NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|751368102|ref|NP_001291441|]
View 

3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7 isoform 2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 2-153 8.26e-80

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 cd08941:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 290  Bit Score: 237.67  E-value: 8.26e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDD---ELHLCLACRNMSKAEAVCAALLASHPTAEVT--IVQVDVSNLQSVFRASKE 76
Cdd:cd08941    1 RKVVLVTGANSGLGLAICERLLAEDDenpELTLILACRNLQRAEAACRALLASHPDARVVfdYVLVDLSNMVSVFAAAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102  77 LKQRFQRLDCIYLNAGIMPNPQLN-----IKALFFGLFSRKVIHMFSTAEGLLTQGDKITADGLQEVFETNVFGHFILVK 151
Cdd:cd08941   81 LKKRYPRLDYLYLNAGIMPNPGIDwigaiKEVLTNPLFAVTNPTYKIQAEGLLSQGDKATEDGLGEVFQTNVFGHYYLIR 160


                 ..
gi 751368102 152 KL 153
Cdd:cd08941  161 EL 162
 
Name Accession Description Interval E-value
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 2-153 8.26e-80

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: 237.67  E-value: 8.26e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDD---ELHLCLACRNMSKAEAVCAALLASHPTAEVT--IVQVDVSNLQSVFRASKE 76
Cdd:cd08941    1 RKVVLVTGANSGLGLAICERLLAEDDenpELTLILACRNLQRAEAACRALLASHPDARVVfdYVLVDLSNMVSVFAAAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102  77 LKQRFQRLDCIYLNAGIMPNPQLN-----IKALFFGLFSRKVIHMFSTAEGLLTQGDKITADGLQEVFETNVFGHFILVK 151
Cdd:cd08941   81 LKKRYPRLDYLYLNAGIMPNPGIDwigaiKEVLTNPLFAVTNPTYKIQAEGLLSQGDKATEDGLGEVFQTNVFGHYYLIR 160


                 ..
gi 751368102 152 KL 153
Cdd:cd08941  161 EL 162
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-153 7.18e-26

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 98.40  E-value: 7.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLASHptAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGA--RVVLVARDAERLEALAAELRAAG--ARVEVVALDVTDPDAVAALAEAVLAR 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751368102  81 FQRLDCIYLNAGIMPnpqlnikalfFGLFsrkvihmfstaeglltqgDKITADGLQEVFETNVFGHFILVKKL 153
Cdd:COG0300   80 FGPIDVLVNNAGVGG----------GGPF------------------EELDLEDLRRVFEVNVFGPVRLTRAL 124
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 3-149 1.02e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 91.24  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLAlCKRLLAEDDElHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06197  17 RVAVVTGANTGLGYE-TAAALAAKGA-HVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASVRAAADALRAAYP 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751368102  83 RLDCIYLNAGIMPNPQlnikalffglfsrkvihmfstaeglltqgdKITADGLQEVFETNVFGHFIL 149
Cdd:PRK06197  95 RIDLLINNAGVMYTPK------------------------------QTTADGFELQFGTNHLGHFAL 131
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-151 6.82e-21

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 84.20  E-value: 6.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102    3 KVVLITGASSGIGLALCKRLLAEDDELHLCLacRNMSKAEAVCAALLASHPtaEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVD--RSEEKLEAVAKELGALGG--KALFIQGDVTDRAQVKALVEQAVERLG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751368102   83 RLDCIYLNAGIMPNpqlnikalffglfsrkviHMFStaeglltqgdKITADGLQEVFETNVFGHFILVK 151
Cdd:pfam00106  77 RLDILVNNAGITGL------------------GPFS----------ELSDEDWERVIDVNLTGVFNLTR 117
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 3-93 1.07e-07

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: 48.63  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102     3 KVVLITGASSGIGLALCkRLLAEDDELHLCLACRN--MSKAEAVCAALLASHpTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:smart00822   1 GTYLITGGLGGLGRALA-RWLAERGARRLVLLSRSgpDAPGAAALLAELEAA-GARVTVVACDVADRDALAAVLAAIPAV 78

                           90
                   ....*....|...
gi 751368102    81 FQRLDCIYLNAGI 93
Cdd:smart00822  79 EGPLTGVIHAAGV 91
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 2-94 1.29e-03

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


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 37.69  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102    2 RKVVLITGASSGIGLALCKRLLAE------------DDELHLCLACRnmskaeAVCAALLASHPtAEVTIVQVDVSNLQS 69
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADgwrvvavdlcadDPAVGYPLATR------AELDAVAAACP-DQVLPVIADVRDPAA 73

                          90       100
                  ....*....|....*....|....*
gi 751368102   70 VFRASKELKQRFQRLDCIYLNAGIM 94
Cdd:TIGR04504  74 LAAAVALAVERWGRLDAAVAAAGVI 98
 
Name Accession Description Interval E-value
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 2-153 8.26e-80

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: 237.67  E-value: 8.26e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDD---ELHLCLACRNMSKAEAVCAALLASHPTAEVT--IVQVDVSNLQSVFRASKE 76
Cdd:cd08941    1 RKVVLVTGANSGLGLAICERLLAEDDenpELTLILACRNLQRAEAACRALLASHPDARVVfdYVLVDLSNMVSVFAAAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102  77 LKQRFQRLDCIYLNAGIMPNPQLN-----IKALFFGLFSRKVIHMFSTAEGLLTQGDKITADGLQEVFETNVFGHFILVK 151
Cdd:cd08941   81 LKKRYPRLDYLYLNAGIMPNPGIDwigaiKEVLTNPLFAVTNPTYKIQAEGLLSQGDKATEDGLGEVFQTNVFGHYYLIR 160


                 ..
gi 751368102 152 KL 153
Cdd:cd08941  161 EL 162
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 3-153 4.24e-28

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: 104.61  E-value: 4.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLclACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05327    2 KVVVITGANSGIGKETARELAKRGAHVII--ACRNEEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751368102  83 RLDCIYLNAGIMPNPQlnikalffglfsrkvihmfstaeglltqgdKITADGLQEVFETNVFGHFILVKKL 153
Cdd:cd05327   80 RLDILINNAGIMAPPR------------------------------RLTKDGFELQFAVNYLGHFLLTNLL 120
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-153 7.18e-26

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 98.40  E-value: 7.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLASHptAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGA--RVVLVARDAERLEALAAELRAAG--ARVEVVALDVTDPDAVAALAEAVLAR 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751368102  81 FQRLDCIYLNAGIMPnpqlnikalfFGLFsrkvihmfstaeglltqgDKITADGLQEVFETNVFGHFILVKKL 153
Cdd:COG0300   80 FGPIDVLVNNAGVGG----------GGPF------------------EELDLEDLRRVFEVNVFGPVRLTRAL 124
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 2-151 6.41e-24

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: 92.94  E-value: 6.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALlashpTAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:COG4221    5 GKVALITGASSGIGAATARALAAAGA--RVVLAARRAERLEALAAEL-----GGRALAVPLDVTDEAAVEAAVAAAVAEF 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102  82 QRLDCIYLNAGIMPnpqlnikalfFGLFsrkvihmfstaeglltqgDKITADGLQEVFETNVFGHFILVK 151
Cdd:COG4221   78 GRLDVLVNNAGVAL----------LGPL------------------EELDPEDWDRMIDVNVKGVLYVTR 119
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 3-154 8.45e-24

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: 92.93  E-value: 8.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLASHptAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:COG1028    7 KVALVTGGSSGIGRAIARALAAEGA--RVVITDRDAEALEAAAAELRAAG--GRALAVAADVTDEAAVEALVAAAVAAFG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751368102  83 RLDCIYLNAGIMPNPQLnikalffglfsrkvihmfstaeglltqgDKITADGLQEVFETNVFGHFILVKKLW 154
Cdd:COG1028   83 RLDILVNNAGITPPGPL----------------------------EELTEEDWDRVLDVNLKGPFLLTRAAL 126
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-154 3.65e-23

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: 90.81  E-value: 3.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLAShptAEVTIVQVDVSNLQSVFRASKELKQRFQRL 84
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGA--KVVLADRNEEALAELAAIEALG---GNAVAVQADVSDEEDVEALVEEALEEFGRL 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102  85 DCIYLNAGIMPNPQLnikalffglfsrkvihmfstaeglltqgDKITADGLQEVFETNVFGHFILVKKLW 154
Cdd:cd05233   76 DILVNNAGIARPGPL----------------------------EELTDEDWDRVLDVNLTGVFLLTRAAL 117
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 3-149 1.02e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 91.24  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLAlCKRLLAEDDElHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06197  17 RVAVVTGANTGLGYE-TAAALAAKGA-HVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASVRAAADALRAAYP 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751368102  83 RLDCIYLNAGIMPNPQlnikalffglfsrkvihmfstaeglltqgdKITADGLQEVFETNVFGHFIL 149
Cdd:PRK06197  95 RIDLLINNAGVMYTPK------------------------------QTTADGFELQFGTNHLGHFAL 131
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 3-146 8.54e-22

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: 87.67  E-value: 8.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLAShptaeVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIAT--ARNPDKLESLGELLNDN-----LEVLELDVTDEESIKAAVKEVIERFG 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751368102  83 RLDCIYLNAGIMpnpqlnikalffglfsrkvihMFSTAEGlltqgdkITADGLQEVFETNVFGH 146
Cdd:cd05374   74 RIDVLVNNAGYG---------------------LFGPLEE-------TSIEEVRELFEVNVFGP 109
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 2-153 4.71e-21

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: 86.80  E-value: 4.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLAlCKRLLAEDDELHLCLACRNMSKAEAvcAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:cd09810    1 KGTVVITGASSGLGLA-AAKALARRGEWHVVMACRDFLKAEQ--AAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751368102  82 QRLDCIYLNAGI-MPnpqlnikalffglfSRKVIHMfstaeglltqgdkiTADGLQEVFETNVFGHFILVKKL 153
Cdd:cd09810   78 RPLDALVCNAAVyLP--------------TAKEPRF--------------TADGFELTVGVNHLGHFLLTNLL 122
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-151 6.82e-21

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 84.20  E-value: 6.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102    3 KVVLITGASSGIGLALCKRLLAEDDELHLCLacRNMSKAEAVCAALLASHPtaEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVD--RSEEKLEAVAKELGALGG--KALFIQGDVTDRAQVKALVEQAVERLG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751368102   83 RLDCIYLNAGIMPNpqlnikalffglfsrkviHMFStaeglltqgdKITADGLQEVFETNVFGHFILVK 151
Cdd:pfam00106  77 RLDILVNNAGITGL------------------GPFS----------ELSDEDWERVIDVNLTGVFNLTR 117
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 5-154 8.44e-20

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: 81.96  E-value: 8.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCKRLLAeDDELHLCLACRNMSKAEAVcAALLASHPtaEVTIVQVDVSNLQSvfRASKELKQRFQ-- 82
Cdd:cd05325    1 VLITGASRGIGLELVRQLLA-RGNNTVIATCRDPSAATEL-AALGASHS--RLHILELDVTDEIA--ESAEAVAERLGda 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751368102  83 RLDCIYLNAGIMPNPQLnikalffglfsrkvihmfstaeglltqGDKITADGLQEVFETNVFGHFILVKKLW 154
Cdd:cd05325   75 GLDVLINNAGILHSYGP---------------------------ASEVDSEDLLEVFQVNVLGPLLLTQAFL 119
PRK05854 PRK05854
SDR family oxidoreductase;
3-153 1.40e-19

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 82.81  E-value: 1.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK05854  15 KRAVVTGASDGLGLGLARRLAAAGAE--VILPVRNRAKGEAAVAAIRTAVPDAKLSLRALDLSSLASVAALGEQLRAEGR 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751368102  83 RLDCIYLNAGIMPNPQlnikalffglfsRKVihmfstaeglltqgdkiTADGLQEVFETNVFGHFILVKKL 153
Cdd:PRK05854  93 PIHLLINNAGVMTPPE------------RQT-----------------TADGFELQFGTNHLGHFALTAHL 134
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 3-153 2.56e-19

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: 80.74  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDeLHLCLACRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGP-GTVILTARDVERGQAAVEKLRAEGLSVRF--HQLDVTDDASIEAAADFVEEKYG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751368102  83 RLDCIYLNAGIMpnpqlnikalffglfsrkvihmfstaeGLLTQGDKITADGLQEVFETNVFGHFILVKKL 153
Cdd:cd05324   78 GLDILVNNAGIA---------------------------FKGFDDSTPTREQARETMKTNFFGTVDVTQAL 121
PRK08251 PRK08251
SDR family oxidoreductase;
1-93 1.36e-18

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 79.21  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK08251   1 TRQKILITGASSGLGAGMAREFAAKGRDLALC--ARRTDRLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDE 78

                         90
                 ....*....|...
gi 751368102  81 FQRLDCIYLNAGI 93
Cdd:PRK08251  79 LGGLDRVIVNAGI 91
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-93 1.74e-18

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 78.66  E-value: 1.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAedDELHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAA--DGAKVVIYDSNEEAAEALAAELRAA--GGEARVLVFDVSDEAAVRALIEAAVEA 79

                         90
                 ....*....|...
gi 751368102  81 FQRLDCIYLNAGI 93
Cdd:PRK05653  80 FGALDILVNNAGI 92
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
1-154 3.99e-18

Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 78.88  E-value: 3.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALlaSHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:COG5748    5 QKSTVIITGASSGVGLYAAKALADRG--WHVIMACRDLEKAEAAAQEL--GIPPDSYTIIHIDLASLESVRRFVADFRAL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751368102  81 FQRLDCIYLNAGI-MPnpqlnikalffglfsrkvihmfstaegLLTQgDKITADGLQEVFETNVFGHFILVKKLW 154
Cdd:COG5748   81 GRPLDALVCNAAVyYP---------------------------LLKE-PLRSPDGYELSVATNHLGHFLLCNLLL 127
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 3-99 3.74e-17

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: 75.20  E-value: 3.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELhlcLAC-RNMSKAEAVCAAllasHPtaEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:COG3967    6 NTILITGGTSGIGLALAKRLHARGNTV---IITgRREEKLEEAAAA----NP--GLHTIVLDVADPASIAALAEQVTAEF 76

                         90
                 ....*....|....*...
gi 751368102  82 QRLDCIYLNAGIMPNPQL 99
Cdd:COG3967   77 PDLNVLINNAGIMRAEDL 94
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 3-94 3.90e-16

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: 72.34  E-value: 3.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClacrnmSKAEAVCAALLASHPTAEvtIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05370    6 NTVLITGGTSGIGLALARKFLEAGNTVIIT------GRREERLAEAKKELPNIH--TIVLDVGDAESVEALAEALLSEYP 77

                         90
                 ....*....|..
gi 751368102  83 RLDCIYLNAGIM 94
Cdd:cd05370   78 NLDILINNAGIQ 89
PRK12826 PRK12826
SDR family oxidoreductase;
1-95 4.25e-15

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 69.95  E-value: 4.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVV--DICGDDAAATAELVEAAGGKARA--RQVDVRDRAALKAAVAAGVED 80

                         90
                 ....*....|....*
gi 751368102  81 FQRLDCIYLNAGIMP 95
Cdd:PRK12826  81 FGRLDILVANAGIFP 95
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 3-93 5.80e-15

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: 69.20  E-value: 5.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLASH--PTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:cd08939    2 KHVLITGGSSGIGKALAKELVKEGA--NVIIVARSESKLEEAVEEIEAEAnaSGQKVSYISADLSDYEEVEQAFAQAVEK 79

                         90
                 ....*....|...
gi 751368102  81 FQRLDCIYLNAGI 93
Cdd:cd08939   80 GGPPDLVVNCAGI 92
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 3-153 6.02e-15

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: 69.93  E-value: 6.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd09809    2 KVIIITGANSGIGFETARSFALHG--AHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNS 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751368102  83 RLDCIYLNAGIMPNPQlnikalffglfsrkvihmfstaeglltqgdKITADGLQEVFETNVFGHFILVKKL 153
Cdd:cd09809   80 PLHVLVCNAAVFALPW------------------------------TLTEDGLETTFQVNHLGHFYLVQLL 120
PLN00015 PLN00015
protochlorophyllide reductase
 6-153 1.60e-14

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 68.96  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   6 LITGASSGIGLAlCKRLLAEDDELHLCLACRNMSKAEAvcAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQRLD 85
Cdd:PLN00015   1 IITGASSGLGLA-TAKALAETGKWHVVMACRDFLKAER--AAKSAGMPKDSYTVMHLDLASLDSVRQFVDNFRRSGRPLD 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751368102  86 CIYLNAGI-MPNpqlnikalffglfsrkvihmfstaegllTQGDKITADGLQEVFETNVFGHFILVKKL 153
Cdd:PLN00015  78 VLVCNAAVyLPT----------------------------AKEPTFTADGFELSVGTNHLGHFLLSRLL 118
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
2-149 1.72e-14

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 69.49  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEddELHLCLACRNMSKAEAVCAALLASHPtaeVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK08324 422 GKVALVTGAAGGIGKATAKRLAAE--GACVVLADLDEEAAEAAAAELGGPDR---ALGVACDVTDEAAVQAAFEEAALAF 496

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 751368102  82 QRLDCIYLNAGIMPNPQLnikalffglfsrkvihmfstaeglltqgDKITADGLQEVFETNVFGHFIL 149
Cdd:PRK08324 497 GGVDIVVSNAGIAISGPI----------------------------EETSDEDWRRSFDVNATGHFLV 536
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-153 5.23e-14

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 66.82  E-value: 5.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDelHLCLACR-NMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQ 79
Cdd:PRK12825   5 MGRVALVTGAARGLGRAIALRLARAGA--DVVVHYRsDEEAAEELVEAVEALGRRAQA--VQADVTDKAALEAAVAAAVE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751368102  80 RFQRLDCIYLNAGImpnpqlnikalffglFSRKVIHMFStaeglltqgdkitADGLQEVFETNVFGHFILVKKL 153
Cdd:PRK12825  81 RFGRIDILVNNAGI---------------FEDKPLADMS-------------DDEWDEVIDVNLSGVFHLLRAV 126
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
1-95 6.29e-14

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 66.67  E-value: 6.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAedDELHLCLACRNMSKAEAVCAALlaSHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVE--DGFKVAIVDYNEETAQAAADKL--SKDGGKAIAVKADVSDRDQVFAAVRQVVDT 76

                         90
                 ....*....|....*
gi 751368102  81 FQRLDCIYLNAGIMP 95
Cdd:PRK08643  77 FGDLNVVVNNAGVAP 91
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 3-93 8.18e-14

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: 66.03  E-value: 8.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAvcAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGA--KVAVTDRSEEAAAE--TVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG 76

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:cd05333   77 PVDILVNNAGI 87
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 3-151 8.51e-14

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 66.52  E-value: 8.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdelhLCLACrnMSKAEAVCAALLASHPTAeVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06200   7 QVALITGGGSGIGRALVERFLAEG----ARVAV--LERSAEKLASLRQRFGDH-VLVVEGDVTSYADNQRAVDQTVDAFG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751368102  83 RLDCIYLNAGIMPnpqlnikalffglFSRKVIHMfstaeglltQGDKITAdGLQEVFETNVFGHFILVK 151
Cdd:PRK06200  80 KLDCFVGNAGIWD-------------YNTSLVDI---------PAETLDT-AFDEIFNVNVKGYLLGAK 125
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 3-92 1.34e-13

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


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 65.76  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLASHPTaEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGA--KLILTGRRAERLQELADELGAKFPV-KVLPLQLDVSDRESIEAALENLPEEFR 77

                         90
                 ....*....|
gi 751368102  83 RLDCIYLNAG 92
Cdd:cd05346   78 DIDILVNNAG 87
PRK06914 PRK06914
SDR family oxidoreductase;
1-153 1.54e-13

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 65.82  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDdelHLCLAC-RNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKq 79
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKG---YLVIATmRNPEKQENLLSQATQLNLQQNIKVQQLDVTDQNSIHNFQLVLK- 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751368102  80 RFQRLDCIYLNAGimpnpqlnikalffglfsrkvihmfsTAEGLLTqgDKITADGLQEVFETNVFGHfILVKKL 153
Cdd:PRK06914  78 EIGRIDLLVNNAG--------------------------YANGGFV--EEIPVEEYRKQFETNVFGA-ISVTQA 122
PRK07326 PRK07326
SDR family oxidoreductase;
3-151 3.22e-13

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 64.65  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLASHptaEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07326   7 KVALITGGSKGIGFAIAEALLAEGYKVAIT--ARDQKELEEAAAELNNKG---NVLGLAADVRDEADVQRAVDAIVAAFG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751368102  83 RLDCIYLNAGImpnpqlnikalffGLFsRKVihmfstaeglltqgDKITADGLQEVFETNVFGHFILVK 151
Cdd:PRK07326  82 GLDVLIANAGV-------------GHF-APV--------------EELTPEEWRLVIDTNLTGAFYTIK 122
PRK06196 PRK06196
oxidoreductase; Provisional
 3-154 3.50e-13

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 65.09  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALlashptAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06196  27 KTAIVTGGYSGLGLETTRALAQAG--AHVIVPARRPDVAREALAGI------DGVEVVMLDLADLESVRAFAERFLDSGR 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751368102  83 RLDCIYLNAGIMPNPQlnikalffglfSRkvihmfstaeglltqgdkiTADGLQEVFETNVFGHFILVKKLW 154
Cdd:PRK06196  99 RIDILINNAGVMACPE-----------TR-------------------VGDGWEAQFATNHLGHFALVNLLW 140
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 3-97 6.99e-13

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: 63.86  E-value: 6.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClacrNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAIL----DRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFG 76

                         90
                 ....*....|....*
gi 751368102  83 RLDCIYLNAGIMPNP 97
Cdd:cd05323   77 RVDILINNAGILDEK 91
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 3-93 7.64e-13

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 63.92  E-value: 7.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLCLACrnmskaEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK12829  12 LRVLVTGGASGIGRAIAEAFAEAGARVHVCDVS------EAALAATAARLPGAKVTATVADVADPAQVERVFDTAVERFG 85

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK12829  86 GLDVLVNNAGI 96
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-153 2.02e-12

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 62.55  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELHLCLAcRNMSKAEAVCAALLASHPTAEvtIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYD-INEEAAQELLEEIKEEGGDAI--AVKADVSSEEDVENLVEQIVEK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751368102  81 FQRLDCIYLNAGIMpnpqlnikalFFGLFsrkvihmfstaeglltqGDkITADGLQEVFETNVFGHFILVKKL 153
Cdd:PRK05565  81 FGKIDILVNNAGIS----------NFGLV-----------------TD-MTDEEWDRVIDVNLTGVMLLTRYA 125
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 3-92 2.50e-12

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: 62.29  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALlaSHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05344    2 KVALVTAASSGIGLAIARALAREGARVAIC--ARNRENLERAASEL--RAGGAGVLAVVADLTDPEDIDRLVEKAGDAFG 77

                         90
                 ....*....|
gi 751368102  83 RLDCIYLNAG 92
Cdd:cd05344   78 RVDILVNNAG 87
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 3-149 4.34e-12

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: 61.71  E-value: 4.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLclACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIM--ACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEED 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751368102  83 RLDCIYLNAGIMPNPqlnikalffglfsrkviHMfstaeglltqgdkITADGLQEVFETNVFGHFIL 149
Cdd:cd09807   80 RLDVLINNAGVMRCP-----------------YS-------------KTEDGFEMQFGVNHLGHFLL 116
PRK06123 PRK06123
SDR family oxidoreductase;
1-148 5.01e-12

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 61.33  E-value: 5.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCkrLLAEDDELHLCLA-CRNMSKAEAVCAALLASHPTAevTIVQVDVSNLQSVFRASKELKQ 79
Cdd:PRK06123   1 MRKVMIITGASRGIGAATA--LLAAERGYAVCLNyLRNRDAAEAVVQAIRRQGGEA--LAVAADVADEADVLRLFEAVDR 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751368102  80 RFQRLDCIYLNAGIMpNPQLNIkalffglfsrkvihmfstaeglltqgDKITADGLQEVFETNVFGHFI 148
Cdd:PRK06123  77 ELGRLDALVNNAGIL-EAQMRL--------------------------EQMDAARLTRIFATNVVGSFL 118
FabG-like PRK07231
SDR family oxidoreductase;
3-107 7.26e-12

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 61.00  E-value: 7.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVcAALLASHPTAevTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGA--RVVVTDRNEEAAERV-AAEILAGGRA--IAVAADVSDEADVEAAVAAALERFG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 751368102  83 RLDCIYLNAGIMPNPQ---------------LNIKALFFG 107
Cdd:PRK07231  81 SVDILVNNAGTTHRNGplldvdeaefdrifaVNVKSPYLW 120
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 3-151 8.83e-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: 60.83  E-value: 8.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLclacrnMSKAEAVCAALLASHPTAeVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05348    5 EVALITGGGSGLGRALVERFVAEGAKVAV------LDRSAEKVAELRADFGDA-VVGVEGDVRSLADNERAVARCVERFG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751368102  83 RLDCIYLNAGIMPnpqlnikalffglfsrkviHMFSTAEgllTQGDKItADGLQEVFETNVFGHFILVK 151
Cdd:cd05348   78 KLDCFIGNAGIWD-------------------YSTSLVD---IPEEKL-DEAFDELFHINVKGYILGAK 123
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 3-154 1.03e-11

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 60.45  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAeavcAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGY--RVSLGLRNPEDL----AALSASGGDVEA--VPYDARDPEDARALVDALRDRFG 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751368102  83 RLDCIYLNAGIMPNPQLnikalffglfsrkvihmfstaeglltqgDKITADGLQEVFETNVFGHFILVKKLW 154
Cdd:cd08932   73 RIDVLVHNAGIGRPTTL----------------------------REGSDAELEAHFSINVIAPAELTRALL 116
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 3-153 1.21e-11

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: 60.29  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVcAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05332    4 KVVIITGASSGIGEELAYHLARLG--ARLVLSARREERLEEV-KSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751368102  83 RLDCIYLNAGImpnpqlNIKALFfglfsrkvihmfstaeglltQGDKItaDGLQEVFETNVFGHFILVKKL 153
Cdd:cd05332   81 GLDILINNAGI------SMRSLF--------------------HDTSI--DVDRKIMEVNYFGPVALTKAA 123
PRK07063 PRK07063
SDR family oxidoreductase;
3-93 1.84e-11

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 60.06  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELhlCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAV--ALADLDAALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEAFG 85

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK07063  86 PLDVLVNNAGI 96
PRK06181 PRK06181
SDR family oxidoreductase;
2-93 2.32e-11

