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Conserved domains on  [gi|19923931|ref|NP_612421|]
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retinol dehydrogenase 13 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

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
1-242 3.75e-153

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 cd09807:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 274  Bit Score: 427.65  E-value: 3.75e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   1 MEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHF 80
Cdd:cd09807  35 MAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDRLDVLINNAGVMRCPYSKTEDGFEMQFGVNHLGHF 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  81 LLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 160
Cdd:cd09807 115 LLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINFDDLNSE-KSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPG 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931 161 VARTELGRHTGIHGsTFSSTTLGPIFWLLVKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPEAEDEEVARRLWA 240
Cdd:cd09807 194 VVRTELGRHTGIHH-LFLSTLLNPLFWPFVKTPREGAQTSIYLALAEELEGVSGKYFSDCKLKEPAPEAMDEETARRLWE 272

                ..
gi 19923931 241 ES 242
Cdd:cd09807 273 IS 274
 
Name Accession Description Interval E-value
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
1-242 3.75e-153

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: 427.65  E-value: 3.75e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   1 MEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHF 80
Cdd:cd09807  35 MAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDRLDVLINNAGVMRCPYSKTEDGFEMQFGVNHLGHF 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  81 LLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 160
Cdd:cd09807 115 LLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINFDDLNSE-KSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPG 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931 161 VARTELGRHTGIHGsTFSSTTLGPIFWLLVKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPEAEDEEVARRLWA 240
Cdd:cd09807 194 VVRTELGRHTGIHH-LFLSTLLNPLFWPFVKTPREGAQTSIYLALAEELEGVSGKYFSDCKLKEPAPEAMDEETARRLWE 272

                ..
gi 19923931 241 ES 242
Cdd:cd09807 273 IS 274
PRK06197 PRK06197
short chain dehydrogenase; Provisional
2-251 2.36e-68

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 213.35  E-value: 2.36e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFL 81
Cdd:PRK06197  51 DKGKAAAARITAATPGADVTLQELDLTSLASVRAAADALRAAYPRIDLLINNAGVMYTPKQTTADGFELQFGTNHLGHFA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   82 LTNLLLDKLKASAPSRIINLSSLAH-VAGHIDFDDLNWQtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL--H 158
Cdd:PRK06197 131 LTGLLLDRLLPVPGSRVVTVSSGGHrIRAAIHFDDLQWE-RRYNRVAAYGQSKLANLLFTYELQRRLAAAGATTIAVaaH 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  159 PGVARTELGRHTGihgstfsSTTLGPIFWL---LVKSPELAAQPSTYLAVAEELAdvSGKYF--DGLKQK-------APA 226
Cdd:PRK06197 210 PGVSNTELARNLP-------RALRPVATVLaplLAQSPEMGALPTLRAATDPAVR--GGQYYgpDGFGEQrgypkvvASS 280
                        250       260
                 ....*....|....*....|....*
gi 19923931  227 PEAEDEEVARRLWAESARLVGLEAP 251
Cdd:PRK06197 281 AQSHDEDLQRRLWAVSEELTGVSFP 305
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
2-169 1.84e-34

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: 124.13  E-value: 1.84e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGH 79
Cdd:COG1028  41 EALEAAAAELRAA--GGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGplEELTEEDWDRVLDVNLKGP 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:COG1028 119 FLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQ-------------AAYAASKAAVVGLTRSLALELAPRGIRVNAVAP 185
                       170
                ....*....|
gi 19923931 160 GVARTELGRH 169
Cdd:COG1028 186 GPIDTPMTRA 195
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
2-168 1.98e-20

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 85.74  E-value: 1.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931     2 EKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMR-CP-HWTTEDGFEMQFGVNHLGH 79
Cdd:pfam00106  35 EKLEAVAKELGAL--GGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAGITGlGPfSELSDEDWERVIDVNLTGV 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    80 FLLTNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwqtrKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:pfam00106 113 FNLTRAVLPAMIKGSGGRIVNISS---VAGLV----------PYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAVAP 179

                  ....*....
gi 19923931   160 GVARTELGR 168
Cdd:pfam00106 180 GGVDTDMTK 188
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
48-166 2.92e-11

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 61.70  E-value: 2.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    48 DILINNAGVmrCP----HWTTEDGFEMQFGVNHLG-HFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtrk 122
Cdd:TIGR02415  79 DVMVNNAGV--APitpiLEITEEELKKVYNVNVKGvLFGIQAAARQFKKQGHGGKIINAASIAGHEG------------- 143
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 19923931   123 YNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:TIGR02415 144 NPILSAYSSTKFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPM 187
 
Name Accession Description Interval E-value
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
1-242 3.75e-153

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: 427.65  E-value: 3.75e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   1 MEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHF 80
Cdd:cd09807  35 MAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDRLDVLINNAGVMRCPYSKTEDGFEMQFGVNHLGHF 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  81 LLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 160
Cdd:cd09807 115 LLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINFDDLNSE-KSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPG 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931 161 VARTELGRHTGIHGsTFSSTTLGPIFWLLVKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPEAEDEEVARRLWA 240
Cdd:cd09807 194 VVRTELGRHTGIHH-LFLSTLLNPLFWPFVKTPREGAQTSIYLALAEELEGVSGKYFSDCKLKEPAPEAMDEETARRLWE 272

                ..
gi 19923931 241 ES 242
Cdd:cd09807 273 IS 274
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
1-239 1.51e-104

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: 304.15  E-value: 1.51e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   1 MEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHF 80
Cdd:cd05327  35 EEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPRLDILINNAGIMAPPRRLTKDGFELQFAVNYLGHF 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  81 LLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQTRK-YNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:cd05327 115 LLTNLLLPVLKASAPSRIVNVSSIAHRAGPIDFNDLDLENNKeYSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHP 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931 160 GVARTELGRHTGIHgsTFSSTTLGPIFWllvKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPEAEDEEVARRLW 239
Cdd:cd05327 195 GVVRTELLRRNGSF--FLLYKLLRPFLK---KSPEQGAQTALYAATSPELEGVSGKYFSDCKIKMSSSEALDEELAEKLW 269
PRK06197 PRK06197
short chain dehydrogenase; Provisional
2-251 2.36e-68

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 213.35  E-value: 2.36e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFL 81
Cdd:PRK06197  51 DKGKAAAARITAATPGADVTLQELDLTSLASVRAAADALRAAYPRIDLLINNAGVMYTPKQTTADGFELQFGTNHLGHFA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   82 LTNLLLDKLKASAPSRIINLSSLAH-VAGHIDFDDLNWQtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL--H 158
Cdd:PRK06197 131 LTGLLLDRLLPVPGSRVVTVSSGGHrIRAAIHFDDLQWE-RRYNRVAAYGQSKLANLLFTYELQRRLAAAGATTIAVaaH 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  159 PGVARTELGRHTGihgstfsSTTLGPIFWL---LVKSPELAAQPSTYLAVAEELAdvSGKYF--DGLKQK-------APA 226
Cdd:PRK06197 210 PGVSNTELARNLP-------RALRPVATVLaplLAQSPEMGALPTLRAATDPAVR--GGQYYgpDGFGEQrgypkvvASS 280
                        250       260
                 ....*....|....*....|....*
gi 19923931  227 PEAEDEEVARRLWAESARLVGLEAP 251
Cdd:PRK06197 281 AQSHDEDLQRRLWAVSEELTGVSFP 305
PRK06196 PRK06196
oxidoreductase; Provisional
2-251 3.87e-57

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 184.89  E-value: 3.87e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGetlnhhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFL 81
Cdd:PRK06196  61 DVAREALAGIDG------VEVVMLDLADLESVRAFAERFLDSGRRIDILINNAGVMACPETRVGDGWEAQFATNHLGHFA 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   82 LTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWqTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGV 161
Cdd:PRK06196 135 LVNLLWPALAAGAGARVVALSSAGHRRSPIRWDDPHF-TRGYDKWLAYGQSKTANALFAVHLDKLGKDQGVRAFSVHPGG 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  162 ARTELGRHTGI-----------HGSTFSsttlgPIFwllvKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPE-- 228
Cdd:PRK06196 214 ILTPLQRHLPReeqvalgwvdeHGNPID-----PGF----KTPAQGAATQVWAATSPQLAGMGGLYCEDCDIAEPTPKda 284
                        250       260       270
                 ....*....|....*....|....*....|.
gi 19923931  229 --------AEDEEVARRLWAESARLVGLEAP 251
Cdd:PRK06196 285 pwsgvrphAIDPEAAARLWALSAALTGVDAF 315
PRK05854 PRK05854
SDR family oxidoreductase;
3-253 7.90e-51

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 168.71  E-value: 7.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    3 KCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCP-HWTTEDGFEMQFGVNHLGHFL 81
Cdd:PRK05854  50 KGEAAVAAIRTAVPDAKLSLRALDLSSLASVAALGEQLRAEGRPIHLLINNAGVMTPPeRQTTADGFELQFGTNHLGHFA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   82 LTNLLLDKLKAsAPSRIINLSSLAHVAGHIDFDDLNWQtRKYNTKAAYCQSKLAIVLFTKELSRR--LQGSGVTVNALHP 159
Cdd:PRK05854 130 LTAHLLPLLRA-GRARVTSQSSIAARRGAINWDDLNWE-RSYAGMRAYSQSKIAVGLFALELDRRsrAAGWGITSNLAHP 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  160 GVARTELGRHTGIHGSTFSSTTLGPIFWL-----LVKSPELAAQPSTYLAVAEELADvsGKYF--DGLKQKAPAP----- 227
Cdd:PRK05854 208 GVAPTNLLAARPEVGRDKDTLMVRLIRSLsargfLVGTVESAILPALYAATSPDAEG--GAFYgpRGPGELGGGPveqal 285
                        250       260
                 ....*....|....*....|....*...
gi 19923931  228 --EAEDEEVARRLWAESARLVGLEAPSV 253
Cdd:PRK05854 286 ypPLRRNAEAARLWEVSEQLTGVSFPAS 313
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
1-246 1.11e-47

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: 159.68  E-value: 1.11e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   1 MEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHF 80
Cdd:cd09809  35 MSRASAAVSRILEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSPLHVLVCNAAVFALPWTLTEDGLETTFQVNHLGHF 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  81 LLTNLLLDKLKASAPSRIINLSSLAH-------VAGHIDFDDLNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVT 153
Cdd:cd09809 115 YLVQLLEDVLRRSAPARVIVVSSESHrftdlpdSCGNLDFSLLSPPKKKYWSMLAYNRAKLCNILFSNELHRRLSPRGIT 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931 154 VNALHPGVArtelgRHTGIHGSTFSSTTLGPIFWLLVKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPEAEDEE 233
Cdd:cd09809 195 SNSLHPGNM-----MYSSIHRNWWVYTLLFTLARPFTKSMQQGAATTVYCATAPELEGLGGMYFNNCFRCLPSPEAQSEA 269
                       250
                ....*....|...
gi 19923931 234 VARRLWAESARLV 246
Cdd:cd09809 270 TAQQLWELSERLI 282
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
2-248 8.54e-39

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: 137.26  E-value: 8.54e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNHHVnaRHLDLASLKSIREFAAKIIEEEERVDILINNAGVM----RCPHWTtEDGFEMQFGVNHL 77
Cdd:cd09810  37 LKAEQAAQEVGMPKDSYSV--LHCDLASLDSVRQFVDNFRRTGRPLDALVCNAAVYlptaKEPRFT-ADGFELTVGVNHL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  78 GHFLLTNLLLDKLKAS--APSRIINLSSLAH----VAGHID--------------FDDLNWQT--RKYNTKAAYCQSKLA 135
Cdd:cd09810 114 GHFLLTNLLLEDLQRSenASPRIVIVGSITHnpntLAGNVPpratlgdleglaggLKGFNSMIdgGEFEGAKAYKDSKVC 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931 136 IVLFTKELSRRL-QGSGVTVNALHPG-VARTELGRHtgiHGSTFSstTLGPIFWLLV----KSPELAAQPSTYLAVAEEL 209
Cdd:cd09810 194 NMLTTYELHRRLhEETGITFNSLYPGcIAETGLFRE---HYPLFR--TLFPPFQKYItkgyVSEEEAGERLAAVIADPSL 268
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 19923931 210 aDVSGKYFDGLKQKAP-----APEAEDEEVARRLWAESARLVGL 248
Cdd:cd09810 269 -GVSGVYWSWGKASGSfenqsSQESSDDEKARKLWEISEKLVGL 311
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
2-169 1.84e-34

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: 124.13  E-value: 1.84e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGH 79
Cdd:COG1028  41 EALEAAAAELRAA--GGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGplEELTEEDWDRVLDVNLKGP 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:COG1028 119 FLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQ-------------AAYAASKAAVVGLTRSLALELAPRGIRVNAVAP 185
                       170
                ....*....|
gi 19923931 160 GVARTELGRH 169
Cdd:COG1028 186 GPIDTPMTRA 195
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
5-207 5.29e-32

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: 117.38  E-value: 5.29e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   5 EAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRC--PHWTTEDGFEMQFGVNHLGHFLL 82
Cdd:cd05233  33 EALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNNAGIARPgpLEELTDEDWDRVLDVNLTGVFLL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  83 TNLLLDKLKASAPSRIINLSSlahVAGHidfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVA 162
Cdd:cd05233 113 TRAALPHMKKQGGGRIVNISS---VAGL----------RPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLV 179
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19923931 163 RTELGRHTGIHGSTFSSTTLGPIFWLLvkSPELAAQPSTYLAVAE 207
Cdd:cd05233 180 DTPMLAKLGPEEAEKELAAAIPLGRLG--TPEEVAEAVVFLASDE 222
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
2-251 7.80e-32

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


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 119.33  E-value: 7.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKD--IRGETLNHhvnaRHLDLASLKSIREFAAKIIEEEERVDILINNAGV----MRCPHWTtEDGFEMQFGVN 75
Cdd:COG5748  41 EKAEAAAQElgIPPDSYTI----IHIDLASLESVRRFVADFRALGRPLDALVCNAAVyyplLKEPLRS-PDGYELSVATN 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  76 HLGHFLLTNLLLDKLKAS--APSRIINLSSLAH----VAGHI------DFDDLNW------------QTRKYNTKAAYCQ 131
Cdd:COG5748 116 HLGHFLLCNLLLEDLKKSpaSDPRLVILGTVTAnpkeLGGKIpipappDLGDLEGfeagfkapismiDGKKFKPGKAYKD 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931 132 SKLAIVLFTKELSRRL-QGSGVTVNALHPG-VARTELGRHtgiHGSTFSSttlgpIFWLLVK-------SPELAAQPSTY 202
Cdd:COG5748 196 SKLCNVLTMRELHRRYhESTGIVFSSLYPGcVADTPLFRN---HYPLFQK-----LFPLFQKnitggyvSQELAGERVAQ 267
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19923931 203 LAVAEELAdVSGKYFD-GLKQK--------APAPEAEDEEVARRLWAESARLVGLEAP 251
Cdd:COG5748 268 VVADPEYA-QSGVYWSwGNRQKkgrksfvqEVSPEASDDDKAKRLWELSAKLVGLATE 324
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
2-180 5.95e-26

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 101.87  E-value: 5.95e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNHHVnaRHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRC--PHWTTEDGFEMQFGVNHLGH 79
Cdd:COG0300  40 ERLEALAAELRAAGARVEV--VALDVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGGgpFEELDLEDLRRVFEVNVFGP 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:COG0300 118 VRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGM-------------AAYAASKAALEGFSESLRAELAPTGVRVTAVCP 184
                       170       180
                ....*....|....*....|.
gi 19923931 160 GVARTELGRHTGIHGSTFSST 180
Cdd:COG0300 185 GPVDTPFTARAGAPAGRPLLS 205
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
2-219 1.40e-25

