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Conserved domains on  [gi|530378355|ref|XP_005263372|]
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3-oxoacyl-[acyl-carrier-protein] reductase isoform X3 [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10142575)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; 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

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  19011750|19011748|12604210|19027726|20423462

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-181 2.89e-66

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: 203.67  E-value: 2.89e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   5 CAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAieALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd05233   81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160

                        170
                 ....*....|....*....
gi 530378355 163 AKEVARKKIRVNVVAPELI 181
Cdd:cd05233  161 ALELAPYGIRVNAVAPGLV 179
 
Name Accession Description Interval E-value
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-181 2.89e-66

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: 203.67  E-value: 2.89e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   5 CAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAieALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd05233   81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160

                        170
                 ....*....|....*....
gi 530378355 163 AKEVARKKIRVNVVAPELI 181
Cdd:cd05233  161 ALELAPYGIRVNAVAPGLV 179
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-178 1.51e-65

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: 202.32  E-value: 1.51e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:COG1028    5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAAFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:COG1028   85 DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVG 164

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVARKKIRVNVVAP 178
Cdd:COG1028  165 LTRSLALELAPRGIRVNAVAP 185
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-181 3.74e-65

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 201.16  E-value: 3.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraaGGEARVLVFDVSDEAAVRALIEAAVEAFGAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK05653  84 DILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIG 163

                        170       180
                 ....*....|....*....|....
gi 530378355 158 FSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK05653 164 FTKALALELASRGITVNAVAPGFI 187
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-191 4.11e-59

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 183.97  E-value: 4.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355    3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAkelGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 530378355  160 RALAKEVARKKIRVNVVAPELI--PRTVSIRKME 191
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVdtDMTKELREDE 194
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-150 1.53e-13

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 65.97  E-value: 1.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355     9 GGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAA------GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:smart00822   7 GGLGGLGRALARWLAERGARrLVLLSRSGPDAPGAAallaelEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVI 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530378355    82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRtmiqQQGGSIVNVGSIVGLKGNSGQSVYSA 150
Cdd:smart00822  87 HAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTAD----LPLDFFVLFSSIAGVLGSPGQANYAA 151
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 4-181 2.64e-11

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 61.08  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355    4 VCAVFGGSRGIGRAVAQLMAR----KGYRLAVIARNLEGAKAAAGDLGGDHLA-----FSCDVAKEHDVQNTFEELEKhL 74
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERSGlrvvrVSLDLGAEAGLEQLLKALRE-L 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   75 GRVNFLVNAAGINRDGLLVRT-KTEDMVSQL-------HTNLLGSMLTCKAAMRTMIQQQGG--SIVNVGSIVGLKGNSG 144
Cdd:TIGR01500  81 PRPKGLQRLLLINNAGTLGDVsKGFVDLSDStqvqnywALNLTSMLCLTSSVLKAFKDSPGLnrTVVNISSLCAIQPFKG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 530378355  145 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:TIGR01500 161 WALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVL 197
 
Name Accession Description Interval E-value
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-181 2.89e-66

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: 203.67  E-value: 2.89e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   5 CAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAieALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd05233   81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160

                        170
                 ....*....|....*....
gi 530378355 163 AKEVARKKIRVNVVAPELI 181
Cdd:cd05233  161 ALELAPYGIRVNAVAPGLV 179
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 3-181 4.98e-66

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: 203.16  E-value: 4.98e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVeeiKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160

                        170       180
                 ....*....|....*....|..
gi 530378355 160 RALAKEVARKKIRVNVVAPELI 181
Cdd:cd05333  161 KSLAKELASRGITVNAVAPGFI 182
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-178 1.51e-65

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: 202.32  E-value: 1.51e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:COG1028    5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAAFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:COG1028   85 DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVG 164

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVARKKIRVNVVAP 178
Cdd:COG1028  165 LTRSLALELAPRGIRVNAVAP 185
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-181 3.74e-65

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 201.16  E-value: 3.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraaGGEARVLVFDVSDEAAVRALIEAAVEAFGAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK05653  84 DILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIG 163

                        170       180
                 ....*....|....*....|....
gi 530378355 158 FSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK05653 164 FTKALALELASRGITVNAVAPGFI 187
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-181 1.98e-59

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 186.55  E-value: 1.98e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK05557   4 EGKVALVTGASRGIGRAIAERLAAQGANVVInYASSEAGAEALVaeiGALGGKALAVQGDVSDAESVERAVDEAKAEFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK05557  84 VDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGVI 163

                        170       180
                 ....*....|....*....|....*
gi 530378355 157 GFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK05557 164 GFTKSLARELASRGITVNAVAPGFI 188
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 2-178 3.04e-59

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: 185.77  E-value: 3.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:COG4221    5 GKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:COG4221   85 NNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSES 164

                        170
                 ....*....|....*..
gi 530378355 162 LAKEVARKKIRVNVVAP 178
Cdd:COG4221  165 LRAELRPTGIRVTVIEP 181
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-191 4.11e-59

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 183.97  E-value: 4.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355    3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAkelGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 530378355  160 RALAKEVARKKIRVNVVAPELI--PRTVSIRKME 191
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVdtDMTKELREDE 194
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-178 6.68e-58

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 182.76  E-value: 6.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELraaGARVEVVALDVTDPDAVAALAEAVLARFGPI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:COG0300   84 DVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEG 163

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVARKKIRVNVVAP 178
Cdd:COG0300  164 FSESLRAELAPTGVRVTAVCP 184
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-181 2.20e-52

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 168.51  E-value: 2.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR-NLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK12825   5 MGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEaveALGRRAQAVQADVTDKAALEAAVAAAVERFGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK12825  85 IDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGLV 164

                        170       180
                 ....*....|....*....|....*
gi 530378355 157 GFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK12825 165 GLTKALARELAEYGITVNMVAPGDI 189
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-178 1.00e-50

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 164.24  E-value: 1.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-ARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLeeiKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK05565  84 IDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAVN 163

                        170       180
                 ....*....|....*....|..
gi 530378355 157 GFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK05565 164 AFTKALAKELAPSGIRVNAVAP 185
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-178 3.32e-47

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: 154.90  E-value: 3.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   12 RGIGRAVAQLMARKGYRLAVIARNLEGAKAA---AGDLGGDhlAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI-- 86
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVeelAEELGAA--VLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFap 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEV 166
Cdd:pfam13561  84 KLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVEL 161

                         170
                  ....*....|..
gi 530378355  167 ARKKIRVNVVAP 178
Cdd:pfam13561 162 GPRGIRVNAISP 173
PRK12826 PRK12826
SDR family oxidoreductase;
1-181 3.71e-47

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 155.46  E-value: 3.71e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVeaaGGKARARQVDVRDRAALKAAVAAGVEDFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGL-KGNSGQSVYSASKGGLV 156
Cdd:PRK12826  85 DILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPrVGYPGLAHYAASKAGLV 164

                        170       180
                 ....*....|....*....|....*
gi 530378355 157 GFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK12826 165 GFTRALALELAARNITVNSVHPGGV 189
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-181 1.44e-44

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 148.57  E-value: 1.44e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08217   5 DKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNqekLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQ---------LHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIvGLKGNSGQSVY 148
Cdd:PRK08217  85 GLINNAGILRDGLLVKAKDGKVTSKmsleqfqsvIDVNLTGVFLCGREAAAKMIESgSKGVIINISSI-ARAGNMGQTNY 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 530378355 149 SASKGGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK08217 164 SASKAGVAAMTVTWAKELARYGIRVAAIAPGVI 196
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-200 9.03e-43

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 150.38  E-value: 9.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK06484  86 NAGVTDPTMtaTLDTTLEEFARLQAINLTGAYLVAREALRLMIEQgHGAAIVNVASGAGLVALPKRTAYSASKAAVISLT 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530378355 160 RALAKEVARKKIRVNVVAPELIpRTVSIRKMEKGDRINVTL 200
Cdd:PRK06484 166 RSLACEWAAKGIRVNAVLPGYV-RTQMVAELERAGKLDPSA 205
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-178 1.52e-41

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 140.67  E-value: 1.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAA---GDLGGDHL---AFSCDVAKEHDVQNTFEELEKHL 74
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYR--VIATYFSGNDCAKdwfEEYGFTEDqvrLKELDVTDTEECAEALAEIEEEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGG 154
Cdd:PRK12824  79 GPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAG 158

                        170       180
                 ....*....|....*....|....
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK12824 159 MIGFTKALASEGARYGITVNCIAP 182
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 2-181 4.99e-40

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 137.10  E-value: 4.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06841  15 GKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:PRK06841  95 NSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGVVGMTKV 174

                        170       180
                 ....*....|....*....|
gi 530378355 162 LAKEVARKKIRVNVVAPELI 181
Cdd:PRK06841 175 LALEWGPYGITVNAISPTVV 194
PRK06138 PRK06138
SDR family oxidoreductase;
2-181 9.19e-40

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 136.43  E-value: 9.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL--GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06138   5 GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIaaGGRAFARQGDVGSAEAVEALVDFVAARWGRLDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK06138  85 LVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIASLT 164

                        170       180
                 ....*....|....*....|..
gi 530378355 160 RALAKEVARKKIRVNVVAPELI 181
Cdd:PRK06138 165 RAMALDHATDGIRVNAVAPGTI 186
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 3-178 2.15e-39

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: 135.18  E-value: 2.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05347    6 KVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIekeGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:cd05347   86 LVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVAGLT 165

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAP 178
Cdd:cd05347  166 KALATEWARHGIQVNAIAP 184
FabG-like PRK07231
SDR family oxidoreductase;
2-178 3.25e-39

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 134.96  E-value: 3.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILagGRAIAVAADVSDEADVEAAVAAALERFGSVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGIN-RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PRK07231  85 LVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITL 164

                        170       180
                 ....*....|....*....|
gi 530378355 159 SRALAKEVARKKIRVNVVAP 178
Cdd:PRK07231 165 TKALAAELGPDKIRVNAVAP 184
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 2-178 1.83e-38

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 133.09  E-value: 1.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK12429   4 GKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALqkaGGKAIGVAMDVTDEEAINAGIDYAVETFGGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PRK12429  84 ILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIGL 163

                        170       180
                 ....*....|....*....|
gi 530378355 159 SRALAKEVARKKIRVNVVAP 178
Cdd:PRK12429 164 TKVVALEGATHGVTVNAICP 183
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 2-178 2.52e-38

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: 132.38  E-value: 2.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLA-------FSCDVAKEHDVQNTFEELEKHL 74
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANAsgqkvsyISADLSDYEEVEQAFAQAVEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGG 154
Cdd:cd08939   81 GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFA 160

                        170       180
                 ....*....|....*....|....
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd08939  161 LRGLAESLRQELKPYNIRVSVVYP 184
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-198 3.44e-38

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 138.06  E-value: 3.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06484 270 RVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVN 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGL-LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:PRK06484 350 NAGIAEVFKpSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRS 427

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530378355 162 LAKEVARKKIRVNVVAPELIpRTVSIRKMEKGDRINV 198
Cdd:PRK06484 428 LACEWAPAGIRVNTVAPGYI-ETPAVLALKASGRADF 463
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 3-178 5.98e-37

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: 128.89  E-value: 5.98e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd05374   81 NAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESL 160

                        170
                 ....*....|....*.
gi 530378355 163 AKEVARKKIRVNVVAP 178
Cdd:cd05374  161 RLELAPFGIKVTIIEP 176
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 3-184 1.07e-36

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


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 128.34  E-value: 1.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVnYYRSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINR--DGLLVRTKT----EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:cd05349   81 NNALIDFpfDPDQRKTFDtidwEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAKAAL 160

                        170       180
                 ....*....|....*....|....*....
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAPELIPRT 184
Cdd:cd05349  161 LGFTRNMAKELGPYGITVNMVSGGLLKVT 189
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 3-178 1.48e-36

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 128.17  E-value: 1.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALeaaGGRAHAIAADLADPASVQRFFDAAAAALGGLDG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK12939  88 LVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIGMT 167

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAP 178
Cdd:PRK12939 168 RSLARELGGRGITVNAIAP 186
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-181 2.15e-36

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 127.11  E-value: 2.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07666   8 KNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEayGVKVVIaTADVSDYEEVTAAIEQLKNELGSIDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK07666  88 LINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGVLGLT 167

                        170       180
                 ....*....|....*....|..
gi 530378355 160 RALAKEVARKKIRVNVVAPELI 181
Cdd:PRK07666 168 ESLMQEVRKHNIRVTALTPSTV 189
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 3-193 4.47e-36

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 126.98  E-value: 4.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR---NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK08213  13 KTALVTGGSRGLGLQIAEALGEAGARVVLSARkaeELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDgllvrTKTEDMVSQ-----LHTNLLGS-MLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSV----YS 149
Cdd:PRK08213  93 LVNNAGATWG-----APAEDHPVEawdkvMNLNVRGLfLLSQAVAKRSMIPRGYGRIINVASVAGLGGNPPEVMdtiaYN 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 530378355 150 ASKGGLVGFSRALAKEVARKKIRVNVVAPELIPrtvsiRKMEKG 193
Cdd:PRK08213 168 TSKGAVINFTRALAAEWGPHGIRVNAIAPGFFP-----TKMTRG 206
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 3-178 8.68e-36

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: 125.85  E-value: 8.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAeieAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:cd05362   84 ILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAF 161

                        170       180
                 ....*....|....*....|
gi 530378355 159 SRALAKEVARKKIRVNVVAP 178
Cdd:cd05362  162 TRVLAKELGGRGITVNAVAP 181
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 2-178 8.98e-36

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: 125.91  E-value: 8.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05352    8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYgvktKAYKCDVSSQESVEKTFKQIQKDFGKI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRD-GLLVRTKtEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGN--SGQSVYSASKGG 154
Cdd:cd05352   88 DILIANAGITVHkPALDYTY-EQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNrpQPQAAYNASKAA 166

                        170       180
                 ....*....|....*....|....
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd05352  167 VIHLAKSLAVEWAKYFIRVNSISP 190
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 2-184 1.24e-35

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 125.89  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaaAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06171   9 GKIIIVTGGSSGIGLAIVKELLANGANVVNADIH-------GGDGQHENYQFvPTDVSSAEEVNHTVAEIIEKFGRIDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHT---------NLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSAS 151
Cdd:PRK06171  82 VNNAGINIPRLLVDEKDPAGKYELNEaafdkmfniNQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQSCYAAT 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 530378355 152 KGGLVGFSRALAKEVARKKIRVNVVAPELIPRT 184
Cdd:PRK06171 162 KAALNSFTRSWAKELGKHNIRVVGVAPGILEAT 194
PRK07326 PRK07326
SDR family oxidoreductase;
1-178 1.67e-35

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 124.74  E-value: 1.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07326   5 KGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNnkGNVLGLAADVRDEADVQRAVDAIVAAFGGLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PRK07326  85 VLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINISSLAGTNFFAGGAAYNASKFGLVGF 163

                        170       180
                 ....*....|....*....|
gi 530378355 159 SRALAKEVARKKIRVNVVAP 178
Cdd:PRK07326 164 SEAAMLDLRQYGIKVSTIMP 183
PRK06172 PRK06172
SDR family oxidoreductase;
2-181 2.16e-35

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 125.25  E-value: 2.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNL---EGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06172   7 GKVALVTGGAAGIGRATALAFAREGAKVVVADRDAaggEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK06172  87 YAFNNAGIEIEQGRLAEGSEAEFDAImGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHAVIG 166

                        170       180
                 ....*....|....*....|....
gi 530378355 158 FSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK06172 167 LTKSAAIEYAKKGIRVNAVCPAVI 190
PRK07063 PRK07063
SDR family oxidoreductase;
3-181 4.63e-35

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 124.39  E-value: 4.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIardvaGARVLAVPADVTDAASVAAAVAAAEEAFGPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGIN--RDGLlvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK07063  88 DVLVNNAGINvfADPL--AMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKHGL 165

                        170       180
                 ....*....|....*....|....*.
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK07063 166 LGLTRALGIEYAARNVRVNAIAPGYI 191
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 7-181 5.43e-35

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 123.87  E-value: 5.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:PRK12936  11 VTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEGVDILVNNAGI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEV 166
Cdd:PRK12936  91 TKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFSKSLAQEI 170

                        170
                 ....*....|....*
gi 530378355 167 ARKKIRVNVVAPELI 181
Cdd:PRK12936 171 ATRNVTVNCVAPGFI 185
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 2-181 9.45e-35

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: 123.54  E-value: 9.45e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELragGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:cd05344   81 ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGL 160

                        170       180
                 ....*....|....*....|...
gi 530378355 159 SRALAKEVARKKIRVNVVAPELI 181
Cdd:cd05344  161 VKTLSRELAPDGVTVNSVLPGYI 183
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 2-202 1.06e-34

