PRK12936    4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAEL------GERVKIFP--ANLSDRDEVKALGQKAE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462575256 115 DTFGKINFLVNNGG----GQFLspaeHISSKGWHAVLETNLTGTFYMCKAVDQ 163
Cdd:PRK12936   76 ADLEGVDILVNNAGitkdGLFV----RMSDEDWDSVLEVNLTATFRLTRELTH 124
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 40-161 5.87e-13

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 64.66  E-value: 5.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanLPPTKQARVIPiqCNIRNEEEVNNLVKSTLDTFGK 119
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAEL---LNPNPSVEVEI--LDVTDEERNQLVIAELEAELGG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 120 INFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05350    76 LDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAA 117
PRK06484 PRK06484
short chain dehydrogenase; Validated
 36-165 7.45e-13

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 65.64  E-value: 7.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADelqaNLPPTKQArvipIQCNIRNEEEVNNLVKSTLD 115
Cdd:PRK06484    4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERAD----SLGPDHHA----LAMDVSDEAQIREGFEQLHR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462575256 116 TFGKINFLVNNGG--GQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVDQLI 165
Cdd:PRK06484   76 EFGRIDVLVNNAGvtDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLM 127
PRK08264 PRK08264
SDR family oxidoreductase;
35-160 8.46e-13

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 64.14  E-value: 8.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELG-SNVVIASRKLERLKSAADelqanlpptkqaRVIPIQCNIRNEEEVNNLVKST 113
Cdd:PRK08264    4 IKGKVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVTDLGP------------RVVPLQLDVTDPASVAAAAEAA 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462575256 114 LDtfgkINFLVNNGG-----GQFLSPAEhissKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK08264   72 SD----VTILVNNAGifrtgSLLLEGDE----DALRAEMETNYFGPLAMARA 115
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 33-161 8.59e-13

(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: 64.27  E-value: 8.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVI----ASRKLERLKSAADELQANLPPTKQARVIPiqcNIRNEEEVNN 108
Cdd:cd05353     1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlgGDRKGSGKSSSAADKVVDEIKAAGGKAVA---NYDSVEDGEK 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575256 109 LVKSTLDTFGKINFLVNNGG----GQFLSpaehISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05353    78 IVKTAIDAFGRVDILVNNAGilrdRSFAK----MSEEDWDLVMRVHLKGSFKVTRAA 130
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 37-161 1.24e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 63.97  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkqarviPIQCNIRNEEEVNNlvksTLDT 116
Cdd:PRK07060    9 GKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCE----------PLRLDVGDDAAIRA----ALAA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07060   75 AGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHV 119
PRK08340 PRK08340
SDR family oxidoreductase;
41-128 1.35e-12

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 64.06  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  41 IVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQanlpptKQARVIPIQCNIRNEEEVNNLVKSTLDTFGKI 120
Cdd:PRK08340    4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELK------EYGEVYAVKADLSDKDDLKNLVKEAWELLGGI 77


                  ....*...
gi 2462575256 121 NFLVNNGG 128
Cdd:PRK08340   78 DALVWNAG 85
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 35-151 1.69e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 63.77  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRklerlksaadelqaNLPPTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK06523    7 LAGKRALVTGGTKGIGAATVARLLEAGARVVTTAR--------------SRPDDLPEGVEFVAADLTTAEGCAAVARAVL 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462575256 115 DTFGKINFLVNNGGGQ------FLSpaehISSKGWHAVLETNL 151
Cdd:PRK06523   73 ERLGGVDILVHVLGGSsapaggFAA----LTDEEWQDELNLNL 111
PRK05866 PRK05866
SDR family oxidoreductase;
1-149 3.43e-12

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 63.22  E-value: 3.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256   1 MSLRPRRACAQLLWHpaAGMaswakgRSYLAPGLLQGQVAI-----------VTGGATGIGKAIVKELLELGSNVVIASR 69
Cdd:PRK05866    1 MSKRPLRRLTDQLTL--AGM------RPPISPQLLINRPPRqpvdltgkrilLTGASSGIGEAAAEQFARRGATVVAVAR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  70 KLERLKSAADELQANlppTKQARVIPiqCNIRNEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHiSSKGWHAVLET 149
Cdd:PRK05866   73 REDLLDAVADRITRA---GGDAMAVP--CDLSDLDAVDALVADVEKRIGGVDILINNAGRSIRRPLAE-SLDRWHDVERT 146
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 35-160 4.44e-12

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 62.37  E-value: 4.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkqarVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:cd05348     2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDA--------VVGVEGDVRSLADNERAVARCV 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462575256 115 DTFGKINFLVNNGG--GQFLS----PAEHIsSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd05348    74 ERFGKLDCFIGNAGiwDYSTSlvdiPEEKL-DEAFDELFHINVKGYILGAKA 124
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 39-161 4.46e-12

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 62.48  E-value: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRkleRLKSAADELQANLpPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:cd05337     3 VAIVTGASRGIGRAIATELAARGFDIAINDL---PDDDQATEVVAEV-LAAGRRAIYFQADIGELSDHEALLDQAWEDFG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462575256 119 KINFLVNNGG------GQFLSPAEhissKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05337    79 RLDCLVNNAGiavrprGDLLDLTE----DSFDRLIAINLRGPFFLTQAV 123
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 35-161 4.52e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 62.46  E-value: 4.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK08085    7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQ-----EGIKAHAAPFNVTHKQEVEAAIEHIE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK08085   82 KDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAV 128
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
35-161 4.60e-12

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 62.58  E-value: 4.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLE-----LGSNVVIASRKLERLKSAAdelqanlpptkqARVIPIQCNIRNEEEVNNL 109
Cdd:PRK08993    8 LEGKVAVVTGCDTGLGQGMALGLAEagcdiVGINIVEPTETIEQVTALG------------RRFLSLTADLRKIDGIPAL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462575256 110 VKSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK08993   76 LERAVAEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAA 127
PRK05855 PRK05855
SDR family oxidoreductase;
7-160 4.96e-12