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: 100.39  E-value: 1.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMR---CPHWTTEDGFEMQFGVNHLG 78
Cdd:cd05324  36 ERGQAAVEKLRAEGLS--VRFHQLDVTDDASIEAAADFVEEKYGGLDILVNNAGIAFkgfDDSTPTREQARETMKTNFFG 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  79 HFLLTNLLLDKLKASAPSRIINLSSLahvAGHIdfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALH 158
Cdd:cd05324 114 TVDVTQALLPLLKKSPAGRIVNVSSG---LGSL--------------TSAYGVSKAALNALTRILAKELKETGIKVNACC 176
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19923931 159 PGVARTELGRHTGihgstfssttlgpifwllVKSPELAAQPSTYLAVAEELADVSGKYFDG 219
Cdd:cd05324 177 PGWVKTDMGGGKA------------------PKTPEEGAETPVYLALLPPDGEPTGKFFSD 219
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
2-212 1.14e-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: 98.33  E-value: 1.14e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLnhhvnARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGH 79
Cdd:COG4221  40 ERLEALAAELGGRAL-----AVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLeeLDPEDWDRMIDVNVKGV 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:COG4221 115 LYVTRAALPAMRARGSGHIVNISS---IAGLRPYPGG----------AVYAATKAAVRGLSESLRAELRPTGIRVTVIEP 181
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 19923931 160 GVARTELGRHTGIHGSTFSSTTLGPIFWLlvkSPELAAQpsTYLAVAEELADV 212
Cdd:COG4221 182 GAVDTEFLDSVFDGDAEAAAAVYEGLEPL---TPEDVAE--AVLFALTQPAHV 229
PLN00015 PLN00015
protochlorophyllide reductase
2-247 3.64e-23

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 95.54  E-value: 3.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGETLNHHVnaRHLDLASLKSIREFAAKIIEEEERVDILINNAGVM----RCPHWTtEDGFEMQFGVNHL 77
Cdd:PLN00015  33 LKAERAAKSAGMPKDSYTV--MHLDLASLDSVRQFVDNFRRSGRPLDVLVCNAAVYlptaKEPTFT-ADGFELSVGTNHL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   78 GHFLLTNLLLDKLKAS-APSR--II-------------------NLSSLAHVAGhiDFDDLNWQT----RKYNTKAAYCQ 131
Cdd:PLN00015 110 GHFLLSRLLLDDLKKSdYPSKrlIIvgsitgntntlagnvppkaNLGDLRGLAG--GLNGLNSSAmidgGEFDGAKAYKD 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  132 SKLAIVLFTKELSRRLQGS-GVTVNALHPG-VARTELGRHtgiHGSTFSstTLGPIFWLLVkspelaaqpsTYLAVAEE- 208
Cdd:PLN00015 188 SKVCNMLTMQEFHRRYHEEtGITFASLYPGcIATTGLFRE---HIPLFR--LLFPPFQKYI----------TKGYVSEEe 252
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931  209 ----LADV--------SGKYFDGLKQKA-----PAPEAEDEEVARRLWAESARLVG 247
Cdd:PLN00015 253 agkrLAQVvsdpsltkSGVYWSWNGGSAsfenqLSQEASDAEKAKKVWEISEKLVG 308
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
26-248 6.52e-22

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: 91.40  E-value: 6.52e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  26 DLASLKSIREFAAKIiEEEERVDILINNAGVMRCPH-WTTEDGFEMQFGVNHLGHFLLTNllldklKASAPSRIINLSSL 104
Cdd:cd08951  61 DLSSLAETRKLADQV-NAIGRFDAVIHNAGILSGPNrKTPDTGIPAMVAVNVLAPYVLTA------LIRRPKRLIYLSSG 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931 105 AHVAGHIDFDDLNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGsgVTVNALHPGVARTELGrhtgihGSTFSSTTlgp 184
Cdd:cd08951 134 MHRGGNASLDDIDWFNRGENDSPAYSDSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPTKMG------GAGAPDDL--- 202
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923931 185 ifwllvkspELAAQPSTYLAVAEE-LADVSGKYFDGLKQKAPAPEAEDEEVARRLWAESARLVGL 248
Cdd:cd08951 203 ---------EQGHLTQVWLAESDDpQALTSGGYFYHRRLQEPHPASEDSRLQEKLVQALEEVTGV 258
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
2-168 1.98e-20

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 85.74  E-value: 1.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931     2 EKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMR-CP-HWTTEDGFEMQFGVNHLGH 79
Cdd:pfam00106  35 EKLEAVAKELGAL--GGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAGITGlGPfSELSDEDWERVIDVNLTGV 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    80 FLLTNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwqtrKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:pfam00106 113 FNLTRAVLPAMIKGSGGRIVNISS---VAGLV----------PYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAVAP 179

                  ....*....
gi 19923931   160 GVARTELGR 168
Cdd:pfam00106 180 GGVDTDMTK 188
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
7-178 1.48e-18

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: 81.57  E-value: 1.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   7 AAKDIRGETLNHH-VNARHLDLASL--KSIREFAAKIieEEERVDILINNAGVM---RCPHWTTEDGFEMQFGVNHLGHF 80
Cdd:cd05325  35 AATELAALGASHSrLHILELDVTDEiaESAEAVAERL--GDAGLDVLINNAGILhsyGPASEVDSEDLLEVFQVNVLGPL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  81 LLTNLLLDKLKASAPSRIINLSSLAhvaGHI-DFDDLNWqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:cd05325 113 LLTQAFLPLLLKGARAKIINISSRV---GSIgDNTSGGW--------YSYRASKAALNMLTKSLAVELKRDGITVVSLHP 181
                       170
                ....*....|....*....
gi 19923931 160 GVARTELGRHTGIHGSTFS 178
Cdd:cd05325 182 GWVRTDMGGPFAKNKGPIT 200
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
2-217 9.16e-18

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: 79.95  E-value: 9.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFL 81
Cdd:cd09808  36 TRAEEARKEIETESGNQNIFLHIVDMSDPKQVWEFVEEFKEEGKKLHVLINNAGCMVNKRELTEDGLEKNFATNTLGTYI 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  82 LTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQTRKYNTKAAYCQSKLAIVLFTKELSRRlqGSGVTVNALHPGV 161
Cdd:cd09808 116 LTTHLIPVLEKEEDPRVITVSSGGMLVQKLNTNNLQSERTAFDGTMVYAQNKRQQVIMTEQWAKK--HPEIHFSVMHPGW 193
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19923931 162 ARTELGRHT--GIHGStfssttlgpiFWLLVKSPELAAQPSTYLAVAEELADV-SGKYF 217
Cdd:cd09808 194 ADTPAVRNSmpDFHAR----------FKDRLRSEEQGADTVVWLALSSAAAKApSGRFY 242
PRK12939 PRK12939
short chain dehydrogenase; Provisional
2-166 5.71e-17

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 77.70  E-value: 5.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGH 79
Cdd:PRK12939  42 AEARELAAALEAA--GGRAHAIAADLADPASVQRFFDAAAAALGGLDGLVNNAGITNSKSATelDIDTWDAVMNVNVRGT 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   80 FLLTNLLLDKLKASAPSRIINLSSlahvaghidfDDLNWQTRKYntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:PRK12939 120 FLMLRAALPHLRDSGRGRIVNLAS----------DTALWGAPKL---GAYVASKGAVIGMTRSLARELGGRGITVNAIAP 186

                 ....*..
gi 19923931  160 GVARTEL 166
Cdd:PRK12939 187 GLTATEA 193
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
26-166 7.01e-16

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 74.84  E-value: 7.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAGVMRcphWT-----TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIIN 100
Cdd:PRK05557  63 DVSDAESVERAVDEAKAEFGGVDILVNNAGITR---DNllmrmKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIIN 139
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931  101 LSSLAHVAGHIdfddlnwqtrkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK05557 140 ISSVVGLMGNP-------------GQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDM 192
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-165 2.31e-15

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 73.36  E-value: 2.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIRGETLNHHVNAR--HLDLASLKSIREFAAKIIEEEERVDILINNAGVM-RCPHW-TTEDGFEMQFGVNHLGHF 80
Cdd:PRK12825  41 EEAAEELVEAVEALGRRAQavQADVTDKAALEAAVAAAVERFGRIDILVNNAGIFeDKPLAdMSDDEWDEVIDVNLSGVF 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   81 LLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnWQTRkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 160
Cdd:PRK12825 121 HLLRAVVPPMRKQRGGRIVNISSVAGLPG--------WPGR-----SNYAAAKAGLVGLTKALARELAEYGITVNMVAPG 187

                 ....*
gi 19923931  161 VARTE 165
Cdd:PRK12825 188 DIDTD 192
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
6-166 2.55e-15

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 73.26  E-value: 2.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    6 AAAKDIRGE--TLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGHFL 81
Cdd:PRK12824  38 DCAKDWFEEygFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVDILVNNAGITRDSvfKRMSHQEWNDVINTNLNSVFN 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   82 LTNLLLDKLKASAPSRIINLSSLAHVAGHIdfddlnwqtrkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGV 161
Cdd:PRK12824 118 VTQPLFAAMCEQGYGRIINISSVNGLKGQF-------------GQTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGY 184

                 ....*
gi 19923931  162 ARTEL 166
Cdd:PRK12824 185 IATPM 189
PRK06841 PRK06841
short chain dehydrogenase; Provisional
4-168 2.91e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 73.15  E-value: 2.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    4 CEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRC--PHWTTEDGFEMQFGVNHLGHFL 81
Cdd:PRK06841  47 RSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILVNSAGVALLapAEDVSEEDWDKTIDINLKGSFL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   82 LTNLLLDKLKASAPSRIINLSSLAHVAGhIDfddlnwqtrkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGV 161
Cdd:PRK06841 127 MAQAVGRHMIAAGGGKIVNLASQAGVVA-LE------------RHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTV 193

                 ....*..
gi 19923931  162 ARTELGR 168
Cdd:PRK06841 194 VLTELGK 200
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
2-166 1.27e-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: 71.04  E-value: 1.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNHHVNArhLDLASLKSIREFAAKIIEEEERVDILINNAGVmrcphwtTEDGFEMQF--------- 72
Cdd:cd05333  35 EAAAETVEEIKALGGNAAALE--ADVSDREAVEALVEKVEAEFGPVDILVNNAGI-------TRDNLLMRMseedwdavi 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  73 GVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfddlnwQTrkyNtkaaYCQSKLAIVLFTKELSRRLQGSGV 152
Cdd:cd05333 106 NVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPG------QA---N----YAASKAGVIGFTKSLAKELASRGI 172
                       170
                ....*....|....
gi 19923931 153 TVNALHPGVARTEL 166
Cdd:cd05333 173 TVNAVAPGFIDTDM 186
PRK12826 PRK12826
SDR family oxidoreductase;
5-212 1.59e-14

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 71.10  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGV-MRCPHW-TTEDGFEMQFGVNHLGHFLL 82
Cdd:PRK12826  44 AATAELVEAAGGK--ARARQVDVRDRAALKAAVAAGVEDFGRLDILVANAGIfPLTPFAeMDDEQWERVIDVNLTGTFLL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   83 TNLLLDKLKASAPSRIINLSSlahVAGhidfddlnwQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVA 162
Cdd:PRK12826 122 TQAALPALIRAGGGRIVLTSS---VAG---------PRVGYPGLAHYAASKAGLVGFTRALALELAARNITVNSVHPGGV 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 19923931  163 RTELgrhtgihgstfssttLGPIFWLLVKSPELAAQPSTYLAVAEELADV 212
Cdd:PRK12826 190 DTPM---------------AGNLGDAQWAEAIAAAIPLGRLGEPEDIAAA 224
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
8-165 4.15e-14

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: 69.95  E-value: 4.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   8 AKDIRGETLNHHVNARH--LDLASLKSIREFAAKIIEEEERVDILINNAGVM-RCP-HWTTEDGFEMQFGVNHLGHfllt 83
Cdd:cd05374  34 PDKLESLGELLNDNLEVleLDVTDEESIKAAVKEVIERFGRIDVLVNNAGYGlFGPlEETSIEEVRELFEVNVFGP---- 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  84 nllLDKLKASAP-------SRIINLSSLAHVAGHidfddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNA 156
Cdd:cd05374 110 ---LRVTRAFLPlmrkqgsGRIVNVSSVAGLVPT-------------PFLGPYCASKAALEALSESLRLELAPFGIKVTI 173

                ....*....
gi 19923931 157 LHPGVARTE 165
Cdd:cd05374 174 IEPGPVRTG 182
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
2-166 4.50e-14

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 69.83  E-value: 4.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGH 79
Cdd:PRK08226  40 PEIEKLADELCGR--GHRCTAVVADVRDPASVAAAIKRAKEKEGRIDILVNNAGVCRLGSFldMSDEDRDFHIDINIKGV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   80 FLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDlnwqtrkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:PRK08226 118 WNVTKAVLPEMIARKDGRIVMMSS---VTGDMVADP---------GETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICP 185

                 ....*..
gi 19923931  160 GVARTEL 166
Cdd:PRK08226 186 GYVRTPM 192
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
3-171 8.84e-14

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: 68.59  E-value: 8.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   3 KCEAAAKDIRGETlnhHVNARH--------LDLASLKSIREFAAKIIEeeerVDILINNAGVMRcPHWTTEDGF----EM 70
Cdd:cd05354  30 KVYAAVRDPGSAA---HLVAKYgdkvvplrLDVTDPESIKAAAAQAKD----VDVVINNAGVLK-PATLLEEGAlealKQ 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  71 QFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVaghidfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSRRLQGS 150
Cdd:cd05354 102 EMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASL-------------KNFPAMGTYSASKSAAYSLTQGLRAELAAQ 168
                       170       180
                ....*....|....*....|.
gi 19923931 151 GVTVNALHPGVARTELGRHTG 171
Cdd:cd05354 169 GTLVLSVHPGPIDTRMAAGAG 189
PRK12829 PRK12829
short chain dehydrogenase; Provisional
4-165 1.07e-13

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 68.93  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    4 CEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRcPHWTTEDGFEMQF----GVNHLGH 79
Cdd:PRK12829  44 SEAALAATAARLPGAKVTATVADVADPAQVERVFDTAVERFGGLDVLVNNAGIAG-PTGGIDEITPEQWeqtlAVNLNGQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   80 FLLTNLLLDKLKASAPSR-IINLSSLAHVAGhidfddlnwqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALH 158
Cdd:PRK12829 123 FYFARAAVPLLKASGHGGvIIALSSVAGRLG-------------YPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAIL 189

                 ....*..
gi 19923931  159 PGVARTE 165
Cdd:PRK12829 190 PGIVRGP 196
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
5-168 1.60e-13

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: 67.84  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931     5 EAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVmrCPHW------TTEDGFEMQFGVNHLG 78
Cdd:pfam13561  30 EALAKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGF--APKLkgpfldTSREDFDRALDVNLYS 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    79 HFLLTnllldklKASAP-----SRIINLSSlahVAGHIDFDDLNWqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVT 153
Cdd:pfam13561 108 LFLLA-------KAALPlmkegGSIVNLSS---IGAERVVPNYNA----------YGAAKAALEALTRYLAVELGPRGIR 167
                         170
                  ....*....|....*
gi 19923931   154 VNALHPGVARTELGR 168
Cdd:pfam13561 168 VNAISPGPIKTLAAS 182
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
5-166 2.90e-13