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: 123.08  E-value: 1.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05369    3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEIssatGGRAHPIQCDVRDPEAVEAAVDETLKEFGKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINrdgllVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGSIVGLKGNSGQSVYSAS 151
Cdd:cd05369   83 DILINNAAGN-----FLAPAESLSPNgfktvIDIDLNGTFNTTKAVGKRLIEAKhGGSILNISATYAYTGSPFQVHSAAA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530378355 152 KGGLVGFSRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKGDRINVTLRS 202
Cdd:cd05369  158 KAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIE 208
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 3-182 1.87e-34

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: 122.41  E-value: 1.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLE-GAKAAAGDLGGDHLA--FSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENpGAAAELQAINPKVKAtfVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGIN--RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ---GGSIVNVGSIVGLKGNSGQSVYSASKGG 154
Cdd:cd05323   81 LINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkGGVIVNIGSVAGLYPAPQFPVYSASKHG 160

                        170       180
                 ....*....|....*....|....*....
gi 530378355 155 LVGFSRALAKEVARKK-IRVNVVAPELIP 182
Cdd:cd05323  161 VVGFTRSLADLLEYKTgVRVNAICPGFTN 189
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 4-181 2.16e-34

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: 122.35  E-value: 2.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETAnnvRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:cd05339   81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHE 160

                        170       180
                 ....*....|....*....|....
gi 530378355 161 ALAKEVAR---KKIRVNVVAPELI 181
Cdd:cd05339  161 SLRLELKAygkPGIKTTLVCPYFI 184
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 3-181 3.63e-34

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: 122.11  E-value: 3.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAViarNLEGAKAAAGDL-------GGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:cd05358    4 KVALVTGASSGIGKAIAIRLATAGANVVV---NYRSKEDAAEEVveeikavGGKAIAVQADVSKEEDVVALFQSAIKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGSIVGLKGNSGQSVYSASKGG 154
Cdd:cd05358   81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIkGKIINMSSVHEKIPWPGHVNYAASKGG 160

                        170       180
                 ....*....|....*....|....*..
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:cd05358  161 VKMMTKTLAQEYAPKGIRVNAIAPGAI 187
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 2-181 3.93e-34

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: 121.72  E-value: 3.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05341    5 GKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGRLDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:cd05341   85 NNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGLTKS 164

                        170       180
                 ....*....|....*....|..
gi 530378355 162 LAKEVARKK--IRVNVVAPELI 181
Cdd:cd05341  165 AALECATQGygIRVNSVHPGYI 186
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-181 2.60e-33

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 119.72  E-value: 2.60e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAViarNLEGAKAAA-------GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAenlvnelGKEGHDVYAVQADVSKVEDANRLVEEAVNHFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK12935  84 KVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGM 163

                        170       180
                 ....*....|....*....|....*.
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK12935 164 LGFTKSLALELAKTNVTVNAICPGFI 189
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 3-193 3.02e-33

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: 119.52  E-value: 3.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd08944    4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDLLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGI-NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:cd08944   84 NAGAmHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRT 163

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 162 LAKEVARKKIRVNVVAPELI--PRTVSIRKMEKG 193
Cdd:cd08944  164 LAAELRHAGIRCNALAPGLIdtPLLLAKLAGFEG 197
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 3-178 3.41e-33

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: 118.76  E-value: 3.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd08929   81 NAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAA 160

                        170
                 ....*....|....*.
gi 530378355 163 AKEVARKKIRVNVVAP 178
Cdd:cd08929  161 MLDLREANIRVVNVMP 176
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 2-178 4.48e-33

(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: 118.96  E-value: 4.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAV----IARNLEGAKAAAGDL--------GGDHLAFSCDVAkehDVQNTFEE 69
Cdd:cd05353    5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVndlgGDRKGSGKSSSAADKvvdeikaaGGKAVANYDSVE---DGEKIVKT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  70 LEKHLGRVNFLVNAAGINRDGLLVRTKTE--DMVSQLHtnLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSV 147
Cdd:cd05353   82 AIDAFGRVDILVNNAGILRDRSFAKMSEEdwDLVMRVH--LKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQAN 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 530378355 148 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd05353  160 YSAAKLGLLGLSNTLAIEGAKYNITCNTIAP 190
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 3-181 8.46e-33

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 117.98  E-value: 8.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFS-CDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGgIDLVDPQAARRAVDEVNRQFGRLDALV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:PRK12828  88 NIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVARLTEA 167

                        170       180
                 ....*....|....*....|
gi 530378355 162 LAKEVARKKIRVNVVAPELI 181
Cdd:PRK12828 168 LAAELLDRGITVNAVLPSII 187
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 4-177 2.34e-32

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: 116.71  E-value: 2.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVrelGGEAIAVVADVADAAQVERAADTAVERFGRIDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:cd05360   82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTE 161

                        170
                 ....*....|....*..
gi 530378355 161 ALAKEVARKKIRVNVVA 177
Cdd:cd05360  162 SLRAELAHDGAPISVTL 178
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-181 2.56e-32

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 117.47  E-value: 2.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGG-DHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12829  10 DGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGaKVTATVADVADPAQVERVFDTAVERFGGLDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGI-NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK12829  90 LVNNAGIaGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhGGVIIALSSVAGRLGYPGRTPYAASKWAVVG 169

                        170       180
                 ....*....|....*....|....
gi 530378355 158 FSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK12829 170 LVKSLAIELGPLGIRVNAILPGIV 193
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-181 2.69e-32

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 117.13  E-value: 2.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIA----RNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKH 73
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIeaaGGKALGLAFDVRDFAATRAALDAGVEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  74 LGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQ-QQGGSIVNVGSIVGLKGNSGQSVYSASK 152
Cdd:PRK12827  85 FGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIASVAGVRGNRGQVNYAASK 164

                        170       180
                 ....*....|....*....|....*....
gi 530378355 153 GGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK12827 165 AGLIGLTKTLANELAPRGITVNAVAPGAI 193
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 2-178 3.34e-32

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 118.87  E-value: 3.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07109   8 RQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIraaGGEALAVVADVADAEAVQAAADRAEEELGPID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PRK07109  88 TWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGF 167

                        170       180
                 ....*....|....*....|..
gi 530378355 159 SRALAKEV--ARKKIRVNVVAP 178
Cdd:PRK07109 168 TDSLRCELlhDGSPVSVTMVQP 189
PRK09730 PRK09730
SDR family oxidoreductase;
3-207 3.71e-32

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 116.49  E-value: 3.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVnYQQNLHAAQEVVNLItqaGGKAFVLQADISDENQVVAMFTAIDQHDEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGInrdgLLVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQ---QGGSIVNVGSIVGLKGNSGQSV-YS 149
Cdd:PRK09730  82 ALVNNAGI----LFTQCTVENLTAErinrvLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPGEYVdYA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355 150 ASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKG--DRINVTLrsPEQHG 207
Cdd:PRK09730 158 ASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGrvDRVKSNI--PMQRG 215
PRK07035 PRK07035
SDR family oxidoreductase;
3-180 3.84e-32

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 116.65  E-value: 3.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07035   9 KIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIvaaGGKAEALACHIGEMEQIDALFAHIRERHGRLDI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGIN-------RDGLLVRTKTEDMvsqlhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASK 152
Cdd:PRK07035  89 LVNNAAANpyfghilDTDLGAFQKTVDV------NIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITK 162

                        170       180
                 ....*....|....*....|....*...
gi 530378355 153 GGLVGFSRALAKEVARKKIRVNVVAPEL 180
Cdd:PRK07035 163 AAVISMTKAFAKECAPFGIRVNALLPGL 190
PRK09072 PRK09072
SDR family oxidoreductase;
9-178 4.82e-32

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 116.58  E-value: 4.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEG--AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHlGRVNFLVNAAGI 86
Cdd:PRK09072  12 GASGGIGQALAEALAAAGARLLLVGRNAEKleALAARLPYPGRHRWVVADLTSEAGREAVLARAREM-GGINVLINNAGV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEV 166
Cdd:PRK09072  91 NHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRGFSEALRREL 170

                        170
                 ....*....|..
gi 530378355 167 ARKKIRVNVVAP 178
Cdd:PRK09072 171 ADTGVRVLYLAP 182
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 3-178 6.16e-32

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: 115.15  E-value: 6.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDlGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd08932   80 NAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHAL 159

                        170
                 ....*....|....*.
gi 530378355 163 AKEVARKKIRVNVVAP 178
Cdd:cd08932  160 RQEGWDHGVRVSAVCP 175
PRK06123 PRK06123
SDR family oxidoreductase;
1-181 6.37e-32

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 116.03  E-value: 6.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKA---AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK06123   1 MRKVMIITGASRGIGAATALLAAERGYAVCLnYLRNRDAAEAvvqAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGInrdgLLVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQ---QGGSIVNVGSIVGLKGNSGQSV- 147
Cdd:PRK06123  81 LDALVNNAGI----LEAQMRLEQMDAArltriFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVSSMAARLGSPGEYId 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 148 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK06123 157 YAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVI 190
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 1-180 7.77e-32

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: 115.85  E-value: 7.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGdlGGDHLAFS-CDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK--LGDNCRFVpVDVTSEKDVKAALALAKAKFGRLDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGI-------NRDGLLVRtKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG------GSIVNVGSIVGLKGNSGQS 146
Cdd:cd05371   79 VVNCAGIavaaktyNKKGQQPH-SLELFQRVINVNLIGTFNVIRLAAGAMGKNEPdqggerGVIINTASVAAFEGQIGQA 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 147 VYSASKGGLVGFSRALAKEVARKKIRVNVVAPEL 180
Cdd:cd05371  158 AYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGL 191
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 2-178 1.09e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 115.60  E-value: 1.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06057   7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGG--LFVPTDVTDEDAVNALFDTAAETYGSVDIAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGIN--RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGN-SGQSVYSASKGGLVGF 158
Cdd:PRK06057  85 NNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSaTSQISYTASKGGVLAM 164

                        170       180
                 ....*....|....*....|
gi 530378355 159 SRALAKEVARKKIRVNVVAP 178
Cdd:PRK06057 165 SRELGVQFARQGIRVNALCP 184
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 1-178 2.43e-31

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: 114.78  E-value: 2.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLE-GAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05366    1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEeAAKSTIQEIseaGYNAVAVGADVTDKDDVEALIDQAVEKFGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:cd05366   81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSASKFAV 160

                        170       180
                 ....*....|....*....|...
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd05366  161 RGLTQTAAQELAPKGITVNAYAP 183
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 2-178 4.03e-31

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: 114.09  E-value: 4.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05326    4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFvHCDVTVEADVRAAVDTAVARFGRLDIM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGI--NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:cd05326   84 FNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLGL 163

                        170       180
                 ....*....|....*....|
gi 530378355 159 SRALAKEVARKKIRVNVVAP 178
Cdd:cd05326  164 TRSAATELGEHGIRVNCVSP 183
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 2-192 4.60e-31

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 114.75  E-value: 4.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06701  46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdaneTKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELGRL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAG--INRDGLlvrtktEDMVSQ-----LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSA 150
Cdd:PRK06701 126 DILVNNAAfqYPQQSL------EDITAEqldktFKTNIYSYFHMTKAALPHL--KQGSAIINTGSITGYEGNETLIDYSA 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 530378355 151 SKGGLVGFSRALAKEVARKKIRVNVVAP-----ELIPRTVSIRKMEK 192
Cdd:PRK06701 198 TKGAIHAFTRSLAQSLVQKGIRVNAVAPgpiwtPLIPSDFDEEKVSQ 244
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 3-181 5.65e-31

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: 113.40  E-value: 5.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08934    4 KVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELeaeGGKALVLELDVTDEQQVDAAVERTVEALGRLDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:cd08934   84 LVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFS 163

                        170       180
                 ....*....|....*....|..
gi 530378355 160 RALAKEVARKKIRVNVVAPELI 181
Cdd:cd08934  164 EGLRQEVTERGVRVVVIEPGTV 185
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 3-184 8.93e-31

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: 112.87  E-value: 8.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN-----------LEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTF 67
Cdd:cd05338    4 KVAFVTGASRGIGRAIALRLAKAGATVVVAAKTasegdngsaksLPGtieeTAEEIEAAGGQALPIVVDVRDEDQVRALV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  68 EELEKHLGRVNFLVNAAGInrdglLVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGN 142
Cdd:cd05338   84 EATVDQFGRLDILVNNAGA-----IWLSLVEDTPAKrfdlmQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530378355 143 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRT 184
Cdd:cd05338  159 RGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIET 200
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 9-178 9.17e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 113.47  E-value: 9.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINR 88
Cdd:PRK06180  11 GVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVLVNNAGYGH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  89 DGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVAR 168
Cdd:PRK06180  91 EGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKEVAP 170

                        170
                 ....*....|
gi 530378355 169 KKIRVNVVAP 178
Cdd:PRK06180 171 FGIHVTAVEP 180
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 2-178 1.05e-30

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 113.18  E-value: 1.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06198   6 GKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELealGAKAVFVQADLSDVEDCRRVVAAADEAFGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK06198  86 DALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAAYCASKGALA 165

                        170       180
                 ....*....|....*....|..
gi 530378355 157 GFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK06198 166 TLTRNAAYALLRNRIRVNGLNI 187
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 2-178 1.65e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 112.73  E-value: 1.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07825   5 GKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVV-GGPLDVTDPASFAAFLDAVEADLGPIDVLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:PRK07825  84 NNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVGFTDA 163

                        170
                 ....*....|....*..
gi 530378355 162 LAKEVARKKIRVNVVAP 178
Cdd:PRK07825 164 ARLELRGTGVHVSVVLP 180
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 6-181 3.84e-30

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: 111.27  E-value: 3.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH---LAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05350    2 LITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNpsvEVEILDVTDEERNQLVIAELEAELGGLDLVII 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd05350   82 NAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAESL 161

                        170
                 ....*....|....*....
gi 530378355 163 AKEVARKKIRVNVVAPELI 181
Cdd:cd05350  162 RYDVKKRGIRVTVINPGFI 180
PRK07454 PRK07454
SDR family oxidoreductase;
9-178 4.98e-30

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 110.82  E-value: 4.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK07454  13 GASSGIGKATALAFAKAGWDLALVARSqdaLEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDVLINNAG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKE 165
Cdd:PRK07454  93 MAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFTKCLAEE 172

                        170
                 ....*....|...
gi 530378355 166 VARKKIRVNVVAP 178
Cdd:PRK07454 173 ERSHGIRVCTITL 185
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 1-178 8.03e-30

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 110.90  E-value: 8.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYgegmaYGFGADATSEQSVLALSRGVDEIFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGSIVGLKGNSGQSVYSASKGG 154
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFG 160

                        170       180
                 ....*....|....*....|....
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK12384 161 GVGLTQSLALDLAEYGITVHSLML 184
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 1-178 1.15e-29

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 110.90  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK08263  82 VNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSE 161

                        170
                 ....*....|....*...
gi 530378355 161 ALAKEVARKKIRVNVVAP 178
Cdd:PRK08263 162 ALAQEVAEFGIKVTLVEP 179
PRK06124 PRK06124
SDR family oxidoreductase;
3-178 1.55e-29

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 109.80  E-value: 1.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06124  12 QVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALraaGGAAEALAFDIADEEAVAAAFARIDAEHGRLDI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGI-NRDGLLvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PRK06124  92 LVNNVGArDRRPLA-ELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLTGL 170

                        170       180
                 ....*....|....*....|
gi 530378355 159 SRALAKEVARKKIRVNVVAP 178
Cdd:PRK06124 171 MRALAAEFGPHGITSNAIAP 190
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
1-178 1.83e-29

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 109.82  E-value: 1.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLskdGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINrDGLLVRTKTEDMVSQLH-TNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK08643  81 NVVVNNAGVA-PTTPIETITEEQFDKVYnINVGGVIWGIQAAQEAFKKLgHGGKIINATSQAGVVGNPELAVYSSTKFAV 159

                        170       180
                 ....*....|....*....|...
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK08643 160 RGLTQTAARDLASEGITVNAYAP 182
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 3-178 1.91e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 109.42  E-value: 1.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFscDVAKEHDVQNTFEELekhlGRVNFLVN 82
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRL--DVGDDAAIRAALAAA----GAFDGLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMI-QQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:PRK07060  84 CAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIaAGRGGSIVNVSSQAALVGLPDHLAYCASKAALDAITRV 163

                        170
                 ....*....|....*..
gi 530378355 162 LAKEVARKKIRVNVVAP 178
Cdd:PRK07060 164 LCVELGPHGIRVNSVNP 180
PRK06947 PRK06947
SDR family oxidoreductase;
1-181 2.48e-29

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 109.12  E-value: 2.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVGInYARDAAAAEETADavrAAGGRACVVAGDVANEADVIAMFDAVQSAFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGL-LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ---GGSIVNVGSIVGLKGNSGQSV-YSAS 151
Cdd:PRK06947  81 LDALVNNAGIVAPSMpLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrGGAIVNVSSIASRLGSPNEYVdYAGS 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 530378355 152 KGGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK06947 161 KGAVDTLTLGLAKELGPHGVRVNAVRPGLI 190
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 3-178 5.03e-29

