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Conserved domains on  [gi|388856966|emb|CCF49386|]
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probable NADP-dependent mannitol dehydrogenase [Ustilago hordei]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
3-260 3.94e-104

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05352:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 252  Bit Score: 302.71  E-value: 3.94e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   3 FVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQ 82
Cdd:cd05352    2 DLFSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  83 DELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYNQeglnkP 162
Cdd:cd05352   82 KDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQG--KGSLIITASMSGTIVNR-----P 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 LTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSD 242
Cdd:cd05352  155 QPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASD 234
                        250
                 ....*....|....*...
gi 388856966 243 KASYLTGSVIRPDGGFTI 260
Cdd:cd05352  235 ASSYTTGSDLIIDGGYTC 252
 
Name Accession Description Interval E-value
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
3-260 3.94e-104

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: 302.71  E-value: 3.94e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   3 FVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQ 82
Cdd:cd05352    2 DLFSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  83 DELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYNQeglnkP 162
Cdd:cd05352   82 KDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQG--KGSLIITASMSGTIVNR-----P 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 LTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSD 242
Cdd:cd05352  155 QPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASD 234
                        250
                 ....*....|....*...
gi 388856966 243 KASYLTGSVIRPDGGFTI 260
Cdd:cd05352  235 ASSYTTGSDLIIDGGYTC 252
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
6-260 7.18e-76

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: 230.44  E-value: 7.18e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:COG1028    3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA-GGRALAVAADVTDEAAVEALVAAAVAAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSseiynqeGLNKPLTQ 165
Cdd:COG1028   82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGG--GRIVNISSIA-------GLRGSPGQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:COG1028  153 AAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALlgAEEVREALAARIPLGRLGTPEEVAAAVLFLASDA 232
                        250
                 ....*....|....*..
gi 388856966 244 ASYLTGSVIRPDGGFTI 260
Cdd:COG1028  233 ASYITGQVLAVDGGLTA 249
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
5-257 1.01e-58

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 186.90  E-value: 1.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAEL-RAAGGEARVLVFDVSDEAAVRALIEAAVEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSEIYNQEglnkplt 164
Cdd:PRK05653  80 FGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARY--GRIVNISSVSGVTGNPG------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKA 244
Cdd:PRK05653 151 QTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAA 230
                        250
                 ....*....|...
gi 388856966 245 SYLTGSVIRPDGG 257
Cdd:PRK05653 231 SYITGQVIPVNGG 243
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
18-259 1.06e-50

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: 165.68  E-value: 1.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   18 NRGIGLAMSKAVANAGANVAIFYRShPKAQEAAAEVAKEFGVqcRAYQCDVGDAELVKKTLKQAQDELGQVTGLLANAGV 97
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLN-EALAKRVEELAEELGA--AVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   98 S--VVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIEsgfkKGSIVITSSMSSEIYNqeglnkPLTQVfYNSSKGAV 175
Cdd:pfam13561  82 ApkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE----GGSIVNLSSIGAERVV------PNYNA-YGAAKAAL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  176 TNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDA--KIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLTGSVIR 253
Cdd:pfam13561 151 EALTRYLAVELGPRGIRVNAISPGPIKTLAASGIPGfdELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLY 230

                  ....*.
gi 388856966  254 PDGGFT 259
Cdd:pfam13561 231 VDGGYT 236
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
13-260 8.92e-10

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: 57.63  E-value: 8.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   13 VVTGGNRGIGLAMSKAVANAGANVAIFY-RSHPKAQEAAAEVAKE---FGVQCRAyqcdvgDAELVKKTLKQAQD----- 83
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYhRSAAAASTLAAELNARrpnSAVTCQA------DLSNSATLFSRCEAiidac 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   84 --ELGQVTGLLANAgvSVVKPAVELTSDDFRYV-----YDTNVLGVFNSaKAVAQLWIESGF---KKGSIVITSSMSSEI 153
Cdd:TIGR02685  79 frAFGRCDVLVNNA--SAFYPTPLLRGDAGEGVgdkksLEVQVAELFGS-NAIAPYFLIKAFaqrQAGTRAEQRSTNLSI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  154 YN--QEGLNKPLTQ-VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFcnTEQTSGMDAKIRDFQASSIPMGRFSEPH 230
Cdd:TIGR02685 156 VNlcDAMTDQPLLGfTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL--SLLPDAMPFEVQEDYRRKVPLGQREASA 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 388856966  231 EQ-ADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:TIGR02685 234 EQiADVVIFLVSPKAKYITGTCIKVDGGLSL 264
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
11-124 4.78e-09