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 67.47  E-value: 2.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   5 EAAAKDIRGETLNHH-VNARHL--DLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTT--EDGFEMQFGVNHLGH 79
Cdd:cd08940  37 AAEIEAVRAGLAAKHgVKVLYHgaDLSKPAAIEDMVAYAQRQFGGVDILVNNAGIQHVAPIEDfpTEKWDAIIALNLSAV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:cd08940 117 FHTTRLALPHMKKQGWGRIINIASVHGLVASAN-------------KSAYVAAKHGVVGLTKVVALETAGTGVTCNAICP 183

                ....*..
gi 19923931 160 GVARTEL 166
Cdd:cd08940 184 GWVLTPL 190
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
8-191 3.25e-13

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: 67.80  E-value: 3.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   8 AKDIRGETLNHHVNAR------HLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCP--HWT---------------- 63
Cdd:cd08941  43 AEAACRALLASHPDARvvfdyvLVDLSNMVSVFAAAKELKKRYPRLDYLYLNAGIMPNPgiDWIgaikevltnplfavtn 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  64 -----------------TEDGFEMQFGVNHLGHFLLTNLLLDKLKASA-PSRIINLSSLAHVAGHIDFDDlnWQTRkyNT 125
Cdd:cd08941 123 ptykiqaegllsqgdkaTEDGLGEVFQTNVFGHYYLIRELEPLLCRSDgGSQIIWTSSLNASPKYFSLED--IQHL--KG 198
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931 126 KAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELgrhtgihgstfSSTTLGPIFWLLVK 191
Cdd:cd08941 199 PAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTTNL-----------TYGILPPFTWTLAL 253
FabG-like PRK07231
SDR family oxidoreductase;
5-166 9.49e-13

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 66.01  E-value: 9.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIRGETLNHHVNARHLDLASLKSIREFAakiIEEEERVDILINNAGVMRCP---HWTTEDGFEMQFGVNHLGHFL 81
Cdd:PRK07231  43 ERVAAEILAGGRAIAVAADVSDEADVEAAVAAA---LERFGSVDILVNNAGTTHRNgplLDVDEAEFDRIFAVNVKSPYL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   82 LTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLNWqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGV 161
Cdd:PRK07231 120 WTQAAVPAMRGEGGGAIVNVAS---TAGLRPRPGLGW----------YNASKGAVITLTKALAAELGPDKIRVNAVAPVV 186

                 ....*
gi 19923931  162 ARTEL 166
Cdd:PRK07231 187 VETGL 191
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
26-166 2.22e-12

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: 64.99  E-value: 2.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  26 DLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLLTnllldklKASAP-----SRI 98
Cdd:cd05362  61 DVSDPSQVARLFDAAEKAFGGVDILVNNAGVMLKKPIaeTSEEEFDRMFTVNTKGAFFVL-------QEAAKrlrdgGRI 133
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923931  99 INLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:cd05362 134 INISSSLTAAYTPNY-------------GAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
2-160 4.47e-12

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: 64.04  E-value: 4.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIR--GETLNHHVnarhlDLASLKSIREFAAKIIEEEERVDILINNAGVMrcphWTT------EDGFEMQFG 73
Cdd:cd08942  41 EACADAAEELSayGECIAIPA-----DLSSEEGIEALVARVAERSDRLDVLVNNAGAT----WGApleafpESGWDKVMD 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  74 VNHLGHFLLTNLLLDKLKASA----PSRIINLSSLAHVAGhidfddlnwqtrKYNTKAAYCQSKLAIVLFTKELSRRLQG 149
Cdd:cd08942 112 INVKSVFFLTQALLPLLRAAAtaenPARVINIGSIAGIVV------------SGLENYSYGASKAAVHQLTRKLAKELAG 179
                       170
                ....*....|.
gi 19923931 150 SGVTVNALHPG 160
Cdd:cd08942 180 EHITVNAIAPG 190
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
2-171 6.04e-12

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 63.64  E-value: 6.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGetLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMR---CPHWTTEDgFEMQFGVNHLG 78
Cdd:PRK05653  40 EAAEALAAELRA--AGGEARVLVFDVSDEAAVRALIEAAVEAFGALDILVNNAGITRdalLPRMSEED-WDRVIDVNLTG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   79 HFLLTnllldklKASAPS-------RIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSG 151
Cdd:PRK05653 117 TFNVV-------RAALPPmikarygRIVNISSVSGVTGNPGQ-------------TNYSAAKAGVIGFTKALALELASRG 176
                        170       180
                 ....*....|....*....|
gi 19923931  152 VTVNALHPGVARTELGRHTG 171
Cdd:PRK05653 177 ITVNAVAPGFIDTDMTEGLP 196
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
48-166 2.20e-11

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: 62.39  E-value: 2.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  48 DILINNAGVMRCPHW--TTEDGFEMQFGVNHLG-HFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLnwqtrkyn 124
Cdd:cd05366  82 DVMVNNAGIAPITPLltITEEDLKKVYAVNVFGvLFGIQAAARQFKKLGHGGKIINASS---IAGVQGFPNL-------- 150
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19923931 125 tkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:cd05366 151 --GAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM 190
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
19-168 2.26e-11

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 62.10  E-value: 2.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  19 HVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMR--CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPS 96
Cdd:cd05331  41 PLRLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAGVLRpgATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTG 120
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923931  97 RIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 168
Cdd:cd05331 121 AIVTVASNAAHVPRISM-------------AAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQR 179
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
48-166 2.92e-11

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 61.70  E-value: 2.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    48 DILINNAGVmrCP----HWTTEDGFEMQFGVNHLG-HFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtrk 122
Cdd:TIGR02415  79 DVMVNNAGV--APitpiLEITEEELKKVYNVNVKGvLFGIQAAARQFKKQGHGGKIINAASIAGHEG------------- 143
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 19923931   123 YNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:TIGR02415 144 NPILSAYSSTKFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPM 187
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-165 3.36e-11

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 61.58  E-value: 3.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    1 MEKCEAAAKDIRgetlnHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGV--MRCPHWTTEDGFEMQFGVNHLG 78
Cdd:PRK07067  40 PARARLAALEIG-----PAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILFNNAALfdMAPILDISRDSYDRLFAVNVKG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   79 H-FLLTNLLLDKLKASAPSRIINLSSLahvAGHidfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:PRK07067 115 LfFLMQAVARHMVEQGRGGKIINMASQ---AGR----------RGEALVSHYCATKAAVISYTQSAALALIRHGINVNAI 181

                 ....*...
gi 19923931  158 HPGVARTE 165
Cdd:PRK07067 182 APGVVDTP 189
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
2-168 3.39e-11

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: 61.70  E-value: 3.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIR---GETLNHHVNArhLDLASLKSIREfaaKIIEEEERVDILINNAGVMRcPHWTTED------------ 66
Cdd:cd08935  40 EKGDKVAKEITalgGRAIALAADV--LDRASLERARE---EIVAQFGTVDILINGAGGNH-PDATTDPehyepeteqnff 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  67 -----GFEMQFGVNHLGHFLLTNL-LLDKLKASAPSrIINLSSLAhvaGHIDFddlnwqtrkynTK-AAYCQSKLAIVLF 139
Cdd:cd08935 114 dldeeGWEFVFDLNLNGSFLPSQVfGKDMLEQKGGS-IINISSMN---AFSPL-----------TKvPAYSAAKAAVSNF 178
                       170       180
                ....*....|....*....|....*....
gi 19923931 140 TKELSRRLQGSGVTVNALHPGVARTELGR 168
Cdd:cd08935 179 TQWLAVEFATTGVRVNAIAPGFFVTPQNR 207
PRK12828 PRK12828
short chain dehydrogenase; Provisional
25-168 4.24e-11

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 61.35  E-value: 4.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   25 LDLASLKSIREFAAKIIEEEERVDILINNAGVMRcphWTT-EDG----FEMQFGVNHLGHFLLTNLLLDKLKASAPSRII 99
Cdd:PRK12828  61 IDLVDPQAARRAVDEVNRQFGRLDALVNIAGAFV---WGTiADGdadtWDRMYGVNVKTTLNASKAALPALTASGGGRIV 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923931  100 NLSSLAHVaghidfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 168
Cdd:PRK12828 138 NIGAGAAL-------------KAGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNR 193
PRK07825 PRK07825
short chain dehydrogenase; Provisional
20-174 4.69e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 61.50  E-value: 4.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   20 VNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGhflltnlLLDKLKASAP-- 95
Cdd:PRK07825  52 VVGGPLDVTDPASFAAFLDAVEADLGPIDVLVNNAGVMPVGPFldEPDAVTRRILDVNVYG-------VILGSKLAAPrm 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   96 -SR----IINLSSLAhvaGHIDFDDLnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHT 170
Cdd:PRK07825 125 vPRgrghVVNVASLA---GKIPVPGM----------ATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGT 191

                 ....
gi 19923931  171 GIHG 174
Cdd:PRK07825 192 GGAK 195
PRK06484 PRK06484
short chain dehydrogenase; Validated
12-166 4.85e-11

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 62.17  E-value: 4.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   12 RGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGV----MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLL 87
Cdd:PRK06484  45 RADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVNNAGVtdptMTATLDTTLEEFARLQAINLTGAYLVAREAL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   88 DKLKASAP-SRIINLSSLAHVAGhidfddlnwqtrkyNTK-AAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 165
Cdd:PRK06484 125 RLMIEQGHgAAIVNVASGAGLVA--------------LPKrTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQ 190

                 .
gi 19923931  166 L 166
Cdd:PRK06484 191 M 191
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
1-173 6.48e-11

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: 60.56  E-value: 6.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   1 MEKCEAAAKDIRGetlnhhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGF------EMQfgV 74
Cdd:COG3967  39 EEKLEEAAAANPG------LHTIVLDVADPASIAALAEQVTAEFPDLNVLINNAGIMRAEDLLDEAEDladaerEIT--T 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  75 NHLG----------HFlltnllldklKASAPSRIINLSS-LAHVAGHIdfddlnwqtrkyntKAAYCQSKLAIVLFTKEL 143
Cdd:COG3967 111 NLLGpirltaaflpHL----------KAQPEAAIVNVSSgLAFVPLAV--------------TPTYSATKAALHSYTQSL 166
                       170       180       190
                ....*....|....*....|....*....|
gi 19923931 144 SRRLQGSGVTVNALHPGVARTELGRHTGIH 173
Cdd:COG3967 167 RHQLKDTSVKVIELAPPAVDTDLTGGQGGD 196
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
26-173 6.96e-11

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: 60.72  E-value: 6.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  26 DLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFlltnlllDKLKASAPSR------ 97
Cdd:cd05339  56 DVSKREEVYEAAKKIKKEVGDVTILINNAGVVSGKKLleLPDEEIEKTFEVNTLAHF-------WTTKAFLPDMlernhg 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  98 -IINLSSlahVAGHIDFDDLnwqtrkyntkAAYCQSKLAIVLFTKELS---RRLQGSGVTVNALHPGVARTELGRHTGIH 173
Cdd:cd05339 129 hIVTIAS---VAGLISPAGL----------ADYCASKAAAVGFHESLRlelKAYGKPGIKTTLVCPYFINTGMFQGVKTP 195
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
2-211 8.02e-11

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: 60.56  E-value: 8.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLN-----HHVNARHLDLASLKSIREFAAkiieEEERVDILINNAGVmrCPHWT----TEDGFEMQF 72
Cdd:cd05368  25 EGANVIATDINEEKLKelergPGITTRVLDVTDKEQVAALAK----EEGRIDVLFNCAGF--VHHGSildcEDDDWDFAM 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  73 GVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDlnwqtrkynTKAAYCQSKLAIVLFTKELSRRLQGSGV 152
Cdd:cd05368  99 NLNVRSMYLMIKAVLPKMLARKDGSIINMSS---VASSIKGVP---------NRFVYSTTKAAVIGLTKSVAADFAQQGI 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19923931 153 TVNALHPGVARTELGRHTgIHGSTFSSTTLGPIfwllvkspeLAAQPSTYLAVAEELAD 211
Cdd:cd05368 167 RCNAICPGTVDTPSLEER-IQAQPDPEEALKAF---------AARQPLGRLATPEEVAA 215
PRK06949 PRK06949
SDR family oxidoreductase;
1-169 2.91e-10

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 59.01  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    1 MEKCEAAAKDIRGETLNHHVNArhLDLASLKSIREFAAKIIEEEERVDILINNAGV---MRCPHWTTEDgFEMQFGVNHL 77
Cdd:PRK06949  43 VERLKELRAEIEAEGGAAHVVS--LDVTDYQSIKAAVAHAETEAGTIDILVNNSGVsttQKLVDVTPAD-FDFVFDTNTR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   78 GHFLLTNLLLDKLKASA--------PSRIINLSSLA--HVAGHIdfddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRL 147
Cdd:PRK06949 120 GAFFVAQEVAKRMIARAkgagntkpGGRIINIASVAglRVLPQI---------------GLYCMSKAAVVHMTRAMALEW 184
                        170       180
                 ....*....|....*....|..
gi 19923931  148 QGSGVTVNALHPGVARTELGRH 169
Cdd:PRK06949 185 GRHGINVNAICPGYIDTEINHH 206
PRK07060 PRK07060
short chain dehydrogenase; Provisional
25-166 3.57e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 58.57  E-value: 3.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   25 LDLASLKSIREFAAkiieEEERVDILINNAG--VMRCPHWTTEDGFEMQFGVNHLGHFLLTnllldklKASAPSR----- 97
Cdd:PRK07060  60 LDVGDDAAIRAALA----AAGAFDGLVNCAGiaSLESALDMTAEGFDRVMAVNARGAALVA-------RHVARAMiaagr 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923931   98 ---IINLSSlahVAGHIDFDDLnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK07060 129 ggsIVNVSS---QAALVGLPDH----------LAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
2-166 5.44e-10

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 58.09  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGH 79
Cdd:PRK12935  42 EAAENLVNELGKE--GHDVYAVQADVSKVEDANRLVEEAVNHFGKVDILVNNAGITRDRTFKklNREDWERVIDVNLSSV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   80 FLLTNLLLDKLKASAPSRIINLSSLAHVAGhiDFDDLNwqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:PRK12935 120 FNTTSAVLPYITEAEEGRIISISSIIGQAG--GFGQTN-----------YSAAKAGMLGFTKSLALELAKTNVTVNAICP 186

                 ....*..
gi 19923931  160 GVARTEL 166
Cdd:PRK12935 187 GFIDTEM 193
PRK12937 PRK12937
short chain dehydrogenase; Provisional
22-166 5.88e-10

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 57.83  E-value: 5.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   22 ARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTED--GFEMQFGVNHLGHFLLTnllldklKASAP---- 95
Cdd:PRK12937  59 AVQADVADAAAVTRLFDAAETAFGRIDVLVNNAGVMPLGTIADFDleDFDRTIATNLRGAFVVL-------REAARhlgq 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923931   96 -SRIINLSSlahvaghidfddlNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK12937 132 gGRIINLST-------------SVIALPLPGYGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
2-160 6.21e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 58.03  E-value: 6.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGETLNHHVNARhlDLASLKSIREFAAKIIEEEERVDILINNAGVMrcphW--TTED----GFEMQFGVN 75
Cdd:PRK08213  47 EELEEAAAHLEALGIDALWIAA--DVADEADIERLAEETLERFGHVDILVNNAGAT----WgaPAEDhpveAWDKVMNLN 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   76 HLGHF-LLTNLLLDKLKASAPSRIINLSSLAHVAGHiDFDDLNwqTRKYNTkaaycqSKLAIVLFTKELSRRLQGSGVTV 154
Cdd:PRK08213 121 VRGLFlLSQAVAKRSMIPRGYGRIINVASVAGLGGN-PPEVMD--TIAYNT------SKGAVINFTRALAAEWGPHGIRV 191