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 108.29  E-value: 5.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAViarNLEGAKAAAGDL-------GGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK12937   6 KVAIVTGASRGIGAAIARRLAADGFAVAV---NYAGSAAAADELvaeieaaGGRAIAVQADVADAAAVTRLFDAAETAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK12937  83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAASKAAV 160

                        170       180
                 ....*....|....*....|...
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK12937 161 EGLVHVLANELRGRGITVNAVAP 183
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 2-181 7.15e-29

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: 108.27  E-value: 7.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA------AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:cd05364    3 GKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEEtrqsclQAGVSEKKILLVVADLTEEEGQDRIISTTLAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGgSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:cd05364   83 RLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKG-EIVNVSSVAGGRSFPGVLYYCISKAAL 161

                        170       180
                 ....*....|....*....|....*.
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:cd05364  162 DQFTRCTALELAPKGVRVNSVSPGVI 187
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-178 7.47e-29

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: 107.86  E-value: 7.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05345    4 EGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGI---NRDGLLVRTKTEDMVSQLhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:cd05345   84 VNNAGIthrNKPMLEVDEEEFDRVFAV--NVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVT 161

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVARKKIRVNVVAP 178
Cdd:cd05345  162 ATKAMAVELAPRNIRVNCLCP 182
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
3-181 7.81e-29

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 107.79  E-value: 7.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV--------IARNLEGAKAaagdLGGDHLAFSCDVAKEHDVQNTFEELEKHL 74
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnsprRVKWLEDQKA----LGFDFIASEGNVGDWDSTKAAFDKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGG 154
Cdd:PRK12938  80 GEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAG 159

                        170       180
                 ....*....|....*....|....*..
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK12938 160 IHGFTMSLAQEVATKGVTVNTVSPGYI 186
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
3-183 9.39e-29

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 112.63  E-value: 9.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGG--DHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGpdRALGVACDVTDEAAVQAAFEEAALAFGGVDIV 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08324 503 VSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIASKNAVNPGPNFGAYGAAKAAELHLV 582

                        170       180
                 ....*....|....*....|....
gi 530378355 160 RALAKEVARKKIRVNVVAPELIPR 183
Cdd:PRK08324 583 RQLALELGPDGIRVNGVNPDAVVR 606
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 2-178 1.10e-28

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 108.06  E-value: 1.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08277  10 GKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIkaaGGEALAVKADVLDKESLEQARQQILEDFGPCD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINR---------DGLLVRTKT------EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNS 143
Cdd:PRK08277  90 ILINGAGGNHpkattdnefHELIEPTKTffdldeEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFTPLT 169

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530378355 144 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK08277 170 KVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAP 204
PRK07074 PRK07074
SDR family oxidoreductase;
1-178 1.45e-28

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 107.55  E-value: 1.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-LAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARfVPVACDLTDAASLAAALANAAAERGPVDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGnSGQSVYSASKGGLVGFS 159
Cdd:PRK07074  81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAA-LGHPAYSAAKAGLIHYT 159

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAP 178
Cdd:PRK07074 160 KLLAVEYGRFGIRANAVAP 178
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 1-205 3.05e-28

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: 106.52  E-value: 3.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDhLAFSC--DVAKEHDVQNTFEELEKHLG 75
Cdd:cd05332    2 QGKVVIITGASSGIGEELAYHLARLGARLVLSARReerLEEVKSECLELGAP-SPHVVplDMSDLEDAEQVVEEALKLFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:cd05332   81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHAL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAPELIPRTVSIRK-------MEKGDRINVTLRSPEQ 205
Cdd:cd05332  161 QGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNAlsgdgsmSAKMDDTTANGMSPEE 217
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 3-193 5.25e-28

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 105.94  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD--LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAaqGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:cd08943   82 VSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLA 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 160 RALAKEVARKKIRVNVVAPELIPRTVSIRKMEKG 193
Cdd:cd08943  162 RCLALEGGEDGIRVNTVNPDAVFRGSKIWEGVWR 195
PRK06181 PRK06181
SDR family oxidoreductase;
2-178 8.26e-28

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 105.45  E-value: 8.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNetrLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQgGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK06181  81 ILVNNAGITMWSRFDELTDLSVFERVmRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGYAASKHALHG 159

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVARKKIRVNVVAP 178
Cdd:PRK06181 160 FFDSLRIELADDGVAVTVVCP 180
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-181 8.66e-28

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 108.77  E-value: 8.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAA----AGDLGGDHLAfsCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08261 211 KVALVTGAARGIGAAIAEVLARDGAH--VVCLDVPAAGEAlaavANRVGGTALA--LDITAPDAPARIAEHLAERHGGLD 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTE--DMVsqLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK08261 287 IVVHNAGITRDKTLANMDEArwDSV--LAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVI 364

                        170       180
                 ....*....|....*....|....*
gi 530378355 157 GFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK08261 365 GLVQALAPLLAERGITINAVAPGFI 389
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
2-178 1.16e-27

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 105.11  E-value: 1.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07067   6 GKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK07067  86 NNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGEALVSHYCATKAAVISYTQ 165

                        170
                 ....*....|....*...
gi 530378355 161 ALAKEVARKKIRVNVVAP 178
Cdd:PRK07067 166 SAALALIRHGINVNAIAP 183
PRK08628 PRK08628
SDR family oxidoreductase;
2-178 1.44e-27

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 104.66  E-value: 1.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK08628   7 DKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEElrALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINrDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMrTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08628  87 LVNNAGVN-DGVGLEAGREAFVASLERNLIHYYVMAHYCL-PHLKASRGAIVNISSKTALTGQGGTSGYAAAKGAQLALT 164

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAP 178
Cdd:PRK08628 165 REWAVALAKDGVRVNAVIP 183
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 2-192 1.56e-27

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: 105.07  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA-----AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05355   26 GKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAeetkkLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:cd05355  106 LDILVNNAAYQHPQESIEDITTEQLEKtFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGSPHLLDYAATKGAI 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAP-----ELIPRTVSIRKMEK 192
Cdd:cd05355  184 VAFTRGLSLQLAEKGIRVNAVAPgpiwtPLIPSSFPEEKVSE 225
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 1-174 1.67e-27

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: 104.85  E-value: 1.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA----GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVAdeinAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:cd05322   81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDgIQGRIIQINSKSGKVGSKHNSGYSAAKFGG 160

                        170
                 ....*....|....*....
gi 530378355 156 VGFSRALAKEVARKKIRVN 174
Cdd:cd05322  161 VGLTQSLALDLAEHGITVN 179
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 1-178 2.19e-27

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: 104.34  E-value: 2.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELtnlyKNRVIALELDITSKESIKELIESYLEKFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVR---TKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGL--------KGNSGQ 145
Cdd:cd08930   81 IDILINNAYPSPKVWGSRfeeFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGViapdfriyENTQMY 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530378355 146 S--VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd08930  161 SpvEYSVIKAGIIHLTKYLAKYYADTGIRVNAISP 195
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-178 2.94e-27

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 104.21  E-value: 2.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVAdeiNKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQ-QQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PRK13394  88 LVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGL 167

                        170       180
                 ....*....|....*....|
gi 530378355 159 SRALAKEVARKKIRVNVVAP 178
Cdd:PRK13394 168 ARVLAKEGAKHNVRSHVVCP 187
PRK05867 PRK05867
SDR family oxidoreductase;
7-181 7.07e-27

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 102.81  E-value: 7.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK05867  14 ITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIgtsGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDIAVCN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSV--YSASKGGLVGFSR 160
Cdd:PRK05867  94 AGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIINVPQQVshYCASKAAVIHLTK 173

                        170       180
                 ....*....|....*....|.
gi 530378355 161 ALAKEVARKKIRVNVVAPELI 181
Cdd:PRK05867 174 AMAVELAPHKIRVNSVSPGYI 194
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 2-205 9.34e-27

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 102.30  E-value: 9.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVqntFEELEKHLGR- 76
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYgvetKTIAADFSAGDDI---YERIEKELEGl 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 -VNFLVNAAGINRD--GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKG 153
Cdd:cd05356   78 dIGILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530378355 154 GLVGFSRALAKEVARKKIRVNVVAPELIprtVSirKMEKGDRINVTLRSPEQ 205
Cdd:cd05356  158 FLDFFSRALYEEYKSQGIDVQSLLPYLV---AT--KMSKIRKSSLFVPSPEQ 204
PRK05650 PRK05650
SDR family oxidoreductase;
9-178 1.18e-26

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 102.81  E-value: 1.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK05650   7 GAASGLGRAIALRWAREGWRLALADVNEEGGEETLkllREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVNNAG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKE 165
Cdd:PRK05650  87 VASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETLLVE 166

                        170
                 ....*....|...
gi 530378355 166 VARKKIRVNVVAP 178
Cdd:PRK05650 167 LADDEIGVHVVCP 179
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-184 1.18e-26

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 102.48  E-value: 1.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR-VN 78
Cdd:PRK08642   4 SEQTVLVTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGKpIT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAA-------GINRDGLLVRTkTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSivglkgNSGQSV---- 147
Cdd:PRK08642  84 TVVNNAladfsfdGDARKKADDIT-WEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGT------NLFQNPvvpy 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530378355 148 --YSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRT 184
Cdd:PRK08642 157 hdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTT 195
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-202 1.28e-26

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 102.17  E-value: 1.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGV--FTIKCDVGNRDQVKKSKEVVEKEFGRVDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGI-------NRDgllvRTKTEDMVSqlhTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGL-KGNSGQSVYSASKG 153
Cdd:PRK06463  85 NNAGImylmpfeEFD----EEKYNKMIK---INLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTAAEGTTFYAITKA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530378355 154 GLVGFSRALAKEVARKKIRVNVVAPELIPR--TVSIRKMEKGDRINVTLRS 202
Cdd:PRK06463 158 GIIILTRRLAFELGKYGIRVNAVAPGWVETdmTLSGKSQEEAEKLRELFRN 208
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 4-173 1.88e-26

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 101.31  E-value: 1.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA----AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEAllvdIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:cd05373   81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALA 160

                        170
                 ....*....|....
gi 530378355 160 RALAKEVARKKIRV 173
Cdd:cd05373  161 QSMARELGPKGIHV 174
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 2-178 3.55e-26

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: 101.46  E-value: 3.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG----GDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNragpGSCKFVPCDVTKEEDIKTLISVTVERFGRI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLV-RTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGgSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:cd08933   89 DCLVNNAGWHPPHQTTdETSAQEFRDLLNLNLISYFLASKYALPHLRKSQG-NIINLSSLVGSIGQKQAAPYVATKGAIT 167

                        170       180
                 ....*....|....*....|..
gi 530378355 157 GFSRALAKEVARKKIRVNVVAP 178
Cdd:cd08933  168 AMTKALAVDESRYGVRVNCISP 189
PRK06398 PRK06398
aldose dehydrogenase; Validated
 2-193 3.86e-26

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 101.06  E-value: 3.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGakaaagDLGGDHlaFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06398   6 DKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS------YNDVDY--FKVDVSNKEQVIKGIDYVISKYGRIDILV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:PRK06398  78 NNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVLGLTRS 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 162 LAKEVArKKIRVNVVAPELI--PRTVSIRKMEKG 193
Cdd:PRK06398 158 IAVDYA-PTIRCVAVCPGSIrtPLLEWAAELEVG 190
PRK08589 PRK08589
SDR family oxidoreductase;
2-181 4.23e-26

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 101.39  E-value: 4.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKG-YRLAV-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK08589   6 NKVAVITGASTGIGQASAIALAQEGaYVLAVdIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQqGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PRK08589  86 LFNNAGVDNAAGRIHEYPVDVFDKiMAVDMRGTFLMTKMLLPLMMEQ-GGSIINTSSFSGQAADLYRSGYNAAKGAVINF 164

                        170       180
                 ....*....|....*....|...
gi 530378355 159 SRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK08589 165 TKSIAIEYGRDGIRANAIAPGTI 187
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 9-187 7.10e-26

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: 100.05  E-value: 7.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAA 84
Cdd:cd05346    7 GASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFpvkvLPLQLDVSDRESIEAALENLPEEFRDIDILVNNA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  85 GINRdGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd05346   87 GLAL-GLdpAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQFSLNL 165

                        170       180
                 ....*....|....*....|....*
gi 530378355 163 AKEVARKKIRVNVVAPELIPRTVSI 187
Cdd:cd05346  166 RKDLIGTGIRVTNIEPGLVETEFSL 190
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 7-181 1.00e-25

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: 99.83  E-value: 1.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHL-GRVNFLVN 82
Cdd:cd05329   11 VTGGTKGIGYAIVEELAGLGAEVYTCARNqkeLDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFgGKLNILVN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd05329   91 NAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGALNQLTRSL 170

                        170
                 ....*....|....*....
gi 530378355 163 AKEVARKKIRVNVVAPELI 181
Cdd:cd05329  171 ACEWAKDNIRVNAVAPWVI 189
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
3-192 1.11e-25

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 99.87  E-value: 1.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA--GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK08226   7 KTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADelCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVG-LKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08226  87 VNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYALTKAAIVGLT 166

                        170       180       190
                 ....*....|....*....|....*....|...
gi 530378355 160 RALAKEVARKKIRVNVVAPELIpRTVSIRKMEK 192
Cdd:PRK08226 167 KSLAVEYAQSGIRVNAICPGYV-RTPMAESIAR 198
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 3-178 1.15e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 99.98  E-value: 1.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDhlafsCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPGVELLE-----LDVTDDASVQAAVDEVIARAGRIDVLVN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:PRK06179  80 NAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVEGYSESL 159

                        170
                 ....*....|....*.
gi 530378355 163 AKEVARKKIRVNVVAP 178
Cdd:PRK06179 160 DHEVRQFGIRVSLVEP 175
PRK06914 PRK06914
SDR family oxidoreductase;
1-178 1.53e-25

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 100.10  E-value: 1.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAK-----AAAGDLGGDHLAFSCDVAKEHDVQNtFEELEKHLG 75
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQEnllsqATQLNLQQNIKVQQLDVTDQNSIHN-FQLVLKEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYAL 160

                        170       180
                 ....*....|....*....|...
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEP 183
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 3-178 1.65e-25

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: 99.08  E-value: 1.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELekhlGRVNFLVN 82
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGAN--VIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEE----GRIDVLFN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVG-LKGNSGQSVYSASKGGLVGFSRA 161
Cdd:cd05368   77 CAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYSTTKAAVIGLTKS 156

                        170
                 ....*....|....*..
gi 530378355 162 LAKEVARKKIRVNVVAP 178
Cdd:cd05368  157 VAADFAQQGIRCNAICP 173
PRK06114 PRK06114
SDR family oxidoreductase;
2-178 1.75e-25

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 99.47  E-value: 1.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD----LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06114   8 GQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEhieaAGRRAIQIAADVTSKADLRAAVARTEAELGAL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRdgllvRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSG--QSVYSA 150
Cdd:PRK06114  88 TLAVNAAGIAN-----ANPAEEMEEEqwqtvMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGllQAHYNA 162

                        170       180
                 ....*....|....*....|....*...
gi 530378355 151 SKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK06114 163 SKAGVIHLSKSLAMEWVGRGIRVNSISP 190
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 2-178 1.88e-25

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 99.31  E-value: 1.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK08265   6 GKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFGRVDILV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 N-AAGINRDGLlvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK08265  86 NlACTYLDDGL--ASSRADWLAALDVNLVSAAMLAQAAHPHLA-RGGGAIVNFTSISAKFAQTGRWLYPASKAAIRQLTR 162

                        170
                 ....*....|....*...
gi 530378355 161 ALAKEVARKKIRVNVVAP 178
Cdd:PRK08265 163 SMAMDLAPDGIRVNSVSP 180
PRK07856 PRK07856
SDR family oxidoreductase;
2-181 1.88e-25

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 99.24  E-value: 1.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlegAKAAAGDLGGDHLAfsCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07856   6 GRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR---APETVDGRPAEFHA--ADVRDPDQVAALVDAIVERHGRLDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK07856  81 NNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQpGGGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNLTR 160

                        170       180
                 ....*....|....*....|.
gi 530378355 161 ALAKEVArKKIRVNVVAPELI 181
Cdd:PRK07856 161 SLAVEWA-PKVRVNAVVVGLV 180
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 2-178 2.36e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 98.88  E-value: 2.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR---NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07890   5 GKVVVVSGVGPGLGRTLAVRAARAGADVVLAARtaeRLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVN-AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQqGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK07890  85 ALVNnAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAES-GGSIVMINSMVLRHSQPKYGAYKMAKGALLA 163

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVARKKIRVNVVAP 178
Cdd:PRK07890 164 ASQSLATELGPQGIRVNSVAP 184
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 2-178 2.60e-25