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 63.46  E-value: 4.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256   7 RACAQLLWHPAAGMASWAKGRSYLAP--GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAn 84
Cdd:PRK05855  283 AAVAEFVDAVEGGPPARALLRARVGRprGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRA- 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  85 lpptKQARVIPIQCNIRNEEEVNNLVKSTLDTFGKINFLVNNGG----GQFL-SPAEHisskgWHAVLETNLTGTFYMCK 159
Cdd:PRK05855  362 ----AGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDIVVNNAGigmaGGFLdTSAED-----WDRVLDVNLWGVIHGCR 432


                  .
gi 2462575256 160 A 160
Cdd:PRK05855  433 L 433
PRK12743 PRK12743
SDR family oxidoreductase;
38-155 5.05e-12

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 62.36  E-value: 5.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKLER-LKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK12743    3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEgAKETAEEVRS-----HGVRAEIRQLDLSDLPEGAQALDKLIQR 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTF 155
Cdd:PRK12743   78 LGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAF 116
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 31-160 5.13e-12

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 62.20  E-value: 5.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  31 APGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADEL-QANLPptkQARVIPIQCNIRNEEEVNNL 109
Cdd:PRK08945    6 KPDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIeAAGGP---QPAIIPLDLLTATPQNYQQL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462575256 110 VKSTLDTFGKINFLVNNGG--GQfLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK08945   83 ADTIEEQFGRLDGVLHNAGllGE-LGPMEQQDPEVWQDVMQVNVNATFMLTQA 134
PRK06914 PRK06914
SDR family oxidoreductase;
37-161 5.99e-12

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 62.35  E-value: 5.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLER---LKSAADelQANLpptkQARVIPIQCNIRNEEEVNNlVKST 113
Cdd:PRK06914    3 KKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKqenLLSQAT--QLNL----QQNIKVQQLDVTDQNSIHN-FQLV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 114 LDTFGKINFLVNNGG---GQFlspAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06914   76 LKEIGRIDLLVNNAGyanGGF---VEEIPVEEYRKQFETNVFGAISVTQAV 123
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 31-161 6.21e-12

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 62.27  E-value: 6.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  31 APGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLV 110
Cdd:PRK12823    2 MNQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELRAA-----GGEALALTADLETYAGAQAAM 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462575256 111 KSTLDTFGKINFLVNN-GGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12823   76 AAAVEAFGRIDVLINNvGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAV 127
PRK06182 PRK06182
short chain dehydrogenase; Validated
 36-153 6.31e-12

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 62.28  E-value: 6.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADelqanlpptkqARVIPIQCNIRNEEEVNNLVKSTLD 115
Cdd:PRK06182    2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLAS-----------LGVHPLSLDVTDEASIKAAVDTIIA 70

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462575256 116 TFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTG 153
Cdd:PRK06182   71 EEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFG 108
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 35-161 7.40e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 61.74  E-value: 7.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIasrkLERLKSAADELQANLPPTKqARVIPIqcNIRNEEEVNNLVKSTL 114
Cdd:PRK12828    5 LQGKVVAITGGFGGLGRATAAWLAARGARVAL----IGRGAAPLSQTLPGVPADA-LRIGGI--DLVDPQAARRAVDEVN 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12828   78 RQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAA 124
PRK06128 PRK06128
SDR family oxidoreductase;
28-160 1.32e-11

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 61.41  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  28 SYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERlKSAADELQANLPPTKQARVIPiqCNIRNEEEVN 107
Cdd:PRK06128   46 SYKGFGRLQGRKALITGADSGIGRATAIAFAREGADIALNYLPEEE-QDAAEVVQLIQAEGRKAVALP--GDLKDEAFCR 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462575256 108 NLVKSTLDTFGKINFLVNNGGGQ-FLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK06128  123 QLVERAVKELGGLDILVNIAGKQtAVKDIADITTEQFDATFKTNVYAMFWLCKA 176
PRK09072 PRK09072
SDR family oxidoreductase;
35-167 2.09e-11

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 60.73  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanlppTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK09072    3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARL------PYPGRHRWVVADLTSEAGREAVLARAR 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462575256 115 DtFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVdqLIWL 167
Cdd:PRK09072   77 E-MGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRAL--LPLL 126
PRK07069 PRK07069
short chain dehydrogenase; Validated
 40-159 2.24e-11

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 60.49  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIAS-RKLERLKSAADELQANL-PPTKQArvipIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:PRK07069    2 AFITGAAGGLGRAIARRMAEQGAKVFLTDiNDAAGLDAFAAEINAAHgEGVAFA----AVQDVTDEAQWQALLAQAADAM 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 118 GKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCK 159
Cdd:PRK07069   78 GGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCK 119
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 35-143 2.34e-11

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 60.54  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLE-RLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLV-KS 112
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEA-----RGGKCIPVRCDHSDDDEVEALFeRV 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462575256 113 TLDTFGKINFLVNNGGGQFLSPAEHISSKGW 143
Cdd:cd09763    76 AREQQGRLDILVNNAYAAVQLILVGVAKPFW 106
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 37-128 2.73e-11

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: 60.56  E-value: 2.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlppTKQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd09807     1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRD---TLNHEVIVRHLDLASLKSIRAFAAEFLAE 77

                          90
                  ....*....|..
gi 2462575256 117 FGKINFLVNNGG 128
Cdd:cd09807    78 EDRLDVLINNAG 89
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 40-161 4.25e-11

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 59.62  E-value: 4.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIAS-RKlerlKSAADELQANLPptKQARVIPIQCNIRNE-----EEVNNLVKST 113
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNTVIATcRD----PSAATELAALGA--SHSRLHILELDVTDEiaesaEAVAERLGDA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 114 ldtfgKINFLVNNGGgqFLSP---AEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05325    75 -----GLDVLINNAG--ILHSygpASEVDSEDLLEVFQVNVLGPLLLTQAF 118
PRK06196 PRK06196
oxidoreductase; Provisional
 35-155 6.07e-11

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 59.70  E-value: 6.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanlpptKQARVIPIqcNIRNEEEVNNLVKSTL 114
Cdd:PRK06196   24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI-------DGVEVVML--DLADLESVRAFAERFL 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462575256 115 DTFGKINFLVNNGGgqFLSPAEHISSKGWHAVLETNLTGTF 155
Cdd:PRK06196   95 DSGRRIDILINNAG--VMACPETRVGDGWEAQFATNHLGHF 133
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 39-164 7.04e-11