                 ....*.
gi 19923931  155 NALHPG 160
Cdd:PRK08213 192 NAIAPG 197
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
2-166 8.16e-10

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 57.59  E-value: 8.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAG---VMRCPHWTTEDgFEMQFGVNHLG 78
Cdd:PRK12429  39 EAAAAAAEALQKA--GGKAIGVAMDVTDEEAINAGIDYAVETFGGVDILVNNAGiqhVAPIEDFPTEK-WKKMIAIMLDG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   79 HFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALH 158
Cdd:PRK12429 116 AFLTTKAALPIMKAQGGGRIINMAS---VHGLVGSAG----------KAAYVSAKHGLIGLTKVVALEGATHGVTVNAIC 182

                 ....*...
gi 19923931  159 PGVARTEL 166
Cdd:PRK12429 183 PGYVDTPL 190
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
2-169 1.24e-09

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: 56.96  E-value: 1.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETlNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGH 79
Cdd:cd05352  43 PRAEEKAEELAKKY-GVKTKAYKCDVSSQESVEKTFKQIQKDFGKIDILIANAGITVHKPALdyTYEQWNKVIDVNLNGV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLNWqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:cd05352 122 FNCAQAAAKIFKKQGKGSLIITAS---MSGTIVNRPQPQ--------AAYNASKAAVIHLAKSLAVEWAKYFIRVNSISP 190
                       170
                ....*....|
gi 19923931 160 GVARTELGRH 169
Cdd:cd05352 191 GYIDTDLTDF 200
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
2-172 1.55e-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: 57.04  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLN-HHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTED--GFEMQFGVNHLG 78
Cdd:cd05364  38 ERLEETRQSCLQAGVSeKKILLVVADLTEEEGQDRIISTTLAKFGRLDILVNNAGILAKGGGEDQDieEYDKVMNLNLRA 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  79 HFLLTNLLLDKLKASAPSrIINLSSlahVAGHIDFDDLnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALH 158
Cdd:cd05364 118 VIYLTKLAVPHLIKTKGE-IVNVSS---VAGGRSFPGV----------LYYCISKAALDQFTRCTALELAPKGVRVNSVS 183
                       170
                ....*....|....
gi 19923931 159 PGVARTELGRHTGI 172
Cdd:cd05364 184 PGVIVTGFHRRMGM 197
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
24-204 2.13e-09

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: 56.24  E-value: 2.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  24 HLDLASLKSIREFAAKIIEEEERVDILINNAGV---MRCPHWTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIIN 100
Cdd:cd05341  57 HLDVTDEDGWTAVVDTAREAFGRLDVLVNNAGIltgGTVETTTLEE-WRRLLDINLTGVFLGTRAVIPPMKEAGGGSIIN 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931 101 LSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKE--LSRRLQGSGVTVNALHPGVARTELGRHTGIHGSTFS 178
Cdd:cd05341 136 MSSIEGLVGDPAL-------------AAYNASKGAVRGLTKSaaLECATQGYGIRVNSVHPGYIYTPMTDELLIAQGEMG 202
                       170       180
                ....*....|....*....|....*.
gi 19923931 179 STTLGPIfwLLVKSPELAAQPSTYLA 204
Cdd:cd05341 203 NYPNTPM--GRAGEPDEIAYAVVYLA 226
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
35-166 2.39e-09

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 56.18  E-value: 2.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  35 EFAAKIIE----EEERVDILINNAGVMR--CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVA 108
Cdd:cd05353  73 EDGEKIVKtaidAFGRVDILVNNAGILRdrSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLY 152
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19923931 109 GHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGvARTEL 166
Cdd:cd05353 153 GNFG-------------QANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA-AGSRM 196
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
2-165 2.42e-09

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


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 56.13  E-value: 2.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNHhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVM----RCPHWTTEDGFEMqFGVNHL 77
Cdd:cd05346  35 ERLQELADELGAKFPVK-VLPLQLDVSDRESIEAALENLPEEFRDIDILVNNAGLAlgldPAQEADLEDWETM-IDTNVK 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  78 GHFLLTNLLLDKLKASAPSRIINLSSlahVAGHidfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:cd05346 113 GLLNVTRLILPIMIARNQGHIINLGS---IAGR----------YPYAGGNVYCATKAAVRQFSLNLRKDLIGTGIRVTNI 179

                ....*...
gi 19923931 158 HPGVARTE 165
Cdd:cd05346 180 EPGLVETE 187
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
1-215 2.98e-09

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 56.08  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    1 MEKCEAAAKDirgetLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMR---CPHWTTEDgFEMQFGVNHL 77
Cdd:PRK12936  40 VEKLEALAAE-----LGERVKIFPANLSDRDEVKALGQKAEADLEGVDILVNNAGITKdglFVRMSDED-WDSVLEVNLT 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   78 GHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHidfddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:PRK12936 114 ATFRLTRELTHPMMRRRYGRIINITSVVGVTGN-------------PGQANYCASKAGMIGFSKSLAQEIATRNVTVNCV 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 19923931  158 HPGVARTELgrhTGIHGSTFSSTTLGPIFWLLVKSPELAAQPSTYLAvAEELADVSGK 215
Cdd:PRK12936 181 APGFIESAM---TGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLA-SSEAAYVTGQ 234
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
26-166 3.62e-09

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: 55.77  E-value: 3.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  26 DLASLKSIREFAAKIIEEEERVDILINNAGVMRcPHWTTEDGFEMQ-----FGVN--------HLG-HFlltnllLDKLK 91
Cdd:cd05323  57 DVTSWEQLAAAFKKAIEKFGRVDILINNAGILD-EKSYLFAGKLPPpwektIDVNltgvinttYLAlHY------MDKNK 129
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931  92 ASAPSRIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKEL-SRRLQGSGVTVNALHPGVARTEL 166
Cdd:cd05323 130 GGKGGVIVNIGSVAGLYPAPQF-------------PVYSASKHGVVGFTRSLaDLLEYKTGVRVNAICPGFTNTPL 192
PRK08264 PRK08264
SDR family oxidoreductase;
6-169 4.34e-09

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 55.28  E-value: 4.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    6 AAAKDIRGETLNHH-VNARHLDLASLKSIREFAAKIIEeeerVDILINNAGVMRCPHW---TTEDGFEMQFGVNHLGHFL 81
Cdd:PRK08264  36 AAARDPESVTDLGPrVVPLQLDVTDPASVAAAAEAASD----VTILVNNAGIFRTGSLlleGDEDALRAEMETNYFGPLA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   82 LTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGV 161
Cdd:PRK08264 112 MARAFAPVLAANGGGAIVNVLS---VLSWVNFPNL----------GTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGP 178

                 ....*...
gi 19923931  162 ARTELGRH 169
Cdd:PRK08264 179 IDTDMAAG 186
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
17-168 4.58e-09

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 55.28  E-value: 4.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   17 NHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRC--PHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASA 94
Cdd:PRK08220  47 DYPFATFVLDVSDAAAVAQVCQRLLAETGPLDVLVNAAGILRMgaTDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQR 126
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923931   95 PSRIINLSS-LAHVAghidfddlnwqtRKynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 168
Cdd:PRK08220 127 SGAIVTVGSnAAHVP------------RI--GMAAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQR 187
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
2-171 4.69e-09

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: 55.44  E-value: 4.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGH 79
Cdd:cd05347  40 EKAEEAQQLIEKEGVE--ATAFTCDVSDEEAIKAAVEAIEEDFGKIDILVNNAGIIRRHPAeeFPEAEWRDVIDVNLNGV 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPSRIINLSSLAHVAGHIdfddlnwqtrkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:cd05347 118 FFVSQAVARHMIKQGHGKIINICSLLSELGGP-------------PVPAYAASKGGVAGLTKALATEWARHGIQVNAIAP 184
                       170
                ....*....|..
gi 19923931 160 GVARTELGRHTG 171
Cdd:cd05347 185 GYFATEMTEAVV 196
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
47-168 7.72e-09

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 54.78  E-value: 7.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  47 VDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASA-PSRIINLSSlahVAGHIDFDDLnwqtrky 123
Cdd:cd05351  77 VDLLVNNAAVaiLQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSS---QASQRALTNH------- 146
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19923931 124 ntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 168
Cdd:cd05351 147 ---TVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGR 188
PRK08589 PRK08589
SDR family oxidoreductase;
22-166 1.10e-08

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 54.40  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   22 ARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCP---HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSrI 98
Cdd:PRK08589  58 AYHVDISDEQQVKDFASEIKEQFGRVDVLFNNAGVDNAAgriHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGS-I 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923931   99 INLSSLAHVAGhidfdDLNwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK08589 137 INTSSFSGQAA-----DLY--------RSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPL 191
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
25-165 1.43e-08

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 53.97  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   25 LDLASLKSIREFAAKIIEEEERVDILINNAGVM-RCP--HWTTED-GFEMQFGVNHLGHFLLTNLLLDKLKASApsRIIN 100
Cdd:PRK06935  70 VDLTKPESAEKVVKEALEEFGKIDILVNNAGTIrRAPllEYKDEDwNAVMDINLNSVYHLSQAVAKVMAKQGSG--KIIN 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923931  101 LSSLahvaghidfddLNWQTRKYntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 165
Cdd:PRK06935 148 IASM-----------LSFQGGKF--VPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
45-166 1.45e-08

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


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 53.99  E-value: 1.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  45 ERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFddlnwqtrk 122
Cdd:cd05329  83 GKLNILVNNAGTNIRKEAKdyTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISS---VAGVIAV--------- 150
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19923931 123 yNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:cd05329 151 -PSGAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPL 193
PRK12743 PRK12743
SDR family oxidoreductase;
5-160 2.75e-08

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 53.11  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIRGETLNHHVnaRHLDLASLKSIREFAAKIIEEEERVDILINNAGVMrcphwTTEDGFEMQF-------GVNHL 77
Cdd:PRK12743  41 KETAEEVRSHGVRAEI--RQLDLSDLPEGAQALDKLIQRLGRIDVLVNNAGAM-----TKAPFLDMDFdewrkifTVDVD 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   78 GHF-LLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNA 156
Cdd:PRK12743 114 GAFlCSQIAARHMVKQGQGGRIINITS---VHEHTPLPG----------ASAYTAAKHALGGLTKAMALELVEHGILVNA 180

                 ....
gi 19923931  157 LHPG 160
Cdd:PRK12743 181 VAPG 184
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
2-166 3.07e-08

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: 53.16  E-value: 3.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNHHVnarhlDLASLKSIREFAAKIIEEEERVDILINNAGVM--RCPHWTTEDGFEMQFGVNHLGH 79
Cdd:cd05358  42 EEVVEEIKAVGGKAIAVQA-----DVSKEEDVVALFQSAIKEFGTLDILVNNAGLQgdASSHEMTLEDWNKVIDVNLTGQ 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPS-RIINLSSLAHV---AGHidfddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVN 155
Cdd:cd05358 117 FLCAREAIKRFRKSKIKgKIINMSSVHEKipwPGH----------------VNYAASKGGVKMMTKTLAQEYAPKGIRVN 180
                       170
                ....*....|.
gi 19923931 156 ALHPGVARTEL 166
Cdd:cd05358 181 AIAPGAINTPI 191
PRK12827 PRK12827
short chain dehydrogenase; Provisional
26-169 3.40e-08

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 52.80  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAGVMRC---PHWTTEDgFEMQFGVNHLGHFLLTNLLLD-KLKASAPSRIINL 101
Cdd:PRK12827  67 DVRDFAATRAALDAGVEEFGRLDILVNNAGIATDaafAELSIEE-WDDVIDVNLDGFFNVTQAALPpMIRARRGGRIVNI 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923931  102 SSLAHVAGHidfddlnwqtRKYntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 169
Cdd:PRK12827 146 ASVAGVRGN----------RGQ---VNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADN 200
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-166 3.62e-08

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 52.86  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIR---GETLNHHVNARhldlaslKSIREFAAKIIEEEERVDILINNAGVMRCPHWTT--EDGFEMQFGVNHLGH 79
Cdd:PRK06463  42 ENEAKELRekgVFTIKCDVGNR-------DQVKKSKEVVEKEFGRVDVLVNNAGIMYLMPFEEfdEEKYNKMIKINLNGA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   80 FLLTNLLLDKLKASAPSRIINLSSLAHVAghidfddlnwqTRKYNTkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:PRK06463 115 IYTTYEFLPLLKLSKNGAIVNIASNAGIG-----------TAAEGT-TFYAITKAGIIILTRRLAFELGKYGIRVNAVAP 182

                 ....*..
gi 19923931  160 GVARTEL 166
Cdd:PRK06463 183 GWVETDM 189
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
2-168 3.91e-08

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: 52.31  E-value: 3.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGetlnhhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRcPH-----WTTEDGFEMQFGVNH 76
Cdd:cd05370  40 ERLAEAKKELPN------IHTIVLDVGDAESVEALAEALLSEYPNLDILINNAGIQR-PIdlrdpASDLDKADTEIDTNL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  77 LGHFLLTNLLLDKLKASAPSRIINLSS-LAHVAghidfddlnwqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVN 155
Cdd:cd05370 113 IGPIRLIKAFLPHLKKQPEATIVNVSSgLAFVP--------------MAANPVYCATKAALHSYTLALRHQLKDTGVEVV 178
                       170
                ....*....|...
gi 19923931 156 ALHPGVARTELGR 168
Cdd:cd05370 179 EIVPPAVDTELHE 191
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
26-160 4.76e-08

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: 52.28  E-value: 4.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  26 DLASLKSIREFAAKIIEEEERVDILINNAGVM--RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSs 103
Cdd:cd05357  58 DLSDFAACADLVAAAFRAFGRCDVLVNNASAFypTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINII- 136
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19923931 104 lahvaghidfDDLNWQTRKYNTkaAYCQSKLAIVLFTKELSRRLqGSGVTVNALHPG 160
Cdd:cd05357 137 ----------DAMTDRPLTGYF--AYCMSKAALEGLTRSAALEL-APNIRVNGIAPG 180
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
26-166 4.78e-08

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 52.68  E-value: 4.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  26 DLASLKSIREFAAKIIEEEERVDILINNAGvMRCPHWTTED----GFEMQFGVNHLGHFLLTnllldklKASAP-----S 96
Cdd:cd05355  85 DLGDESFCRDLVKEVVKEFGKLDILVNNAA-YQHPQESIEDitteQLEKTFRTNIFSMFYLT-------KAALPhlkkgS 156
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  97 RIINLSSLAHVAGHIDFDDlnwqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:cd05355 157 SIINTTSVTAYKGSPHLLD-------------YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPL 213
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
46-169 4.90e-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: 52.46  E-value: 4.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  46 RVDILINNAGVMRCPHW----TTEDGFEMQFGVNHLGHFlltNLLLDKLKASAPSR---IINLSSLAHVAGHIdfddlnw 118
Cdd:cd05326  79 RLDIMFNNAGVLGAPCYsileTSLEEFERVLDVNVYGAF---LGTKHAARVMIPAKkgsIVSVASVAGVVGGL------- 148
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19923931 119 qtrkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 169
Cdd:cd05326 149 ------GPHAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTA 193
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
2-169 5.61e-08