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 59.61  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVcAALLASHPtAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAG--AQLVLAARNETRLASL-AQELADHG-GEALVVPTDVSDAEACERLIEAAVARF 76

                         90
                 ....*....|..
gi 751368102  82 QRLDCIYLNAGI 93
Cdd:PRK06181  77 GGIDILVNNAGI 88
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 3-93 2.81e-11

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: 59.46  E-value: 2.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELhlCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05330    4 KVVLITGGGSGLGLATAVRLAKEGAKL--SLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFG 81

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:cd05330   82 RIDGFFNNAGI 92
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 3-94 4.06e-11

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 59.05  E-value: 4.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClACRNMSKAEAVCAALLASHptAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK05557   6 KVALVTGASRGIGRAIAERLAAQGANVVIN-YASSEAGAEALVAEIGALG--GKALAVQGDVSDAESVERAVDEAKAEFG 82

                         90
                 ....*....|..
gi 751368102  83 RLDCIYLNAGIM 94
Cdd:PRK05557  83 GVDILVNNAGIT 94
PRK06484 PRK06484
short chain dehydrogenase; Validated
 2-93 4.55e-11

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 59.48  E-value: 4.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALLASHptaevTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQ--VVVADRNVERARERADSLGPDH-----HALAMDVSDEAQIREGFEQLHREF 77

                         90
                 ....*....|..
gi 751368102  82 QRLDCIYLNAGI 93
Cdd:PRK06484  78 GRIDVLVNNAGV 89
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 2-146 7.45e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 58.38  E-value: 7.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEddelhlclAC------RNMSKAEavcaallashPTAEVTIVQVDVSNLQSVFRASK 75
Cdd:PRK06179   4 SKVALVTGASSGIGRATAEKLARA--------GYrvfgtsRNPARAA----------PIPGVELLELDVTDDASVQAAVD 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751368102  76 ELKQRFQRLDCIYLNAGimpnpqlnikalfFGLFSrkVIHMFSTAEGlltqgdkitadglQEVFETNVFGH 146
Cdd:PRK06179  66 EVIARAGRIDVLVNNAG-------------VGLAG--AAEESSIAQA-------------QALFDTNVFGI 108
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 3-153 1.15e-10

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: 57.99  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLclACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd09808    2 RSFLITGANSGIGKAAALAIAKRGGTVHM--VCRNQTRAEEARKEIETESGNQNIFLHIVDMSDPKQVWEFVEEFKEEGK 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751368102  83 RLDCIYLNAGIMPNPQlnikalffglfsrkvihmfstaeglltqgdKITADGLQEVFETNVFGHFILVKKL 153
Cdd:cd09808   80 KLHVLINNAGCMVNKR------------------------------ELTEDGLEKNFATNTLGTYILTTHL 120
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 3-151 1.22e-10

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 57.86  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLA-EDDELHLCLACRNMSKAEAVCAALLASHPTAeVTIVQVDVSNLQSVFRASKELKQRf 81
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASdPSKRFKVYATMRDLKKKGRLWEAAGALAGGT-LETLQLDVCDSKSVAAAVERVTER- 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102  82 qRLDCIYLNAGImpnpqlnikalffglfsrkvihmfstaeGLLTQGDKITADGLQEVFETNVFGHFILVK 151
Cdd:cd09806   79 -HVDVLVCNAGV----------------------------GLLGPLEALSEDAMASVFDVNVFGTVRMLQ 119
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 5-93 1.27e-10

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: 57.34  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLAshPTAEVTIVQVDVSNLQSVFRASKELKQRFQRL 84
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAG--YNVALAARRTDRLDELKAELLN--PNPSVEVEILDVTDEERNQLVIAELEAELGGL 76


                 ....*....
gi 751368102  85 DCIYLNAGI 93
Cdd:cd05350   77 DLVIINAGV 85
PRK07062 PRK07062
SDR family oxidoreductase;
3-92 1.30e-10

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 57.74  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07062   9 RVAVVTGGSSGIGLATVELLLEAGASVAIC--GRDEERLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEARFG 86

                         90
                 ....*....|
gi 751368102  83 RLDCIYLNAG 92
Cdd:PRK07062  87 GVDMLVNNAG 96
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 3-95 1.44e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 57.36  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLAlCKRLLAEDDElHLCLACRNMSKAEaVCAALLASHPTAevtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06841  16 KVAVVTGGASGIGHA-IAELFAAKGA-RVALLDRSEDVAE-VAAQLLGGNAKG----LVCDVSDSQSVEAAVAAVISAFG 88

                         90
                 ....*....|...
gi 751368102  83 RLDCIYLNAGIMP 95
Cdd:PRK06841  89 RIDILVNSAGVAL 101
PRK08219 PRK08219
SDR family oxidoreductase;
1-93 1.62e-10

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 56.87  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCkRLLAEDDELHLClaCRNMSKAEAVCAAllasHPTAEVtiVQVDVSNLQSVFRASKELKqr 80
Cdd:PRK08219   2 ERPTALITGASRGIGAAIA-RELAPTHTLLLG--GRPAERLDELAAE----LPGATP--FPVDLTDPEAIAAAVEQLG-- 70

                         90
                 ....*....|...
gi 751368102  81 fqRLDCIYLNAGI 93
Cdd:PRK08219  71 --RLDVLVHNAGV 81
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 3-108 2.19e-10

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: 56.90  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLlAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRL-ARDGASVVVNYASSKAAAEEVVAEIEAAGGKAIA--VQADVSDPSQVARLFDAAEKAFG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 751368102  83 RLDCIYLNAGIMPNP--------------QLNIKALFFGL 108
Cdd:cd05362   81 GVDILVNNAGVMLKKpiaetseeefdrmfTVNTKGAFFVL 120
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 3-103 6.35e-10

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: 55.67  E-value: 6.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLaeddEL--HLCLACRNMSKAEAVCAALLASHPtAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:cd05369    4 KVAFITGGGTGIGKAIAKAFA----ELgaSVAIAGRKPEVLEAAAEEISSATG-GRAHPIQCDVRDPEAVEAAVDETLKE 78

                         90       100
                 ....*....|....*....|....*.
gi 751368102  81 FQRLDCIYLNAG---IMPNPQLNIKA 103
Cdd:cd05369   79 FGKIDILINNAAgnfLAPAESLSPNG 104
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-103 7.70e-10

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 55.50  E-value: 7.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEE 84

                         90       100
                 ....*....|....*....|....*.
gi 751368102  81 FQRLDCIYLNAGI---MPNPQLNIKA 103
Cdd:PRK12827  85 FGRLDILVNNAGIatdAAFAELSIEE 110
PRK06947 PRK06947
SDR family oxidoreductase;
1-148 7.88e-10

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 55.58  E-value: 7.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELHLCLAcRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVGINYA-RDAAAAEETADAVRAAGGRACV--VAGDVANEADVIAMFDAVQSA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 751368102  81 FQRLDCIYLNAGIMPNpqlnikalffglfSRKVIHMfstaeglltqgdkiTADGLQEVFETNVFGHFI 148
Cdd:PRK06947  78 FGRLDALVNNAGIVAP-------------SMPLADM--------------DAARLRRMFDTNVLGAYL 118
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
3-93 8.07e-10

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 55.42  E-value: 8.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVcAALLASHPTAevtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07067   7 KVALLTGAASGIGEAVAERYLAEG--ARVVIADIKPARARLA-ALEIGPAAIA----VSLDVTRQDSIDRIVAAAVERFG 79

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK07067  80 GIDILFNNAAL 90
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 1-107 8.16e-10

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: 55.46  E-value: 8.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAedDELHLCLACRNMSKAeAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:cd05366    1 MSKVAIITGAAQGIGRAIAERLAA--DGFNIVLADLNLEEA-AKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEK 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 751368102  81 FQRLDCIYLNAGIMP-NP-------------QLNIKALFFG 107
Cdd:cd05366   78 FGSFDVMVNNAGIAPiTPlltiteedlkkvyAVNVFGVLFG 118
PRK08177 PRK08177
SDR family oxidoreductase;
3-106 8.41e-10

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 55.04  E-value: 8.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLaeDDELHLCLACRNMSKAEAVcaallasHPTAEVTIVQVDVSNLQSVfrasKELKQRF- 81
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLL--ERGWQVTATVRGPQQDTAL-------QALPGVHIEKLDMNDPASL----DQLLQRLq 68

                         90       100       110
                 ....*....|....*....|....*....|....
gi 751368102  82 -QRLDCIYLNAGIM-PNPQLNIKA-------LFF 106
Cdd:PRK08177  69 gQRFDLLFVNAGISgPAHQSAADAtaaeigqLFL 102
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 3-93 8.78e-10

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 55.40  E-value: 8.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAeddelhlclacrnmSKAEAVCAALLASHPTAE-VTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK06171  10 KIIIVTGGSSGIGLAIVKELLA--------------NGANVVNADIHGGDGQHEnYQFVPTDVSSAEEVNHTVAEIIEKF 75

                         90
                 ....*....|..
gi 751368102  82 QRLDCIYLNAGI 93
Cdd:PRK06171  76 GRIDGLVNNAGI 87
PRK07024 PRK07024
SDR family oxidoreductase;
1-145 9.35e-10

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 55.32  E-value: 9.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELHLClACRNmskaeAVCAALLASHP-TAEVTIVQVDVSNLQSVFRASKELKQ 79
Cdd:PRK07024   1 MPLKVFITGASSGIGQALAREYARQGATLGLV-ARRT-----DALQAFAARLPkAARVSVYAADVRDADALAAAAADFIA 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751368102  80 RFQRLDCIYLNAGImpnpqlnikalffglfSRKVIhmfsTAEglltQGDKitaDGLQEVFETNVFG 145
Cdd:PRK07024  75 AHGLPDVVIANAGI----------------SVGTL----TEE----REDL---AVFREVMDTNYFG 113
PRK07201 PRK07201
SDR family oxidoreductase;
3-92 1.10e-09

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 55.73  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRlLAEDDELHLCLAcRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07201 372 KVVLITGASSGIGRATAIK-VAEAGATVFLVA-RNGEALDELVAEIRAKGGTAHA--YTCDLTDSAAVDHTVKDILAEHG 447

                         90
                 ....*....|
gi 751368102  83 RLDCIYLNAG 92
Cdd:PRK07201 448 HVDYLVNNAG 457
PRK07074 PRK07074
SDR family oxidoreductase;
1-92 1.49e-09

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 54.78  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALlashPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGD--RVLALDIDAAALAAFADAL----GDARFVPVACDLTDAASLAAALANAAAE 74

                         90
                 ....*....|..
gi 751368102  81 FQRLDCIYLNAG 92
Cdd:PRK07074  75 RGPVDVLVANAG 86
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 2-73 1.56e-09

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 55.31  E-value: 1.56e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEddELHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRA 73
Cdd:COG3347  425 GRVALVTGGAGGIGRATAARLAAE--GAAVVVADLDGEAAEAAAAELGGGYGADAVDATDVDVTAEAAVAAA 494
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 4-153 1.60e-09

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: 54.56  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   4 VVLITGASSGIGLALCKRLLAEDDElhlcLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQR 83
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAK----VVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGD 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102  84 LDCIYLNAGIMPNpqlnikalffglfsRKVIHMfstaeglltqgdkiTADGLQEVFETNVFGHFILVKKL 153
Cdd:cd05339   77 VTILINNAGVVSG--------------KKLLEL--------------PDEEIEKTFEVNTLAHFWTTKAF 118
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 1-93 1.64e-09

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 54.66  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEG--YRVAVADINSEKAANVAQEINAEYGEGMAYGFGADATSEQSVLALSRGVDEI 78

                         90
                 ....*....|...
gi 751368102  81 FQRLDCIYLNAGI 93
Cdd:PRK12384  79 FGRVDLLVYNAGI 91
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 3-106 1.75e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 54.63  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCkRLLAEDDELHLCLACRNMSKAEAVcAALLASHPTaEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06198   7 KVALVTGGTQGLGAAIA-RAFAERGAAGLVICGRNAEKGEAQ-AAELEALGA-KAVFVQADLSDVEDCRRVVAAADEAFG 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 751368102  83 RLDCIyLNAGIMPN--------PQL-------NIKALFF 106
Cdd:PRK06198  84 RLDAL-VNAAGLTDrgtildtsPELfdrhfavNVRAPFF 121
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 3-95 2.20e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 54.59  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALlasHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK05872  10 KVVVVTGAARGIGAELARRLHARG--AKLALVDLEEAELAALAAEL---GGDDRVLTVVADVTDLAAMQAAAEEAVERFG 84

                         90
                 ....*....|...
gi 751368102  83 RLDCIYLNAGIMP 95
Cdd:PRK05872  85 GIDVVVANAGIAS 97
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 2-95 2.52e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 53.89  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLASHPtAEVTIVQVDVSNLQSVfrasKELKQRF 81
Cdd:PRK06125   7 GKRVLITGASKGIGAAAAEAFAAEG--CHLHLVARDADALEALAADLRAAHG-VDVAVHALDLSSPEAR----EQLAAEA 79

                         90
                 ....*....|....
gi 751368102  82 QRLDCIYLNAGIMP 95
Cdd:PRK06125  80 GDIDILVNNAGAIP 93
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 3-94 3.25e-09

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: 53.70  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd08934    4 KVALVTGASSGIGEATARALAAEGAA--VAIAARRVDRLEALADELEAEGGKALV--LELDVTDEQQVDAAVERTVEALG 79