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 58.83  E-value: 7.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRKLErlkSAADELQANLpPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:cd05357     2 VALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSE---AEAQRLKDEL-NALRNSAVLVQADLSDFAACADLVAAAFRAFG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 119 KINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVDQL 164
Cdd:cd05357    78 RCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARR 123
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-156 8.09e-11

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 58.96  E-value: 8.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlerlksAADELQANLPPTKQA--RVIPIQCNIRNEEEVNNLVKS 112
Cdd:PRK06077    4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKK------RAEEMNETLKMVKENggEGIGVLADVSTREGCETLAKA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 113 TLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFY 156
Cdd:PRK06077   78 TIDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIY 121
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 37-159 8.48e-11

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: 58.74  E-value: 8.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkqarVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd09761     1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPN--------LFFVHGDVADETLVKFVVYAMLEK 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCK 159
Cdd:cd09761    73 LGRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSR 115
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 35-161 1.09e-10

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 58.80  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanlpptKQARVIPIqcNIRNEEEVNNLVKSTL 114
Cdd:PRK07825    3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL-------GLVVGGPL--DVTDPASFAAFLDAVE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 115 DTFGKINFLVNNGG----GQFLSPAEHISskgwHAVLETNLTGTFYMCKAV 161
Cdd:PRK07825   74 ADLGPIDVLVNNAGvmpvGPFLDEPDAVT----RRILDVNVYGVILGSKLA 120
PRK06949 PRK06949
SDR family oxidoreductase;
35-161 1.38e-10

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 58.23  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlppTKQARVIPIqcNIRNEEEVNNLVKSTL 114
Cdd:PRK06949    7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAE---GGAAHVVSL--DVTDYQSIKAAVAHAE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06949   82 TEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEV 128
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 34-160 1.48e-10

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 57.97  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  34 LLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPtkQARVIPIQCNIRNEEEVNNLVKST 113
Cdd:cd05340     1 LLNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGR--QPQWFILDLLTCTSENCQQLAQRI 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 114 LDTFGKINFLVNNGGGQF-LSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd05340    79 AVNYPRLDGVLHNAGLLGdVCPLSEQNPQVWQDV*QVNVNATFMLTQA 126
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 37-160 1.63e-10

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 58.43  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK05876    6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRA-----EGFDVHGVMCDVRHREEVTHLADEAFRL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK05876   81 LGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEA 124
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 37-161 1.79e-10

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 58.13  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptkqaRVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK08263    3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGD--------RLLPLALDVTDRAAVFAAVETAVEH 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK08263   75 FGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAV 119
PRK07806 PRK07806
SDR family oxidoreductase;
32-129 6.14e-10

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 56.27  E-value: 6.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  32 PGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASR-KLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLV 110
Cdd:PRK07806    1 MGDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRqKAPRANKVVAEIEA-----AGGRASAVGADLTDEESVAALM 75

                          90
                  ....*....|....*....
gi 2462575256 111 KSTLDTFGKINFLVNNGGG 129
Cdd:PRK07806   76 DTAREEFGGLDALVLNASG 94
PRK06123 PRK06123
SDR family oxidoreductase;
38-159 6.64e-10

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 56.33  E-value: 6.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRkleRLKSAADELQANLpPTKQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:PRK06123    3 KVMIITGASRGIGAATALLAAERGYAVCLNYL---RNRDAAEAVVQAI-RRQGGEALAVAADVADEADVLRLFEAVDREL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 118 GKINFLVNNGGgqFLSPA---EHISSKGWHAVLETNLTGTFYMCK 159
Cdd:PRK06123   79 GRLDALVNNAG--ILEAQmrlEQMDAARLTRIFATNVVGSFLCAR 121
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 40-161 1.18e-09

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: 55.55  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADelqanlpptkQARVIPIqcNIRNEEEVNNLVKSTLDTFGK 119
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGD----------PLRLTPL--DVADAAAVREVCSRLLAEHGP 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 120 INFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05331    69 IDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAV 110
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 36-161 1.18e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 55.69  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlerlKSAADELQANLPptkqARVIPIQCNIRNEEEVNNLVKSTLD 115
Cdd:PRK06180    3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRS----EAARADFEALHP----DRALARLLDVTDFDAIDAVVADAEA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 116 TFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06180   75 TFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAV 120
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 35-160 1.44e-09

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


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 55.11  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELG-SNVVIASRKLerlkSAADELQANLPPtkqaRVIPIQCNIRNEEEVNNLVKST 113
Cdd:cd05354     1 IKDKTVLVTGANRGIGKAFVESLLAHGaKKVYAAVRDP----GSAAHLVAKYGD----KVVPLRLDVTDPESIKAAAAQA 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 114 LDtfgkINFLVNNGGgqFLSPAEHISSKGWHAV---LETNLTGTFYMCKA 160
Cdd:cd05354    73 KD----VDVVINNAG--VLKPATLLEEGALEALkqeMDVNVFGLLRLAQA 116
PRK06139 PRK06139
SDR family oxidoreductase;
35-157 1.46e-09

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 55.88  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK06139    5 LHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRA-----LGAEVLVVPTDVTDADQVKALATQAA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGG----GQFlspaEHISSKGWHAVLETNLTGtfYM 157
Cdd:PRK06139   80 SFGGRIDVWVNNVGvgavGRF----EETPIEAHEQVIQTNLIG--YM 120
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-159 1.56e-09

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 55.56  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVV---IASRklERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVK 111
Cdd:PRK07792   10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVvndVASA--LDASDVLDEIRA-----AGAKAVAVAGDISQRATADELVA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 112 STlDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCK 159
Cdd:PRK07792   83 TA-VGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTR 129
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 37-161 1.59e-09

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 55.30  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptKQARVIPIQCNIRNE--EEVNNLVKsTL 114
Cdd:cd05356     1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYG--VETKTIAADFSAGDDiyERIEKELE-GL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462575256 115 DtfgkINFLVNNGGGQFLSPAE--HISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05356    78 D----IGILVNNVGISHSIPEYflETPEDELQDIINVNVMATLKMTRLI 122
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 37-128 1.89e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 55.42  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK06197   16 GRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATP---GADVTLQELDLTSLASVRAAADALRAA 92

                          90
                  ....*....|..
gi 2462575256 117 FGKINFLVNNGG 128
Cdd:PRK06197   93 YPRIDLLINNAG 104
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
38-152 2.48e-09