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 98.75  E-value: 2.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08937    4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEilAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGinrdGLLVR-----TKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNsgQSVYSASKGG 154
Cdd:cd08937   84 LINNVG----GTIWAkpyehYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGIY--RIPYSAAKGG 157

                        170       180
                 ....*....|....*....|....
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd08937  158 VNALTASLAFEHARDGIRVNAVAP 181
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 3-195 2.71e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 98.98  E-value: 2.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV---IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGATIVFndiNQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK07097  91 LVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGGLKMLT 170

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAPELI--PRTVSIR-KMEKGDR 195
Cdd:PRK07097 171 KNIASEYGEANIQCNGIGPGYIatPQTAPLReLQADGSR 209
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 2-178 4.43e-25

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: 98.68  E-value: 4.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd08935    5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEItalGGRAIALAADVLDRASLERAREEIVAQFGTVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINR-------DGLLVRTKT-------EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSG 144
Cdd:cd08935   85 ILINGAGGNHpdattdpEHYEPETEQnffdldeEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPLTK 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 145 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd08935  165 VPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAP 198
PRK09242 PRK09242
SDR family oxidoreductase;
2-184 5.40e-25

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 97.90  E-value: 5.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK09242   9 GQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeefpEREVHGLAADVSDDEDRRAILDWVEDHWDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINrdgllVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSAS 151
Cdd:PRK09242  89 LHILVNNAGGN-----IRKAAIDYTEDewrgiFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMT 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530378355 152 KGGLVGFSRALAKEVARKKIRVNVVAPELI--PRT 184
Cdd:PRK09242 164 KAALLQMTRNLAVEWAEDGIRVNAVAPWYIrtPLT 198
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 7-181 5.41e-25

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: 97.81  E-value: 5.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05359    3 VTGGSRGIGKAIALRLAERGADVVInYRKSKDAAAEVAAEieeLGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVLVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 --AAGINRDglLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:cd05359   83 naAAGAFRP--LSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVR 160

                        170       180
                 ....*....|....*....|.
gi 530378355 161 ALAKEVARKKIRVNVVAPELI 181
Cdd:cd05359  161 YLAVELGPRGIRVNAVSPGVI 181
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 2-181 7.07e-25

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: 97.69  E-value: 7.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05363    3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDILV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:cd05363   83 NNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCATKAAVISLTQ 162

                        170       180
                 ....*....|....*....|.
gi 530378355 161 ALAKEVARKKIRVNVVAPELI 181
Cdd:cd05363  163 SAGLNLIRHGINVNAIAPGVV 183
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 6-193 7.40e-25

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: 97.14  E-value: 7.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   6 AVF--GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEEL-EKHLGRVNFLV 81
Cdd:cd08931    2 AIFitGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVvAGALDVTDRAAWAAALADFaAATGGRLDALF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:cd08931   82 NNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEA 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530378355 162 LAKEVARKKIRVNVVAPELIpRTVSIRKMEKG 193
Cdd:cd08931  162 LDVEWARHGIRVADVWPWFV-DTPILTKGETG 192
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 3-178 8.13e-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: 96.92  E-value: 8.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKG-YRLAVIARNLEGAKAAAGDLGGDHL---AFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLRAEGLsvrFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGlkgnSGQSVYSASKGGLVG 157
Cdd:cd05324   81 ILVNNAGIAFKGFDDSTPTREQAREtMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLG----SLTSAYGVSKAALNA 156

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVARKKIRVNVVAP 178
Cdd:cd05324  157 LTRILAKELKETGIKVNACCP 177
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 2-185 1.15e-24

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 97.32  E-value: 1.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN--LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12823   8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSelVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGinrdGLlVRTK------TEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIvglkgnSGQSV----YS 149
Cdd:PRK12823  88 LINNVG----GT-IWAKpfeeyeEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSI------ATRGInrvpYS 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530378355 150 ASKGGLVGFSRALAKEVARKKIRVNVVAP---ELIPRTV 185
Cdd:PRK12823 157 AAKGGVNALTASLAFEYAEHGIRVNAVAPggtEAPPRRV 195
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 2-181 2.41e-24

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: 96.44  E-value: 2.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05330    3 DKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALleiapDAEVLLIKADVSDEAQVEAYVDATVEQFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGIN-RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:cd05330   83 IDGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGV 162

                        170       180
                 ....*....|....*....|....*.
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:cd05330  163 VGLTRNSAVEYGQYGIRINAIAPGAI 188
PRK08267 PRK08267
SDR family oxidoreductase;
6-181 3.19e-24

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 96.16  E-value: 3.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   6 AVF--GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEELEKHL-GRVNFLV 81
Cdd:PRK08267   3 SIFitGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAwTGALDVTDRAAWDAALADFAAATgGRLDVLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:PRK08267  83 NNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEA 162

                        170       180
                 ....*....|....*....|
gi 530378355 162 LAKEVARKKIRVNVVAPELI 181
Cdd:PRK08267 163 LDLEWRRHGIRVADVMPLFV 182
PRK07831 PRK07831
SDR family oxidoreductase;
13-180 3.37e-24

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 95.87  E-value: 3.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  13 GIGRAVAQLMARKGYRLAVI---ARNL-EGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGIN 87
Cdd:PRK07831  29 GIGSATARRALEEGARVVISdihERRLgETADELAAELGLGRVeAVVCDVTSEAQVDALIDAAVERLGRLDVLVNNAGLG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  88 RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMI-QQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEV 166
Cdd:PRK07831 109 GQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRaRGHGGVIVNNASVLGWRAQHGQAHYAAAKAGVMALTRCSALEA 188

                        170
                 ....*....|....
gi 530378355 167 ARKKIRVNVVAPEL 180
Cdd:PRK07831 189 AEYGVRINAVAPSI 202
PRK07774 PRK07774
SDR family oxidoreductase;
2-181 5.23e-24

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 95.20  E-value: 5.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07774   6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIvadGGTAIAVQVDVSDPDSAKAMADATVSAFGGID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRD---GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVG-LKGNsgqsVYSASKGG 154
Cdd:PRK07774  86 YLVNNAAIYGGmklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAwLYSN----FYGLAKVG 161

                        170       180
                 ....*....|....*....|....*..
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK07774 162 LNGLTQQLARELGGMNIRVNAIAPGPI 188
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 7-178 5.32e-24

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: 95.23  E-value: 5.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAGdlgGDHL-AFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:cd05331    3 VTGAAQGIGRAVARHLLQAGAT--VIALDLPFVLLLEY---GDPLrLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKE 165
Cdd:cd05331   78 VLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLE 157

                        170
                 ....*....|...
gi 530378355 166 VARKKIRVNVVAP 178
Cdd:cd05331  158 LAPYGVRCNVVSP 170
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 2-178 5.72e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 95.38  E-value: 5.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07478   6 GKVAIITGASSGIGRAAAKLFAREGAKVVVGARRqaeLDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGGLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLK-GNSGQSVYSASKGGLV 156
Cdd:PRK07478  86 IAFNNAGTLGEMGPVAEMSLEGWREtLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTaGFPGMAAYAASKAGLI 165

                        170       180
                 ....*....|....*....|..
gi 530378355 157 GFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK07478 166 GLTQVLAAEYGAQGIRVNALLP 187
PRK07062 PRK07062
SDR family oxidoreductase;
2-174 1.17e-23

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 94.72  E-value: 1.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK07062   8 GRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFpgarlLAARCDVLDEADVAAFAAAVEARFGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK07062  88 VDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAARAGLL 167

                        170
                 ....*....|....*...
gi 530378355 157 GFSRALAKEVARKKIRVN 174
Cdd:PRK07062 168 NLVKSLATELAPKGVRVN 185
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 1-178 1.49e-23

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: 94.44  E-value: 1.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGyrlAVIARNLEGAKA--------AAGDLGGDHLAFSCDVAKEHDVQNTFEELEK 72
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAG---ANIVLNGFGDAAeieavragLAAKHGVKVLYHGADLSKPAAIEDMVAYAQR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  73 HLGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASK 152
Cdd:cd08940   78 QFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAK 157

                        170       180
                 ....*....|....*....|....*.
gi 530378355 153 GGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd08940  158 HGVVGLTKVVALETAGTGVTCNAICP 183
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-192 1.64e-23

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 94.03  E-value: 1.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIA--RNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06935  16 KVAIVTGGNTGLGQGYAVALAKAGADIIITThgTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDIL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK06935  96 VNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTASKHGVAGLTK 175

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 161 ALAKEVARKKIRVNVVAPELIP--RTVSIRKMEK 192
Cdd:PRK06935 176 AFANELAAYNIQVNAIAPGYIKtaNTAPIRADKN 209
PLN02253 PLN02253
xanthoxin dehydrogenase
 3-195 2.05e-23

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 94.50  E-value: 2.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLA--FSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PLN02253  19 KVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVcfFHCDVTVEDDVSRAVDFTVDKFGTLDIM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PLN02253  99 VNNAGLTGPPCpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSKHAVLGL 178

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530378355 159 SRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKGDR 195
Cdd:PLN02253 179 TRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDER 215
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 3-178 2.88e-23

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 93.41  E-value: 2.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKaaagdlgGDHLA-FSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQE-------DYPFAtFVLDVSDAAAVAQVCQRLLAETGPLDVLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:PRK08220  82 NAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSLAKC 161

                        170
                 ....*....|....*..
gi 530378355 162 LAKEVARKKIRVNVVAP 178
Cdd:PRK08220 162 VGLELAPYGVRCNVVSP 178
PRK07069 PRK07069
short chain dehydrogenase; Validated
 7-181 3.80e-23

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 92.85  E-value: 3.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARN-LEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLTDINdAAGLDAFAAEINAAHgegvaFAAVQDVTDEAQWQALLAQAADAMGGLSVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK07069  84 VNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVASLTK 163

                        170       180
                 ....*....|....*....|...
gi 530378355 161 ALAKEVARKK--IRVNVVAPELI 181
Cdd:PRK07069 164 SIALDCARRGldVRCNSIHPTFI 186
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 2-181 3.98e-23

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 93.25  E-value: 3.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR-NLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08936   7 GKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIkkaGGEAIAVKGDVTVESDVVNLIQTAVKEFGTL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK08936  87 DVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPLFVHYAASKGGVK 166

                        170       180
                 ....*....|....*....|....*
gi 530378355 157 GFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK08936 167 LMTETLAMEYAPKGIRVNNIGPGAI 191
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-181 4.48e-23

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 93.10  E-value: 4.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK12745   1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINDRpddeELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGI---NRDGLLvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG------GSIVNVGSIVGLKGNSGQSV 147
Cdd:PRK12745  81 IDCLVNNAGVgvkVRGDLL-DLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVSPNRGE 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 148 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK12745 160 YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLI 193
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-177 4.86e-23

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 92.86  E-value: 4.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-ARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEieaLGRKALAVKANVGDVEKIKEMFAQIDEEFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVN--AAGINRDGLLVRTKTEDMVsqLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGG 154
Cdd:PRK08063  83 LDVFVNnaASGVLRPAMELEESHWDWT--MNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKAA 160

                        170       180
                 ....*....|....*....|...
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVA 177
Cdd:PRK08063 161 LEALTRYLAVELAPKGIAVNAVS 183
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 9-182 5.77e-23

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: 92.53  E-value: 5.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINR 88
Cdd:COG3967   12 GGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLH-TIVLDVADPASIAALAEQVTAEFPDLNVLINNAGIMR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  89 DGLLVRTKT--EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALakev 166
Cdd:COG3967   91 AEDLLDEAEdlADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYTQSL---- 166

                        170
                 ....*....|....*....
gi 530378355 167 aR---KKIRVNVVapELIP 182
Cdd:COG3967  167 -RhqlKDTSVKVI--ELAP 182
PRK07201 PRK07201
SDR family oxidoreductase;
3-171 1.26e-22

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 95.02  E-value: 1.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGATVFLVARNgeaLDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDY 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGinRDgllVRTKTEDMVSQLH-------TNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIvGLKGNSGQ-SVYSAS 151
Cdd:PRK07201 452 LVNNAG--RS---IRRSVENSTDRFHdyertmaVNYFGAVRLILGLLPHMRERRFGHVVNVSSI-GVQTNAPRfSAYVAS 525

                        170       180
                 ....*....|....*....|
gi 530378355 152 KGGLVGFSRALAKEVARKKI 171
Cdd:PRK07201 526 KAALDAFSDVAASETLSDGI 545
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-181 1.28e-22

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 91.71  E-value: 1.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06077   6 DKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKkraeEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK06077  86 DILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKAAVIN 163

                        170       180
                 ....*....|....*....|....
gi 530378355 158 FSRALAKEVArKKIRVNVVAPELI 181
Cdd:PRK06077 164 LTKYLALELA-PKIRVNAIAPGFV 186
PRK07832 PRK07832
SDR family oxidoreductase;
3-178 1.79e-22

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 91.64  E-value: 1.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD---LGG---DHLAFscDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADaraLGGtvpEHRAL--DISDYDAVAAFAADIHAAHGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK07832  79 MDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAgRGGHLVNVSSAAGLVALPWHAAYSASKFGL 158

                        170       180
                 ....*....|....*....|...
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK07832 159 RGLSEVLRFDLARHGIGVSVVVP 181
PRK12743 PRK12743
SDR family oxidoreductase;
1-178 2.26e-22

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 91.25  E-value: 2.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-ARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITwHSDEEGAKETAEEvrsHGVRAEIRQLDLSDLPEGAQALDKLIQRLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK12743  81 IDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAAKHAL 160

                        170       180
                 ....*....|....*....|...
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK12743 161 GGLTKAMALELVEHGILVNAVAP 183
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 2-181 2.54e-22

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


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 91.03  E-value: 2.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05343    6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECqsagYPTLFPYQCDLSNEEQILSMFSAIRTQHQGV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ--QGGSIVNVGSIVG--LKGNSGQSVYSASKG 153
Cdd:cd05343   86 DVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERnvDDGHIININSMSGhrVPPVSVFHFYAATKH 165

                        170       180       190
                 ....*....|....*....|....*....|
gi 530378355 154 GLVGFSRALAKEV--ARKKIRVNVVAPELI 181
Cdd:cd05343  166 AVTALTEGLRQELreAKTHIRATSISPGLV 195
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 9-178 3.25e-22

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 90.58  E-value: 3.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK08085  16 GSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLrqeGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVLINNAG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKE 165
Cdd:PRK08085  96 IQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGAVKMLTRGMCVE 175

                        170
                 ....*....|...
gi 530378355 166 VARKKIRVNVVAP 178
Cdd:PRK08085 176 LARHNIQVNGIAP 188
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-178 4.66e-22

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 89.64  E-value: 4.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAGDLGgdhlafscdvAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQ--VYGVDKQDKPDLSGNFH----------FLQLDLSDDLEPLFDWVPSVDIL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGInRDGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PRK06550  72 CNTAGI-LDDYkpLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGF 150

                        170       180
                 ....*....|....*....|
gi 530378355 159 SRALAKEVARKKIRVNVVAP 178
Cdd:PRK06550 151 TKQLALDYAKDGIQVFGIAP 170
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 3-178 4.76e-22

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: 90.29  E-value: 4.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08945    4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELreaGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRT--MIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:cd08945   84 LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVG 163

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVARKKIRVNVVAP 178
Cdd:cd08945  164 FTKALGLELARTGITVNAVCP 184
PRK05855 PRK05855
SDR family oxidoreductase;
2-181 2.25e-21

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 91.20  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAeliRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPD 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK05855 395 IVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAYAPSRSLPAYATSKAAVLM 474

                        170       180
                 ....*....|....*....|....
gi 530378355 158 FSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK05855 475 LSECLRAELAAAGIGVTAICPGFV 498
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 2-186 2.50e-21

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 88.37  E-value: 2.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFS---CDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd08936   10 NKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTgtvCHVGKAEDRERLVATAVNLHGGVD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINR-DGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:cd08936   90 ILVSNAAVNPfFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKTALLG 169

                        170       180
                 ....*....|....*....|....*....
gi 530378355 158 FSRALAKEVARKKIRVNVVAPELIPRTVS 186
Cdd:cd08936  170 LTKNLAPELAPRNIRVNCLAPGLIKTSFS 198
PRK07775 PRK07775
SDR family oxidoreductase;
7-178 2.75e-21

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 88.66  E-value: 2.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK07775  15 VAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIradGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLVSG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALA 163
Cdd:PRK07775  95 AGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTNLQ 174

                        170
                 ....*....|....*
gi 530378355 164 KEVARKKIRVNVVAP 178
Cdd:PRK07775 175 MELEGTGVRASIVHP 189
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 3-184 3.10e-21