                         90
                 ....*....|..
gi 751368102  83 RLDCIYLNAGIM 94
Cdd:cd08934   80 RLDILVNNAGIM 91
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 2-95 3.80e-09

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 53.59  E-value: 3.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDDELHLCLAcRNMSKAEAVCAALLASHPTAevTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVNYA-GSAAAADELVAEIEAAGGRA--IAVQADVADAAAVTRLFDAAETAF 81

                         90
                 ....*....|....
gi 751368102  82 QRLDCIYLNAGIMP 95
Cdd:PRK12937  82 GRIDVLVNNAGVMP 95
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-95 4.98e-09

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 53.04  E-value: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELhLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK12745   1 MRPVALVTGGRRGIGLGIARALAAAGFDL-AINDRPDDEELAATQQELRAL--GVEVIFFPADVADLSAHEAMLDAAQAA 77

                         90
                 ....*....|....*
gi 751368102  81 FQRLDCIYLNAGIMP 95
Cdd:PRK12745  78 WGRIDCLVNNAGVGV 92
PRK09072 PRK09072
SDR family oxidoreductase;
3-93 5.24e-09

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 53.02  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALlaSHPtAEVTIVQVDVSNLQSVfRASKELKQRFQ 82
Cdd:PRK09072   6 KRVLLTGASGGIGQALAEALAAAG--ARLLLVGRNAEKLEALAARL--PYP-GRHRWVVADLTSEAGR-EAVLARAREMG 79

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK09072  80 GINVLINNAGV 90
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 2-94 8.10e-09

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: 52.41  E-value: 8.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALL-ASHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:cd05364    3 GKVAIITGSSSGIGAGTAILFARLG--ARLALTGRDAERLEETRQSCLqAGVSEKKILLVVADLTEEEGQDRIISTTLAK 80

                         90
                 ....*....|....
gi 751368102  81 FQRLDCIYLNAGIM 94
Cdd:cd05364   81 FGRLDILVNNAGIL 94
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 2-145 8.36e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 53.00  E-value: 8.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK07109   8 RQVVVITGASAGVGRATARAFARRGA--KVVLLARGEEGLEALAAEIRAA--GGEALAVVADVADAEAVQAAADRAEEEL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751368102  82 QRLDCIYLNAGIMpnpqlnikalffglfsrkvihMFSTAeglltqgDKITADGLQEVFETNVFG 145
Cdd:PRK07109  84 GPIDTWVNNAMVT---------------------VFGPF-------EDVTPEEFRRVTEVTYLG 119
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 2-151 1.15e-08

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: 52.01  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDDELhlcLACRNMSKAEAVCAALLASHPTAevTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAV---VVADIDPEIAEKVAEAAQGGPRA--LGVQCDVTSEAQVQSAFEQAVLEF 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102  82 QRLDCIYLNAGIMPnpqlnikalffglfSRKVihmfstaeglltqgDKITADGLQEVFETNVFGHFILVK 151
Cdd:cd08943   76 GGLDIVVSNAGIAT--------------SSPI--------------AETSLEDWNRSMDINLTGHFLVSR 117
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-94 1.31e-08

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 52.09  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLcLACRNMSKAEAVcaallashPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06463   8 KVALITGGTRGIGRAIAEAFLREGAKVAV-LYNSAENEAKEL--------REKGVFTIKCDVGNRDQVKKSKEVVEKEFG 78

                         90
                 ....*....|..
gi 751368102  83 RLDCIYLNAGIM 94
Cdd:PRK06463  79 RVDVLVNNAGIM 90
PRK06500 PRK06500
SDR family oxidoreductase;
3-93 1.39e-08

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 51.88  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALlashpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06500   7 KTALITGGTSGIGLETARQFLAEG--ARVAITGRDPASLEAARAEL-----GESALVIRADAGDVAAQKALAQALAEAFG 79

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK06500  80 RLDAVFINAGV 90
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-93 1.54e-08

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 52.16  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELhlCLACRNMSKAEAVCAALLASHPTaevtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06484 270 RVVAITGGARGIGRAVADRFAAAGDRL--LIIDRDAEGAKKLAEALGDEHLS-----VQADITDEAAVESAFAQIQARWG 342

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK06484 343 RLDVLVNNAGI 353
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 4-93 2.39e-08

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: 51.13  E-value: 2.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   4 VVLITGASSGIGLALCKRLLAEDDELHLCLACRNmskAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQR 83
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARS---EEPLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDGE 77

                         90
                 ....*....|
gi 751368102  84 LDCIYLNAGI 93
Cdd:cd05367   78 RDLLINNAGS 87
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 3-151 2.39e-08

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: 51.38  E-value: 2.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLASHPtAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd08933   10 KVVIVTGGSRGIGRGIVRAFVENGAKVVFC--ARGEAAGQALESELNRAGP-GSCKFVPCDVTKEEDIKTLISVTVERFG 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751368102  83 RLDCIYLNAGIMPNPQlnikalffglfsrkvihmfstaeglltQGDKITADGLQEVFETNVFGHFILVK 151
Cdd:cd08933   87 RIDCLVNNAGWHPPHQ---------------------------TTDETSAQEFRDLLNLNLISYFLASK 128
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 4-95 2.40e-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: 51.60  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   4 VVLITGASSGIGLALCKRLL-AEDDELHLC----LACRNMSKAEAVcAALLAshPTAEVTIVQVDVSNLQSVFRASKELK 78
Cdd:cd08953  207 VYLVTGGAGGIGRALARALArRYGARLVLLgrspLPPEEEWKAQTL-AALEA--LGARVLYISADVTDAAAVRRLLEKVR 283

                         90
                 ....*....|....*..
gi 751368102  79 QRFQRLDCIYLNAGIMP 95
Cdd:cd08953  284 ERYGAIDGVIHAAGVLR 300
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 3-95 2.53e-08

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 51.13  E-value: 2.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAedDELHLCLACRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAE--AGATVAFNDGLAAEARELAAALEAAGGRAHA--IAADLADPASVQRFFDAAAAALG 83

                         90
                 ....*....|...
gi 751368102  83 RLDCIYLNAGIMP 95
Cdd:PRK12939  84 GLDGLVNNAGITN 96
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 3-95 2.64e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 51.27  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALlashptaEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06057   8 RVAVITGGGSGIGLATARRLAAEG--ATVVVGDIDPEAGKAAADEV-------GGLFVPTDVTDEDAVNALFDTAAETYG 78

                         90
                 ....*....|...
gi 751368102  83 RLDCIYLNAGIMP 95
Cdd:PRK06057  79 SVDIAFNNAGISP 91
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 3-101 2.71e-08

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: 50.92  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCkRLLAEDDElHLCLACRNMSKAEAVCAALLashpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05326    5 KVAIITGGASGIGEATA-RLFAKHGA-RVVIADIDDDAGQAVAAELG----DPDISFVHCDVTVEADVRAAVDTAVARFG 78

                         90
                 ....*....|....*....
gi 751368102  83 RLDCIYLNAGIMPNPQLNI 101
Cdd:cd05326   79 RLDIMFNNAGVLGAPCYSI 97
PRK06194 PRK06194
hypothetical protein; Provisional
 3-93 3.30e-08

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 51.17  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEddELHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06194   7 KVAVITGAASGFGLAFARIGAAL--GMKLVLADVQQDALDRAVAELRAQ--GAEVLGVRTDVSDAAQVEALADAALERFG 82

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK06194  83 AVHLLFNNAGV 93
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 5-91 4.67e-08

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: 50.43  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCkRLLAEDDeLHLCLACRNmSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQRL 84
Cdd:cd05359    1 ALVTGGSRGIGKAIA-LRLAERG-ADVVINYRK-SKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRL 77


                 ....*..
gi 751368102  85 DCIYLNA 91
Cdd:cd05359   78 DVLVSNA 84
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-93 5.21e-08

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 50.07  E-value: 5.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07666   8 KNALITGAGRGIGRAVAIALAKEG--VNVGLLARTEENLKAVAEEVEAY--GVKVVIATADVSDYEEVTAAIEQLKNELG 83

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK07666  84 SIDILINNAGI 94
PRK07806 PRK07806
SDR family oxidoreductase;
3-148 5.85e-08

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 50.10  E-value: 5.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMS-KAEAVCAALLASHPTAevTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK07806   7 KTALVTGSSRGIGADTAKILAGAG--AHVVVNYRQKApRANKVVAEIEAAGGRA--SAVGADLTDEESVAALMDTAREEF 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751368102  82 QRLDCIYLNA-GIMPNP-------QLNIKALffglfsrkvIHMFSTAEGLLTQGDKItadglqeVFETNVFGHFI 148
Cdd:PRK07806  83 GGLDALVLNAsGGMESGmdedyamRLNRDAQ---------RNLARAALPLMPAGSRV-------VFVTSHQAHFI 141
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 3-99 7.05e-08

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: 49.82  E-value: 7.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVcAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05343    7 RVALVTGASVGIGAAVARALVQHGMKVVGC--ARRVDKIEAL-AAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQ 83

                         90
                 ....*....|....*...
gi 751368102  83 RLDCIYLNAGIM-PNPQL 99
Cdd:cd05343   84 GVDVCINNAGLArPEPLL 101
PRK07035 PRK07035
SDR family oxidoreductase;
3-106 8.11e-08

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 49.63  E-value: 8.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCkRLLAEDDElHLCLACRNMSKAEAVCAALLASHPTAEVTIVQV-DVSNLQSVFrasKELKQRF 81
Cdd:PRK07035   9 KIALVTGASRGIGEAIA-KLLAQQGA-HVIVSSRKLDGCQAVADAIVAAGGKAEALACHIgEMEQIDALF---AHIRERH 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 751368102  82 QRLDCIYLNAGimPNPQ-----------------LNIKALFF 106
Cdd:PRK07035  84 GRLDILVNNAA--ANPYfghildtdlgafqktvdVNIRGYFF 123
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 3-93 1.07e-07

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: 48.63  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102     3 KVVLITGASSGIGLALCkRLLAEDDELHLCLACRN--MSKAEAVCAALLASHpTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:smart00822   1 GTYLITGGLGGLGRALA-RWLAERGARRLVLLSRSgpDAPGAAALLAELEAA-GARVTVVACDVADRDALAAVLAAIPAV 78

                           90
                   ....*....|...
gi 751368102    81 FQRLDCIYLNAGI 93
Cdd:smart00822  79 EGPLTGVIHAAGV 91
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 3-145 1.17e-07

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: 49.33  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElHLCLACRNMSKAeavcAALLASHPtAEVTIVQVDVSNLQSVfrasKELKQRFQ 82
Cdd:cd05354    4 KTVLVTGANRGIGKAFVESLLAHGAK-KVYAAVRDPGSA----AHLVAKYG-DKVVPLRLDVTDPESI----KAAAAQAK 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751368102  83 RLDCIYLNAGImpnpqlnikalffglfsrkvihmfSTAEGLLTQGDkitADGLQEVFETNVFG 145
Cdd:cd05354   74 DVDVVINNAGV------------------------LKPATLLEEGA---LEALKQEMDVNVFG 109
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 3-93 1.67e-07

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 48.73  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAvcAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK12429   5 KVALVTGAASGIGLEIALALAKEG--AKVVIADLNDEAAAA--AAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFG 80

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK12429  81 GVDILVNNAGI 91
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 3-111 2.12e-07

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: 48.73  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLAcRNMSKAEAVCAALLASHptaeVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDK--VVFA-DIDEERGADFAEAEGPN----LFFVHGDVADETLVKFVVYAMLEKLG 74

                         90       100
                 ....*....|....*....|....*....
gi 751368102  83 RLDCIYLNAGIMpNPQlNIKALFFGLFSR 111
Cdd:cd09761   75 RIDVLVNNAARG-SKG-ILSSLLLEEWDR 101
PRK06138 PRK06138
SDR family oxidoreductase;
3-92 2.41e-07

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 48.61  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLAShptAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06138   6 RVAIVTGAGSGIGRATAKLFAREG--ARVVVADRDAEAAERVAAAIAAG---GRAFARQGDVGSAEAVEALVDFVAARWG 80

                         90
                 ....*....|
gi 751368102  83 RLDCIYLNAG 92
Cdd:PRK06138  81 RLDVLVNNAG 90
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 2-91 2.85e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 48.14  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAvcAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEG--ANVVITGRTKEKLEE--AKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKF 76

                         90
                 ....*....|
gi 751368102  82 QRLDCIYLNA 91
Cdd:PRK07677  77 GRIDALINNA 86
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-94 3.04e-07

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 48.03  E-value: 3.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK08217   6 KVIVITGGAQGLGRAMAEYLAQKG--AKLALIDLNQEKLEEAVAECGAL--GTEVRGYAANVTDEEDVEATFAQIAEDFG 81

                         90
                 ....*....|..
gi 751368102  83 RLDCIYLNAGIM 94
Cdd:PRK08217  82 QLNGLINNAGIL 93
PRK06182 PRK06182
short chain dehydrogenase; Validated
 2-92 3.12e-07

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 48.03  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDDELHlcLACRNMSKAEAvcaalLAShptAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK06182   3 KKVALVTGASSGIGKATARRLAAQGYTVY--GAARRVDKMED-----LAS---LGVHPLSLDVTDEASIKAAVDTIIAEE 72