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: 52.16  E-value: 5.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGEtlNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQ--FGVNHLGH 79
Cdd:cd08934  38 DRLEALADELEAE--GGKALVLELDVTDEQQVDAAVERTVEALGRLDILVNNAGIMLLGPVEDADTTDWTrmIDTNLLGL 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwqtrKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:cd08934 116 MYTTHAALPHHLLRNKGTIVNISS---VAGRV----------AVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEP 182
                       170
                ....*....|
gi 19923931 160 GVARTELGRH 169
Cdd:cd08934 183 GTVDTELRDH 192
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
26-166 1.01e-07

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: 51.77  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  26 DLASLKSIREFAAKIIEEEERVDILINNAGvMRCPHWTTED----GFEMQFGVNHLGHFLLTNLLLDKLKASApSRIINL 101
Cdd:cd08933  67 DVTKEEDIKTLISVTVERFGRIDCLVNNAG-WHPPHQTTDEtsaqEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINL 144
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923931 102 SSLAHVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:cd08933 145 SSLVGSIGQKQ-------------AAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPL 196
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
2-169 1.22e-07

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 51.44  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIR---GETLNHHVNArhLDLASLKSIREfaaKIIEEEERVDILINNAGVMRcPHWTT-------------- 64
Cdd:PRK08277  45 EKAEAVVAEIKaagGEALAVKADV--LDKESLEQARQ---QILEDFGPCDILINGAGGNH-PKATTdnefhelieptktf 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   65 ----EDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAhvaghiDFDDLnwqtrkynTK-AAYCQSKLAIVLF 139
Cdd:PRK08277 119 fdldEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMN------AFTPL--------TKvPAYSAAKAAISNF 184
                        170       180       190
                 ....*....|....*....|....*....|
gi 19923931  140 TKELSRRLQGSGVTVNALHPGVARTELGRH 169
Cdd:PRK08277 185 TQWLAVHFAKVGIRVNAIAPGFFLTEQNRA 214
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
26-168 1.34e-07

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 51.00  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS 103
Cdd:PRK05565  63 DVSSEEDVENLVEQIVEKFGKIDILVNNAGISNFGLVTdmTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISS 142
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931  104 LahvaghidfddlnW-QTRKYNTkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 168
Cdd:PRK05565 143 I-------------WgLIGASCE-VLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWS 194
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
26-166 1.55e-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: 50.85  E-value: 1.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  26 DLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWT---TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLS 102
Cdd:cd05345  59 DVTKRADVEAMVEAALSKFGRLDILVNNAGITHRNKPMlevDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIA 138
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923931 103 SLAHVAGHidfDDLNWqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:cd05345 139 STAGLRPR---PGLTW----------YNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPL 189
PRK07035 PRK07035
SDR family oxidoreductase;
1-164 2.04e-07

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 50.78  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    1 MEKCEAAAKDIRGETLNHHVNARHLdlASLKSIREFAAKIIEEEERVDILINNAGVMrcPHW-----TTEDGFEMQFGVN 75
Cdd:PRK07035  42 LDGCQAVADAIVAAGGKAEALACHI--GEMEQIDALFAHIRERHGRLDILVNNAAAN--PYFghildTDLGAFQKTVDVN 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   76 HLGHFLLTNLLLDKLKASAPSRIINLSSLAHV-AGHidfddlnWQtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTV 154
Cdd:PRK07035 118 IRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVsPGD-------FQ-------GIYSITKAAVISMTKAFAKECAPFGIRV 183
                        170
                 ....*....|
gi 19923931  155 NALHPGVART 164
Cdd:PRK07035 184 NALLPGLTDT 193
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
2-160 2.16e-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: 50.41  E-value: 2.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNHHVnARHLDLASLKSIREFAAKIIEEEERVDILINNAGV-----MRCPHWTTEDGFEMQFGVNH 76
Cdd:cd08930  37 PALEQLKEELTNLYKNRVI-ALELDITSKESIKELIESYLEKFGRIDILINNAYPspkvwGSRFEEFPYEQWNEVLNVNL 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  77 LGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHiDFDdlNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNA 156
Cdd:cd08930 116 GGAFLCSQAFIKLFKKQGKGSIINIASIYGVIAP-DFR--IYENTQMYSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNA 192

                ....
gi 19923931 157 LHPG 160
Cdd:cd08930 193 ISPG 196
PRK07774 PRK07774
SDR family oxidoreductase;
2-170 2.29e-07

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 50.51  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVM---------RCPhWtteDGFEMQF 72
Cdd:PRK07774  41 EGAERVAKQIVADGGT--AIAVQVDVSDPDSAKAMADATVSAFGGIDYLVNNAAIYggmkldlliTVP-W---DYYKKFM 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   73 GVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAhvaghidfddlNWQTRKYntkaaYCQSKLAIVLFTKELSRRLQGSGV 152
Cdd:PRK07774 115 SVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTA-----------AWLYSNF-----YGLAKVGLNGLTQQLARELGGMNI 178
                        170
                 ....*....|....*...
gi 19923931  153 TVNALHPGVARTELGRHT 170
Cdd:PRK07774 179 RVNAIAPGPIDTEATRTV 196
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
5-166 2.36e-07

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: 50.57  E-value: 2.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   5 EAAAKDIRGetlnhHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW---TTEDGFEMQFGVNHLGHFL 81
Cdd:cd08944  41 QAVVAQIAG-----GALALRVDVTDEQQVAALFERAVEEFGGLDLLVNNAGAMHLTPAiidTDLAVWDQTMAINLRGTFL 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  82 LTNLLLDKLKASAPSRIINLSSLAHVAGHIdfddlnwqtrkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGV 161
Cdd:cd08944 116 CCRHAAPRMIARGGGSIVNLSSIAGQSGDP-------------GYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGL 182

                ....*
gi 19923931 162 ARTEL 166
Cdd:cd08944 183 IDTPL 187
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
6-166 2.67e-07

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: 50.15  E-value: 2.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   6 AAAKDIRGETLNHHVNAR--HLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW----TTEDGFEMQFGVNHLGH 79
Cdd:cd05337  37 DQATEVVAEVLAAGRRAIyfQADIGELSDHEALLDQAWEDFGRLDCLVNNAGIAVRPRGdlldLTEDSFDRLIAINLRGP 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 F------LLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVT 153
Cdd:cd05337 117 FfltqavARRMVEQPDRFDGPHRSIIFVTSINAYLVSPN-------------RGEYCISKAGLSMATRLLAYRLADEGIA 183
                       170
                ....*....|...
gi 19923931 154 VNALHPGVARTEL 166
Cdd:cd05337 184 VHEIRPGLIHTDM 196
PRK07791 PRK07791
short chain dehydrogenase; Provisional
41-217 3.25e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 50.06  E-value: 3.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   41 IEEEERVDILINNAGVMRCPHW--TTEDGFEMQFGVnHL-GHFLLTNLLLD----KLKASAP--SRIINLSSLAHVAGHI 111
Cdd:PRK07791  87 VETFGGLDVLVNNAGILRDRMIanMSEEEWDAVIAV-HLkGHFATLRHAAAywraESKAGRAvdARIINTSSGAGLQGSV 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  112 DfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPgVARTelgRHTGIHGSTFSSTTLGPIFWLLvk 191
Cdd:PRK07791 166 G-------------QGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP-AART---RMTETVFAEMMAKPEEGEFDAM-- 226
                        170       180
                 ....*....|....*....|....*.
gi 19923931  192 SPELAAQPSTYLAVAEElADVSGKYF 217
Cdd:PRK07791 227 APENVSPLVVWLGSAES-RDVTGKVF 251
PRK06914 PRK06914
SDR family oxidoreductase;
1-164 3.59e-07

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 50.02  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    1 MEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAaKIIEEEERVDILINNAG------VMRCPhwttEDGFEMQFGV 74
Cdd:PRK06914  37 PEKQENLLSQATQLNLQQNIKVQQLDVTDQNSIHNFQ-LVLKEIGRIDLLVNNAGyanggfVEEIP----VEEYRKQFET 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   75 NHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHIDFDDLnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTV 154
Cdd:PRK06914 112 NVFGAISVTQAVLPYMRKQKSGKIINISS---ISGRVGFPGL----------SPYVSSKYALEGFSESLRLELKPFGIDV 178
                        170
                 ....*....|
gi 19923931  155 NALHPGVART 164
Cdd:PRK06914 179 ALIEPGSYNT 188
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
17-160 3.68e-07

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: 49.67  E-value: 3.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  17 NHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRcpHWTTEDG----FEMQFGVNHLGHFLLTNLLLDKLKA 92
Cdd:cd08932  44 GGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHNAGIGR--PTTLREGsdaeLEAHFSINVIAPAELTRALLPALRE 121
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923931  93 SAPSRIINLSSLAHVAGHidfddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 160
Cdd:cd08932 122 AGSGRVVFLNSLSGKRVL-------------AGNAGYSASKFALRALAHALRQEGWDHGVRVSAVCPG 176
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
5-169 4.08e-07

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: 49.69  E-value: 4.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   5 EAAAKDIRgeTLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLL 82
Cdd:cd05360  38 HELAREVR--ELGGEAIAVVADVADAAQVERAADTAVERFGRIDTWVNNAGVAVFGRFedVTPEEFRRVFDVNYLGHVYG 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  83 TNLLLDKLKASAPSRIINLSSLAHVAGhidfddLNWQtrkyntkAAYCQSKLAIVLFTKELSRRLQGSG--VTVNALHPG 160
Cdd:cd05360 116 TLAALPHLRRRGGGALINVGSLLGYRS------APLQ-------AAYSASKHAVRGFTESLRAELAHDGapISVTLVQPT 182
                       170
                ....*....|....*..
gi 19923931 161 V--------ARTELGRH 169
Cdd:cd05360 183 AmntpffghARSYMGKK 199
PRK06701 PRK06701
short chain dehydrogenase; Provisional
34-166 4.36e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 50.03  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   34 REFAAKIIEEEERVDILINNAGVMRcpHWT-----TEDGFEMQFGVNHLGHFLLTnllldklKASAP-----SRIINLSS 103
Cdd:PRK06701 112 KDAVEETVRELGRLDILVNNAAFQY--PQQslediTAEQLDKTFKTNIYSYFHMT-------KAALPhlkqgSAIINTGS 182
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19923931  104 LAHVAGHIDFDDlnwqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK06701 183 ITGYEGNETLID-------------YSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPL 232
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
19-165 5.08e-07

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 49.54  E-value: 5.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  19 HVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPS 96
Cdd:cd05363  50 AACAISLDVTDQASIDRCVAALVDRWGSIDILVNNAALfdLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRG 129
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  97 -RIINLSSLAHVAGHIdfddlnwqtrkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 165
Cdd:cd05363 130 gKIINMASQAGRRGEA-------------LVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
24-170 5.17e-07

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: 49.51  E-value: 5.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  24 HLDLASLKSIREFAAKIIEEEERVDILINNAGV-MRCP-HWTTEDGFEMQFGVNHLGhflltnlLLDKLKASAPS----- 96
Cdd:cd05332  59 PLDMSDLEDAEQVVEEALKLFGGLDILINNAGIsMRSLfHDTSIDVDRKIMEVNYFG-------PVALTKAALPHliers 131
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931  97 --RIINLSSlahVAGHIdfddlnwqtrKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHT 170
Cdd:cd05332 132 qgSIVVVSS---IAGKI----------GVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNA 194
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
2-160 6.18e-07

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: 49.19  E-value: 6.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRC--PHWTTEDGFEMQFGVNHLGH 79
Cdd:cd05344  36 ENLERAASELRAGGAG--VLAVVADLTDPEDIDRLVEKAGDAFGRVDILVNNAGGPPPgpFAELTDEDWLEAFDLKLLSV 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNwqtrkyntkaaycQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:cd05344 114 IRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSN-------------VARAGLIGLVKTLSRELAPDGVTVNSVLP 180

                .
gi 19923931 160 G 160
Cdd:cd05344 181 G 181
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
2-164 6.56e-07

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 49.07  E-value: 6.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGvmRCPHWTTED-GFEMQFGV---NHL 77
Cdd:cd08945  38 EGLATTVKELREAGVE--ADGRTCDVRSVPEIEALVAAAVARYGPIDVLVNNAG--RSGGGATAElADELWLDVvetNLT 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  78 GHFLLTNLLLDK--LKASAPSRIINLSSLAHVAGHIdfddlnwqtrkynTKAAYCQSKLAIVLFTKELSRRLQGSGVTVN 155
Cdd:cd08945 114 GVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVV-------------HAAPYSASKHGVVGFTKALGLELARTGITVN 180

                ....*....
gi 19923931 156 ALHPGVART 164
Cdd:cd08945 181 AVCPGFVET 189
PRK06138 PRK06138
SDR family oxidoreductase;
22-168 6.83e-07

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 48.99  E-value: 6.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   22 ARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW--TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRII 99
Cdd:PRK06138  57 ARQGDVGSAEAVEALVDFVAARWGRLDVLVNNAGFGCGGTVvtTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIV 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923931  100 NLSSLAHVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 168
Cdd:PRK06138 137 NTASQLALAGGRG-------------RAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFR 192
PRK12747 PRK12747
short chain dehydrogenase; Provisional
44-166 7.09e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 48.92  E-value: 7.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   44 EERVDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASapSRIINLSSLAHVAGHIDFddlnwqtr 121
Cdd:PRK12747  86 STKFDILINNAGIGPGAfiEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDN--SRIINISSAATRISLPDF-------- 155
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 19923931  122 kyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK12747 156 -----IAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM 195
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
2-160 1.21e-06

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 48.49  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCP---HWTTEDgFEMQFGVNHLG 78
Cdd:PRK12384  37 EKAANVAQEINAEYGEGMAYGFGADATSEQSVLALSRGVDEIFGRVDLLVYNAGIAKAAfitDFQLGD-FDRSLQVNLVG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   79 HFL-LTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtRKYNTkaAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:PRK12384 116 YFLcAREFSRLMIRDGIQGRIIQINSKSGKVG-----------SKHNS--GYSAAKFGGVGLTQSLALDLAEYGITVHSL 182

                 ...
gi 19923931  158 HPG 160
Cdd:PRK12384 183 MLG 185
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
2-165 1.31e-06

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: 48.02  E-value: 1.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNHHVNARH--LDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHL 77
Cdd:cd08939  36 SKLEEAVEEIEAEANASGQKVSYisADLSDYEEVEQAFAQAVEKGGPPDLVVNCAGISIPGLFEdlTAEEFERGMDVNYF 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  78 GHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:cd08939 116 GSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGY-------------SAYCPSKFALRGLAESLRQELKPYNIRVSVV 182

                ....*...
gi 19923931 158 HPGVARTE 165
Cdd:cd08939 183 YPPDTDTP 190
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
33-164 1.46e-06

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 48.04  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   33 IREFAAKIIEEEERVDILINNAGVM---RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAH-VA 108
Cdd:PRK06550  54 LSDDLEPLFDWVPSVDILCNTAGILddyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASfVA 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931  109 GhidfddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 164
Cdd:PRK06550 134 G--------------GGGAAYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKT 175
PRK06484 PRK06484
short chain dehydrogenase; Validated
8-164 1.89e-06

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 48.31  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    8 AKDIRGETLNHHVnARHLDLASLKSIREFAAKIIEEEERVDILINNAG---VMRCPHWTTEDGFEMQFGVNHLGHFLLTN 84
Cdd:PRK06484 306 AKKLAEALGDEHL-SVQADITDEAAVESAFAQIQARWGRLDVLVNNAGiaeVFKPSLEQSAEDFTRVYDVNLSGAFACAR 384
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   85 LLLDKLkaSAPSRIINLSSlahVAGHIDFDDLNwqtrkyntkaAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 164
Cdd:PRK06484 385 AAARLM--SQGGVIVNLGS---IASLLALPPRN----------AYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK09242 PRK09242
SDR family oxidoreductase;
5-166 1.96e-06