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 54.69  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASR-KLERLKSAADElqanlpptKQARVIPIQCNIRNEEEVNNLVKS---- 112
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRtENKELTKLAEQ--------YNSNLTFHSLDLQDVHELETNFNEilss 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 113 -TLDTFGKInFLVNNGGG-QFLSPAEHISSKGWHAVLETNLT 152
Cdd:PRK06924   74 iQEDNVSSI-HLINNAGMvAPIKPIEKAESEELITNVHLNLL 114
PRK08589 PRK08589
SDR family oxidoreductase;
33-161 2.61e-09

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 54.78  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlERLKSAADELQANLPPTKQARVipiqcNIRNEEEVNNLVKS 112
Cdd:PRK08589    2 KRLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIA-EAVSETVDKIKSNGGKAKAYHV-----DISDEQQVKDFASE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462575256 113 TLDTFGKINFLVNN-----GGGQFLS-PAEHisskgWHAVLETNLTGTFYMCKAV 161
Cdd:PRK08589   76 IKEQFGRVDVLFNNagvdnAAGRIHEyPVDV-----FDKIMAVDMRGTFLMTKML 125
PRK09730 PRK09730
SDR family oxidoreductase;
39-159 2.91e-09

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 54.47  E-value: 2.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVviASRKLERLKSAADELqaNLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:PRK09730    3 IALVTGGSRGIGRATALLLAQEGYTV--AVNYQQNLHAAQEVV--NLITQAGGKAFVLQADISDENQVVAMFTAIDQHDE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 119 KINFLVNNGGGQFL-SPAEHISSKGWHAVLETNLTGTFYMCK 159
Cdd:PRK09730   79 PLAALVNNAGILFTqCTVENLTAERINRVLSTNVTGYFLCCR 120
PRK05650 PRK05650
SDR family oxidoreductase;
42-160 3.01e-09

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 54.66  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  42 VTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpPTKQARVIPiqCNIRNEEEVNNLVKSTLDTFGKIN 121
Cdd:PRK05650    5 ITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLRE---AGGDGFYQR--CDVRDYSQLTALAQACEEKWGGID 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 122 FLVNNGG---GQFLspaEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK05650   80 VIVNNAGvasGGFF---EELSLEDWDWQIAINLMGVVKGCKA 118
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 39-161 3.17e-09

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: 54.31  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQARVipiqCNIRNEEEVNNLVKSTLDTFG 118
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVP----TDARDEDEVIALFDLIEEEIG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462575256 119 KINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05373    77 PLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREA 119
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 35-161 4.53e-09

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: 54.01  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanlpPTkqarVIPIQCNIRNEEEvnnlVKSTL 114
Cdd:cd05351     5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVREC-----PG----IEPVCVDLSDWDA----TEEAL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05351    72 GSVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIV 118
PRK06500 PRK06500
SDR family oxidoreductase;
35-160 4.54e-09

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 53.81  E-value: 4.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkqarVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK06500    4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGES--------ALVIRADAGDVAAQKALAQALA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK06500   76 EAFGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQA 121
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 33-155 1.37e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 52.75  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlpptkQARVIPIQC----------NIRN 102
Cdd:PRK07791    2 GLLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIGVGLDGSASGGSAA------QAVVDEIVAaggeavangdDIAD 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575256 103 EEEVNNLVKSTLDTFGKINFLVNNGG----GQFLSPAEhissKGWHAVLETNLTGTF 155
Cdd:PRK07791   76 WDGAANLVDAAVETFGGLDVLVNNAGilrdRMIANMSE----EEWDAVIAVHLKGHF 128
PRK07775 PRK07775
SDR family oxidoreductase;
40-161 1.45e-08

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 52.83  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlppTKQARVIPIqcNIRNEEEVNNLVKSTLDTFGK 119
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRAD---GGEAVAFPL--DVTDPDSVKSFVAQAEEALGE 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462575256 120 INFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK07775   88 IEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAV 129
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 33-124 1.69e-08

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: 52.33  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  33 GLLQGQVAIVTGGAT--GIGKAIVKELLELGSNVVIASRKlERLKSAADELQANLPPtkqARVIPiqCNIRNEEEVNNLV 110
Cdd:COG0623     1 GLLKGKRGLITGVANdrSIAWGIAKALHEEGAELAFTYQG-EALKKRVEPLAEELGS---ALVLP--CDVTDDEQIDALF 74

                          90
                  ....*....|....
gi 2462575256 111 KSTLDTFGKINFLV 124
Cdd:COG0623    75 DEIKEKWGKLDFLV 88
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
35-161 3.47e-08

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 51.44  E-value: 3.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKlerlksAADELQANLPPTKQaRVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK12481    6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVA------EAPETQAQVEALGR-KFHFITADLIQQKDIDSIVSQAV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12481   79 EVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAV 125
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 6-121 3.57e-08

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 51.98  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256   6 RRACAQLLWHP----AAGMASWAKGRSYLapgllqgqvaiVTGGATGIGKAIVKELLEL-GSNVVIASR-----KLERLK 75
Cdd:cd08953   181 LRYVQTLEPLPlpagAAASAPLKPGGVYL-----------VTGGAGGIGRALARALARRyGARLVLLGRsplppEEEWKA 249

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256  76 SAADELQANlpptkQARVIPIQCNIRNEEEVNNLVKSTLDTFGKIN 121
Cdd:cd08953   250 QTLAALEAL-----GARVLYISADVTDAAAVRRLLEKVRERYGAID 290
PRK08219 PRK08219
SDR family oxidoreductase;
39-153 3.65e-08

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 51.09  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLElGSNVVIASRKLERLKSAADELqanlpptkqARVIPIQCNIRNEEEvnnlVKSTLDTFG 118
Cdd:PRK08219    5 TALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELAAEL---------PGATPFPVDLTDPEA----IAAAVEQLG 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462575256 119 KINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTG 153
Cdd:PRK08219   71 RLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVA 105
PRK05717 PRK05717
SDR family oxidoreductase;
37-159 5.09e-08