                         90
                 ....*....|.
gi 751368102  82 QRLDCIYLNAG 92
Cdd:PRK06182  73 GRIDVLVNNAG 83
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-122 3.20e-07

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: 48.16  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALlashPTAEVTIvQVDVSNLQSVFRASKELKQR 80
Cdd:cd05345    4 EGKVAIVTGAGSGFGEGIARRFAQEG--ARVVIADINADGAERVAADI----GEAAIAI-QADVTKRADVEAMVEAALSK 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 751368102  81 FQRLDCIYLNAGI--MPNP-------------QLNIKALFfgLFSRKVI-HMFSTAEG 122
Cdd:cd05345   77 FGRLDILVNNAGIthRNKPmlevdeeefdrvfAVNVKSIY--LSAQALVpHMEEQGGG 132
PRK09135 PRK09135
pteridine reductase; Provisional
 1-91 3.47e-07

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 48.00  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRN-MSKAEAVCAALLASHPTAeVTIVQVDVSNLQSVFRASKELKQ 79
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAG--YRVAIHYHRsAAEADALAAELNALRPGS-AAALQADLLDPDALPELVAACVA 81

                         90
                 ....*....|..
gi 751368102  80 RFQRLDCIYLNA 91
Cdd:PRK09135  82 AFGRLDALVNNA 93
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-96 3.72e-07

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: 47.81  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   12 SGIGLALCKRLLAEDDELhlCLACRNMSKAEAVcAALLASHPTAevtIVQVDVSNLQSVFRASKELKQRFQRLDCIYLNA 91
Cdd:pfam13561   6 SGIGWAIARALAEEGAEV--VLTDLNEALAKRV-EELAEELGAA---VLPCDVTDEEQVEALVAAAVEKFGRLDILVNNA 79


                  ....*
gi 751368102   92 GIMPN 96
Cdd:pfam13561  80 GFAPK 84
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 5-93 4.77e-07

ketoreductase (KR) and fatty acid synthase (FAS), 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. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. 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. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in 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: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 47.76  E-value: 4.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCkRLLAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELkQRFQRL 84
Cdd:cd05274  153 YLITGGLGGLGLLVA-RWLAARGARHLVLLSRRGPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAEL-AAGGPL 230


                 ....*....
gi 751368102  85 DCIYLNAGI 93
Cdd:cd05274  231 AGVIHAAGV 239
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 3-95 5.30e-07

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: 47.33  E-value: 5.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAAlLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd08930    3 KIILITGAAGLIGKAFCKALLSAGAR--LILADINAPALEQLKEE-LTNLYKNRVIALELDITSKESIKELIESYLEKFG 79

                         90
                 ....*....|...
gi 751368102  83 RLDCIYLNAGIMP 95
Cdd:cd08930   80 RIDILINNAYPSP 92
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 3-93 6.17e-07

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: 47.12  E-value: 6.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLAS-HPTAevtivqVDVSNLQSVFRASKELKQRF 81
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGIC--ARDEARLAAAAAQELEGvLGLA------GDVRDEADVRRAVDAMEEAF 72

                         90
                 ....*....|..
gi 751368102  82 QRLDCIYLNAGI 93
Cdd:cd08929   73 GGLDALVNNAGV 84
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 1-94 6.69e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 47.34  E-value: 6.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELhlCLACRNMSKaeavCAALLASHPTAEVTIvQVDVSNLQSVFRASKELKQR 80
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRV--VATARDTAT----LADLAEKYGDRLLPL-ALDVTDRAAVFAAVETAVEH 74

                         90
                 ....*....|....
gi 751368102  81 FQRLDCIYLNAGIM 94
Cdd:PRK08263  75 FGRLDIVVNNAGYG 88
PRK08264 PRK08264
SDR family oxidoreductase;
3-145 6.71e-07

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 47.19  E-value: 6.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdelhlclacrnmskAEAVCAAllASHP------TAEVTIVQVDVSNLQSVFRASKE 76
Cdd:PRK08264   7 KVVLVTGANRGIGRAFVEQLLARG--------------AAKVYAA--ARDPesvtdlGPRVVPLQLDVTDPASVAAAAEA 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751368102  77 LKQrfqrLDCIYLNAGImpnpqlnikalffglfsrkvihmFSTAEGLLTQgdkiTADGLQEVFETNVFG 145
Cdd:PRK08264  71 ASD----VTILVNNAGI-----------------------FRTGSLLLEG----DEDALRAEMETNYFG 108
PRK05693 PRK05693
SDR family oxidoreductase;
3-144 6.94e-07

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 47.09  E-value: 6.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCkrlLAEDDELHLCLA-CRNMSKAEAVCAALLAShptaevtiVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK05693   2 PVVLITGCSSGIGRALA---DAFKAAGYEVWAtARKAEDVEALAAAGFTA--------VQLDVNDGAALARLAEELEAEH 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751368102  82 QRLDCIYLNAGimpnpqlnikalfFGlfsrkvihmfstAEGLLTQGDkitADGLQEVFETNVF 144
Cdd:PRK05693  71 GGLDVLINNAG-------------YG------------AMGPLLDGG---VEAMRRQFETNVF 105
PRK08589 PRK08589
SDR family oxidoreductase;
3-93 6.96e-07

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 47.08  E-value: 6.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLlAEDDELHLCLACRnmSKAEAVCAALlaSHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK08589   7 KVAVITGASTGIGQASAIAL-AQEGAYVLAVDIA--EAVSETVDKI--KSNGGKAKAYHVDISDEQQVKDFASEIKEQFG 81

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK08589  82 RVDVLFNNAGV 92
PRK08628 PRK08628
SDR family oxidoreductase;
3-93 7.31e-07

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 46.88  E-value: 7.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdelhlclA-----CRNMSKAEAVcAALLASHPTAEVtiVQVDVSNLQSVFRASKEL 77
Cdd:PRK08628   8 KVVIVTGGASGIGAAISLRLAEEG-------AipvifGRSAPDDEFA-EELRALQPRAEF--VQVDLTDDAQCRDAVEQT 77

                         90
                 ....*....|....*.
gi 751368102  78 KQRFQRLDCIYLNAGI 93
Cdd:PRK08628  78 VAKFGRIDGLVNNAGV 93
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
5-105 8.51e-07

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 46.90  E-value: 8.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCKRLLAEDDELHlCLAcRNMSKAEAVCAAllashptAEVTIVQVDVSNLQSVFRAskelkqrFQRL 84
Cdd:COG0451    2 ILVTGGAGFIGSHLARRLLARGHEVV-GLD-RSPPGAANLAAL-------PGVEFVRGDLRDPEALAAA-------LAGV 65

                         90       100
                 ....*....|....*....|.
gi 751368102  85 DCIYLNAGIMPNPQLNIKALF 105
Cdd:COG0451   66 DAVVHLAAPAGVGEEDPDETL 86
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-93 8.79e-07

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 46.68  E-value: 8.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAedDELHLCLACRNmSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLN--DGYRVIATYFS-GNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEE 77

                         90
                 ....*....|...
gi 751368102  81 FQRLDCIYLNAGI 93
Cdd:PRK12824  78 EGPVDILVNNAGI 90
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-91 8.91e-07

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 46.64  E-value: 8.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELHLCLAcRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYA-RSRKAAEETAEEIEAL--GRKALAVKANVGDVEKIKEMFAQIDEE 79

                         90
                 ....*....|.
gi 751368102  81 FQRLDCIYLNA 91
Cdd:PRK08063  80 FGRLDVFVNNA 90
PRK08017 PRK08017
SDR family oxidoreductase;
1-145 1.07e-06

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 46.62  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRnmsKAEAVcaallASHPTAEVTIVQVDVSNLQSVFRASKE-LKQ 79
Cdd:PRK08017   1 MQKSVLITGCSSGIGLEAALELKRRG--YRVLAACR---KPDDV-----ARMNSLGFTGILLDLDDPESVERAADEvIAL 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751368102  80 RFQRLDCIYLNAGimpnpqlnikalfFGLFsrkvihmfstaeGLLTQgdkITADGLQEVFETNVFG 145
Cdd:PRK08017  71 TDNRLYGLFNNAG-------------FGVY------------GPLST---ISRQQMEQQFSTNFFG 108
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 3-94 1.10e-06

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: 46.71  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAvCAALLASHPTAevtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd08944    4 KVAIVTGAGAGIGAACAARLAREG--ARVVVADIDGGAAQA-VVAQIAGGALA----LRVDVTDEQQVAALFERAVEEFG 76

                         90
                 ....*....|..
gi 751368102  83 RLDCIYLNAGIM 94
Cdd:cd08944   77 GLDLLVNNAGAM 88
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 2-97 1.20e-06

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: 46.30  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDDELhLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:cd05337    1 RPVAIVTGASRGIGRAIATELAARGFDI-AINDLPDDDQATEVVAEVLAA--GRRAIYFQADIGELSDHEALLDQAWEDF 77

                         90
                 ....*....|....*.
gi 751368102  82 QRLDCIYLNAGIMPNP 97
Cdd:cd05337   78 GRLDCLVNNAGIAVRP 93
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 2-98 1.47e-06

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in 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: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 46.33  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDDELHlcLACRNMSKAEAVCAALlashPTAEvTIVQVDVSNLQSVFRASKELKQrF 81
Cdd:cd08951    7 MKRIFITGSSDGLGLAAARTLLHQGHEVV--LHARSQKRAADAKAAC----PGAA-GVLIGDLSSLAETRKLADQVNA-I 78

                         90
                 ....*....|....*..
gi 751368102  82 QRLDCIYLNAGIMPNPQ 98
Cdd:cd08951   79 GRFDAVIHNAGILSGPN 95
PRK09242 PRK09242
SDR family oxidoreductase;
3-153 1.56e-06

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 46.28  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK09242  10 QTALITGASKGIGLAIAREFLGLGAD--VLIVARDADALAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDHWD 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751368102  83 RLDCIYLNAGImpnpqlNIkalffglfSRKVIhmfstaeglltqgdKITADGLQEVFETNVFGHFILVKKL 153
Cdd:PRK09242  88 GLHILVNNAGG------NI--------RKAAI--------------DYTEDEWRGIFETNLFSAFELSRYA 130
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
3-93 1.86e-06

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 45.83  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHlclacrNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVI------SISRTENKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQ 75

                         90
                 ....*....|....*
gi 751368102  83 --RLDCIYL--NAGI 93
Cdd:PRK06924  76 edNVSSIHLinNAGM 90
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 2-92 1.97e-06

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: 45.99  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:cd08945    3 SEVALVTGATSGIGLAIARRLGKEGLRVFVC--ARGEEGLATTVKELREA--GVEADGRTCDVRSVPEIEALVAAAVARY 78

                         90
                 ....*....|.
gi 751368102  82 QRLDCIYLNAG 92
Cdd:cd08945   79 GPIDVLVNNAG 89
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-145 2.13e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 45.68  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDdelHLCLA-CRNMSKAeavcAALLASHPTAEVTIVqVDVSNLQSVFRASKELKQ 79
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAG---HRVVGtVRSEAAR----ADFEALHPDRALARL-LDVTDFDAIDAVVADAEA 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751368102  80 RFQRLDCIYLNAGImpnpqlnikalffGLFSrkvihmfSTAEGLLTQgdkitadgLQEVFETNVFG 145
Cdd:PRK06180  75 TFGPIDVLVNNAGY-------------GHEG-------AIEESPLAE--------MRRQFEVNVFG 112
PRK05650 PRK05650
SDR family oxidoreductase;
5-93 2.26e-06

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 45.80  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALlaSHPTAEVTIVQVDVSNLQSVFRASKELKQRFQRL 84
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWR--LALADVNEEGGEETLKLL--REAGGDGFYQRCDVRDYSQLTALAQACEEKWGGI 78


                 ....*....
gi 751368102  85 DCIYLNAGI 93
Cdd:PRK05650  79 DVIVNNAGV 87
PRK07454 PRK07454
SDR family oxidoreductase;
1-93 2.82e-06

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 45.34  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCkRLLAEDDeLHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK07454   5 SMPRALITGASSGIGKATA-LAFAKAG-WDLALVARSQDALEALAAELRST--GVKAAAYSIDLSNPEAIAPGIAELLEQ 80

                         90
                 ....*....|...
gi 751368102  81 FQRLDCIYLNAGI 93
Cdd:PRK07454  81 FGCPDVLINNAGM 93
PRK07774 PRK07774
SDR family oxidoreductase;
3-94 3.27e-06

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 45.12  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALLASHPTAevTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07774   7 KVAIVTGAAGGIGQAYAEALAREGAS--VVVADINAEGAERVAKQIVADGGTA--IAVQVDVSDPDSAKAMADATVSAFG 82

                         90
                 ....*....|..
gi 751368102  83 RLDCIYLNAGIM 94
Cdd:PRK07774  83 GIDYLVNNAAIY 94
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 3-95 3.47e-06

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 45.17  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLAshpTAEVtIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARGARVALI--GRGAAPLSQTLPGVPA---DALR-IGGIDLVDPQAARRAVDEVNRQFG 81

                         90
                 ....*....|...
gi 751368102  83 RLDCIYLNAGIMP 95
Cdd:PRK12828  82 RLDALVNIAGAFV 94
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 3-122 4.01e-06