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 88.58  E-value: 3.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV--IARNLEGAKAAAG----------DLGGDHLAFSCDVAKEHDVQNTFEEL 70
Cdd:PRK07791   7 RVVIVTGAGGGIGRAHALAFAAEGARVVVndIGVGLDGSASGGSaaqavvdeivAAGGEAVANGDDIADWDGAANLVDAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  71 EKHLGRVNFLVNAAGINRDGLLVRTKTE--DMVSQLHtnLLGSMLTCK-AAMRTMIQQQGG-----SIVNVGSIVGLKGN 142
Cdd:PRK07791  87 VETFGGLDVLVNNAGILRDRMIANMSEEewDAVIAVH--LKGHFATLRhAAAYWRAESKAGravdaRIINTSSGAGLQGS 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530378355 143 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPelIPRT 184
Cdd:PRK07791 165 VGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP--AART 204
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 7-178 5.49e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 87.27  E-value: 5.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:PRK06523  14 VTGGTKGIGAATVARLLEAGARVVTTARS------RPDDLPEGVEFVAADLTTAEGCAAVARAVLERLGGVDILVHVLGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 NR---DGLLVRTKtEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVG-LKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:PRK06523  88 SSapaGGFAALTD-EEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRrLPLPESTTAYAAAKAALSTYSKSL 166

                        170
                 ....*....|....*.
gi 530378355 163 AKEVARKKIRVNVVAP 178
Cdd:PRK06523 167 SKEVAPKGVRVNTVSP 182
PRK06128 PRK06128
SDR family oxidoreductase;
9-178 6.90e-21

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 87.99  E-value: 6.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA-----GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK06128  62 GADSGIGRATAIAFAREGADIALNYLPEEEQDAAEvvqliQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGLDILVNI 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  84 AG---INRDglLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK06128 142 AGkqtAVKD--IADITTEQFDATFKTNVYAMFWLCKAAIPHL--PPGASIINTGSIQSYQPSPTLLDYASTKAAIVAFTK 217

                        170
                 ....*....|....*...
gi 530378355 161 ALAKEVARKKIRVNVVAP 178
Cdd:PRK06128 218 ALAKQVAEKGIRVNAVAP 235
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-203 8.34e-21

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: 86.56  E-value: 8.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD----LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05357    5 VTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDelnaLRNSAVLVQADLSDFAACADLVAAAFRAFGRCDVLVN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd05357   85 NASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLTRSA 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530378355 163 AKEVArKKIRVNVVAPELIPRTVsirKMEKGDRINVTLRSP 203
Cdd:cd05357  165 ALELA-PNIRVNGIAPGLILLPE---DMDAEYRENALRKVP 201
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 2-178 1.46e-20

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: 86.00  E-value: 1.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08942    6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSayGECIAIPADLSSEEGIEALVARVAERSDRLDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLL--VRTKTEDMVSQLHTNllgSMLTCKAAMRTMIQQQG-----GSIVNVGSIVGLKGNSGQSV-YSAS 151
Cdd:cd08942   86 LVNNAGATWGAPLeaFPESGWDKVMDINVK---SVFFLTQALLPLLRAAAtaenpARVINIGSIAGIVVSGLENYsYGAS 162

                        170       180
                 ....*....|....*....|....*..
gi 530378355 152 KGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd08942  163 KAAVHQLTRKLAKELAGEHITVNAIAP 189
PRK06139 PRK06139
SDR family oxidoreductase;
2-167 2.72e-20

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 86.70  E-value: 2.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06139   7 GAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEecrALGAEVLVVPTDVTDADQVKALATQAASFGGRID 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PRK06139  87 VWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLRGF 166


                 ....*....
gi 530378355 159 SRALAKEVA 167
Cdd:PRK06139 167 SEALRGELA 175
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-178 3.33e-20

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 85.99  E-value: 3.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV--IARNLEGAKAAA--GDLGGDHLAFSCDVAkEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07792  13 KVAVVTGAAAGLGRAEALGLARLGATVVVndVASALDASDVLDeiRAAGAKAVAVAGDIS-QRATADELVATAVGLGGLD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAM---RTMIQQQGGS----IVNVGSIVGLKGNSGQSVYSAS 151
Cdd:PRK07792  92 IVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAaywRAKAKAAGGPvygrIVNTSSEAGLVGPVGQANYGAA 171

                        170       180
                 ....*....|....*....|....*..
gi 530378355 152 KGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK07792 172 KAGITALTLSAARALGRYGVRANAICP 198
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 2-175 3.79e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 85.79  E-value: 3.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAF--SCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK05872   9 GKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLtvVADVTDLAAMQAAAEEAVERFGGIDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK05872  89 VVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALI-ERRGYVLQVSSLAAFAAAPGMAAYCASKAGVEAFA 167

                        170
                 ....*....|....*.
gi 530378355 160 RALAKEVARKKIRVNV 175
Cdd:PRK05872 168 NALRLEVAHHGVTVGS 183
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 3-181 3.85e-20

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: 84.94  E-value: 3.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLaVIARNLEGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKV-VFADIDEERGADFAEAEGPNLFFvHGDVADETLVKFVVYAMLEKLGRIDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:cd09761   81 NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELI-KNKGRIINIASTRAFQSEPDSEAYAASKGGLVALTHA 159

                        170       180
                 ....*....|....*....|
gi 530378355 162 LAKEVARkKIRVNVVAPELI 181
Cdd:cd09761  160 LAMSLGP-DIRVNCISPGWI 178
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 4-178 2.56e-19

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


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 82.62  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAiqqAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VN-AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:cd05365   81 VNnAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMT 160

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAP 178
Cdd:cd05365  161 RNLAFDLGPKGIRVNAVAP 179
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 2-190 2.84e-19

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: 83.04  E-value: 2.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFS-CDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIkketGNAKVEVIqLDLSSLASVRQFAEEFLARFPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGInrdGLLVRTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGN------------- 142
Cdd:cd05327   81 LDILINNAGI---MAPPRRLTKDgFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPidfndldlennke 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 530378355 143 -SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVSIRKM 190
Cdd:cd05327  158 ySPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVV-RTELLRRN 205
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 2-181 3.21e-19

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 82.59  E-value: 3.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06113  11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVdeiQQLGGQAFACRCDITSEQELSALADFALSKLGKVD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGF 158
Cdd:PRK06113  91 ILVNNAGGGGPKPF-DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHL 169

                        170       180
                 ....*....|....*....|...
gi 530378355 159 SRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK06113 170 VRNMAFDLGEKNIRVNGIAPGAI 192
PRK07577 PRK07577
SDR family oxidoreductase;
2-178 7.84e-19

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 81.31  E-value: 7.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaAAGDLGGDHLAfsCDVAKEHDVQNTFEELEKHlGRVNFLV 81
Cdd:PRK07577   3 SRTVLVTGATKGIGLALSLRLANLGHQVIGIARS------AIDDFPGELFA--CDLADIEQTAATLAQINEI-HPVDAIV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIvGLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:PRK07577  74 NNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSR-AIFGALDRTSYSAAKSALVGCTRT 152

                        170
                 ....*....|....*..
gi 530378355 162 LAKEVARKKIRVNVVAP 178
Cdd:PRK07577 153 WALELAEYGITVNAVAP 169
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 2-178 1.25e-18

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: 81.24  E-value: 1.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05348    4 GEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGKLDCFI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGLLVRTKTEDMVSQL-----HTNLLGSMLTCKAAMRTMIQQQGGSIVNVgSIVGLKGNSGQSVYSASKGGLV 156
Cdd:cd05348   84 GNAGIWDYSTSLVDIPEEKLDEAfdelfHINVKGYILGAKAALPALYATEGSVIFTV-SNAGFYPGGGGPLYTASKHAVV 162

                        170       180
                 ....*....|....*....|..
gi 530378355 157 GFSRALAKEVArKKIRVNVVAP 178
Cdd:cd05348  163 GLVKQLAYELA-PHIRVNGVAP 183
PRK08264 PRK08264
SDR family oxidoreductase;
2-173 1.54e-18

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 80.32  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRA-VAQLMARKGYRLAVIARNLEGAKaaagDLGGDHLAFSCDVAKEHDVQntfeELEKHLGRVNFL 80
Cdd:PRK08264   6 GKVVLVTGANRGIGRAfVEQLLARGAAKVYAAARDPESVT----DLGPRVVPLQLDVTDPASVA----AAAEAASDVTIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08264  78 VNNAGIFRTGSLLLEGDEDaLRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWSLT 157

                        170
                 ....*....|....
gi 530378355 160 RALAKEVARKKIRV 173
Cdd:PRK08264 158 QALRAELAPQGTRV 171
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 4-181 2.03e-18

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: 80.58  E-value: 2.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDLpdddQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGIN---RDGLLvrTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQG------GSIVNVGSI--VGLKGNSGQsv 147
Cdd:cd05337   83 LVNNAGIAvrpRGDLL--DLTEDSFDRLiAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSInaYLVSPNRGE-- 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 148 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:cd05337  159 YCISKAGLSMATRLLAYRLADEGIAVHEIRPGLI 192
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 7-178 4.35e-18

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 78.72  E-value: 4.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEElekhLGRVNFLVNAAGI 86
Cdd:cd11730    3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGA--LARPADVAAELEVWALAQE----LGPLDLLVYAAGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqqQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEV 166
Cdd:cd11730   77 ILGKPLARTKPAAWRRILDANLTGAALVLKHALALLA--AGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVARKEV 154

                        170
                 ....*....|..
gi 530378355 167 arKKIRVNVVAP 178
Cdd:cd11730  155 --RGLRLTLVRP 164
PRK09186 PRK09186
flagellin modification protein A; Provisional
 2-178 4.90e-18

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 79.65  E-value: 4.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGD-----HLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK09186   4 GKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEfkskkLSLVELDITDQESLEEFLSKSAEKYGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAginrdglLVRTKT----------EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGL------- 139
Cdd:PRK09186  84 IDGAVNCA-------YPRNKDygkkffdvslDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVvapkfei 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530378355 140 -KGNSGQSV--YSASKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK09186 157 yEGTSMTSPveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSP 198
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 2-192 6.70e-18

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: 79.05  E-value: 6.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEgakaaagDLggDHLAFSC--------DVAkehDVQNTFEELEKH 73
Cdd:cd05351    7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQA-------DL--DSLVRECpgiepvcvDLS---DWDATEEALGSV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  74 lGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGSIVGLKGNSGQSVYSASK 152
Cdd:cd05351   75 -GPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCSTK 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530378355 153 GGLVGFSRALAKEVARKKIRVNVVAPeliprTVSIRKMEK 192
Cdd:cd05351  154 AALDMLTKVMALELGPHKIRVNSVNP-----TVVMTDMGR 188
PRK06500 PRK06500
SDR family oxidoreductase;
1-178 1.25e-17

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 78.07  E-value: 1.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06500   5 QGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGRLDAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTkTEDMVSQL-HTNLLGSMLTCKAAMRtmIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK06500  85 FINAGVAKFAPLEDW-DEAMFDRSfNTNVKGPYFLIQALLP--LLANPASIVLNGSINAHIGMPNSSVYAASKAALLSLA 161

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAP 178
Cdd:PRK06500 162 KTLSGELLPRGIRVNAVSP 180
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 2-178 2.10e-17

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 77.69  E-value: 2.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06200   6 GQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCFV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRDGL-LVRTKTEDMVSQL----HTNLLGSMLTCKAAMRTMIqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK06200  86 GNAGIWDYNTsLVDIPAETLDTAFdeifNVNVKGYLLGAKAALPALK-ASGGSMIFTLSNSSFYPGGGGPLYTASKHAVV 164

                        170       180
                 ....*....|....*....|..
gi 530378355 157 GFSRALAKEVArKKIRVNVVAP 178
Cdd:PRK06200 165 GLVRQLAYELA-PKIRVNGVAP 185
PRK06182 PRK06182
short chain dehydrogenase; Validated
 3-181 6.63e-17

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 76.54  E-value: 6.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAgDLGGDHLAFscDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLA-SLGVHPLSL--DVTDEASIKAAVDTIIAEEGRIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:PRK06182  81 NAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDAL 160

                        170
                 ....*....|....*....
gi 530378355 163 AKEVARKKIRVNVVAPELI 181
Cdd:PRK06182 161 RLEVAPFGIDVVVIEPGGI 179
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 7-178 8.10e-17

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 74.93  E-value: 8.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaaagdlGGDHLafsCDVAKEHDVQNTFEElekhLGRVNFLVNAAGI 86
Cdd:cd11731    3 VIGATGTIGLAVAQLLSAHGHEVITAGRS-----------SGDYQ---VDITDEASIKALFEK----VGHFDAIVSTAGD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEV 166
Cdd:cd11731   65 AEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAIEL 142

                        170
                 ....*....|..
gi 530378355 167 ARkKIRVNVVAP 178
Cdd:cd11731  143 PR-GIRINAVSP 153
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 7-178 8.19e-17

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 75.81  E-value: 8.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:cd05370   10 ITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNIH-TIVLDVGDAESVEALAEALLSEYPNLDILINNAGI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 --NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAK 164
Cdd:cd05370   89 qrPIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAALHSYTLALRH 168

                        170
                 ....*....|....
gi 530378355 165 EVARKKIRVNVVAP 178
Cdd:cd05370  169 QLKDTGVEVVEIVP 182
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 4-178 9.49e-17

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: 75.79  E-value: 9.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   4 VCAVFGGSRGIGRAVAQLMARKGY--RLAVIARNLEGAKAAAGDL-GGDHLAF-SCDVAKEHDVQNTFEEL-EKHLGRVN 78
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEELrPGLRVTTvKADLSDAAGVEQLLEAIrKLDGERDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:cd05367   81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAARDM 160

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEvaRKKIRVNVVAP 178
Cdd:cd05367  161 FFRVLAAE--EPDVRVLSYAP 179
PRK06482 PRK06482
SDR family oxidoreductase;
1-178 1.22e-16

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 75.92  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLegakAAAGDLG---GDHL-AFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK06482   1 MSKTWFITGASSGFGRGMTERLLARGDRVAATVRRP----DALDDLKaryGDRLwVLQLDVTDSAAVRAVVDRAFAALGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK06482  77 IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIE 156

                        170       180
                 ....*....|....*....|..
gi 530378355 157 GFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK06482 157 GFVEAVAQEVAPFGIEFTIVEP 178
PRK08251 PRK08251
SDR family oxidoreductase;
9-181 1.79e-16

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 74.97  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK08251   9 GASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYpgikvAVAALDVNDHDQVFEVFAEFRDELGGLDRVIVN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSG-QSVYSASKGGLVGFSRAL 162
Cdd:PRK08251  89 AGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGvKAAYAASKAGVASLGEGL 168

                        170
                 ....*....|....*....
gi 530378355 163 AKEVARKKIRVNVVAPELI 181
Cdd:PRK08251 169 RAELAKTPIKVSTIEPGYI 187
PRK06949 PRK06949
SDR family oxidoreductase;
3-181 2.51e-16

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 74.80  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIeaeGGAAHVVSLDVTDYQSIKAAVAHAETEAGTIDI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGS--------IVNVGSIVGLKGNSGQSVYSAS 151
Cdd:PRK06949  90 LVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASVAGLRVLPQIGLYCMS 169

                        170       180       190
                 ....*....|....*....|....*....|
gi 530378355 152 KGGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK06949 170 KAAVVHMTRAMALEWGRHGINVNAICPGYI 199
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 7-196 2.56e-16

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 74.99  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLraeGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFSN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:PRK05876  91 AGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQgTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAETL 170

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 163 AKEVARKKIRVNVvapeLIPRTVSIRKMEKGDRI 196
Cdd:PRK05876 171 AREVTADGIGVSV----LCPMVVETNLVANSERI 200
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 7-178 3.84e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 74.42  E-value: 3.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFscDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07523  15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGlsahaLAF--DVTDHDAVRAAIDAFEAEIGPIDILV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAGINRdgllvRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK07523  93 NNAGMQF-----RTPLEDFPADaferlLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAVG 167

                        170       180
                 ....*....|....*....|..
gi 530378355 157 GFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK07523 168 NLTKGMATDWAKHGLQCNAIAP 189
PRK05866 PRK05866
SDR family oxidoreductase;
9-176 3.85e-16

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 74.78  E-value: 3.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK05866  47 GASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRItraGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILINNAG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  86 INrdgllVRTKTEDMVSQLH-------TNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQ-SVYSASKGGLVG 157
Cdd:PRK05866 127 RS-----IRRPLAESLDRWHdvertmvLNYYAPLRLIRGLAPGMLERGDGHIINVATWGVLSEASPLfSVYNASKAALSA 201

                        170
                 ....*....|....*....
gi 530378355 158 FSRALAKEVARKKIRVNVV 176
Cdd:PRK05866 202 VSRVIETEWGDRGVHSTTL 220
PRK05693 PRK05693
SDR family oxidoreductase;
3-181 4.71e-16

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 74.44  E-value: 4.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLE--GAKAAAGdlggdHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEdvEALAAAG-----FTAVQLDVNDGAALARLAEELEAEHGGLDVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLgSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK05693  77 INNAGYGAMGPLLDGGVEAMRRQFETNVF-AVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSD 155