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 47.82  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAG--VMRCPHWTTEDGFEMQFGVNHLGHFLL 82
Cdd:PRK09242  47 AQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDHWDGLHILVNNAGgnIRKAAIDYTEDEWRGIFETNLFSAFEL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   83 TNLLLDKLKASAPSRIINLSSlahVAGHIDFddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVA 162
Cdd:PRK09242 127 SRYAHPLLKQHASSAIVNIGS---VSGLTHV----------RSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYI 193

                 ....
gi 19923931  163 RTEL 166
Cdd:PRK09242 194 RTPL 197
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
5-164 2.80e-06

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 47.06  E-value: 2.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   5 EAAAKDIRGETLNHHVNARHLDL----ASLKSIREFAAKiieEEERVDILINNAGVMRCpHWTTEDGFE---MQFGVNHL 77
Cdd:cd08931  34 EDGLAALAAELGAENVVAGALDVtdraAWAAALADFAAA---TGGRLDALFNNAGVGRG-GPFEDVPLAahdRMVDINVK 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  78 GHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:cd08931 110 GVLNGAYAALPYLKATPGARVINTASSSAIYGQPDL-------------AVYSATKFAVRGLTEALDVEWARHGIRVADV 176

                ....*..
gi 19923931 158 HPGVART 164
Cdd:cd08931 177 WPWFVDT 183
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
25-167 3.39e-06

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 47.00  E-value: 3.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  25 LDLASLKSIREFAAKIIEEEERVDILINNAGVMrcphWTT--EDG----FEMQFGVNHLGHFLLTNLLLDKLKASAPSRI 98
Cdd:cd05338  71 VDVRDEDQVRALVEATVDQFGRLDILVNNAGAI----WLSlvEDTpakrFDLMQRVNLRGTYLLSQAALPHMVKAGQGHI 146
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923931  99 INLSS---LAHVAGHidfddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELG 167
Cdd:cd05338 147 LNISPplsLRPARGD----------------VAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPA 202
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
24-169 3.50e-06

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: 46.90  E-value: 3.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  24 HLDLASLKSIREFAAKIIEEEERVDILINNAGVM----------RCPHwTTEDgFEMQFGVNHLGHFLLTNLLLDKLKAS 93
Cdd:cd05371  53 PVDVTSEKDVKAALALAKAKFGRLDIVVNCAGIAvaaktynkkgQQPH-SLEL-FQRVINVNLIGTFNVIRLAAGAMGKN 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  94 APSR------IINLSSLAHVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELG 167
Cdd:cd05371 131 EPDQggergvIINTASVAAFEGQIG-------------QAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLL 197

                ..
gi 19923931 168 RH 169
Cdd:cd05371 198 AG 199
PRK06128 PRK06128
SDR family oxidoreductase;
26-166 3.90e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 47.16  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAG----VMRCPHWTTEDgFEMQFGVNHLGHFLLTNLLLDKLKASApsRIINL 101
Cdd:PRK06128 114 DLKDEAFCRQLVERAVKELGGLDILVNIAGkqtaVKDIADITTEQ-FDATFKTNVYAMFWLCKAAIPHLPPGA--SIINT 190
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923931  102 SSLahvaghidfddlnwqtRKYNTKAA---YCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK06128 191 GSI----------------QSYQPSPTlldYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
PRK07577 PRK07577
SDR family oxidoreductase;
26-175 4.45e-06

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 46.64  E-value: 4.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEeRVDILINNAGVMR--------CPHWTTEDGFEMQFGVNHLGHFLLTNllldklKASAPSR 97
Cdd:PRK07577  49 DLADIEQTAATLAQINEIH-PVDAIVNNVGIALpqplgkidLAALQDVYDLNVRAAVQVTQAFLEGM------KLREQGR 121
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923931   98 IINLSSLAhVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGS 175
Cdd:PRK07577 122 IVNICSRA-IFGALD-------------RTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRQTRPVGS 185
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
48-164 5.80e-06

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 46.26  E-value: 5.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   48 DILINNAGVM-RCPHWT-TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPS-RIINLSSLAHVAGHIDFddlnwqtrkyn 124
Cdd:PRK08643  81 NVVVNNAGVApTTPIETiTEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGgKIINATSQAGVVGNPEL----------- 149
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19923931  125 tkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 164
Cdd:PRK08643 150 --AVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKT 187
PRK06500 PRK06500
SDR family oxidoreductase;
26-166 6.35e-06

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 46.10  E-value: 6.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAGV---MRCPHWTtEDGFEMQFGVNHLGHFLLTNLLLDKLKASApSRIINLS 102
Cdd:PRK06500  60 DAGDVAAQKALAQALAEAFGRLDAVFINAGVakfAPLEDWD-EAMFDRSFNTNVKGPYFLIQALLPLLANPA-SIVLNGS 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923931  103 SLAHVAghidfddlnwqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK06500 138 INAHIG--------------MPNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPL 187
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
26-166 6.62e-06

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 46.11  E-value: 6.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW----TTEDGFEMQFGVNHLGHF-----LLTNLLLDKLKASAPS 96
Cdd:PRK12745  60 DVADLSAHEAMLDAAQAAWGRIDCLVNNAGVGVKVRGdlldLTPESFDRVLAINLRGPFfltqaVAKRMLAQPEPEELPH 139
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19923931   97 R-IINLSSLAHVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK12745 140 RsIVFVSSVNAIMVSPN-------------RGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
2-165 7.30e-06

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 46.02  E-value: 7.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNHHvnARHLDLASLKSIREFAAKIIEEEERVDILINNAG---VMRCPHWTTEDGFEMQFGVNHLG 78
Cdd:cd05365  34 EGAEAVAAAIQQAGGQAI--GLECNVTSEQDLEAVVKATVSQFGGITILVNNAGgggPKPFDMPMTEEDFEWAFKLNLFS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  79 HFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALH 158
Cdd:cd05365 112 AFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRI-------------AAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVA 178

                ....*..
gi 19923931 159 PGVARTE 165
Cdd:cd05365 179 PGAVKTD 185
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
24-168 8.64e-06

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: 46.12  E-value: 8.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  24 HLDLASLKSIREfAAKIIEE---EERVDILINNAGVMRCP---HWTTEDGFEMQFGVNHLGhflltnlLLDKLKA----- 92
Cdd:cd09805  54 QLDVTKPEQIKR-AAQWVKEhvgEKGLWGLVNNAGILGFGgdeELLPMDDYRKCMEVNLFG-------TVEVTKAflpll 125
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19923931  93 -SAPSRIINLSSlahVAGHIDFddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 168
Cdd:cd09805 126 rRAKGRVVNVSS---MGGRVPF----------PAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITG 189
PRK07454 PRK07454
SDR family oxidoreductase;
20-166 9.03e-06

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 45.72  E-value: 9.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   20 VNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRcphwtTEDGFEMQFG-------VNHLGHFLLTNLLLDKLKA 92
Cdd:PRK07454  57 AAAYSIDLSNPEAIAPGIAELLEQFGCPDVLINNAGMAY-----TGPLLEMPLSdwqwviqLNLTSVFQCCSAVLPGMRA 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923931   93 SAPSRIINLSSlahVAGHIDFDDlnWqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK07454 132 RGGGLIINVSS---IAARNAFPQ--W--------GAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL 192
PRK07326 PRK07326
SDR family oxidoreductase;
5-170 1.03e-05

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 45.39  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDirgetLNHHVNARHL--DLASLKSIREFAAKIIEEEERVDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHF 80
Cdd:PRK07326  44 EEAAAE-----LNNKGNVLGLaaDVRDEADVQRAVDAIVAAFGGLDVLIANAGVghFAPVEELTPEEWRLVIDTNLTGAF 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   81 LLTNLLLDKLKASApSRIINLSSLAhvaghidfddlnwQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 160
Cdd:PRK07326 119 YTIKAAVPALKRGG-GYIINISSLA-------------GTNFFAGGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPG 184
                        170
                 ....*....|
gi 19923931  161 VARTELGRHT 170
Cdd:PRK07326 185 SVATHFNGHT 194
PRK06180 PRK06180
short chain dehydrogenase; Provisional
5-165 1.20e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 45.29  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIrgETLN-HHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVmrcPHW-----TTEDGFEMQFGVNHLG 78
Cdd:PRK06180  38 EAARADF--EALHpDRALARLLDVTDFDAIDAVVADAEATFGPIDVLVNNAGY---GHEgaieeSPLAEMRRQFEVNVFG 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   79 hflltnlLLDKLKASAPS-------RIINLSSlahVAGHIDFDDLnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSG 151
Cdd:PRK06180 113 -------AVAMTKAVLPGmrarrrgHIVNITS---MGGLITMPGI----------GYYCGSKFALEGISESLAKEVAPFG 172
                        170
                 ....*....|....
gi 19923931  152 VTVNALHPGVARTE 165
Cdd:PRK06180 173 IHVTAVEPGSFRTD 186
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
26-198 1.99e-05

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: 44.42  E-value: 1.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  26 DLASLKSIREFAAKIIEEEERVDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS 103
Cdd:cd08929  54 DVRDEADVRRAVDAMEEAFGGLDALVNNAGVgvMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGS 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931 104 LAHVaghidfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTgihgstfssttlG 183
Cdd:cd08929 134 LAGK-------------NAFKGGAAYNASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGSP------------E 188
                       170
                ....*....|....*
gi 19923931 184 PIFWLLvkSPELAAQ 198
Cdd:cd08929 189 GQAWKL--APEDVAQ 201
PRK06181 PRK06181
SDR family oxidoreductase;
26-166 2.29e-05

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 44.58  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAGV-MRCPHWTTEDG--FEMQFGVNHLGHFLLTNLLLDKLKASApSRIINLS 102
Cdd:PRK06181  58 DVSDAEACERLIEAAVARFGGIDILVNNAGItMWSRFDELTDLsvFERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVS 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923931  103 SLAHVAGhidfddlnwqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK06181 137 SLAGLTG-------------VPTRSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATDI 187
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
5-166 2.43e-05

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 44.50  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIR---GETLNHHVNARHLDlaslkSIREFAAKIIEEEERVDILINNAG---VMRCPHWTTEDGFEMQfGVNHLG 78
Cdd:PRK13394  45 NAVADEINkagGKAIGVAMDVTNED-----AVNAGIDKVAERFGSVDILVSNAGiqiVNPIENYSFADWKKMQ-AIHVDG 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   79 HFLLTNLL-LDKLKASAPSRIINLSSL-AHVAGHIdfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNA 156
Cdd:PRK13394 119 AFLTTKAAlKHMYKDDRGGVVIYMGSVhSHEASPL--------------KSAYVTAKHGLLGLARVLAKEGAKHNVRSHV 184
                        170
                 ....*....|
gi 19923931  157 LHPGVARTEL 166
Cdd:PRK13394 185 VCPGFVRTPL 194
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
18-165 2.77e-05

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 44.13  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   18 HHVNArhlDLASLKSIREFAAKIIEEEERVDILINNAGVMRcphwtTEDGFEMQ-------FGVNHLG-HFLLTNLLLDK 89
Cdd:PRK12481  58 HFITA---DLIQQKDIDSIVSQAVEVMGHIDILINNAGIIR-----RQDLLEFGnkdwddvININQKTvFFLSQAVAKQF 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931   90 LKASAPSRIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTE 165
Cdd:PRK12481 130 VKQGNGGKIINIASMLSFQGGIRV-------------PSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
10-161 2.90e-05

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 44.23  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   10 DIR-GETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVM-----------RCPHWTTEDGFEMQFGVNHL 77
Cdd:PRK06171  40 DIHgGDGQHENYQFVPTDVSSAEEVNHTVAEIIEKFGRIDGLVNNAGINiprllvdekdpAGKYELNEAAFDKMFNINQK 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   78 GHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:PRK06171 120 GVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEG-------------QSCYAATKAALNSFTRSWAKELGKHNIRVVGV 186

                 ....
gi 19923931  158 HPGV 161
Cdd:PRK06171 187 APGI 190
PRK05650 PRK05650
SDR family oxidoreductase;
24-226 2.94e-05

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 44.26  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   24 HLDLASLKSIREFAAKIIEEEERVDILINNAGVmrcphwTTEDGFE--------MQFGVNHLGHFLLTNLLLDKLKASAP 95
Cdd:PRK05650  55 RCDVRDYSQLTALAQACEEKWGGIDVIVNNAGV------ASGGFFEelsledwdWQIAINLMGVVKGCKAFLPLFKRQKS 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   96 SRIINLSSLAHVAgHIDFDDlnwqtrKYNTkaaycqSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELgrhtgihGS 175
Cdd:PRK05650 129 GRIVNIASMAGLM-QGPAMS------SYNV------AKAGVVALSETLLVELADDEIGVHVVCPSFFQTNL-------LD 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  176 TFSSTTLG---PIFWLLVKSPELAAQPSTYL--AVAEE----LADVSGKYFDGLKQKAPA 226
Cdd:PRK05650 189 SFRGPNPAmkaQVGKLLEKSPITAADIADYIyqQVAKGefliLPHEQGRRAWQLKRQAPQ 248
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
24-166 3.66e-05

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 44.02  E-value: 3.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  24 HLDLASLKSIREFAAKIIEEEERV-DILINNAGVmrcPHWTtedGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLS 102
Cdd:cd05328  37 IADLSTPEGRAAAIADVLARCSGVlDGLVNCAGV---GGTT---VAGLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVS 110
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923931 103 SLAHVAGHIDFDDLN--------------WQTRKYNTKAAYCQSKLAIVLFTKELSRR-LQGSGVTVNALHPGVARTEL 166
Cdd:cd05328 111 SIAGAGWAQDKLELAkalaagtearavalAEHAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPI 189
PRK05855 PRK05855
SDR family oxidoreductase;
19-174 4.28e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 44.20  E-value: 4.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   19 HVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGV-MRCPHW-TTEDGFEMQFGVNHLG--H----FLLTNLlldkl 90
Cdd:PRK05855 365 VAHAYRVDVSDADAMEAFAEWVRAEHGVPDIVVNNAGIgMAGGFLdTSAEDWDRVLDVNLWGviHgcrlFGRQMV----- 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   91 KASAPSRIINLSSLAHVAghidfddlnwQTRKYNtkaAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHT 170
Cdd:PRK05855 440 ERGTGGHIVNVASAAAYA----------PSRSLP---AYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVATT 506

                 ....
gi 19923931  171 GIHG 174
Cdd:PRK05855 507 RFAG 510
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
2-168 4.80e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 43.59  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGETLNHHVNArhLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTT--EDGFEMQFGVNHLGH 79
Cdd:PRK08085  44 ERAELAVAKLRQEGIKAHAAP--FNVTHKQEVEAAIEHIEKDIGPIDVLINNAGIQRRHPFTEfpEQEWNDVIAVNQTAV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   80 FLLTNLLLDKLKASAPSRIINLSSLAHVAGHidfddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:PRK08085 122 FLVSQAVARYMVKRQAGKIINICSMQSELGR-------------DTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAP 188

                 ....*....
gi 19923931  160 GVARTELGR 168
Cdd:PRK08085 189 GYFKTEMTK 197
PRK06182 PRK06182
short chain dehydrogenase; Validated
25-168 4.84e-05