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: 45.04  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRlLAEDDElHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05347    6 KVALVTGASRGIGFGIASG-LAEAGA-NIVINSRNEEKAEEAQQLIEKE--GVEATAFTCDVSDEEAIKAAVEAIEEDFG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 751368102  83 RLDCIYLNAGIMPNPQ--------------LNIKALFFglFSRKVI-HMFSTAEG 122
Cdd:cd05347   82 KIDILVNNAGIIRRHPaeefpeaewrdvidVNLNGVFF--VSQAVArHMIKQGHG 134
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 3-92 4.75e-06

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: 44.83  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLAShptAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd08937    5 KVVVVTGAAQGIGRGVAERLAGEGA--RVLLVDRSELVHEVLAEILAAG---DAAHVHTADLETYAGAQGVVRAAVERFG 79

                         90
                 ....*....|
gi 751368102  83 RLDCIYLNAG 92
Cdd:cd08937   80 RVDVLINNVG 89
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 3-91 6.20e-06

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: 44.37  E-value: 6.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLCLAcRNMSKAEAVcAALLASHPTAevtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYY-RSTESAEAV-AAEAGERAIA----IQADVRDRDQVQAMIEEAKNHFG 74


                 ....*....
gi 751368102  83 RLDCIYLNA 91
Cdd:cd05349   75 PVDTIVNNA 83
PRK07577 PRK07577
SDR family oxidoreductase;
2-81 6.38e-06

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 44.33  E-value: 6.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLL------------AEDD---ELHLC-LAcrNMSKAEAVCAALLASHPTAEVT------- 58
Cdd:PRK07577   3 SRTVLVTGATKGIGLALSLRLAnlghqvigiarsAIDDfpgELFACdLA--DIEQTAATLAQINEIHPVDAIVnnvgial 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 751368102  59 ---IVQVDVSNLQSVF----RASKELKQRF 81
Cdd:PRK07577  81 pqpLGKIDLAALQDVYdlnvRAAVQVTQAF 110
PRK09730 PRK09730
SDR family oxidoreductase;
3-148 6.46e-06

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 44.46  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLCLAcRNMSKAEAVCAALLASHPTAevTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQ-QNLHAAQEVVNLITQAGGKA--FVLQADISDENQVVAMFTAIDQHDE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751368102  83 RLDCIYLNAGImpnpqlnikalffgLFSRkvihmfSTAEGLltqgdkiTADGLQEVFETNVFGHFI 148
Cdd:PRK09730  79 PLAALVNNAGI--------------LFTQ------CTVENL-------TAERINRVLSTNVTGYFL 117
PRK06398 PRK06398
aldose dehydrogenase; Validated
 3-93 7.24e-06

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 44.05  E-value: 7.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHlclacrNMSKAEAvcaallashPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06398   7 KVAIVTGGSQGIGKAVVNRLKEEGSNVI------NFDIKEP---------SYNDVDYFKVDVSNKEQVIKGIDYVISKYG 71

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK06398  72 RIDILVNNAGI 82
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
3-93 7.29e-06

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 44.41  E-value: 7.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCkRLLAEDDElHLCLACRNmSKAEAVCAALLAshPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK08226   7 KTALITGALQGIGEGIA-RVFARHGA-NLILLDIS-PEIEKLADELCG--RGHRCTAVVADVRDPASVAAAIKRAKEKEG 81

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK08226  82 RIDILVNNAGV 92
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 4-93 7.53e-06

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: 43.91  E-value: 7.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   4 VVLITGASSGIGLALCkrLLAEDDELHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRFQR 83
Cdd:cd05360    2 VVVITGASSGIGRATA--LAFAERGAKVVLAARSAEALHELAREVREL--GGEAIAVVADVADAAQVERAADTAVERFGR 77

                         90
                 ....*....|
gi 751368102  84 LDCIYLNAGI 93
Cdd:cd05360   78 IDTWVNNAGV 87
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 3-93 9.27e-06

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: 43.91  E-value: 9.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALlashpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05341    6 KVAIVTGGARGLGLAHARLLVAEGAK--VVLSDILDEEGQAAAAEL-----GDAARFFHLDVTDEDGWTAVVDTAREAFG 78

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:cd05341   79 RLDVLVNNAGI 89
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-95 9.64e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 43.78  E-value: 9.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALlashptAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07825   6 KVVAITGGARGIGLATARALAALG--ARVAIGDLDEALAKETAAEL------GLVVGGPLDVTDPASFAAFLDAVEADLG 77

                         90
                 ....*....|...
gi 751368102  83 RLDCIYLNAGIMP 95
Cdd:PRK07825  78 PIDVLVNNAGVMP 90
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 3-148 1.42e-05

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 43.35  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK08277  11 KVAVITGGGGVLGGAMAKELARAG--AKVAILDRNQEKAEAVVAEIKAAGGEALA--VKADVLDKESLEQARQQILEDFG 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751368102  83 RLDcIYLNA--GIMP-----NPQLNIKA---LFFGLfsrkvihmfstaeglltqgdkiTADGLQEVFETNVFGHFI 148
Cdd:PRK08277  87 PCD-ILINGagGNHPkattdNEFHELIEptkTFFDL----------------------DEEGFEFVFDLNLLGTLL 139
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 3-93 1.64e-05

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: 43.09  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAeddelhlclacrnmskAEAVCAALLASHPTAE-------------VTIVQVDVSNLQS 69
Cdd:cd05352    9 KVAIVTGGSRGIGLAIARALAE----------------AGADVAIIYNSAPRAEekaeelakkygvkTKAYKCDVSSQES 72

                         90       100
                 ....*....|....*....|....
gi 751368102  70 VFRASKELKQRFQRLDCIYLNAGI 93
Cdd:cd05352   73 VEKTFKQIQKDFGKIDILIANAGI 96
PRK07041 PRK07041
SDR family oxidoreductase;
6-70 1.77e-05

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 43.10  E-value: 1.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751368102   6 LITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLASHPtaeVTIVQVDVSNLQSV 70
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGA--RVTIASRSRDRLAAAARALGGGAP---VRTAALDITDEAAV 60
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 3-127 1.81e-05

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: 42.99  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVcAALLASHPTAevtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05363    4 KTALITGSARGIGRAFAQAYVREGAR--VAIADINLEAARAT-AAEIGPAACA----ISLDVTDQASIDRCVAALVDRWG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 751368102  83 RLDCIYLNAGIMP-NPQLNI-KALFFGLFSRKVIHMF----STAEGLLTQG 127
Cdd:cd05363   77 SIDILVNNAALFDlAPIVDItRESYDRLFAINVSGTLfmmqAVARAMIAQG 127
PRK09186 PRK09186
flagellin modification protein A; Provisional
 3-88 1.98e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 43.05  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLCLAcrNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK09186   5 KTILITGAGGLIGSALVKAILEAGGIVIAADI--DKEALNELLESLGKEFKSKKLSLVELDITDQESLEEFLSKSAEKYG 82

                         90
                 ....*....|
gi 751368102  83 RLD----CIY 88
Cdd:PRK09186  83 KIDgavnCAY 92
PRK06482 PRK06482
SDR family oxidoreductase;
1-92 2.22e-05

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 42.80  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELhlclaCRNMSKAEAVcAALLASHPTAeVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK06482   1 MSKTWFITGASSGFGRGMTERLLARGDRV-----AATVRRPDAL-DDLKARYGDR-LWVLQLDVTDSAAVRAVVDRAFAA 73

                         90
                 ....*....|..
gi 751368102  81 FQRLDCIYLNAG 92
Cdd:PRK06482  74 LGRIDVVVSNAG 85
PRK12743 PRK12743
SDR family oxidoreductase;
1-94 2.72e-05

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 42.71  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLAlCKRLLAE-----------DDElhlclacrnmsKAEAVCAALLASHPTAEVtiVQVDVSNLQS 69
Cdd:PRK12743   1 MAQVAIVTASDSGIGKA-CALLLAQqgfdigitwhsDEE-----------GAKETAEEVRSHGVRAEI--RQLDLSDLPE 66

                         90       100
                 ....*....|....*....|....*
gi 751368102  70 VFRASKELKQRFQRLDCIYLNAGIM 94
Cdd:PRK12743  67 GAQALDKLIQRLGRIDVLVNNAGAM 91
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 3-93 3.29e-05

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: 42.37  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdelhlCLACRNM----SKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELK 78
Cdd:cd05358    4 KVALVTGASSGIGKAIAIRLATAG-----ANVVVNYrskeDAAEEVVEEIKAV--GGKAIAVQADVSKEEDVVALFQSAI 76

                         90
                 ....*....|....*
gi 751368102  79 QRFQRLDCIYLNAGI 93
Cdd:cd05358   77 KEFGTLDILVNNAGL 91
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 3-96 3.94e-05

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: 41.82  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVcAALLASHPTAEVTIVQVDVSNLQSVFrasKELKQRFQ 82
Cdd:cd05356    2 TWAVVTGATDGIGKAYAEELAKRG--FNVILISRTQEKLDAV-AKEIEEKYGVETKTIAADFSAGDDIY---ERIEKELE 75

                         90
                 ....*....|....*.
gi 751368102  83 RLDCIYL--NAGIMPN 96
Cdd:cd05356   76 GLDIGILvnNVGISHS 91
PRK07814 PRK07814
SDR family oxidoreductase;
3-122 4.08e-05

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 42.07  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLL-AEDDELhlcLACRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK07814  11 QVAVVTGAGRGLGAAIALAFAeAGADVL---IAARTESQLDEVAEQIRAAGRRAHV--VAADLAHPEATAGLAGQAVEAF 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 751368102  82 QRLDCIYLN-AGIMPNPQLNIKALF------------FGLFSRKVIHMFSTAEG 122
Cdd:PRK07814  86 GRLDIVVNNvGGTMPNPLLSTSTKDladaftfnvataHALTVAAVPLMLEHSGG 139
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 3-103 4.94e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 41.71  E-value: 4.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAedDELHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK05875   8 RTYLVTGGGSGIGKGVAAGLVA--AGAAVMIVGRNPDKLAAAAEEIEALKGAGAVRYEPADVTDEDQVARAVDAATAWHG 85

                         90       100
                 ....*....|....*....|....*
gi 751368102  83 RLDCIYLNAG----IMPNPQLNIKA 103
Cdd:PRK05875  86 RLHGVVHCAGgsetIGPITQIDSDA 110
PRK05993 PRK05993
SDR family oxidoreductase;
1-153 4.98e-05

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 41.94  E-value: 4.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGlALCKRLLAEDDeLHLCLACRnmsKAEAVcAALLASHPTAevtiVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK05993   3 MKRSILITGCSSGIG-AYCARALQSDG-WRVFATCR---KEEDV-AALEAEGLEA----FQLDYAEPESIAALVAQVLEL 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751368102  81 FQ-RLDCIYlNAGIMPNPqlniKALffglfsrkvihmfstaEGLLTqgdkitaDGLQEVFETNVFGHFILVKKL 153
Cdd:PRK05993  73 SGgRLDALF-NNGAYGQP----GAV----------------EDLPT-------EALRAQFEANFFGWHDLTRRV 118
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 4-94 5.94e-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: 41.01  E-value: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102    4 VVLITGASSGIGLALCkRLLAEDDELHLCLACRNMSKAEAVCAAL--LASHpTAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:pfam08659   2 TYLITGGLGGLGRELA-RWLAERGARHLVLLSRSAAPRPDAQALIaeLEAR-GVEVVVVACDVSDPDAVAALLAEIKAEG 79

                          90
                  ....*....|...
gi 751368102   82 QRLDCIYLNAGIM 94
Cdd:pfam08659  80 PPIRGVIHAAGVL 92
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 3-93 6.30e-05

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 41.51  E-value: 6.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLashptaEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05371    3 LVAVVTGGASGLGLATVERLLAQG--AKVVILDLPNSPGETVAKLGD------NCRFVPVDVTSEKDVKAALALAKAKFG 74

                         90
                 ....*....|..
gi 751368102  83 RLDcIYLN-AGI 93
Cdd:cd05371   75 RLD-IVVNcAGI 85
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-93 7.56e-05

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 41.14  E-value: 7.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLCLacrNMSK--AEAVCAALlaSHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVINY---NSSKeaAENLVNEL--GKEGHDVYAVQADVSKVEDANRLVEEAVNH 81

                         90
                 ....*....|...
gi 751368102  81 FQRLDCIYLNAGI 93
Cdd:PRK12935  82 FGKVDILVNNAGI 94
PRK08267 PRK08267
SDR family oxidoreductase;
2-93 8.01e-05

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 41.08  E-value: 8.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   2 RKVVLITGASSGIGLALCKRLLAED------DelhlclacRNmskaEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASK 75
Cdd:PRK08267   1 MKSIFITGAASGIGRATALLFAAEGwrvgayD--------IN----EAGLAALAAELGAGNAWTGALDVTDRAAWDAALA 68

                         90
                 ....*....|....*....
gi 751368102  76 ELKQRF-QRLDCIYLNAGI 93
Cdd:PRK08267  69 DFAAATgGRLDVLFNNAGI 87
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 1-93 8.51e-05

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: 41.30  E-value: 8.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLASHPTAEVTIvQVDVSNLQSVFRASKELKQR 80
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAG--YDVAVADINSENAEKVADEINAEYGEKAYGF-GADATNEQSVIALSKGVDEI 77

                         90
                 ....*....|...
gi 751368102  81 FQRLDCIYLNAGI 93
Cdd:cd05322   78 FKRVDLLVYSAGI 90
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 3-92 8.54e-05