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 51.04  E-value: 5.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkqarVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:PRK05717   10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGEN--------AWFIAMDVADEAQVAAGVAEVLGQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 117 FGKINFLVNNGG--GQFLSPAEHISSKGWHAVLETNLTGTFYMCK 159
Cdd:PRK05717   82 FGRLDALVCNAAiaDPHNTTLESLSLAHWNRVLAVNLTGPMLLAK 126
PRK06482 PRK06482
SDR family oxidoreductase;
42-161 6.00e-08

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 50.88  E-value: 6.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  42 VTGGATGIGKAIVKELLELGSNVVIASRKLERLksaaDELQANLPPtkqaRVIPIQCNIRNEEEVNNLVKSTLDTFGKIN 121
Cdd:PRK06482    7 ITGASSGFGRGMTERLLARGDRVAATVRRPDAL----DDLKARYGD----RLWVLQLDVTDSAAVRAVVDRAFAALGRID 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462575256 122 FLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06482   79 VVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAA 118
PRK07041 PRK07041
SDR family oxidoreductase;
41-109 7.52e-08

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 50.42  E-value: 7.52e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462575256  41 IVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkqARVIPIQCNIRNEEEVNNL 109
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGG------APVRTAALDITDEAAVDAF 63
PRK09134 PRK09134
SDR family oxidoreductase;
39-126 7.82e-08

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 50.70  E-value: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRkleRLKSAADELQANLpPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:PRK09134   11 AALVTGAARRIGRAIALDLAAHGFDVAVHYN---RSRDEAEALAAEI-RALGRRAVALQADLADEAEVRALVARASAALG 86


                  ....*...
gi 2462575256 119 KINFLVNN 126
Cdd:PRK09134   87 PITLLVNN 94
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 39-128 9.66e-08

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 50.46  E-value: 9.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSN-----VVIASRKLERLKSAADELQANLPPTKQaRVIPIQCNIRNEEEVNNLVKST 113
Cdd:cd08941     3 VVLVTGANSGLGLAICERLLAEDDEnpeltLILACRNLQRAEAACRALLASHPDARV-VFDYVLVDLSNMVSVFAAAKEL 81

                          90
                  ....*....|....*
gi 2462575256 114 LDTFGKINFLVNNGG 128
Cdd:cd08941    82 KKRYPRLDYLYLNAG 96
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 39-161 1.52e-07

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 49.77  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELL--ELGSNVVIAS----RKLERLKSAADELqanLPPTKQArvipIQCNIRNEEEVNNLVKS 112
Cdd:cd09806     2 VVLITGCSSGIGLHLAVRLAsdPSKRFKVYATmrdlKKKGRLWEAAGAL---AGGTLET----LQLDVCDSKSVAAAVER 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462575256 113 TLDtfGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd09806    75 VTE--RHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAF 121
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 36-161 1.83e-07

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: 49.39  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKsaadELQANlpPTKQARVIpiqcNIRNEEEVNNLVKStld 115
Cdd:cd05368     1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLK----ELERG--PGITTRVL----DVTDKEQVAALAKE--- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 116 tFGKINFLVNNGG----GQFLSPAEhissKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd05368    68 -EGRIDVLFNCAGfvhhGSILDCED----DDWDFAMNLNVRSMYLMIKAV 112
PRK08703 PRK08703
SDR family oxidoreductase;
32-160 2.17e-07

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 49.16  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  32 PGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQArvIPIQCNIRNEEEVNNLVK 111
Cdd:PRK08703    1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFA--IRFDLMSAEEKEFEQFAA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462575256 112 STLDTF-GKINFLVNNGGGQF-LSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK08703   79 TIAEATqGKLDGIVHCAGYFYaLSPLDFQTVAEWVNQYRINTVAPMGLTRA 129
PRK06947 PRK06947
SDR family oxidoreductase;
38-158 5.14e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 48.26  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKlerlKSAADELQANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAARGWSVGINYAR----DAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAF 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 118 GKINFLVNNGGgqFLSPAEHISSKGWH---AVLETNLTGTfYMC 158
Cdd:PRK06947   79 GRLDALVNNAG--IVAPSMPLADMDAArlrRMFDTNVLGA-YLC 119
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 39-128 1.43e-06

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 46.83  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLEL----GSNVVIASRKLERLKSAADELQANLPptkQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERS---GLRVVRVSLDLGAEAGLEQLLKALR 78

                          90
                  ....*....|....*...
gi 2462575256 115 DTFGKINF----LVNNGG 128
Cdd:TIGR01500  79 ELPRPKGLqrllLINNAG 96
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 38-159 1.56e-06

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (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. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in 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: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 47.13  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGS-NVVIASRKLERLKSAADELqaNLPPTkqaRVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd09810     2 GTVVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEV--GMPKD---SYSVLHCDLASLDSVRQFVDNFRRT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 117 FGKINFLVNNGGGQFLSPAE-HISSKGWHAVLETNLTGTFYMCK 159
Cdd:cd09810    77 GRPLDALVCNAAVYLPTAKEpRFTADGFELTVGVNHLGHFLLTN 120
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
41-160 2.40e-06

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 46.51  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  41 IVTGGATGIGKAIVKELLELGSNVVIASrkleRLKSAADELQAnlpptkQARVIPIQCNIRNEEEVNNLvkstldtFGKI 120
Cdd:COG0451     3 LVTGGAGFIGSHLARRLLARGHEVVGLD----RSPPGAANLAA------LPGVEFVRGDLRDPEALAAA-------LAGV 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462575256 121 NFLVNNGGgqFLSPAEHisskGWHAVLETNLTGTFYMCKA 160
Cdd:COG0451    66 DAVVHLAA--PAGVGEE----DPDETLEVNVEGTLNLLEA 99
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 17-83 5.77e-06

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 44.69  E-value: 5.77e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575256  17 AAGMASWAKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQA 83
Cdd:cd01078     8 AAAAVAAAGKALELMGKDLKGKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRA 74
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 37-124 6.61e-06

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: 44.88  E-value: 6.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGAT--GIGKAIVKELLELGSNVVIA--SRKLE-RLKSAADELQANlpptkqARVIPiqCNIRNEEEVNNLVK 111
Cdd:cd05372     1 GKRILITGIANdrSIAWGIAKALHEAGAELAFTyqPEALRkRVEKLAERLGES------ALVLP--CDVSNDEEIKELFA 72