                        170       180
                 ....*....|....*....|.
gi 530378355 161 ALAKEVARKKIRVNVVAPELI 181
Cdd:PRK05693 156 ALRLELAPFGVQVMEVQPGAI 176
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 2-178 5.31e-16

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: 73.60  E-value: 5.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQ-LMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKehdvQNTFEELEKHLGRVNFL 80
Cdd:cd05354    3 DKTVLVTGANRGIGKAFVEsLLAHGAKKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTD----PESIKAAAAQAKDVDVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINR-DGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:cd05354   79 INNAGVLKpATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSLT 158

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAP 178
Cdd:cd05354  159 QGLRAELAAQGTLVLSVHP 177
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
7-204 6.48e-16

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 73.56  E-value: 6.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIAR--NLEGAKAAaGDLGGDHLAFSCDVAKEHDVQNTFEE----LEKHLGRVNFL 80
Cdd:PRK06924   6 ITGTSQGLGEAIANQLLEKGTHVISISRteNKELTKLA-EQYNSNLTFHSLDLQDVHELETNFNEilssIQEDNVSSIHL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAG----INRDGllvRTKTEDMVSQLHTNLLGSMLTCKAAM-RTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK06924  85 INNAGmvapIKPIE---KAESEELITNVHLNLLAPMILTSTFMkHTKDWKVDKRVINISSGAAKNPYFGWSAYCSSKAGL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530378355 156 VGFSRALAKEVARKKIRVNVVApeLIPRTV------SIRKMEKGDRINV----------TLRSPE 204
Cdd:PRK06924 162 DMFTQTVATEQEEEEYPVKIVA--FSPGVMdtnmqaQIRSSSKEDFTNLdrfitlkeegKLLSPE 224
PRK09135 PRK09135
pteridine reductase; Provisional
 1-178 7.31e-16

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 73.42  E-value: 7.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN-LEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELnalrPGSAAALQADLLDPDALPELVAACVAAFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGinrdgLLVRTKTEDMVSQLHTNLLGSMLtcKA------AMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYS 149
Cdd:PRK09135  85 RLDALVNNAS-----SFYPTPLGSITEAQWDDLFASNL--KApfflsqAAAPQLRKQRGAIVNITDIHAERPLKGYPVYC 157

                        170       180
                 ....*....|....*....|....*....
gi 530378355 150 ASKGGLVGFSRALAKEVArKKIRVNVVAP 178
Cdd:PRK09135 158 AAKAALEMLTRSLALELA-PEVRVNAVAP 185
PRK08219 PRK08219
SDR family oxidoreductase;
1-178 7.93e-16

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 73.04  E-value: 7.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARkGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEelekHLGRVNFL 80
Cdd:PRK08219   2 ERPTALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELAAELPGAT-PFPVDLTDPEAIAAAVE----QLGRLDVL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSM-LTckAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08219  76 VHNAGVADLGPVAESTVDEWRATLEVNVVAPAeLT--RLLLPALRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALA 153

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEvARKKIRVNVVAP 178
Cdd:PRK08219 154 DALREE-EPGNVRVTSVHP 171
PRK07814 PRK07814
SDR family oxidoreductase;
2-178 8.52e-16

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 73.66  E-value: 8.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07814  10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEqirAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK07814  90 IVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGgGSVINISSTMGRLAGRGFAAYGTAKAALAH 169

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVArKKIRVNVVAP 178
Cdd:PRK07814 170 YTRLAALDLC-PRIRVNAIAP 189
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 3-184 2.60e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 72.02  E-value: 2.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTkekLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINrdgLLVRtkTEDMV-----SQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGqSVYSAS-K 152
Cdd:PRK07677  82 LINNAAGN---FICP--AEDLSvngwnSVIDIVLNGTFYCSQAVGKYWIEKgIKGNIINMVATYAWDAGPG-VIHSAAaK 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 530378355 153 GGLVGFSRALAKEVARK-KIRVNVVAPELIPRT 184
Cdd:PRK07677 156 AGVLAMTRTLAVEWGRKyGIRVNAIAPGPIERT 188
PRK06194 PRK06194
hypothetical protein; Provisional
 3-182 4.09e-15

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 71.97  E-value: 4.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLA---VIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06194   7 KVAVITGAASGFGLAFARIGAALGMKLVladVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ------QGGSIVNVGSIVGLKGNSGQSVYSASKG 153
Cdd:PRK06194  87 LFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpaYEGHIVNTASMAGLLAPPAMGIYNVSKH 166

                        170       180       190
                 ....*....|....*....|....*....|.
gi 530378355 154 GLVGFSRALAK--EVARKKIRVNVVAPELIP 182
Cdd:PRK06194 167 AVVSLTETLYQdlSLVTDQVGASVLCPYFVP 197
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 7-178 4.52e-15

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: 71.17  E-value: 4.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRA-VAQLMARKGYRLAVIARNLEGAKAAAGdLGGDHLAFSC---DVAKEhdVQNTFEELEKHLG--RVNFL 80
Cdd:cd05325    3 ITGASRGIGLElVRQLLARGNNTVIATCRDPSAATELAA-LGASHSRLHIlelDVTDE--IAESAEAVAERLGdaGLDVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKT-EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVG---LKGNSGQSVYSASKGGLV 156
Cdd:cd05325   80 INNAGILHSYGPASEVDsEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsigDNTSGGWYSYRASKAALN 159

                        170       180
                 ....*....|....*....|..
gi 530378355 157 GFSRALAKEVARKKIRVNVVAP 178
Cdd:cd05325  160 MLTKSLAVELKRDGITVVSLHP 181
PRK07024 PRK07024
SDR family oxidoreductase;
7-178 4.74e-15

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 71.50  E-value: 4.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VF--GGSRGIGRAVAQLMARKGYRLAVIARNLEG--AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK07024   5 VFitGASSGIGQALAREYARQGATLGLVARRTDAlqAFAARLPKAARVSVYAADVRDADALAAAAADFIAAHGLPDVVIA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRdGLLVRTkTED---MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK07024  85 NAGISV-GTLTEE-REDlavFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYL 162

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAP 178
Cdd:PRK07024 163 ESLRVELRPAGVRVVTIAP 181
PRK05717 PRK05717
SDR family oxidoreductase;
3-191 6.10e-15

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 71.07  E-value: 6.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALVC 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGIN--RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMrTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK05717  91 NAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCA-PYLRAHNGAIVNLASTRARQSEPDTEAYAASKGGLLALTH 169

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530378355 161 ALAKEVArKKIRVNVVAPELI-PRTVSIRKME 191
Cdd:PRK05717 170 ALAISLG-PEIRVNAVSPGWIdARDPSQRRAE 200
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-178 7.32e-15

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 70.70  E-value: 7.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGyrLAVIARNLEGA---KAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12481   9 KVAIITGCNTGLGQGMAIGLAKAG--ADIVGVGVAEApetQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINR--DGLLVRTKTEDMVSQLHTNLLgSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK12481  87 LINNAGIIRrqDLLEFGNKDWDDVININQKTV-FFLSQAVAKQFVKQGNGGKIINIASMLSFQGGIRVPSYTASKSAVMG 165

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVARKKIRVNVVAP 178
Cdd:PRK12481 166 LTRALATELSQYNINVNAIAP 186
PRK07041 PRK07041
SDR family oxidoreductase;
7-181 8.54e-15

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 70.07  E-value: 8.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH--LAFSCDVAKEHDVQNTFEElekhLGRVNFLVNAA 84
Cdd:PRK07041   2 VVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGApvRTAALDITDEAAVDAFFAE----AGPFDHVVITA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  85 GINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAmrtmIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAK 164
Cdd:PRK07041  78 ADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAA----RIAPGGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLAL 153

                        170
                 ....*....|....*..
gi 530378355 165 EVArkKIRVNVVAPELI 181
Cdd:PRK07041 154 ELA--PVRVNTVSPGLV 168
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 3-204 2.87e-14

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 69.40  E-value: 2.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHL-GRV 77
Cdd:cd09763    4 KIALVTGASRGIGRGIALQLGEAGATVYITGRTilpqLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQqGRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAA-GINRDGLLVRTKT---------EDMVSqlhTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKgNSGQSV 147
Cdd:cd09763   84 DILVNNAyAAVQLILVGVAKPfweepptiwDDINN---VGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLE-YLFNVA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530378355 148 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVSIRKMEKGDRINVTLRSPE 204
Cdd:cd09763  160 YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFV-RTELVLEMPEDDEGSWHAKERD 215
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 2-178 5.84e-14

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 67.99  E-value: 5.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAK------AAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:cd05340    4 DRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRqvadhiNEEGGRQPQWFILDLLTCTSENCQQLAQRIAVNYP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVN-FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGG 154
Cdd:cd05340   84 RLDgVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFA 163

                        170       180
                 ....*....|....*....|....
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd05340  164 TEGL*QVLADEYQQRNLRVNCINP 187
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 3-178 5.94e-14

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: 68.26  E-value: 5.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMAR---KGYRLAVIARNL---EGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKhlG 75
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLkkkGRLWEAAGALAGGTLETlQLDVCDSKSVAAAVERVTE--R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:cd09806   79 HVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFAL 158

                        170       180
                 ....*....|....*....|...
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd09806  159 EGLCESLAVQLLPFNVHLSLIEC 181
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-178 9.14e-14

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 67.98  E-value: 9.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVI-----ARNLEGAKAaagdLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08993  11 KVAVVTGCDTGLGQGMALGLAEAGCDIVGInivepTETIEQVTA----LGRRFLSLTADLRKIDGIPALLERAVAEFGHI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK08993  87 DILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMLSFQGGIRVPSYTASKSGVM 166

                        170       180
                 ....*....|....*....|..
gi 530378355 157 GFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK08993 167 GVTRLMANEWAKHNINVNAIAP 188
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 3-181 1.31e-13

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: 67.49  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHL-----AFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLnheviVRHLDLASLKSIRAFAAEFLAEEDRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRdglLVRTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKG-------NSGQS--- 146
Cdd:cd09807   82 DVLINNAGVMR---CPYSKTEDgFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGkinfddlNSEKSynt 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530378355 147 --VYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:cd09807  159 gfAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVV 195
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 76-178 1.32e-13

Short-chain dehydrogenases/reductases (SDR); 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 (KR) 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: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 66.39  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:cd02266   31 RRDVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAAL 110

                         90       100
                 ....*....|....*....|...
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd02266  111 DGLAQQWASEGWGNGLPATAVAC 133
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-150 1.53e-13

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 65.97  E-value: 1.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355     9 GGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAA------GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:smart00822   7 GGLGGLGRALARWLAERGARrLVLLSRSGPDAPGAAallaelEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVI 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530378355    82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRtmiqQQGGSIVNVGSIVGLKGNSGQSVYSA 150
Cdd:smart00822  87 HAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTAD----LPLDFFVLFSSIAGVLGSPGQANYAA 151
PRK09291 PRK09291
SDR family oxidoreductase;
1-178 1.75e-13

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 66.95  E-value: 1.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRL---AVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEElekhlgRV 77
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNViagVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDRAQAAEW------DV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:PRK09291  75 DVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEA 154

                        170       180
                 ....*....|....*....|.
gi 530378355 158 FSRALAKEVARKKIRVNVVAP 178
Cdd:PRK09291 155 IAEAMHAELKPFGIQVATVNP 175
PRK07985 PRK07985
SDR family oxidoreductase;
2-196 1.80e-13

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 67.33  E-value: 1.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-----ARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK07985  49 DRKALVTGGDSGIGRAAAIAYAREGADVAISylpveEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALGG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLH-TNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK07985 129 LDIMALVAGKQVAIPDIADLTSEQFQKTFaINVFALFWLTQEAIPLL--PKGASIITTSSIQAYQPSPHLLDYAATKAAI 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKGDRI 196
Cdd:PRK07985 207 LNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISGGQTQDKI 247
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-150 2.80e-13

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 65.28  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355    9 GGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAAG------DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:pfam08659   7 GGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAQAliaeleARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIRGVI 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530378355   82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSmltcKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSA 150
Cdd:pfam08659  87 HAAGVLRDALLENMTDEDWRRVLAPKVTGT----WNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAA 151
PRK08278 PRK08278
SDR family oxidoreductase;
9-204 4.40e-13

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 66.08  E-value: 4.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIAR------NLEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08278  13 GASRGIGLAIALRAARDGANIVIAAKtaephpKLPGtihtAAEEIEAAGGQALPLVGDVRDEDQVAAAVAKAVERFGGID 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAG-INRDGLL-VRTKTEDMVSQLhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGN--SGQSVYSASKGG 154
Cdd:PRK08278  93 ICVNNASaINLTGTEdTPMKRFDLMQQI--NVRGTFLVSQACLPHLKKSENPHILTLSPPLNLDPKwfAPHTAYTMAKYG 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530378355 155 LVGFSRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKGDRINVTLRSPE 204
Cdd:PRK08278 171 MSLCTLGLAEEFRDDGIAVNALWPRTTIATAAVRNLLGGDEAMRRSRTPE 220
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 3-178 5.51e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 65.75  E-value: 5.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV-- 77
Cdd:PRK07576  10 KNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVaqlQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPIdv 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 -------NFLVNAAGINRDGLlvRTKTEdmvsqlhTNLLGSMLTCKAAMRTMiQQQGGSIVNVGSIVGLKGNSGQSVYSA 150
Cdd:PRK07576  90 lvsgaagNFPAPAAGMSANGF--KTVVD-------IDLLGTFNVLKAAYPLL-RRPGASIIQISAPQAFVPMPMQAHVCA 159

                        170       180
                 ....*....|....*....|....*...
gi 530378355 151 SKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK07576 160 AKAGVDMLTRTLALEWGPEGIRVNSIVP 187
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-181 8.52e-13

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 64.78  E-value: 8.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFScDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK05786   6 KKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNenkLKRMKKTLSKYGNIHYVVG-DVSSTESARNVIEKAAKVLNAIDG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 L-VNAAGINRDGLLVRTKTEDMvsqLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGL-KGNSGQSVYSASKGGLVG 157
Cdd:PRK05786  85 LvVTVGGYVEDTVEEFSGLEEM---LTNHIKIPLYAVNASLRFL--KEGSSIVLVSSMSGIyKASPDQLSYAVAKAGLAK 159

                        170       180
                 ....*....|....*....|....
gi 530378355 158 FSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK05786 160 AVEILASELLGRGIRVNGIAPTTI 183
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 2-181 1.33e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 64.82  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK05875   7 DRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIealkgAGAVRYEPADVTDEDQVARAVDAATAWHGR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRD-GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK05875  87 LHGVVHCAGGSETiGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKSAV 166

                        170       180
                 ....*....|....*....|....*.
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK05875 167 DHLMKLAADELGPSWVRVNSIRPGLI 192
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 9-178 1.55e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 64.29  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVqntfEELEKHLGRVNFLVNAA 84
Cdd:PRK06125  14 GASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHgvdvAVHALDLSSPEAR----EQLAAEAGDIDILVNNA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  85 GINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVgsiVGLKGNSGQSVY---SASKGGLVGFSRA 161
Cdd:PRK06125  90 GAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV---IGAAGENPDADYicgSAGNAALMAFTRA 166

                        170
                 ....*....|....*..
gi 530378355 162 LAKEVARKKIRVNVVAP 178
Cdd:PRK06125 167 LGGKSLDDGVRVVGVNP 183
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 3-181 1.63e-12

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. 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: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 63.88  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlEGAKAAAGDLGGDHlafSCDVAKEHDVqntFEELEKHLGRVNFLVN 82
Cdd:cd05334    2 RVVLVYGGRGALGSAVVQAFKSRGWWVASIDLA-ENEEADASIIVLDS---DSFTEQAKQV---VASVARLSGKVDALIC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAG-----INRDGLLVRTkTEDMVSQlhtNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVG 157
Cdd:cd05334   75 VAGgwaggSAKSKSFVKN-WDLMWKQ---NLWTSFIASHLATKHL--LSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQ 148

                        170       180
                 ....*....|....*....|....*.
gi 530378355 158 FSRALAKE--VARKKIRVNVVAPELI 181
Cdd:cd05334  149 LTQSLAAEnsGLPAGSTANAILPVTL 174
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 7-164 1.66e-12

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 65.47  E-value: 1.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARK-GYRLAVIAR--------NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd08953  210 VTGGAGGIGRALARALARRyGARLVLLGRsplppeeeWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYGAI 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSmltckAAMRTMIQQQG-GSIVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:cd08953  290 DGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGL-----LNLAQALADEPlDFFVLFSSVSAFFGGAGQADYAAANAFLD 364


                 ....*...
gi 530378355 157 GFSRALAK 164
Cdd:cd08953  365 AFAAYLRQ 372
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-178 1.06e-11