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: 41.22  E-value: 8.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRlLAEDDelhlclacrnmskAEAVCAA------LLASHPTAEVTI----------------V 60
Cdd:cd05338    4 KVAFVTGASRGIGRAIALR-LAKAG-------------ATVVVAAktasegDNGSAKSLPGTIeetaeeieaaggqalpI 69

                         90       100       110
                 ....*....|....*....|....*....|..
gi 751368102  61 QVDVSNLQSVFRASKELKQRFQRLDCIYLNAG 92
Cdd:cd05338   70 VVDVRDEDQVRALVEATVDQFGRLDILVNNAG 101
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 5-95 1.05e-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: 40.60  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCKRLLAEDDELHlcLACRNMSKAEAVCAallashptAEVTIVQVDVSNLQSVFRAskelkqrFQRL 84
Cdd:COG0702    2 ILVTGATGFIGRRVVRALLARGHPVR--ALVRDPEKAAALAA--------AGVEVVQGDLDDPESLAAA-------LAGV 64

                         90
                 ....*....|.
gi 751368102  85 DCIYLNAGIMP 95
Cdd:COG0702   65 DAVFLLVPSGP 75
PRK05866 PRK05866
SDR family oxidoreductase;
3-92 1.12e-04

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 40.88  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALLASHPTAEvtIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK05866  41 KRILLTGASSGIGEAAAEQFARRGAT--VVAVARREDLLDAVADRITRAGGDAM--AVPCDLSDLDAVDALVADVEKRIG 116

                         90
                 ....*....|
gi 751368102  83 RLDCIYLNAG 92
Cdd:PRK05866 117 GVDILINNAG 126
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-153 1.13e-04

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 40.72  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDElhlclacrnmskaeaVCAALLASHP--TAEVTIVQVDVSNlqsvfrASKELK 78
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQ---------------VYGVDKQDKPdlSGNFHFLQLDLSD------DLEPLF 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751368102  79 QRFQRLDcIYLN-AGIMPNPQlnikalffglfsrkvihmfSTAEglltqgdkITADGLQEVFETNVFGHFILVKKL 153
Cdd:PRK06550  63 DWVPSVD-ILCNtAGILDDYK-------------------PLLD--------TSLEEWQHIFDTNLTSTFLLTRAY 110
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 3-94 1.66e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 40.30  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07478   7 KVAIITGASSGIGRAAAKLFAREGAK--VVVGARRQAELDQLVAEIRAE--GGEAVALAGDVRDEAYAKALVALAVERFG 82

                         90
                 ....*....|..
gi 751368102  83 RLDCIYLNAGIM 94
Cdd:PRK07478  83 GLDIAFNNAGTL 94
SDR_a6 cd05267
atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only ...
 3-100 1.83e-04

atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only a partial match to a prototypical glycine-rich NAD(P)-binding motif consensus, GXXG, which conserves part of the motif of extended SDR. Furthermore, they lack the characteristic active site residues of the SDRs. This subgroup is related to phenylcoumaran benzylic ether reductase, an NADPH-dependent aromatic alcohol reductase. One member is identified as a putative NAD-dependent epimerase/dehydratase. 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: 187577 [Multi-domain]  Cd Length: 203  Bit Score: 40.04  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDeLHLCLACRNMSKaeavcaaLLASHPtAEVTIVQVDVSNlqsvfraSKELKQRFQ 82
Cdd:cd05267    1 KKVLILGANGEIAREATTMLLENSN-VELTLFLRNAHR-------LLHLKS-ARVTVVEGDALN-------SDDLKAAMR 64

                         90
                 ....*....|....*...
gi 751368102  83 RLDCIYLNAGIMPNPQLN 100
Cdd:cd05267   65 GQDVVYANLGGTDLDQQA 82
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 3-93 1.88e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 39.99  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALlashpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK08265   7 KVAIVTGGATLIGAAVARALVAAG--ARVAIVDIDADNGAAVAASL-----GERARFIATDITDDAAIERAVATVVARFG 79

                         90
                 ....*....|....*..
gi 751368102  83 RLD------CIYLNAGI 93
Cdd:PRK08265  80 RVDilvnlaCTYLDDGL 96
PRK06139 PRK06139
SDR family oxidoreductase;
3-93 2.23e-04

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 40.09  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGlalckRLLAEDDELH---LCLACRNMSKAEAV---CAALlashpTAEVTIVQVDVSNLQSVFRASKE 76
Cdd:PRK06139   8 AVVVITGASSGIG-----QATAEAFARRgarLVLAARDEEALQAVaeeCRAL-----GAEVLVVPTDVTDADQVKALATQ 77

                         90
                 ....*....|....*..
gi 751368102  77 LKQRFQRLDCIYLNAGI 93
Cdd:PRK06139  78 AASFGGRIDVWVNNVGV 94
PRK07832 PRK07832
SDR family oxidoreductase;
3-93 3.16e-04

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 39.64  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLclacrnmSKAEAVCAALLASHPTAEVTIV----QVDVSNLQSVFRASKELK 78
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFL-------TDRDADGLAQTVADARALGGTVpehrALDISDYDAVAAFAADIH 73

                         90
                 ....*....|....*
gi 751368102  79 QRFQRLDCIYLNAGI 93
Cdd:PRK07832  74 AAHGSMDVVMNIAGI 88
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 1-133 3.77e-04

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 39.15  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDdelhlclacrnmskaEAVCAALLASHPT------AEVTIVQVDVSNLQSVFRAS 74
Cdd:PRK06483   1 MPAPILITGAGQRIGLALAWHLLAQG---------------QPVIVSYRTHYPAidglrqAGAQCIQADFSTNAGIMAFI 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751368102  75 KELKQRFQRLDCIYLNAGI-MP-NPQLNIKALFFGLFSrkvIHMFS------TAEGLLTQGDKITAD 133
Cdd:PRK06483  66 DELKQHTDGLRAIIHNASDwLAeKPGAPLADVLARMMQ---IHVNApyllnlALEDLLRGHGHAASD 129
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 5-93 3.97e-04

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: 39.20  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102    5 VLITGASSGIGLALCKRLLAEDDELHlCLAcrnmSKAEAVCAALLashptAEVTIVQVDVSNLQSVFRASKElkqrfQRL 84
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVI-GLD----RLTSASNTARL-----ADLRFVEGDLTDRDALEKLLAD-----VRP 65


                  ....*....
gi 751368102   85 DCIYLNAGI 93
Cdd:pfam01370  66 DAVIHLAAV 74
PRK07102 PRK07102
SDR family oxidoreductase;
3-69 4.05e-04

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 39.14  E-value: 4.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751368102   3 KVVLITGASSGIGLAlCKRLLAEDDElHLCLACRNMSKAEAVCAALLASHpTAEVTIVQVDVSNLQS 69
Cdd:PRK07102   2 KKILIIGATSDIARA-CARRYAAAGA-RLYLAARDVERLERLADDLRARG-AVAVSTHELDILDTAS 65
PRK06101 PRK06101
SDR family oxidoreductase;
4-94 4.10e-04

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 39.08  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   4 VVLITGASSGIGLALCKRLLAEDDELhlcLAC-RNmskaEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQR-- 80
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQV---IACgRN----QSVLDELHTQ--SANIFTLAFDVTDHPGTKAALSQLPFIpe 73

                         90
                 ....*....|....*..
gi 751368102  81 ---FQRLDCIYLNAGIM 94
Cdd:PRK06101  74 lwiFNAGDCEYMDDGKV 90
NAD_binding_10 pfam13460
NAD(P)H-binding;
9-73 4.61e-04

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 38.74  E-value: 4.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751368102    9 GASSGIGLALCKRLLAEDDELHLcLAcRNMSKAEAVCAAllashptAEVTIVQVDVSNLQSVFRA 73
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTA-LV-RNPEKLADLEDH-------PGVEVVDGDVLDPDDLAEA 56
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 3-106 5.12e-04

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: 39.00  E-value: 5.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClacrnMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd08942    7 KIVLVTGGSRGIGRMIAQGFLEAGARVIIS-----ARKAEACADAAEELSAYGECIAIPADLSSEEGIEALVARVAERSD 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 751368102  83 RLDCIYLNAG-----------------IMpnpQLNIKALFF 106
Cdd:cd08942   82 RLDVLVNNAGatwgapleafpesgwdkVM---DINVKSVFF 119
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 3-119 6.02e-04

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: 38.59  E-value: 6.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd08935    6 KVAVITGGTGVLGGAMARALAQAG--AKVAALGRNQEKGDKVAKEITAL--GGRAIALAADVLDRASLERAREEIVAQFG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 751368102  83 RLDcIYLNA--GIMPNP-------QLNIKALFFGLFSRKVIHMFST 119
Cdd:cd08935   82 TVD-ILINGagGNHPDAttdpehyEPETEQNFFDLDEEGWEFVFDL 126
PRK06172 PRK06172
SDR family oxidoreductase;
3-93 6.28e-04

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 38.58  E-value: 6.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06172   8 KVALVTGGAAGIGRATALAFAREG--AKVVVADRDAAGGEETVALIREA--GGEALFVACDVTRDAEVKALVEQTIAAYG 83

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK06172  84 RLDYAFNNAGI 94
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 3-92 6.62e-04

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 38.39  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLClacrnmSKAEAV--CAALLAShPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK12823   9 KVVVVTGAAQGIGRGVALRAAAEGARVVLV------DRSELVheVAAELRA-AGGEALALTADLETYAGAQAAMAAAVEA 81

                         90
                 ....*....|..
gi 751368102  81 FQRLDCIYLNAG 92
Cdd:PRK12823  82 FGRIDVLINNVG 93
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 3-145 6.85e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 38.40  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRllAEDDELHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07890   6 KVVVVSGVGPGLGRTLAVR--AARAGADVVLAARTAERLDEVAAEIDDL--GRRALAVPTDITDEDQCANLVALALERFG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751368102  83 RLDCIYLNAGIMPNpqlnikalfFGLFSRkvihmfstaeglltqgdkITADGLQEVFETNVFG 145
Cdd:PRK07890  82 RVDALVNNAFRVPS---------MKPLAD------------------ADFAHWRAVIELNVLG 117
PRK09009 PRK09009
SDR family oxidoreductase;
5-85 7.37e-04

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 38.51  E-value: 7.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCKRLLAEDDELHlclacrnmskaeaVCAALLASHPTAE---VTIVQVDVSNLQSVfrasKELKQRF 81
Cdd:PRK09009   3 ILIVGGSGGIGKAMVKQLLERYPDAT-------------VHATYRHHKPDFQhdnVQWHALDVTDEAEI----KQLSEQF 65


                 ....
gi 751368102  82 QRLD 85
Cdd:PRK09009  66 TQLD 69
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 3-145 8.30e-04

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


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 38.41  E-value: 8.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLlaedDEL--HLCLACRNMSKAEavcAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKL----DSLgfTVLAGCLTKNGPG---AKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEH 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751368102  81 FQRLDCIYL--NAGIMpnpqlnikalffglfsrkvihmfstaeGLLTQGDKITADGLQEVFETNVFG 145
Cdd:cd09805   74 VGEKGLWGLvnNAGIL---------------------------GFGGDEELLPMDDYRKCMEVNLFG 113
PLN02253 PLN02253
xanthoxin dehydrogenase
 3-114 9.43e-04

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 38.27  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCkRLLAEDDElHLCLACRNMSKAEAVCAAlLASHPTaeVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PLN02253  19 KVALVTGGATGIGESIV-RLFHKHGA-KVCIVDLQDDLGQNVCDS-LGGEPN--VCFFHCDVTVEDDVSRAVDFTVDKFG 93

                         90       100       110
                 ....*....|....*....|....*....|..
gi 751368102  83 RLDCIYLNAGIMPNPQLNIKALFFGLFsRKVI 114
Cdd:PLN02253  94 TLDIMVNNAGLTGPPCPDIRNVELSEF-EKVF 124
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 3-92 1.06e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 37.96  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAeddelhlclacrnmSKAEAVCAALLASHPTAE-VTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK06523  10 KRALVTGGTKGIGAATVARLLE--------------AGARVVTTARSRPDDLPEgVEFVAADLTTAEGCAAVARAVLERL 75

                         90
                 ....*....|.
gi 751368102  82 QRLDCIYLNAG 92
Cdd:PRK06523  76 GGVDILVHVLG 86
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 3-97 1.06e-03

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 37.78  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEddELHLCLACRNmSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK08936   8 KVVVITGGSTGLGRAMAVRFGKE--KAKVVINYRS-DEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84

                         90
                 ....*....|....*
gi 751368102  83 RLDCIYLNAGiMPNP 97
Cdd:PRK08936  85 TLDVMINNAG-IENA 98
PRK08278 PRK08278
SDR family oxidoreductase;
3-92 1.27e-03

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 37.58  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRlLAEDdelhlclacrnmsKAEAVCAALLAS-HPTAEVTI----------------VQVDVS 65
Cdd:PRK08278   7 KTLFITGASRGIGLAIALR-AARD-------------GANIVIAAKTAEpHPKLPGTIhtaaeeieaaggqalpLVGDVR 72

                         90       100
                 ....*....|....*....|....*..
gi 751368102  66 NLQSVFRASKELKQRFQRLDCIYLNAG 92
Cdd:PRK08278  73 DEDQVAAAVAKAVERFGGIDICVNNAS 99
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 3-106 1.28e-03