                          90
                  ....*....|...
gi 2462575256 112 STLDTFGKINFLV 124
Cdd:cd05372    73 EVKKDWGKLDGLV 85
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 35-129 8.65e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 44.65  E-value: 8.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAnlppTKQARVIPIQCNIRNEEEVNNLVKSTl 114
Cdd:PRK06125    5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRA----AHGVDVAVHALDLSSPEAREQLAAEA- 79

                          90
                  ....*....|....*
gi 2462575256 115 dtfGKINFLVNNGGG 129
Cdd:PRK06125   80 ---GDIDILVNNAGA 91
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
38-161 1.54e-05

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 43.85  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLpptkQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:PRK12938    4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKAL----GFDFIASEGNVGDWDSTKAAFDKVKAEV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 118 GKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK12938   80 GEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQV 123
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 41-154 1.59e-05

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 43.32  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  41 IVTGGATGIGKAIVKELLELG-SNVVIASR---KLERLKSAADELQAnlpptKQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGaRHLVLLSRsaaPRPDAQALIAELEA-----RGVEVVVVACDVSDPDAVAALLAEIKAE 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462575256 117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGT 154
Cdd:pfam08659  79 GPPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGT 116
PRK12746 PRK12746
SDR family oxidoreductase;
35-165 1.63e-05

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 43.87  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIasrKLERLKSAADELQANLpPTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK12746    4 LDGKVALVTGASRGIGRAIAMRLANDGALVAI---HYGRNKQAADETIREI-ESNGGKAFLIEADLNSIDGVKKLVEQLK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575256 115 DTF------GKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVDQLI 165
Cdd:PRK12746   80 NELqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL 136
PRK07985 PRK07985
SDR family oxidoreductase;
27-160 1.74e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 43.83  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  27 RSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLErlKSAADELQANLPPT-KQARVIPiqCNIRNEEE 105
Cdd:PRK07985   39 KTYVGSGRLKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVE--EEDAQDVKKIIEECgRKAVLLP--GDLSDEKF 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575256 106 VNNLVKSTLDTFGKINFLVNNGGGQFLSP-AEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK07985  115 ARSLVHEAHKALGGLDIMALVAGKQVAIPdIADLTSEQFQKTFAINVFALFWLTQE 170
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 32-133 3.30e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 43.06  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  32 PGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAAD-----ELQANLPPTKQARVIPIQCNIRNEEEV 106
Cdd:PRK08303    3 MKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTRARRSEYDrpetiEETAELVTAAGGRGIAVQVDHLVPEQV 82

                          90       100
                  ....*....|....*....|....*...
gi 2462575256 107 NNLVKSTLDTFGKINFLVNN-GGGQFLS 133
Cdd:PRK08303   83 RALVERIDREQGRLDILVNDiWGGEKLF 110
PRK05854 PRK05854
SDR family oxidoreductase;
35-155 4.52e-05

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 42.75  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkQARVIPIQCNIRNEEEVNNLVKsTL 114
Cdd:PRK05854   12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVP---DAKLSLRALDLSSLASVAALGE-QL 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462575256 115 DTFGK-INFLVNNGGgqFLSPAE-HISSKGWHAVLETNLTGTF 155
Cdd:PRK05854   88 RAEGRpIHLLINNAG--VMTPPErQTTADGFELQFGTNHLGHF 128
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 39-134 4.88e-05

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: 42.61  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRKLErlkSAADELQANLPPTKQARVIPIQCNIRNEEEV----NNLVKSTL 114
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSA---AAASTLAAELNARRPNSAVTCQADLSNSATLfsrcEAIIDACF 79

                          90       100
                  ....*....|....*....|
gi 2462575256 115 DTFGKINFLVNNGGGQFLSP 134
Cdd:TIGR02685  80 RAFGRCDVLVNNASAFYPTP 99
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 35-161 4.89e-05

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 42.53  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkqARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK08339    6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESN----VDVSYIVADLTKREDLERTVKELK 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256 115 DTFGKINFLVNNGG---GQFLspaeHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK08339   82 NIGEPDIFFFSTGGpkpGYFM----EMSMEDWEGAVKLLLYPAVYLTRAL 127
PRK08267 PRK08267
SDR family oxidoreductase;
42-160 5.92e-05

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 42.23  E-value: 5.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  42 VTGGATGIGKAIVKELLELGSNVVIASRKlerlKSAADELQANLPPTkqaRVIPIQCNIRNEEEVNNLVKS-TLDTFGKI 120
Cdd:PRK08267    6 ITGAASGIGRATALLFAAEGWRVGAYDIN----EAGLAALAAELGAG---NAWTGALDVTDRAAWDAALADfAAATGGRL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462575256 121 NFLVNNGG----GQFlspaEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:PRK08267   79 DVLFNNAGilrgGPF----EDIPLEAHDRVIDINVKGVLNGAHA 118
PRK06720 PRK06720
hypothetical protein; Provisional
 35-128 6.59e-05

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 41.50  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqANLppTKQARVIPIqcNIRNEEEVNNLVKSTL 114
Cdd:PRK06720   14 LAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEI-TNL--GGEALFVSY--DMEKQGDWQRVISITL 88

                          90
                  ....*....|....
gi 2462575256 115 DTFGKINFLVNNGG 128
Cdd:PRK06720   89 NAFSRIDMLFQNAG 102
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 41-164 6.64e-05

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 41.31  E-value: 6.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256   41 IVTGGATGIGKAIVKELLELG-SNVVIASR---KLERLKSAADELQANLpptkqARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGaRRLVLLSRsgpDAPGAAALLAELEAAG-----ARVTVVACDVADRDALAAVLAAIPAV 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462575256  117 FGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVDQL 164
Cdd:smart00822  79 EGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADL 126
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 37-161 8.63e-05

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup 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. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in 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: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 41.81  E-value: 8.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlppTKQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd09808     1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETE---SGNQNIFLHIVDMSDPKQVWEFVEEFKEE 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256 117 FGKINFLVNNGGgqFLSPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:cd09808    78 GKKLHVLINNAG--CMVNKRELTEDGLEKNFATNTLGTYILTTHL 120
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
 41-111 1.06e-04