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 43.80  E-value: 4.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   25 LDLASLKSIREFAAKIIEEEERVDILINNAG------VMRCPhwtTEDGfEMQFGVNHLGHFLLTNLLLDKLKASAPSRI 98
Cdd:PRK06182  53 LDVTDEASIKAAVDTIIAEEGRIDVLVNNAGygsygaIEDVP---IDEA-RRQFEVNLFGAARLTQLVLPHMRAQRSGRI 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   99 INLSSlahVAGHIdFDDLNwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 168
Cdd:PRK06182 129 INISS---MGGKI-YTPLG---------AWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGD 185
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
26-166 5.24e-05

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 43.46  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAGVMR--CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS 103
Cdd:PRK12938  61 NVGDWDSTKAAFDKVKAEVGEIDVLVNNAGITRdvVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISS 140
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19923931  104 LAHVAGHidFDDLNWQTrkyntkaaycqSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK12938 141 VNGQKGQ--FGQTNYST-----------AKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDM 190
PRK06123 PRK06123
SDR family oxidoreductase;
33-175 6.82e-05

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 43.23  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   33 IREFAAkIIEEEERVDILINNAGV----MRCPHWtteDGFEMQ--FGVNHLGHFLLTNLLLDKLKASAPSR---IINLSS 103
Cdd:PRK06123  68 LRLFEA-VDRELGRLDALVNNAGIleaqMRLEQM---DAARLTriFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSS 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931  104 LAHVAG----HIDfddlnwqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTElgrhtgIHGS 175
Cdd:PRK06123 144 MAARLGspgeYID----------------YAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTE------IHAS 197
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
26-172 8.28e-05

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 42.75  E-value: 8.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS 103
Cdd:PRK07666  64 DVSDYEEVTAAIEQLKNELGSIDILINNAGISKFGKFLelDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISS 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923931  104 LAHVAGhidfddlnwqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGI 172
Cdd:PRK07666 144 TAGQKG-------------AAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGL 199
PRK12746 PRK12746
SDR family oxidoreductase;
26-166 9.47e-05

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 42.71  E-value: 9.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEE------RVDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASApsR 97
Cdd:PRK12746  64 DLNSIDGVKKLVEQLKNELQirvgtsEIDILVNNAGIgtQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEG--R 141
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923931   98 IINLSSLAHVAGhidfddlnwqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK12746 142 VINISSAEVRLG-------------FTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
PRK08017 PRK08017
SDR family oxidoreductase;
25-164 1.06e-04

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 42.38  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   25 LDLASLKSIREFAAKIIE-EEERVDILINNAGV-MRCPHWT-TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINL 101
Cdd:PRK08017  52 LDLDDPESVERAADEVIAlTDNRLYGLFNNAGFgVYGPLSTiSRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMT 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19923931  102 SSlahVAGHIdfddlnwQTRKyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 164
Cdd:PRK08017 132 SS---VMGLI-------STPG---RGAYAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRT 181
PRK06124 PRK06124
SDR family oxidoreductase;
2-165 1.08e-04

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 42.39  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGETLNhhVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVM-RCP--HWTTEDGFEMqFGVNHLG 78
Cdd:PRK06124  46 ATLEAAVAALRAAGGA--AEALAFDIADEEAVAAAFARIDAEHGRLDILVNNVGARdRRPlaELDDAAIRAL-LETDLVA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   79 HFLLTNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwqTRKYNtkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALH 158
Cdd:PRK06124 123 PILLSRLAAQRMKRQGYGRIIAITS---IAGQV--------ARAGD--AVYPAAKQGLTGLMRALAAEFGPHGITSNAIA 189

                 ....*..
gi 19923931  159 PGVARTE 165
Cdd:PRK06124 190 PGYFATE 196
PRK07832 PRK07832
SDR family oxidoreductase;
5-174 1.27e-04

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 42.34  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIR--GETLNHHvnaRHLDLASLKSIREFAAKIIEEEERVDILINNAGVmrcPHWTTEDGFEMQ-----FGVNHL 77
Cdd:PRK07832  38 AQTVADARalGGTVPEH---RALDISDYDAVAAFAADIHAAHGSMDVVMNIAGI---SAWGTVDRLTHEqwrrmVDVNLM 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   78 G--HfLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddLNWQtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVN 155
Cdd:PRK07832 112 GpiH-VIETFVPPMVAAGRGGHLVNVSSAAGLVA------LPWH-------AAYSASKFGLRGLSEVLRFDLARHGIGVS 177
                        170
                 ....*....|....*....
gi 19923931  156 ALHPGVARTELGRHTGIHG 174
Cdd:PRK07832 178 VVVPGAVKTPLVNTVEIAG 196
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
2-165 1.58e-04

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: 42.06  E-value: 1.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGETLNhhvnARHLDLASLKSIREFAAKIieEEERVDILINNAGV--MRCPHWTTEDGFEMQFGVNHLGH 79
Cdd:cd09806  41 GRLWEAAGALAGGTLE----TLQLDVCDSKSVAAAVERV--TERHVDVLVCNAGVglLGPLEALSEDAMASVFDVNVFGT 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  80 FLLTNLLLDKLKASAPSRIINLSSLAHVAGhIDFDDLnwqtrkyntkaaYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:cd09806 115 VRMLQAFLPDMKRRGSGRILVTSSVGGLQG-LPFNDV------------YCASKFALEGLCESLAVQLLPFNVHLSLIEC 181

                ....*.
gi 19923931 160 GVARTE 165
Cdd:cd09806 182 GPVHTA 187
PRK06198 PRK06198
short chain dehydrogenase; Provisional
2-165 1.73e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 41.91  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIR-GETLNHHVNArhlDLASLKSIREFAAKIIEEEERVDILINNAGVM-RCPHW-TTEDGFEMQFGVNHLG 78
Cdd:PRK06198  42 EKGEAQAAELEaLGAKAVFVQA---DLSDVEDCRRVVAAADEAFGRLDALVNAAGLTdRGTILdTSPELFDRHFAVNVRA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   79 HFLLTNLLLDKLKA-SAPSRIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:PRK06198 119 PFFLMQEAIKLMRRrKAEGTIVNIGSMSAHGGQPFL-------------AAYCASKGALATLTRNAAYALLRNRIRVNGL 185

                 ....*...
gi 19923931  158 HPGVARTE 165
Cdd:PRK06198 186 NIGWMATE 193
PRK06172 PRK06172
SDR family oxidoreductase;
33-168 1.95e-04

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 41.66  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   33 IREFAAKIIEEEERVDILINNAGVMRCPHWT---TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAG 109
Cdd:PRK06172  71 VKALVEQTIAAYGRLDYAFNNAGIEIEQGRLaegSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGA 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19923931  110 HIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGR 168
Cdd:PRK06172 151 APKM-------------SIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFR 196
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
25-160 1.98e-04

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 41.70  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   25 LDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLS 102
Cdd:PRK12859  75 LDLTQNDAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSnlTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMT 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19923931  103 S---LAHVAGHIdfddlnwqtrkyntkaAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 160
Cdd:PRK12859 155 SgqfQGPMVGEL----------------AYAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
PRK07775 PRK07775
SDR family oxidoreductase;
1-167 2.20e-04

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 41.66  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    1 MEKCEAAAKDIR---GETLNHHvnarhLDLASLKSIREFAAKIIEEEERVDILINNAGVMR--CPHWTTEDGFEMQFGVN 75
Cdd:PRK07775  44 VEKCEELVDKIRadgGEAVAFP-----LDVTDPDSVKSFVAQAEEALGEIEVLVSGAGDTYfgKLHEISTEQFESQVQIH 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   76 HLGHFLLTNLLLDKLKASAPSRIINLSSlahvaghidfdDLNWQTRKYntKAAYCQSKLAIVLFTKELSRRLQGSGVTVN 155
Cdd:PRK07775 119 LVGANRLATAVLPGMIERRRGDLIFVGS-----------DVALRQRPH--MGAYGAAKAGLEAMVTNLQMELEGTGVRAS 185
                        170
                 ....*....|..
gi 19923931  156 ALHPGVARTELG 167
Cdd:PRK07775 186 IVHPGPTLTGMG 197
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
26-198 2.22e-04

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 41.63  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAGV-MRCPHWTTEDGF-EMQFGVNHLGHFLLTNLLLDKLKASApsRIINLSS 103
Cdd:PRK06077  64 DVSTREGCETLAKATIDRYGVADILVNNAGLgLFSPFLNVDDKLiDKHISTDFKSVIYCSQELAKEMREGG--AIVNIAS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  104 LAHVaghidfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSRRLqGSGVTVNALHPGVARTELG----RHTGIHGSTFSS 179
Cdd:PRK06077 142 VAGI-------------RPAYGLSIYGAMKAAVINLTKYLALEL-APKIRVNAIAPGFVKTKLGeslfKVLGMSEKEFAE 207
                        170       180       190
                 ....*....|....*....|....*....|
gi 19923931  180 --TTLGPIF---------WLLVKSPELAAQ 198
Cdd:PRK06077 208 kfTLMGKILdpeevaefvAAILKIESITGQ 237
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
26-169 2.39e-04

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 41.24  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNA--GVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS 103
Cdd:PRK08063  62 NVGDVEKIKEMFAQIDEEFGRLDVFVNNAasGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSS 141
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931  104 LahvaGHIdfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 169
Cdd:PRK08063 142 L----GSI---------RYLENYTTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKH 194
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
26-169 2.74e-04

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: 41.18  E-value: 2.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  26 DLASLKSIREFAAKIIEEEERVDILINNA--GVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSS 103
Cdd:cd05359  56 DVSQPQDVEEMFAAVKERFGRLDVLVSNAaaGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISS 135
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931 104 LAhvaghidfddlnwQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRH 169
Cdd:cd05359 136 LG-------------SIRALPNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAH 188
PRK07074 PRK07074
SDR family oxidoreductase;
5-165 2.75e-04

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 41.29  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCP--HWTTEDGFEMQFGVNHLGHFLL 82
Cdd:PRK07074  36 AAALAAFADALGDARFVPVACDLTDAASLAAALANAAAERGPVDVLVANAGAARAAslHDTTPASWRADNALNLEAAYLC 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   83 TNLLLDKLKASAPSRIINLSSL--AHVAGHidfddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPG 160
Cdd:PRK07074 116 VEAVLEGMLKRSRGAVVNIGSVngMAALGH----------------PAYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPG 179

                 ....*
gi 19923931  161 VARTE 165
Cdd:PRK07074 180 TVKTQ 184
PRK07109 PRK07109
short chain dehydrogenase; Provisional
5-169 3.08e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 41.45  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIRGetLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGV-MRCPHW-TTEDGFEMQFGVNHLGHFLL 82
Cdd:PRK07109  46 EALAAEIRA--AGGEALAVVADVADAEAVQAAADRAEEELGPIDTWVNNAMVtVFGPFEdVTPEEFRRVTEVTYLGVVHG 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   83 TNLLLDKLKASAPSRIINLSSLAHVAGhidfddLNWQtrkyntkAAYCQSKLAIVLFTKELSRRLQ--GSGVTVNALHPG 160
Cdd:PRK07109 124 TLAALRHMRPRDRGAIIQVGSALAYRS------IPLQ-------SAYCAAKHAIRGFTDSLRCELLhdGSPVSVTMVQPP 190
                        170
                 ....*....|....*..
gi 19923931  161 V--------ARTELGRH 169
Cdd:PRK07109 191 AvntpqfdwARSRLPVE 207
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
2-216 3.14e-04

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 41.09  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDirgetLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGV-------MRCPHWTTEDGFEMQFGV 74
Cdd:PRK06200  41 EKLASLRQR-----FGDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCFVGNAGIwdyntslVDIPAETLDTAFDEIFNV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   75 NHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLqGSGVTV 154
Cdd:PRK06200 116 NVKGYLLGAKAALPALKASGGSMIFTLSNSSFYPG--------------GGGPLYTASKHAVVGLVRQLAYEL-APKIRV 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923931  155 NALHPGVARTELGrhtGIHGSTFSSTTLGPIfwllvksPELAA--QPSTYLAVAEELADVSGKY 216
Cdd:PRK06200 181 NGVAPGGTVTDLR---GPASLGQGETSISDS-------PGLADmiAAITPLQFAPQPEDHTGPY 234
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
19-160 3.38e-04

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: 41.18  E-value: 3.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  19 HVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGV-------MRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLK 91
Cdd:cd05348  51 AVVGVEGDVRSLADNERAVARCVERFGKLDCFIGNAGIwdystslVDIPEEKLDEAFDELFHINVKGYILGAKAALPALY 130
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923931  92 ASAPSRIINLSSLAHVAGhidfddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLqGSGVTVNALHPG 160
Cdd:cd05348 131 ATEGSVIFTVSNAGFYPG--------------GGGPLYTASKHAVVGLVKQLAYEL-APHIRVNGVAPG 184
PRK07069 PRK07069
short chain dehydrogenase; Validated
34-164 3.49e-04

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 40.85  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   34 REFAAKIIEEEERVDILINNAGVMR--CPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSlahVAGHI 111
Cdd:PRK07069  67 QALLAQAADAMGGLSVLVNNAGVGSfgAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISS---VAAFK 143
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19923931  112 DFDDLnwqtrkyntkAAYCQSKLAIVLFTKELSRRL--QGSGVTVNALHPGVART 164
Cdd:PRK07069 144 AEPDY----------TAYNASKAAVASLTKSIALDCarRGLDVRCNSIHPTFIRT 188
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
32-164 3.65e-04

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 40.92  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   32 SIREFAAKIIEEEE---RVDILINNAGVM--RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPS-------RII 99
Cdd:PRK07792  72 SQRATADELVATAVglgGLDIVVNNAGITrdRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAKAaggpvygRIV 151
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923931  100 NLSSLAHVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGvART 164
Cdd:PRK07792 152 NTSSEAGLVGPVG-------------QANYGAAKAGITALTLSAARALGRYGVRANAICPR-ART 202
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
9-166 5.99e-04

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


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 40.01  E-value: 5.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   9 KDIRGETL--NHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGV---MRCPHWTTEDGFEMqFGVNHLGHFLLT 83
Cdd:cd05350  36 DELKAELLnpNPSVEVEILDVTDEERNQLVIAELEAELGGLDLVIINAGVgkgTSLGDLSFKAFRET-IDTNLLGAAAIL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  84 NLLLDKLKASAPSRIINLSSLAHVAGhidfddlnwqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVAR 163
Cdd:cd05350 115 EAALPQFRAKGRGHLVLISSVAALRG-------------LPGAAAYSASKAALSSLAESLRYDVKKRGIRVTVINPGFID 181

                ...
gi 19923931 164 TEL 166
Cdd:cd05350 182 TPL 184
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
1-160 7.06e-04

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 40.05  E-value: 7.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    1 MEKCEAAAKdirgetlNHHVNARHL--DLASLKSIREFAAKIIEEEERVDILINNAGVM-RCP--HWTTEDgFEMQFGVN 75
Cdd:PRK07097  47 VDKGLAAYR-------ELGIEAHGYvcDVTDEDGVQAMVSQIEKEVGVIDILVNNAGIIkRIPmlEMSAED-FRQVIDID 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   76 HLGHFlltnlllDKLKASAPS-------RIINLSSLAHVAGHidfddlnwqtrkyNTKAAYCQSKLAIVLFTKELSRRLQ 148
Cdd:PRK07097 119 LNAPF-------IVSKAVIPSmikkghgKIINICSMMSELGR-------------ETVSAYAAAKGGLKMLTKNIASEYG 178
                        170
                 ....*....|..
gi 19923931  149 GSGVTVNALHPG 160
Cdd:PRK07097 179 EANIQCNGIGPG 190
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-160 7.50e-04