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: 37.64  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNmSKAEA--VCAALLASHPTAevTIVQVDVSNLQSVFRASKELKQR 80
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEG--YRVVVHYNR-SEAEAqrLKDELNALRNSA--VLVQADLSDFAACADLVAAAFRA 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 751368102  81 FQRLDCIYLNAGI-MPNP-------------QLNIKALFF 106
Cdd:cd05357   76 FGRCDVLVNNASAfYPTPlgqgsedawaelfGINLKAPYL 115
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 3-114 1.28e-03

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 37.73  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELhlclaCRNMSKAEAVCAALLASHPTA-EVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGATI-----VFNDINQELVDKGLAAYRELGiEAHGYVCDVTDEDGVQAMVSQIEKEV 85

                         90       100       110
                 ....*....|....*....|....*....|....
gi 751368102  82 QRLDCIYLNAGIMPN-PQLNIKALFFglfsRKVI 114
Cdd:PRK07097  86 GVIDILVNNAGIIKRiPMLEMSAEDF----RQVI 115
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 2-94 1.29e-03

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


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 37.69  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102    2 RKVVLITGASSGIGLALCKRLLAE------------DDELHLCLACRnmskaeAVCAALLASHPtAEVTIVQVDVSNLQS 69
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADgwrvvavdlcadDPAVGYPLATR------AELDAVAAACP-DQVLPVIADVRDPAA 73

                          90       100
                  ....*....|....*....|....*
gi 751368102   70 VFRASKELKQRFQRLDCIYLNAGIM 94
Cdd:TIGR04504  74 LAAAVALAVERWGRLDAAVAAAGVI 98
PRK06949 PRK06949
SDR family oxidoreductase;
3-147 1.40e-03

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 37.43  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAK--VVLASRRVERLKELRAEIEAEGGAAHV--VSLDVTDYQSIKAAVAHAETEAG 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751368102  83 RLDCIYLNAGImpnpqlnikalffglfsrkvihmfSTAEGLLtqgdKITADGLQEVFETNVFGHF 147
Cdd:PRK06949  86 TIDILVNNSGV------------------------STTQKLV----DVTPADFDFVFDTNTRGAF 122
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
 5-70 1.41e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); 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. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. 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 KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 37.63  E-value: 1.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751368102   5 VLITGASSGIGLALCKRLLAEDDELHLCLACRnmSKAEAVCAALLASHPT---AEVTIVQVDVSNLQSV 70
Cdd:cd08956  196 VLITGGTGTLGALLARHLVTEHGVRHLLLVSR--RGPDAPGAAELVAELAalgAEVTVAACDVADRAAL 262
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 1-84 1.50e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 37.69  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASsGIGLALCKRLLAEDdelHLCLACRNMSKAEAVCAALL-ASHptaEVTIVQVDVSNLQSVfrasKELKQ 79
Cdd:PRK06940   1 MKEVVVVIGAG-GIGQAIARRVGAGK---KVLLADYNEENLEAAAKTLReAGF---DVSTQEVDVSSRESV----KALAA 69


                 ....*
gi 751368102  80 RFQRL 84
Cdd:PRK06940  70 TAQTL 74
PRK06124 PRK06124
SDR family oxidoreductase;
3-92 1.62e-03

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 37.38  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCkRLLAEDDElHLCLACRNMSKAEAVCAALLASHPTAEVTIvqVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06124  12 QVALVTGSARGLGFEIA-RALAGAGA-HVLVNGRNAATLEAAVAALRAAGGAAEALA--FDIADEEAVAAAFARIDAEHG 87

                         90
                 ....*....|
gi 751368102  83 RLDCIYLNAG 92
Cdd:PRK06124  88 RLDILVNNVG 97
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 6-93 1.71e-03

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 37.44  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   6 LITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAALLASHPTAEVTIvqVDVSNLQSVFRASKELKQRFQRLD 85
Cdd:PRK07523  14 LVTGSSQGIGYALAEGLAQAGAE--VILNGRDPAKLAAAAESLKGQGLSAHALA--FDVTDHDAVRAAIDAFEAEIGPID 89


                 ....*...
gi 751368102  86 CIYLNAGI 93
Cdd:PRK07523  90 ILVNNAGM 97
PRK07023 PRK07023
SDR family oxidoreductase;
6-93 1.94e-03

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 37.30  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   6 LITGASSGIGLALCKRLLAEDDELhLCLA-CRNMSkaeavcaalLASHPTAEVTIVQVDVSNLQSVFR-ASKELKQRFQR 83
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLLQPGIAV-LGVArSRHPS---------LAAAAGERLAEVELDLSDAAAAAAwLAGDLLAAFVD 74

                         90
                 ....*....|...
gi 751368102  84 LDCIYL---NAGI 93
Cdd:PRK07023  75 GASRVLlinNAGT 87
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 1-93 2.22e-03

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: 37.04  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELHLClACRNMSKAEAVCAALLASHpTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAGANIVLN-GFGDAAEIEAVRAGLAAKH-GVKVLYHGADLSKPAAIEDMVAYAQRQ 78

                         90
                 ....*....|...
gi 751368102  81 FQRLDCIYLNAGI 93
Cdd:cd08940   79 FGGVDILVNNAGI 91
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-91 2.45e-03

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 36.99  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MRKVVLITGASSGIGLALCKRLLAEDDELHLclacrNMSKAEAVCAALLASHPTAEVTIvQVDVSNLQSVFRASKELKQR 80
Cdd:PRK08642   4 SEQTVLVTGGSRGLGAAIARAFAREGARVVV-----NYHQSEDAAEALADELGDRAIAL-QADVTDREQVQAMFATATEH 77

                         90
                 ....*....|..
gi 751368102  81 F-QRLDCIYLNA 91
Cdd:PRK08642  78 FgKPITTVVNNA 89
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-93 2.77e-03

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 36.80  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLAShpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAG--AAVAIADLNQDGANAVADEINKA--GGKAIGVAMDVTNEDAVNAGIDKVAERFG 83

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK13394  84 SVDILVSNAGI 94
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
 5-73 2.81e-03

atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. 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: 187556 [Multi-domain]  Cd Length: 293  Bit Score: 36.94  E-value: 2.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCKRLLAEDDELhLCLaCRNMSKaeavcaalLASHPTAE-VTIVQVDVSNLQSVFRA 73
Cdd:cd05245    1 VLVTGATGYVGGRLVPRLLQEGHQV-RAL-VRSPEK--------LADRPWSErVTVVRGDLEDPESLRAA 60
PRK12742 PRK12742
SDR family oxidoreductase;
3-93 2.98e-03

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 36.66  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLCLAcrnmSKAEAvcAALLASHPTAEVtiVQVDVSNLQSVFraskELKQRFQ 82
Cdd:PRK12742   7 KKVLVLGGSRGIGAAIVRRFVTDGANVRFTYA----GSKDA--AERLAQETGATA--VQTDSADRDAVI----DVVRKSG 74

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK12742  75 ALDILVVNAGI 85
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 3-76 3.40e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 36.62  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLAlCKRLLAED--------------DELHLCLACRNMS---KAEAVCAALLASHPTAEVTIVQVDVS 65
Cdd:PRK07060  10 KSVLVTGASSGIGRA-CAVALAQRgarvvaaarnaaalDRLAGETGCEPLRldvGDDAAIRAALAAAGAFDGLVNCAGIA 88

                         90
                 ....*....|.
gi 751368102  66 NLQSVFRASKE 76
Cdd:PRK07060  89 SLESALDMTAE 99
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 4-92 3.60e-03

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: 36.43  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102    4 VVLITGASSGIGLA----LCKRLLAEDDElhLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSN---LQSVFRASKE 76
Cdd:TIGR01500   2 VCLVTGASRGFGRTiaqeLAKCLKSPGSV--LVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAeagLEQLLKALRE 79

                          90
                  ....*....|....*...
gi 751368102   77 L--KQRFQRLdCIYLNAG 92
Cdd:TIGR01500  80 LprPKGLQRL-LLINNAG 96
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 3-153 4.08e-03

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 36.00  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCK---RLLAeddelHLCLACRNMSKAEAVCAALL-ASHPTAevTIVQVDVSNL--QSVFRASKE 76
Cdd:PRK08945  13 RIILVTGAGDGIGREAALtyaRHGA-----TVILLGRTEEKLEAVYDEIEaAGGPQP--AIIPLDLLTAtpQNYQQLADT 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751368102  77 LKQRFQRLDCIYLNAGIMpnpqlnikalffglfsrkvihmfstaeGLLTQGDKITADGLQEVFETNVFGHFILVKKL 153
Cdd:PRK08945  86 IEEQFGRLDGVLHNAGLL---------------------------GELGPMEQQDPEVWQDVMQVNVNATFMLTQAL 135
PRK12746 PRK12746
SDR family oxidoreductase;
3-93 4.29e-03

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 36.17  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRlLAEDDELHLCLACRNMSKAEAVCAALLASHPTAevTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMR-LANDGALVAIHYGRNKQAADETIREIESNGGKA--FLIEADLNSIDGVKKLVEQLKNELQ 83

                         90
                 ....*....|....*..
gi 751368102  83 ------RLDCIYLNAGI 93
Cdd:PRK12746  84 irvgtsEIDILVNNAGI 100
PRK05717 PRK05717
SDR family oxidoreductase;
3-93 5.18e-03

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 36.02  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALlashpTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEG--WQVVLADLDRERGSKVAKAL-----GENAWFIAMDVADEAQVAAGVAEVLGQFG 83

                         90
                 ....*....|.
gi 751368102  83 RLDCIYLNAGI 93
Cdd:PRK05717  84 RLDALVCNAAI 94
MDH cd00704
Malate dehydrogenase; Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid ...
 5-94 5.60e-03

Malate dehydrogenase; Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. MDHs belong to the NAD-dependent, lactate dehydrogenase (LDH)-like, 2-hydroxycarboxylate dehydrogenase family, which also includes the GH4 family of glycoside hydrolases. They are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133420 [Multi-domain]  Cd Length: 323  Bit Score: 36.10  E-value: 5.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   5 VLITGASSGIGLALCKRL----LAEDD---ELHLCLACRNMSKAEAV------CAALLASHPTA----EVTIVQVDVsnl 67
Cdd:cd00704    3 VLITGAAGQIGYNLLFLIasgeLFGDDqpvILHLLDIPPAMKALEGVvmelqdCAFPLLKGVVIttdpEEAFKDVDV--- 79

                         90       100
                 ....*....|....*....|....*..
gi 751368102  68 qSVFRASKELKQRFQRLDCIYLNAGIM 94
Cdd:cd00704   80 -AILVGAFPRKPGMERADLLRKNAKIF 105
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-92 5.62e-03

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 35.89  E-value: 5.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   1 MR---KVVLITGASSGIGLALCKRLLAEDDElhLCLACRNMSKAEAVCAAlLASHptAEVTIVQVDVSNLQSVFRASKEL 77
Cdd:PRK05786   1 MRlkgKKVAIIGVSEGLGYAVAYFALKEGAQ--VCINSRNENKLKRMKKT-LSKY--GNIHYVVGDVSSTESARNVIEKA 75

                         90
                 ....*....|....*
gi 751368102  78 KQRFQRLDCIYLNAG 92
Cdd:PRK05786  76 AKVLNAIDGLVVTVG 90
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-93 6.02e-03

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 35.97  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCkRLLAEDDelhlclacrnmskAEAVC-------AALLAShpTAEV--TIVQVDVSNLQSVFRA 73
Cdd:PRK08261 211 KVALVTGAARGIGAAIA-EVLARDG-------------AHVVCldvpaagEALAAV--ANRVggTALALDITAPDAPARI 274

                         90       100
                 ....*....|....*....|
gi 751368102  74 SKELKQRFQRLDCIYLNAGI 93
Cdd:PRK08261 275 AEHLAERHGGLDIVVHNAGI 294
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 3-95 6.16e-03

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: 35.52  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   3 KVVLITGASSGIGLALCKRLLAEDDELHLclacrnMSKAEAVCAALLASHptaEVTIVQVDVSNLQSVFRASKElkqrFQ 82
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANVIA------TDINEEKLKELERGP---GITTRVLDVTDKEQVAALAKE----EG 69

                         90
                 ....*....|...
gi 751368102  83 RLDCIYLNAGIMP 95
Cdd:cd05368   70 RIDVLFNCAGFVH 82
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 3-57 7.14e-03

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 35.63  E-value: 7.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751368102   3 KVVLITGASSGIGLALCKRLLA-------------EDDELHLCLACRNMSKAEAV---CAALLASHPTAEV 57
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFVEagakvigfdqaflTQEDYPFATFVLDVSDAAAVaqvCQRLLAETGPLDV 79
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 5-65 8.01e-03

ketoreductase (KR), subgroup 1, 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 KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 35.61  E-value: 8.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751368102   5 VLITGASSGIG--LAlckRLLAEDDELHLCLACRnmSKAEAVCAALLASHPT---AEVTIVQVDVS 65
Cdd:cd08952  233 VLVTGGTGALGahVA---RWLARRGAEHLVLTSR--RGPDAPGAAELVAELTalgARVTVAACDVA 293
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
 4-63 9.47e-03

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. 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: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 35.32  E-value: 9.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368102   4 VVLITGASSGIGLALCKRLLAEDDELHLCLacRNMSKAEAVCAALLASHPTAEVTIVQVD 63
Cdd:cd05227    1 LVLVTGATGFIASHIVEQLLKAGYKVRGTV--RSLSKSAKLKALLKAAGYNDRLEFVIVD 58
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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