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 41.44  E-value: 1.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462575256  41 IVTGGATGIGKAIVKELLELGSNVVIasrkLERLKSAADElqaNLPPTKqARVIPIQCNIRNEEEVNNLVK 111
Cdd:cd05256     3 LVTGGAGFIGSHLVERLLERGHEVIV----LDNLSTGKKE---NLPEVK-PNVKFIEGDIRDDELVEFAFE 65
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-161 1.07e-04

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 41.49  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVViasrklerlksAADeLQANLPPTKQARVipIQCNIRNEeevnnlVKSTLDT 116
Cdd:PRK06550    5 TKTVLITGAASGIGLAQARAFLAQGAQVY-----------GVD-KQDKPDLSGNFHF--LQLDLSDD------LEPLFDW 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462575256 117 FGKINFLVNNGGgqFL---SPAEHISSKGWHAVLETNLTGTFYMCKAV 161
Cdd:PRK06550   65 VPSVDILCNTAG--ILddyKPLLDTSLEEWQHIFDTNLTSTFLLTRAY 110
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 42-80 1.08e-04

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 40.98  E-value: 1.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462575256  42 VTGgATG-IGKAIVKELLELGSNVVIASRKLERLKSAADE 80
Cdd:COG0702     4 VTG-ATGfIGRRVVRALLARGHPVRALVRDPEKAAALAAA 42
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 34-157 1.30e-04

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 41.21  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  34 LLQGQVAIVTGGATGIGKAIVKELLELGSNVVI--ASRKlERLKSAADELQANlpptkQARVIPIQCNIRNEEEVNNLVk 111
Cdd:PRK12747    1 MLKGKVALVTGASRGIGRAIAKRLANDGALVAIhyGNRK-EEAEETVYEIQSN-----GGSAFSIGANLESLHGVEALY- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575256 112 STLDT-------FGKINFLVNNGG---GQFLspaEHISSKGWHAVLETNLTGTFYM 157
Cdd:PRK12747   74 SSLDNelqnrtgSTKFDILINNAGigpGAFI---EETTEQFFDRMVSVNAKAPFFI 126
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
 42-80 2.08e-04

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 40.72  E-value: 2.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462575256  42 VTGgATG-IGKAIVKELLELGSNVVIASRKLERLKSAADE 80
Cdd:cd05269     3 VTG-ATGkLGTAVVELLLAKVASVVALVRNPEKAKAFAAD 41
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
39-84 2.15e-04

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 40.15  E-value: 2.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256  39 VAIVtgGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQAN 84
Cdd:COG2085     1 IGII--GTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPG 44
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
36-84 2.32e-04

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 40.59  E-value: 2.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462575256  36 QGQVAIVtgGATG-IGKAIVKELLELGSNVVIASRKLERLKSAADELQAN 84
Cdd:COG5322   151 KATVAVV--GATGsIGSVCARLLAREVKRLTLVARNLERLEELAEEILRN 198
PRK08251 PRK08251
SDR family oxidoreductase;
38-160 3.16e-04

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 39.92  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  38 QVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPptkQARVIPIQCNIRNEEEVNNLVKSTLDTF 117
Cdd:PRK08251    3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYP---GIKVAVAALDVNDHDQVFEVFAEFRDEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 118 GKINFLVNNGGgqfLSPAEHISSKGWHA---VLETNLTGTFYMCKA 160
Cdd:PRK08251   80 GGLDRVIVNAG---IGKGARLGTGKFWAnkaTAETNFVAALAQCEA 122
PRK08416 PRK08416
enoyl-ACP reductase;
35-126 4.01e-04

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 39.75  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERL-KSAADELQANLppTKQARVIPIqcNIRNEEEVNNLVKST 113
Cdd:PRK08416    6 MKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEaNKIAEDLEQKY--GIKAKAYPL--NILEPETYKELFKKI 81

                          90
                  ....*....|...
gi 2462575256 114 LDTFGKINFLVNN 126
Cdd:PRK08416   82 DEDFDRVDFFISN 94
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 39-111 4.17e-04

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 39.54  E-value: 4.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462575256  39 VAIVTGgATG-IGKAIVKELLELGSNVVIASRkleRLKSAADELQANLPPtkqaRVIPIQCNIRNEEEVNNLVK 111
Cdd:cd05271     2 VVTVFG-ATGfIGRYVVNRLAKRGSQVIVPYR---CEAYARRLLVMGDLG----QVLFVEFDLRDDESIRKALE 67
PRK07832 PRK07832
SDR family oxidoreductase;
40-153 4.45e-04

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 39.64  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQARVIpiqcNIRNEEEVNNLVKSTLDTFGK 119
Cdd:PRK07832    3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRAL----DISDYDAVAAFAADIHAAHGS 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462575256 120 INFLVNNGGGQFLSPAEHISSKGWHAVLETNLTG 153
Cdd:PRK07832   79 MDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMG 112
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 39-82 5.34e-04

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 38.79  E-value: 5.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256  39 VAIVtgGATGIGKAIVKELLELG-SNVVIASRKLERLKSAADELQ 82
Cdd:cd01065    22 VLIL--GAGGAARAVAYALAELGaAKIVIVNRTLEKAKALAERFG 64
NAD_binding_10 pfam13460
NAD(P)H-binding;
45-111 7.26e-04

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 38.35  E-value: 7.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462575256  45 GATG-IGKAIVKELLELGSNVVIASRKLERLKSAADelqanlpptkQARVIPIQCNIRNEEEVNNLVK 111
Cdd:pfam13460   1 GATGkIGRLLVKQLLARGHEVTALVRNPEKLADLED----------HPGVEVVDGDVLDPDDLAEALA 58
PRK05884 PRK05884
SDR family oxidoreductase;
41-151 7.96e-04

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 38.64  E-value: 7.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  41 IVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANlpptkqarviPIQCNIRNE---EEVNNLVKSTLDTF 117
Cdd:PRK05884    4 LVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVD----------AIVCDNTDPaslEEARGLFPHHLDTI 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462575256 118 GKINFLVNNGGG-QFLSPAEHISSkgWHAVLETNL 151
Cdd:PRK05884   74 VNVPAPSWDAGDpRTYSLADTANA--WRNALDATV 106
PRK12742 PRK12742
SDR family oxidoreductase;
35-128 1.08e-03