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 40.06  E-value: 7.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   11 IRGETLNHHVNARHL--DLASLKSIREFAAKIIEEEERVDILINNAGV------------MRCPHWTTE--------DGF 68
Cdd:PRK12748  58 LKEEIESYGVRCEHMeiDLSQPYAPNRVFYAVSERLGDPSILINNAAYsthtrleeltaeQLDKHYAVNvratmllsSAF 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   69 EMQFGVNHLGhflltnllldklkasapsRIINLSSLAHVAGHIDfddlnwqtrkyntKAAYCQSKLAIVLFTKELSRRLQ 148
Cdd:PRK12748 138 AKQYDGKAGG------------------RIINLTSGQSLGPMPD-------------ELAYAATKGAIEAFTKSLAPELA 186
                        170
                 ....*....|..
gi 19923931  149 GSGVTVNALHPG 160
Cdd:PRK12748 187 EKGITVNAVNPG 198
PRK07814 PRK07814
SDR family oxidoreductase;
2-165 7.63e-04

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 40.15  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGETLNHHVNArhLDLASLKSIREFAAKIIEEEERVDILINN-AGVMRCPHWTT-----EDGFEMQFGVN 75
Cdd:PRK07814  45 SQLDEVAEQIRAAGRRAHVVA--ADLAHPEATAGLAGQAVEAFGRLDIVVNNvGGTMPNPLLSTstkdlADAFTFNVATA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   76 HlghflltnlllDKLKASAPS--------RIINLSS-LAHVAGhidfddlnwqtRKYntkAAYCQSKLAIVLFTKELSRR 146
Cdd:PRK07814 123 H-----------ALTVAAVPLmlehsgggSVINISStMGRLAG-----------RGF---AAYGTAKAALAHYTRLAALD 177
                        170
                 ....*....|....*....
gi 19923931  147 LqGSGVTVNALHPGVARTE 165
Cdd:PRK07814 178 L-CPRIRVNAIAPGSILTS 195
PRK06179 PRK06179
short chain dehydrogenase; Provisional
6-166 1.07e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 39.50  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    6 AAAKDIRGETLnhhvnaRHLDLASLKSIREFAAKIIEEEERVDILINNAGVM---RCPHWTTEDGFEMqFGVNHLGHFLL 82
Cdd:PRK06179  39 ARAAPIPGVEL------LELDVTDDASVQAAVDEVIARAGRIDVLVNNAGVGlagAAEESSIAQAQAL-FDTNVFGILRM 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   83 TNLLLDKLKASAPSRIINLSSlahVAGHIdfddlnwqTRKYNtkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVA 162
Cdd:PRK06179 112 TRAVLPHMRAQGSGRIINISS---VLGFL--------PAPYM--ALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYT 178

                 ....
gi 19923931  163 RTEL 166
Cdd:PRK06179 179 KTNF 182
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
26-164 1.24e-03

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 39.47  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   26 DLASLKSIREFAAKIIEEEERVDILINNAGVMRcphwtTEDGFE---------MQFGVNHLgHFLLTNLLLDKLKASAPS 96
Cdd:PRK08993  65 DLRKIDGIPALLERAVAEFGHIDILVNNAGLIR-----REDAIEfsekdwddvMNLNIKSV-FFMSQAAAKHFIAQGNGG 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19923931   97 RIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVART 164
Cdd:PRK08993 139 KIINIASMLSFQGGIRV-------------PSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMAT 193
PLN02253 PLN02253
xanthoxin dehydrogenase
47-166 1.26e-03

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 39.42  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   47 VDILINNAGVM--RCPHWTTED--GFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfddlnwqtrk 122
Cdd:PLN02253  95 LDIMVNNAGLTgpPCPDIRNVElsEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLG---------- 164
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 19923931  123 yntKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PLN02253 165 ---PHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTAL 205
PRK09072 PRK09072
SDR family oxidoreductase;
20-166 1.41e-03

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 39.15  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   20 VNARHLDLASLKSIREFAAKIiEEEERVDILINNAGVMRCPHWT--TEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSR 97
Cdd:PRK09072  55 HRWVVADLTSEAGREAVLARA-REMGGINVLINNAGVNHFALLEdqDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAM 133
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923931   98 IINLSSlahVAGHIDfddlnwqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK09072 134 VVNVGS---TFGSIG----------YPGYASYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAM 189
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
1-159 1.43e-03

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 39.83  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    1 MEKCEAAAKDIRGETlnhHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVM--RCPHWTTEDGFEMQFGVNHLG 78
Cdd:PRK08324 456 EEAAEAAAAELGGPD---RALGVACDVTDEAAVQAAFEEAALAFGGVDIVVSNAGIAisGPIEETSDEDWRRSFDVNATG 532
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   79 HFLLTNLLLDKLKASA-PSRIINLSSLAHVAGHIDFddlnwqtrkyntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:PRK08324 533 HFLVAREAVRIMKAQGlGGSIVFIASKNAVNPGPNF-------------GAYGAAKAAELHLVRQLALELGPDGIRVNGV 599

                 ..
gi 19923931  158 HP 159
Cdd:PRK08324 600 NP 601
PRK06947 PRK06947
SDR family oxidoreductase;
46-175 1.68e-03

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 39.02  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   46 RVDILINNAGVMrCPHWTTED----GFEMQFGVNHLGHF---LLTNLLLDKLKASAPSRIINLSSLAHVAGhidfddlnw 118
Cdd:PRK06947  80 RLDALVNNAGIV-APSMPLADmdaaRLRRMFDTNVLGAYlcaREAARRLSTDRGGRGGAIVNVSSIASRLG--------- 149
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19923931  119 qtrKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTElgrhtgIHGS 175
Cdd:PRK06947 150 ---SPNEYVDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETE------IHAS 197
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
5-218 1.74e-03

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: 38.81  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   5 EAAAKDIRGETLNHHVnarhLDLASLKSIREFAAKIIEEEERVDILINNAGVMRcPH----WTTEDGFEMQFGVN----- 75
Cdd:cd05367  40 ELKEELRPGLRVTTVK----ADLSDAAGVEQLLEAIRKLDGERDLLINNAGSLG-PVskieFIDLDELQKYFDLNltspv 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  76 -----HLGHFlltnllldkLKASAPSRIINLSSLAHVaghidfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSrrLQGS 150
Cdd:cd05367 115 cltstLLRAF---------KKRGLKKTVVNVSSGAAV-------------NPFKGWGLYCSSKAARDMFFRVLA--AEEP 170
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923931 151 GVTVNALHPGVARTELGR------HTGIHGSTFSSttLGPIFWLLvkSPELAAQpsTYLAVAEELADVSGKYFD 218
Cdd:cd05367 171 DVRVLSYAPGVVDTDMQReiretsADPETRSRFRS--LKEKGELL--DPEQSAE--KLANLLEKDKFESGAHVD 238
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
2-160 1.75e-03

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 38.99  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   2 EKCEAAAKDIRGEtlnHHVNARHL--DLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTT---EDgFEMQFGVNH 76
Cdd:cd05322  37 ENAEKVADEINAE---YGEKAYGFgaDATNEQSVIALSKGVDEIFKRVDLLVYSAGIAKSAKITDfelGD-FDRSLQVNL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  77 LGHFLLTNLLLDKL-KASAPSRIINLSSLAHVAGhidfddlnwqtRKYNTkaAYCQSKLAIVLFTKELSRRLQGSGVTVN 155
Cdd:cd05322 113 VGYFLCAREFSKLMiRDGIQGRIIQINSKSGKVG-----------SKHNS--GYSAAKFGGVGLTQSLALDLAEHGITVN 179

                ....*
gi 19923931 156 ALHPG 160
Cdd:cd05322 180 SLMLG 184
PRK07063 PRK07063
SDR family oxidoreductase;
2-75 1.91e-03

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 38.88  E-value: 1.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931    2 EKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAG--VMRCPHWTTEDGFEMQFGVN 75
Cdd:PRK07063  42 ALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEAFGPLDVLVNNAGinVFADPLAMTDEDWRRCFAVD 117
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
1-184 2.22e-03

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: 38.34  E-value: 2.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   1 MEKCEAAAKDIRGETLN----HHVNARHLDlaslkSIREFAAKIIEEEERVDILINNA-GVMRCPhwtTED----GFEMQ 71
Cdd:cd05369  37 PEVLEAAAEEISSATGGrahpIQCDVRDPE-----AVEAAVDETLKEFGKIDILINNAaGNFLAP---AESlspnGFKTV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  72 FGVNHLGHF-LLTNLLLDKLKASAPSRIINLSSlahvaghidfdDLNWQTRKYNTKAAycQSKLAIVLFTKELSRRLQGS 150
Cdd:cd05369 109 IDIDLNGTFnTTKAVGKRLIEAKHGGSILNISA-----------TYAYTGSPFQVHSA--AAKAGVDALTRSLAVEWGPY 175
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19923931 151 GVTVNALHPG-VARTE-LGRHTGIHGSTFSSTTLGP 184
Cdd:cd05369 176 GIRVNAIAPGpIPTTEgMERLAPSGKSEKKMIERVP 211
PRK05867 PRK05867
SDR family oxidoreductase;
129-166 2.61e-03

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 38.48  E-value: 2.61e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 19923931  129 YCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTEL 166
Cdd:PRK05867 161 YCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
KR_fFAS_like_SDR_c_like cd08928
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c) ...
95-167 3.17e-03

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c)-like SDRs; KR domain of FAS, including the fungal-type multidomain FAS alpha chain, and the single domain daunorubicin C-13 ketoreductase. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD(P)-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Single domain 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: 187633 [Multi-domain]  Cd Length: 248  Bit Score: 38.04  E-value: 3.17e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931  95 PSRIINLSSLAHVAGHIDFDDLNWQTRKYNT---KAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELG 167
Cdd:cd08928 123 PKGLVKIQKQLRGQETRPAQVILPFSPNHGTfgdDGAYSESKLHLETLFNRWASESWGNDLTVCGAHIGWTRGTLG 198
PRK05993 PRK05993
SDR family oxidoreductase;
24-173 3.31e-03

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 38.08  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   24 HLDLASLKSIREFAAKIIEEEE-RVDILINN-----AGVMrcphwttED----GFEMQFGVNHLGHFLLTNLLLDKLKAS 93
Cdd:PRK05993  53 QLDYAEPESIAALVAQVLELSGgRLDALFNNgaygqPGAV-------EDlpteALRAQFEANFFGWHDLTRRVIPVMRKQ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   94 APSRIINLSS-LAHVAghidfddlnwqtrkYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELgRHTGI 172
Cdd:PRK05993 126 GQGRIVQCSSiLGLVP--------------MKYRGAYNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRF-RANAL 190

                 .
gi 19923931  173 H 173
Cdd:PRK05993 191 A 191
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-166 4.24e-03

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 37.89  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    5 EAAAKDIRGETLnhhvnarHLDLASLKSIREFAAKIIEEEERVDILINNAGV--------MrcphwtTEDGFEMQFGVNH 76
Cdd:PRK08261 250 AAVANRVGGTAL-------ALDITAPDAPARIAEHLAERHGGLDIVVHNAGItrdktlanM------DEARWDSVLAVNL 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   77 LGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDfddlnwQTrkyNtkaaYCQSKLAIVLFTKELSRRLQGSGVTVNA 156
Cdd:PRK08261 317 LAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRG------QT---N----YAASKAGVIGLVQALAPLLAERGITINA 383
                        170
                 ....*....|
gi 19923931  157 LHPGVARTEL 166
Cdd:PRK08261 384 VAPGFIETQM 393
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
12-160 4.47e-03

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: 37.56  E-value: 4.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  12 RGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVM--RCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDK 89
Cdd:cd09761  41 FAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLVNNAARGskGILSSLLLEEWDRILSVNLTGPYELSRYCRDE 120
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923931  90 LKASApSRIINLSSlahvaghidfddlnwqTRKYNTKA---AYCQSKLAIVLFTKELSRRLqGSGVTVNALHPG 160
Cdd:cd09761 121 LIKNK-GRIINIAS----------------TRAFQSEPdseAYAASKGGLVALTHALAMSL-GPDIRVNCISPG 176
PRK06125 PRK06125
short chain dehydrogenase; Provisional
2-172 4.71e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 37.72  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    2 EKCEAAAKDIRGETlNHHVNARHLDLASLKSIREFAAKIIEeeerVDILINNAG-VMRCPHWTTED-----GFEMQ-FGV 74
Cdd:PRK06125  42 DALEALAADLRAAH-GVDVAVHALDLSSPEAREQLAAEAGD----IDILVNNAGaIPGGGLDDVDDaawraGWELKvFGY 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   75 NHLghfllTNLLLDKLKASAPSRIINLSSLAHVAghIDFDdlnwqtrkYNTKAAycqSKLAIVLFTKELSRRLQGSGVTV 154
Cdd:PRK06125 117 IDL-----TRLAYPRMKARGSGVIVNVIGAAGEN--PDAD--------YICGSA---GNAALMAFTRALGGKSLDDGVRV 178
                        170
                 ....*....|....*...
gi 19923931  155 NALHPGVARTElgRHTGI 172
Cdd:PRK06125 179 VGVNPGPVATD--RMLTL 194
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
1-214 5.27e-03

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: 37.50  E-value: 5.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   1 MEKCEAAAKDIRGETLNHHVNArhlDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWT---TEDGFEMQFGVNHL 77
Cdd:cd05330  40 LEAAKAALLEIAPDAEVLLIKA---DVSDEAQVEAYVDATVEQFGRIDGFFNNAGIEGKQNLTedfGADEFDKVVSINLR 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931  78 GHFLLTNLLLDKLKASAPSRIINLSSLAHVaghidfddlnwqtRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:cd05330 117 GVFYGLEKVLKVMREQGSGMIVNTASVGGI-------------RGVGNQSGYAAAKHGVVGLTRNSAVEYGQYGIRINAI 183
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19923931 158 HPGVARTELgrhtgIHGSTfssTTLGPIFWLLVKSPELAAQPSTYLAVAEELADVSG 214
Cdd:cd05330 184 APGAILTPM-----VEGSL---KQLGPENPEEAGEEFVSVNPMKRFGEPEEVAAVVA 232
PRK08628 PRK08628
SDR family oxidoreductase;
25-159 5.60e-03

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 37.25  E-value: 5.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   25 LDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHW-TTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSrIINLSS 103
Cdd:PRK08628  62 VDLTDDAQCRDAVEQTVAKFGRIDGLVNNAGVNDGVGLeAGREAFVASLERNLIHYYVMAHYCLPHLKASRGA-IVNISS 140
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19923931  104 LAHVAGhidfddlnwqtrKYNTkAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHP 159
Cdd:PRK08628 141 KTALTG------------QGGT-SGYAAAKGAQLALTREWAVALAKDGVRVNAVIP 183
PRK07890 PRK07890
short chain dehydrogenase; Provisional
1-160 6.37e-03

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 37.24  E-value: 6.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931    1 MEKCEAAAKDIRGetLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNA---GVMRCPHWTTEDGFEMQFGVNHL 77
Cdd:PRK07890  39 AERLDEVAAEIDD--LGRRALAVPTDITDEDQCANLVALALERFGRVDALVNNAfrvPSMKPLADADFAHWRAVIELNVL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923931   78 GHFLLTNLLLDKLKASAPSrIINLSSLahVAGHidfddlnwQTRKYntkAAYCQSKLAIVLFTKELSRRLQGSGVTVNAL 157
Cdd:PRK07890 117 GTLRLTQAFTPALAESGGS-IVMINSM--VLRH--------SQPKY---GAYKMAKGALLAASQSLATELGPQGIRVNSV 182

                 ...
gi 19923931  158 HPG 160
Cdd:PRK07890 183 APG 185
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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