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 62.11  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSR--GIGRAVAQLMARKGYRL---------------------AVIARNLE--GAKAAAGDLggdhlafscDV 57
Cdd:PRK12859   7 KVAVVTGVSRldGIGAAICKELAEAGADIfftywtaydkempwgvdqdeqIQLQEELLknGVKVSSMEL---------DL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  58 AKEHDVQNTFEELEKHLGRVNFLVNAAGINRDgLLVRTKTEDMVSQLH-TNLLGSMLTCKAAMRTMIQQQGGSIVNVGSI 136
Cdd:PRK12859  78 TQNDAPKELLNKVTEQLGYPHILVNNAAYSTN-NDFSNLTAEELDKHYmVNVRATTLLSSQFARGFDKKSGGRIINMTSG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530378355 137 VGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK12859 157 QFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINP 198
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 5-204 2.25e-11

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 60.92  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   5 CAVF--GGSRGIGRAVAQLMARKGYRLAVIARNLEG----------AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEK 72
Cdd:cd09762    4 KTLFitGASRGIGKAIALKAARDGANVVIAAKTAEPhpklpgtiytAAEEIEAAGGKALPCIVDIRDEDQVRAAVEKAVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  73 HLGRVNFLV-NAAGIN-RDGLLVRTKTEDMVSQLhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGN--SGQSVY 148
Cdd:cd09762   84 KFGGIDILVnNASAISlTGTLDTPMKRYDLMMGV--NTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKwfKNHTAY 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530378355 149 SASKGGLVGFSRALAKEVARKKIRVNVvapeLIPRTV---SIRKMEKGDRINVTLRSPE 204
Cdd:cd09762  162 TMAKYGMSMCVLGMAEEFKPGGIAVNA----LWPRTAiatAAMNMLGGVDVAACCRKPE 216
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 2-178 2.42e-11

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 61.04  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLA-FSCDV--AKEHDVQNTFEELEKHLG 75
Cdd:PRK08945  12 DRIILVTGAGDGIGREAALTYARHGATVILLGRTeekLEAVYDEIEAAGGPQPAiIPLDLltATPQNYQQLADTIEEQFG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  76 RVNFLVNAAGInrdgLLVRT----KTEDMVSQ-LHTNLLGS-MLTcKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYS 149
Cdd:PRK08945  92 RLDGVLHNAGL----LGELGpmeqQDPEVWQDvMQVNVNATfMLT-QALLPLLLKSPAASLVFTSSSVGRQGRANWGAYA 166

                        170       180
                 ....*....|....*....|....*....
gi 530378355 150 ASKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK08945 167 VSKFATEGMMQVLADEYQGTNLRVNCINP 195
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 4-181 2.64e-11

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 61.08  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355    4 VCAVFGGSRGIGRAVAQLMAR----KGYRLAVIARNLEGAKAAAGDLGGDHLA-----FSCDVAKEHDVQNTFEELEKhL 74
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERSGlrvvrVSLDLGAEAGLEQLLKALRE-L 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   75 GRVNFLVNAAGINRDGLLVRT-KTEDMVSQL-------HTNLLGSMLTCKAAMRTMIQQQGG--SIVNVGSIVGLKGNSG 144
Cdd:TIGR01500  81 PRPKGLQRLLLINNAGTLGDVsKGFVDLSDStqvqnywALNLTSMLCLTSSVLKAFKDSPGLnrTVVNISSLCAIQPFKG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 530378355  145 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:TIGR01500 161 WALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVL 197
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 3-203 2.97e-11

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 60.67  E-value: 2.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFG--GSRGIGRAVAQLMARKGYRLAVIARN--LEG-AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05372    2 KRILITGiaNDRSIAWGIAKALHEAGAELAFTYQPeaLRKrVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGI-NRDGLLVRTktedmvsqLHTNLLGSMLT-----------CKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQ 145
Cdd:cd05372   82 DGLVHSIAFaPKVQLKGPF--------LDTSRKGFLKAldisayslvslAKAALPIM--NPGGSIVTLSYLGSERVVPGY 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530378355 146 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVS------IRKMEKGdrinVTLRSP 203
Cdd:cd05372  152 NVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPI-KTLAasgitgFDKMLEY----SEQRAP 210
PRK08017 PRK08017
SDR family oxidoreductase;
1-178 4.85e-11

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 60.10  E-value: 4.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAkAAAGDLGGDHLAFSCDVAKEHDvQNTFEELEKHLGRVNFL 80
Cdd:PRK08017   1 MQKSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDV-ARMNSLGFTGILLDLDDPESVE-RAADEVIALTDNRLYGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGS-MLTCkAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08017  79 FNNAGFGVYGPLSTISRQQMEQQFSTNFFGThQLTM-LLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWS 157

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAP 178
Cdd:PRK08017 158 DALRMELRHSGIKVSLIEP 176
PRK09134 PRK09134
SDR family oxidoreductase;
7-178 6.90e-11

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 59.94  E-value: 6.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK09134  14 VTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAaeiRALGRRAVALQADLADEAEVRALVARASAALGPITLLVN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGI-NRDglLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK09134  94 NASLfEYD--SAASFTRASWDRhMATNLRAPFVLAQAFARALPADARGLVVNMIDQRVWNLNPDFLSYTLSKAALWTATR 171

                        170
                 ....*....|....*...
gi 530378355 161 ALAKEVArKKIRVNVVAP 178
Cdd:PRK09134 172 TLAQALA-PRIRVNAIGP 188
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 5-178 1.63e-10

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: 58.83  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   5 CAVF--GGSRGIGRAVAQLMARKGYRL--AVIARNLEGAK----AAAGDLGGDHLafscDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd09805    1 KAVLitGCDSGFGNLLAKKLDSLGFTVlaGCLTKNGPGAKelrrVCSDRLRTLQL----DVTKPEQIKRAAQWVKEHVGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNF--LVNAAGIN---RDGLLvrTKTEDMVSQLHTNLLGSMLTCKAaMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSAS 151
Cdd:cd09805   77 KGLwgLVNNAGILgfgGDEEL--LPMDDYRKCMEVNLFGTVEVTKA-FLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCAS 153

                        170       180
                 ....*....|....*....|....*..
gi 530378355 152 KGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:cd09805  154 KAAVEAFSDSLRRELQPWGVKVSIIEP 180
PRK12746 PRK12746
SDR family oxidoreductase;
3-178 2.03e-10

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 58.51  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHL---- 74
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIesnGGKAFLIEADLNSIDGVKKLVEQLKNELqirv 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  75 --GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASK 152
Cdd:PRK12746  87 gtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSIAYGLSK 164

                        170       180
                 ....*....|....*....|....*.
gi 530378355 153 GGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK12746 165 GALNTMTLPLAKHLGERGITVNTIMP 190
PRK12744 PRK12744
SDR family oxidoreductase;
2-178 2.52e-10

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 58.21  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG-------DLGGDHLAFSCDVAKEHDVQNTFEELEKHL 74
Cdd:PRK12744   8 GKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEetvaavkAAGAKAVAFQADLTTAAAVEKLFDDAKAAF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVN-VGSIVGlKGNSGQSVYSASKG 153
Cdd:PRK12744  88 GRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIVTlVTSLLG-AFTPFYSAYAGSKA 164

                        170       180
                 ....*....|....*....|....*
gi 530378355 154 GLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK12744 165 PVEHFTRAASKEFGARGISVTAVGP 189
PRK08703 PRK08703
SDR family oxidoreductase;
2-178 2.70e-10

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 58.02  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA------AAGdlGGDHLAFSCDVAKEHDvqNTFEEL----- 70
Cdd:PRK08703   6 DKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKvydaivEAG--HPEPFAIRFDLMSAEE--KEFEQFaatia 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  71 EKHLGRVNFLVNAAGINRDGLLVRTKT-EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYS 149
Cdd:PRK08703  82 EATQGKLDGIVHCAGYFYALSPLDFQTvAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFG 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 530378355 150 ASKGGLVGFSRALAKEVAR-KKIRVNVVAP 178
Cdd:PRK08703 162 ASKAALNYLCKVAADEWERfGNLRANVLVP 191
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 7-184 3.33e-10

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 57.84  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAGL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 NRdGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAK 164
Cdd:PRK10538  85 AL-GLepAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRT 163

                        170       180
                 ....*....|....*....|
gi 530378355 165 EVARKKIRVNVVAPELIPRT 184
Cdd:PRK10538 164 DLHGTAVRVTDIEPGLVGGT 183
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 7-178 4.63e-10

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 57.34  E-value: 4.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFG--GSRGIGRAVAQLMARKGYRLAVIARN--LEG-AKAAAGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:COG0623   10 ITGvaNDRSIAWGIAKALHEEGAELAFTYQGeaLKKrVEPLAEELGSA-LVLPCDVTDDEQIDALFDEIKEKWGKLDFLV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAG-------------INRDGLLvrtKTEDmVS--QLHtnllgSMltCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQS 146
Cdd:COG0623   89 HSIAfapkeelggrfldTSREGFL---LAMD-ISaySLV-----AL--AKAAEPLM--NEGGSIVTLTYLGAERVVPNYN 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530378355 147 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:COG0623  156 VMGVAKAALEASVRYLAADLGPKGIRVNAISA 187
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 9-162 1.25e-09

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 56.62  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYR-LAVIARN-----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKhLGRVNFLVN 82
Cdd:cd05274  157 GGLGGLGLLVARWLAARGARhLVLLSRRgpaprAAARAALLRAGGARVSVVRCDVTDPAALAALLAELAA-GGPLAGVIH 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCkaamRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRAL 162
Cdd:cd05274  236 AAGVLRDALLAELTPAAFAAVLAAKVAGALNLH----ELTPDLPLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAAQR 311
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-178 2.79e-09

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 55.08  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSR--GIGRAVAQLMARKGYR------------LAVIARNLEGA--KAAAGDLGGDHLAFSCDVAKEHDVQ 64
Cdd:PRK12748   4 MKKIALVTGASRlnGIGAAVCRRLAAKGIDifftywspydktMPWGMHDKEPVllKEEIESYGVRCEHMEIDLSQPYAPN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  65 NTFEELEKHLGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVgsivglkgNSG 144
Cdd:PRK12748  84 RVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINL--------TSG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530378355 145 QSV--------YSASKGGLVGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK12748 156 QSLgpmpdelaYAATKGAIEAFTKSLAPELAEKGITVNAVNP 197
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 4-180 4.35e-09

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


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 54.93  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355    4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAK---AAAGDLGGDHLAFSC--DVAKEHDVQNTFEEL----EKHL 74
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAAstlAAELNARRPNSAVTCqaDLSNSATLFSRCEAIidacFRAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHT------NLLGSMLTCKAAM-RTMIQQQGG----------SIVNVGSIV 137
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPLLRGDAGEGVGDKKSlevqvaELFGSNAIAPYFLiKAFAQRQAGtraeqrstnlSIVNLCDAM 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 530378355  138 GLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPEL 180
Cdd:TIGR02685 163 TDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL 205
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 60-181 1.75e-08

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 52.96  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  60 EHDVQNTFEELEKHLGRVNFLVNAAGINRD-GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVG 138
Cdd:cd05361   56 EQKPEELVDAVLQAGGAIDVLVSNDYIPRPmNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVP 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530378355 139 LKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:cd05361  136 KKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFF 178
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 3-181 1.92e-08

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 52.77  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFE----ELEKHL 74
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIhYGNRKEEAEETVYEIqsnGGSAFSIGANLESLHGVEALYSsldnELQNRT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  75 GRVNF--LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASK 152
Cdd:PRK12747  85 GSTKFdiLINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFIAYSMTK 162

                        170       180
                 ....*....|....*....|....*....
gi 530378355 153 GGLVGFSRALAKEVARKKIRVNVVAPELI 181
Cdd:PRK12747 163 GAINTMTFTLAKQLGARGITVNAILPGFI 191
PRK12742 PRK12742
SDR family oxidoreductase;
7-178 3.03e-08

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 52.07  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLA-VIARNLEGAKAAAGDLGGDhlAFSCDVAKEHDVQNTFEELekhlGRVNFLVNAAG 85
Cdd:PRK12742  11 VLGGSRGIGAAIVRRFVTDGANVRfTYAGSKDAAERLAQETGAT--AVQTDSADRDAVIDVVRKS----GALDILVVNAG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGN-SGQSVYSASKGGLVGFSRALAK 164
Cdd:PRK12742  85 IAVFGDALELDADDIDRLFKINIHAPYHASVEAARQM--PEGGRIIIIGSVNGDRMPvAGMAAYAASKSALQGMARGLAR 162

                        170
                 ....*....|....
gi 530378355 165 EVARKKIRVNVVAP 178
Cdd:PRK12742 163 DFGPRGITINVVQP 176
PRK07023 PRK07023
SDR family oxidoreductase;
7-178 3.26e-08

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 51.94  E-value: 3.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGA-KAAAGDLGGDHLafsCDVAKEHDVQ-----NTFEELEKHLGRVnFL 80
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVLGVARSRHPSlAAAAGERLAEVE---LDLSDAAAAAawlagDLLAAFVDGASRV-LL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  81 VNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK07023  82 INNAGTVEPIGPLATLDAAAIARaVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAALDHHA 161

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEvARKKIRVNVVAP 178
Cdd:PRK07023 162 RAVALD-ANRALRIVSLAP 179
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
12-188 6.88e-08

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 51.27  E-value: 6.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  12 RGIGRAVAQLMARKGYRLAVI---ARNLEGAKAAAGDLGG-DHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA-AGI 86
Cdd:PRK08594  19 RSIAWGIARSLHNAGAKLVFTyagERLEKEVRELADTLEGqESLLLPCDVTSDEEITACFETIKEEVGVIHGVAHCiAFA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 NRD---GLLVRTKTEDMVsqLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALA 163
Cdd:PRK08594  99 NKEdlrGEFLETSRDGFL--LAQNISAYSLTAVAREAKKLMTEGGSIVTLTYLGGERVVQNYNVMGVAKASLEASVKYLA 176

                        170       180
                 ....*....|....*....|....*
gi 530378355 164 KEVARKKIRVNVVAPELIpRTVSIR 188
Cdd:PRK08594 177 NDLGKDGIRVNAISAGPI-RTLSAK 200
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 11-181 2.08e-07

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 49.85  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  11 SRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGG----DHLAFSCDVAKEHDVQNTFEELeKHLGRVNFLVNAAGI 86
Cdd:PRK08339  17 SKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSesnvDVSYIVADLTKREDLERTVKEL-KNIGEPDIFFFSTGG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEV 166
Cdd:PRK08339  96 PKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRISMAGLVRTLAKEL 175

                        170
                 ....*....|....*
gi 530378355 167 ARKKIRVNVVAPELI 181
Cdd:PRK08339 176 GPKGITVNGIMPGII 190
PRK07102 PRK07102
SDR family oxidoreductase;
7-178 2.96e-07

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 49.15  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFScdvakEHDVqNTFEE----LEKHLGRVNF 79
Cdd:PRK07102   6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLrarGAVAVSTH-----ELDI-LDTAShaafLDSLPALPDI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFS 159
Cdd:PRK07102  80 VLIAVGTLGDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTAFL 159

                        170
                 ....*....|....*....
gi 530378355 160 RALAKEVARKKIRVNVVAP 178
Cdd:PRK07102 160 SGLRNRLFKSGVHVLTVKP 178
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
11-174 3.60e-07

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 49.20  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  11 SRGIGRAVAQLMARKGYRLA---VIARNLEGAKAAAGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGIN 87
Cdd:PRK08690  17 ERSIAYGIAKACREQGAELAftyVVDKLEERVRKMAAELDSE-LVFRCDVASDDEINQVFADLGKHWDGLDGLVHSIGFA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  88 -RDGL---LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALA 163
Cdd:PRK08690  96 pKEALsgdFLDSISREAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSYLGAVRAIPNYNVMGMAKASLEAGIRFTA 175

                        170
                 ....*....|.
gi 530378355 164 KEVARKKIRVN 174
Cdd:PRK08690 176 ACLGKEGIRCN 186
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 7-189 4.66e-07

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 49.09  E-value: 4.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH---------LAFSCDVAKE-HDVQNTFEELEkhlgr 76
Cdd:PLN02780  58 VTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYsktqiktvvVDFSGDIDEGvKRIKETIEGLD----- 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  77 VNFLVNAAGINRD-GLLVRTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQGGSIVNVGS--IVGLKGNSGQSVYSASK 152
Cdd:PLN02780 133 VGVLINNVGVSYPyARFFHEVDEELLKNLiKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSgaAIVIPSDPLYAVYAATK 212

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530378355 153 GGLVGFSRALAKEVARKKIRVNVVAPELIP-RTVSIRK 189
Cdd:PLN02780 213 AYIDQFSRCLYVEYKKSGIDVQCQVPLYVAtKMASIRR 250
PRK08416 PRK08416
enoyl-ACP reductase;
3-177 9.74e-07