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 38.58  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVI--ASRklerlKSAADELQANLPPTKqarvipIQCNIRNEEEvnnlVKS 112
Cdd:PRK12742    4 FTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFtyAGS-----KDAAERLAQETGATA------VQTDSADRDA----VID 68

                          90
                  ....*....|....*.
gi 2462575256 113 TLDTFGKINFLVNNGG 128
Cdd:PRK12742   69 VVRKSGALDILVVNAG 84
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-126 1.13e-03

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 38.52  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGA--TGIGKAIVKELLELGSNVV----IASRKLERLKSAADE---LQANLPpTKQARVIPIQCNIRNEEE 105
Cdd:PRK12748    3 LMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFftywSPYDKTMPWGMHDKEpvlLKEEIE-SYGVRCEHMEIDLSQPYA 81

                          90       100
                  ....*....|....*....|.
gi 2462575256 106 VNNLVKSTLDTFGKINFLVNN 126
Cdd:PRK12748   82 PNRVFYAVSERLGDPSILINN 102
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
34-120 1.14e-03

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 38.56  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  34 LLQGQVAIVTGGAT--GIGKAIVKELLELGSNVVIASRKlERLKSAADELQANLpptKQARVIPIQCNIRNEEEVNNLVK 111
Cdd:PRK08594    4 SLEGKTYVVMGVANkrSIAWGIARSLHNAGAKLVFTYAG-ERLEKEVRELADTL---EGQESLLLPCDVTSDEEITACFE 79


                  ....*....
gi 2462575256 112 STLDTFGKI 120
Cdd:PRK08594   80 TIKEEVGVI 88
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-128 1.26e-03

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 38.66  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASrklerLKSAADELQANlppTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK08261  208 LAGKVALVTGAARGIGAAIAEVLARDGAHVVCLD-----VPAAGEALAAV---ANRVGGTALALDITAPDAPARIAEHLA 279

                          90
                  ....*....|....
gi 2462575256 115 DTFGKINFLVNNGG 128
Cdd:PRK08261  280 ERHGGLDIVVHNAG 293
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 40-160 1.50e-03

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 38.05  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADelqanlpptkqARVIPIQCNIRNEEEVNNLVKSTldtfgK 119
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARL-----------ADLRFVEGDLTDRDALEKLLADV-----R 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 120 INFLVNNGGgqflspaehISSKGWH-----AVLETNLTGTFYMCKA 160
Cdd:pfam01370  65 PDAVIHLAA---------VGGVGASiedpeDFIEANVLGTLNLLEA 101
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 37-94 1.52e-03

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 38.31  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQARVI 94
Cdd:PLN02780   53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTVV 110
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-160 1.91e-03

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 37.82  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  35 LQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanlppTKQARVIPIQCNIRNEEEVNNLVKSTL 114
Cdd:PRK05786    3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTL------SKYGNIHYVVGDVSSTESARNVIEKAA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462575256 115 DTFGKINFLVNNGGGQFLSPAEHISskGWHAVLETNLTGTFYMCKA 160
Cdd:PRK05786   77 KVLNAIDGLVVTVGGYVEDTVEEFS--GLEEMLTNHIKIPLYAVNA 120
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 45-106 2.37e-03

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 36.41  E-value: 2.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462575256  45 GATGIGKAIVKELLELGS--NVVIASRKLERLKSAADELqanlpptKQARVIPIQCNIRNEEEV 106
Cdd:pfam03435   5 GAGSVGQGVAPLLARHFDvdRITVADRTLEKAQALAAKL-------GGVRFIAVAVDADNYEAV 61
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 37-170 3.39e-03

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. 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. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in 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: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 37.19  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  37 GQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELqanLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDT 116
Cdd:cd09809     1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRI---LEEWHKARVEAMTLDLASLRSVQRFAEAFKAK 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462575256 117 FGKINFLVNNgGGQFLSPAEhISSKGWHAVLETNLTGTFYMckaVDQLIWLLCL 170
Cdd:cd09809    78 NSPLHVLVCN-AAVFALPWT-LTEDGLETTFQVNHLGHFYL---VQLLEDVLRR 126
PRK05693 PRK05693
SDR family oxidoreductase;
39-128 6.48e-03

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 36.31  E-value: 6.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  39 VAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAAdelqanlpptkQARVIPIQCNIRNEEEVNNLVKSTLDTFG 118
Cdd:PRK05693    3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALA-----------AAGFTAVQLDVNDGAALARLAEELEAEHG 71

                          90
                  ....*....|
gi 2462575256 119 KINFLVNNGG 128
Cdd:PRK05693   72 GLDVLINNAG 81
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 40-160 7.54e-03

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 35.64  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575256  40 AIVTGGATGIGKAIVKELLELGSNVVIASRKLERlksaadelqanlpptkqarvipIQCNIRNEEEVNNLVKSTldtfGK 119
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGD----------------------YQVDITDEASIKALFEKV----GH 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462575256 120 INFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKA 160
Cdd:cd11731    55 FDAIVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRH 95
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
 31-83 7.85e-03

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 35.93  E-value: 7.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462575256  31 APGLLQGQVAIVTGgATGIGKAIVKELLELG-SNVVIASRKLERLKSAADELQA 83
Cdd:PRK00258  117 LGVDLKGKRILILG-AGGAARAVILPLLDLGvAEITIVNRTVERAEELAKLFGA 169
PLN02240 PLN02240
UDP-glucose 4-epimerase
 42-113 8.33e-03

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 36.09  E-value: 8.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462575256  42 VTGGATGIGKAIVKELLELGSNVVIAS-------RKLERLKSAADELQANLPPTKqarvipiqCNIRNEEEVNNLVKST 113
Cdd:PLN02240   10 VTGGAGYIGSHTVLQLLLAGYKVVVIDnldnsseEALRRVKELAGDLGDNLVFHK--------VDLRDKEALEKVFAST 80
PLN02520 PLN02520
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
 35-79 8.72e-03

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase


Pssm-ID: 178135 [Multi-domain]  Cd Length: 529  Bit Score: 36.28  E-value: 8.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462575256  35 LQGQVAIVTGgATGIGKAIVKELLELGSNVVIASRKLERLKSAAD 79
Cdd:PLN02520  377 LAGKLFVVIG-AGGAGKALAYGAKEKGARVVIANRTYERAKELAD 420
 
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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