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 47.84  E-value: 9.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLA-VIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08416   9 KTLVISGGTRGIGKAIVYEFAQSGVNIAfTYNSNVEEANKIAEDLeqkyGIKAKAYPLNILEPETYKELFKKIDEDFDRV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINRD------GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNSGQSVYSAS 151
Cdd:PRK08416  89 DFFISNAIISGRavvggyTKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISLSSTGNLVYIENYAGHGTS 168

                        170       180
                 ....*....|....*....|....*.
gi 530378355 152 KGGLVGFSRALAKEVARKKIRVNVVA 177
Cdd:PRK08416 169 KAAVETMVKYAATELGEKNIRVNAVS 194
PRK07806 PRK07806
SDR family oxidoreductase;
2-185 1.69e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 47.02  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK07806   6 GKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkaprANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLV-NAAGINRDGLlvrtkTEDMVSQLHTNLLGSMLTckAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSV-----YSAS 151
Cdd:PRK07806  86 DALVlNASGGMESGM-----DEDYAMRLNRDAQRNLAR--AALPLM--PAGSRVVFVTSHQAHFIPTVKTMpeyepVARS 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530378355 152 KGGLVGFSRALAKEVARKKIRVNVVAPELIPRTV 185
Cdd:PRK07806 157 KRAGEDALRALRPELAEKGIGFVVVSGDMIEGTV 190
PRK05993 PRK05993
SDR family oxidoreductase;
1-178 2.31e-06

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 46.94  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAaagdLGGDHL-AFSCDVAKEHDVQNTFEE-LEKHLGRVN 78
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAA----LEAEGLeAFQLDYAEPESIAALVAQvLELSGGRLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLG-SMLTCKA--AMRTmiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGL 155
Cdd:PRK05993  79 ALFNNGAYGQPGAVEDLPTEALRAQFEANFFGwHDLTRRVipVMRK---QGQGRIVQCSSILGLVPMKYRGAYNASKFAI 155

                        170       180
                 ....*....|....*....|...
gi 530378355 156 VGFSRALAKEVARKKIRVNVVAP 178
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEP 178
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
43-177 2.35e-06

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 46.67  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  43 AGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINR----DGLLVRTKTEDMVSQLHTNLLGSMLTCKAA 118
Cdd:PRK08159  56 AAELGAF-VAGHCDVTDEASIDAVFETLEKKWGKLDFVVHAIGFSDkdelTGRYVDTSRDNFTMTMDISVYSFTAVAQRA 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530378355 119 MRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVA 177
Cdd:PRK08159 135 EKLM--TDGGSILTLTYYGAEKVMPHYNVMGVAKAALEASVKYLAVDLGPKNIRVNAIS 191
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 7-162 4.65e-06

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 45.97  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIA-RNLEGAKAAAGDLG---GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd09810    6 ITGASSGLGLAAAKALARRGEWHVVMAcRDFLKAEQAAQEVGmpkDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDALVC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 AAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGS--IVNVGSIVG----LKGNSGQsvySASKGGL 155
Cdd:cd09810   86 NAAVYLPTAKEPRFTADGFELtVGVNHLGHFLLTNLLLEDLQRSENASprIVIVGSITHnpntLAGNVPP---RATLGDL 162


                 ....*..
gi 530378355 156 VGFSRAL 162
Cdd:cd09810  163 EGLAGGL 169
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-155 4.66e-06

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 46.13  E-value: 4.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLafscdvakEHDVQNtFEELEKHLGRVNFLVNAAGI 86
Cdd:COG0451    4 VTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFV--------RGDLRD-PEALAAALAGVDAVVHLAAP 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530378355  87 nrdgllVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQqggsIVNVGSIvglkgnsgqSVYSASKGGL 155
Cdd:COG0451   75 ------AGVGEEDPDETLEVNVEGTLNLLEAARAAGVKR----FVYASSS---------SVYGDGEGPI 124
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 9-182 8.76e-06

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 45.18  E-value: 8.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKhLGRVNFLVNAAGINR 88
Cdd:cd08951   14 GSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNA-IGRFDAVIHNAGILS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  89 DGlLVRTKTEDMVSQLHTNLLGS-MLTCKAA-------MRTMIQQQGGSIVNVGSIVGLKGNSGQSvYSASKgglvGFSR 160
Cdd:cd08951   93 GP-NRKTPDTGIPAMVAVNVLAPyVLTALIRrpkrliyLSSGMHRGGNASLDDIDWFNRGENDSPA-YSDSK----LHVL 166

                        170       180
                 ....*....|....*....|....
gi 530378355 161 ALAKEVAR--KKIRVNVVAPELIP 182
Cdd:cd08951  167 TLAAAVARrwKDVSSNAVHPGWVP 190
PRK08862 PRK08862
SDR family oxidoreductase;
10-180 1.01e-05

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 44.71  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  10 GSRgIGRAVAQLMARKGYRLAVIARNLEGAKA---AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV-NFLVNAAG 85
Cdd:PRK08862  14 GSV-LGRTISCHFARLGATLILCDQDQSALKDtyeQCSALTDNVYSFQLKDFSQESIRHLFDAIEQQFNRApDVLVNNWT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLT----CKAAMRTmiQQQGGSIVNVGSivgLKGNSGQSVYSASKGGLVGFSRA 161
Cdd:PRK08862  93 SSPLPSLFDEQPSESFIQQLSSLASTLFTygqvAAERMRK--RNKKGVIVNVIS---HDDHQDLTGVESSNALVSGFTHS 167

                        170
                 ....*....|....*....
gi 530378355 162 LAKEVARKKIRVNVVAPEL 180
Cdd:PRK08862 168 WAKELTPFNIRVGGVVPSI 186
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 7-178 1.80e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 43.65  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARkgyRLAVIArnlegakaaAGDLGGDHLAfscDVAKEHDVQNTFEELekhlGRVNFLVNAAGI 86
Cdd:PRK07578   5 VIGASGTIGRAVVAELSK---RHEVIT---------AGRSSGDVQV---DITDPASIRALFEKV----GKVDAVVSAAGK 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEV 166
Cdd:PRK07578  66 VHFAPLAEMTDEDFNVGLQSKLMGQVNLVLIGQHYL--NDGGSFTLTSGILSDEPIPGGASAATVNGALEGFVKAAALEL 143

                        170
                 ....*....|..
gi 530378355 167 ARKkIRVNVVAP 178
Cdd:PRK07578 144 PRG-IRINVVSP 154
PRK08340 PRK08340
SDR family oxidoreductase;
7-85 2.12e-05

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 44.03  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAA 84
Cdd:PRK08340   5 VTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKeyGEVYAVKADLSDKDDLKNLVKEAWELLGGIDALVWNA 84


                 .
gi 530378355  85 G 85
Cdd:PRK08340  85 G 85
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 9-181 2.39e-05

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 43.77  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV-NAA--- 84
Cdd:PRK06483   9 GAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGLRQAGA--QCIQADFSTNAGIMAFIDELKQHTDGLRAIIhNASdwl 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  85 ----GINRDGLLvrtktEDMVsQLHTN---LLGsmLTCKAAMRTmiQQQGGS-IVNVGSIVGLKGNSGQSVYSASKGGLV 156
Cdd:PRK06483  87 aekpGAPLADVL-----ARMM-QIHVNapyLLN--LALEDLLRG--HGHAASdIIHITDYVVEKGSDKHIAYAASKAALD 156

                        170       180
                 ....*....|....*....|....*
gi 530378355 157 GFSRALAKEVArKKIRVNVVAPELI 181
Cdd:PRK06483 157 NMTLSFAAKLA-PEVKVNSIAPALI 180
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
14-177 3.84e-05

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 43.07  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  14 IGRAVAQLMARKG------YRLAVIARNLegaKAAAGDLGGDHLAfSCDVAKEHDVQNTFEELEKHLGRVNFLVNA-AGI 86
Cdd:PRK06603  22 ISWAIAQLAKKHGaelwftYQSEVLEKRV---KPLAEEIGCNFVS-ELDVTNPKSISNLFDDIKEKWGSFDFLLHGmAFA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  87 NRD---GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALA 163
Cdd:PRK06603  98 DKNelkGRYVDTSLENFHNSLHISCYSLLELSRSAEALM--HDGGSIVTLTYYGAEKVIPNYNVMGVAKAALEASVKYLA 175

                        170
                 ....*....|....
gi 530378355 164 KEVARKKIRVNVVA 177
Cdd:PRK06603 176 NDMGENNIRVNAIS 189
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 6-203 4.96e-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: 42.87  E-value: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   6 AVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAgDLGgdhlafscdvAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHT--VIGIDLREADVIA-DLS----------TPEGRAAAIADVLARCSGVLDGLVNCAG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  86 INrdgllVRTKTEDMVSqlhTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSIVGLKGNS---------------------- 143
Cdd:cd05328   70 VG-----GTTVAGLVLK---VNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAQdklelakalaagtearavalae 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530378355 144 -----GQSVYSASKGGLVGFSRALAKE-VARKKIRVNVVAPELI--PRTVSIRKMEKGDRINVTLRSP 203
Cdd:cd05328  142 hagqpGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVetPILQAFLQDPRGGESVDAFVTP 209
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
12-177 6.48e-05

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 42.42  E-value: 6.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  12 RGIGRAVAQLMARKGYRLAVIARNLEGAKAA---AGDLGGDHLaFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA-AGIN 87
Cdd:PRK08415  17 KSIAYGIAKACFEQGAELAFTYLNEALKKRVepiAQELGSDYV-YELDVSKPEHFKSLAESLKKDLGKIDFIVHSvAFAP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  88 RDGL---LVRTKTEDMVSQLHTNLLgSMLTCKAAMRTMIqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAK 164
Cdd:PRK08415  96 KEALegsFLETSKEAFNIAMEISVY-SLIELTRALLPLL-NDGASVLTLSYLGGVKYVPHYNVMGVAKAALESSVRYLAV 173

                        170
                 ....*....|...
gi 530378355 165 EVARKKIRVNVVA 177
Cdd:PRK08415 174 DLGKKGIRVNAIS 186
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 10-94 7.40e-05

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


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 40.65  E-value: 7.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   10 GSRGIGRAVAQLMARKG--YRLAVIARNLEGAKAAAGDLGGDHLafscdVAKEHDVQNTFEELEKHLGRVNFLVNAAGIN 87
Cdd:pfam03435   5 GAGSVGQGVAPLLARHFdvDRITVADRTLEKAQALAAKLGGVRF-----IAVAVDADNYEAVLAALLKEGDLVVNLSPPT 79


                  ....*..
gi 530378355   88 RDGLLVR 94
Cdd:pfam03435  80 LSLDVLK 86
PRK05884 PRK05884
SDR family oxidoreductase;
7-178 1.14e-04

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 41.72  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDhlAFSCDVAKEHDVQNTFEELEKHLgrvNFLVN---- 82
Cdd:PRK05884   5 VTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVD--AIVCDNTDPASLEEARGLFPHHL---DTIVNvpap 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  83 --AAGINRDGLLVRTKTEdMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVgsiVGLKGNSGqSVYSASKGGLVGFSR 160
Cdd:PRK05884  80 swDAGDPRTYSLADTANA-WRNALDATVLSAVLTVQSVGDHL--RSGGSIISV---VPENPPAG-SAEAAIKAALSNWTA 152

                        170
                 ....*....|....*...
gi 530378355 161 ALAKEVARKKIRVNVVAP 178
Cdd:PRK05884 153 GQAAVFGTRGITINAVAC 170
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
55-177 1.20e-04

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 41.62  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  55 CDVAKEHDVQNTFEELEKHLGRVNFLVNA-AGINRDGL---LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSI 130
Cdd:PRK07370  66 CDVQDDAQIEETFETIKQKWGKLDILVHClAFAGKEELigdFSATSREGFARALEISAYSLAPLCKAAKPLM--SEGGSI 143

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 530378355 131 VNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVA 177
Cdd:PRK07370 144 VTLTYLGGVRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAIS 190
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 3-89 1.36e-04

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 41.46  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAA--AGDLGGdHLAFSCDVAkehdvqnTFEELEKHLGRVNFL 80
Cdd:cd05271    1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEAYARRLlvMGDLGQ-VLFVEFDLR-------DDESIRKALEGSDVV 72


                 ....*....
gi 530378355  81 VNAAGINRD 89
Cdd:cd05271   73 INLVGRLYE 81
PRK06196 PRK06196
oxidoreductase; Provisional
 3-86 1.77e-04

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 41.21  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAfSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06196  27 KTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDGVEVV-MLDLADLESVRAFAERFLDSGRRIDILIN 105


                 ....
gi 530378355  83 AAGI 86
Cdd:PRK06196 106 NAGV 109
PRK06953 PRK06953
SDR family oxidoreductase;
7-155 2.48e-04

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 40.44  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAkAAAGDLGGDhlAFSCDVAKEHDVQNTFEELEKHlgRVNFLVNAAGI 86
Cdd:PRK06953   6 IVGASRGIGREFVRQYRADGWRVIATARDAAAL-AALQALGAE--ALALDVADPASVAGLAWKLDGE--ALDAAVYVAGV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530378355  87 --NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMrTMIQQQGGSIVNV----GSIVGLKGNSGQsVYSASKGGL 155
Cdd:PRK06953  81 ygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILL-PLVEAAGGVLAVLssrmGSIGDATGTTGW-LYRASKAAL 153
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 3-136 2.62e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 40.78  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARItaatpGADVTLQELDLTSLASVRAAADALRAAYPRI 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  78 NFLVNAAGINrdgLLVRTKTEDMVS-QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGSI 136
Cdd:PRK06197  97 DLLINNAGVM---YTPKQTTADGFElQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSG 153
PRK07984 PRK07984
enoyl-ACP reductase FabI;
12-177 1.89e-03

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 38.34  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  12 RGIGRAVAQLMARKGYRLAVIARN--LEG-AKAAAGDLGGDhLAFSCDVAKEHDVQNTFEELEK----HLGRVNFLVNAA 84
Cdd:PRK07984  18 LSIAYGIAQAMHREGAELAFTYQNdkLKGrVEEFAAQLGSD-IVLPCDVAEDASIDAMFAELGKvwpkFDGFVHSIGFAP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  85 GINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqQQGGSIVNVGSIVGLKGNSGQSVYSASKGGLVGFSRALAK 164
Cdd:PRK07984  97 GDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSML-NPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMAN 175

                        170
                 ....*....|...
gi 530378355 165 EVARKKIRVNVVA 177
Cdd:PRK07984 176 AMGPEGVRVNAIS 188
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
6-46 2.00e-03

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 37.91  E-value: 2.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530378355   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARN-------LEGAKAAAGDL 46
Cdd:COG2910    3 AVIGATGRVGSLIVREALARGHEVTALVRNpeklpdeHPGLTVVVGDV 50
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
48-177 2.08e-03

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 38.19  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  48 GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINR----DGLLVRTKTEdmvsqlhtNLLGSMLTCKAAMRTMI 123
Cdd:PRK06505  57 GSDFVLPCDVEDIASVDAVFEALEKKWGKLDFVVHAIGFSDknelKGRYADTTRE--------NFSRTMVISCFSFTEIA 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355 124 QQQGGSIVNVGSIVGLKGNSGQ------SVYSASKGGLVGFSRALAKEVARKKIRVNVVA 177
Cdd:PRK06505 129 KRAAKLMPDGGSMLTLTYGGSTrvmpnyNVMGVAKAALEASVRYLAADYGPQGIRVNAIS 188
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 6-63 4.25e-03

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 37.27  E-value: 4.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530378355   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDV 63
Cdd:PRK08655   4 SIIGGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEYANDNIDAAKDADI 61
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
6-50 4.65e-03

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 37.13  E-value: 4.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530378355   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH 50
Cdd:COG5322  155 AVVGATGSIGSVCARLLAREVKRLTLVARNLERLEELAEEILRNP 199
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 2-43 5.00e-03

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


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 36.60  E-value: 5.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530378355   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA 43
Cdd:cd01078   28 GKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAA 69
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 7-205 5.37e-03

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: 36.80  E-value: 5.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFS--CDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd09808    6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIeteSGNQNIFLhiVDMSDPKQVWEFVEEFKEEGKKLHVLI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378355  82 NAAG-------INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIV---NVGSIVGLKGN-SGQSVYSA 150
Cdd:cd09808   86 NNAGcmvnkreLTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGGMLVqklNTNNLQSERTAfDGTMVYAQ 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530378355 151 SKGGLVGFSRALAKevARKKIRVNVVAPELIPrTVSIRKMEKG--DRINVTLRSPEQ 205
Cdd:cd09808  166 NKRQQVIMTEQWAK--KHPEIHFSVMHPGWAD-TPAVRNSMPDfhARFKDRLRSEEQ 219
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
11-85 6.99e-03

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 36.34  E-value: 6.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530378355  11 SRGIGRAVAQLMARKGYRLA---VIARNLEGAKAAAGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK06997  17 NRSIAYGIAKACKREGAELAftyVGDRFKDRITEFAAEFGSD-LVFPCDVASDEQIDALFASLGQHWDGLDGLVHSIG 93
 
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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