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: 54.41  E-value: 4.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966    11 TIVVTGGNRGIGLA---------------MSkavanaganvaifyRSHPKAQEAAAEVA--KEFGVQCRAYQCDVGDAEL 73
Cdd:smart00822   2 TYLITGGLGGLGRAlarwlaergarrlvlLS--------------RSGPDAPGAAALLAelEAAGARVTVVACDVADRDA 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 388856966    74 VKKTLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFN 124
Cdd:smart00822  68 LAAVLAAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWN 118
 
Name Accession Description Interval E-value
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
3-260 3.94e-104

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: 302.71  E-value: 3.94e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   3 FVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQ 82
Cdd:cd05352    2 DLFSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  83 DELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYNQeglnkP 162
Cdd:cd05352   82 KDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQG--KGSLIITASMSGTIVNR-----P 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 LTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSD 242
Cdd:cd05352  155 QPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASD 234
                        250
                 ....*....|....*...
gi 388856966 243 KASYLTGSVIRPDGGFTI 260
Cdd:cd05352  235 ASSYTTGSDLIIDGGYTC 252
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
6-260 7.18e-76

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: 230.44  E-value: 7.18e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:COG1028    3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA-GGRALAVAADVTDEAAVEALVAAAVAAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSseiynqeGLNKPLTQ 165
Cdd:COG1028   82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGG--GRIVNISSIA-------GLRGSPGQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:COG1028  153 AAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALlgAEEVREALAARIPLGRLGTPEEVAAAVLFLASDA 232
                        250
                 ....*....|....*..
gi 388856966 244 ASYLTGSVIRPDGGFTI 260
Cdd:COG1028  233 ASYITGQVLAVDGGLTA 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
12-252 1.39e-59

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: 188.65  E-value: 1.39e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAevAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGL 91
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAA--IEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  92 LANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSseiynqeGLNKPLTQVFYNSS 171
Cdd:cd05233   79 VNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQ--GGGRIVNISSVA-------GLRPLPGQAAYAAS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 172 KGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQT-SGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLTGS 250
Cdd:cd05233  150 KAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLaKLGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQ 229

                 ..
gi 388856966 251 VI 252
Cdd:cd05233  230 VI 231
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
5-257 1.01e-58

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 186.90  E-value: 1.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAEL-RAAGGEARVLVFDVSDEAAVRALIEAAVEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSEIYNQEglnkplt 164
Cdd:PRK05653  80 FGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARY--GRIVNISSVSGVTGNPG------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKA 244
Cdd:PRK05653 151 QTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAA 230
                        250
                 ....*....|...
gi 388856966 245 SYLTGSVIRPDGG 257
Cdd:PRK05653 231 SYITGQVIPVNGG 243
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
6-259 8.26e-56

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: 179.48  E-value: 8.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:cd05347    2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKE-GVEATAFTCDVSDEEAIKAAVEAIEEDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEiynQEGLNKPLtq 165
Cdd:cd05347   81 GKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQG--HGKIINICSLLSE---LGGPPVPA-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 vfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:cd05347  154 --YAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVvaDPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDA 231
                        250
                 ....*....|....*.
gi 388856966 244 ASYLTGSVIRPDGGFT 259
Cdd:cd05347  232 SDYVNGQIIFVDGGWL 247
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
7-257 1.01e-53

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: 173.93  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVitsSMSSeIYNQEGLnkPLtQV 166
Cdd:cd05369   81 KIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAK-HGGSIL---NISA-TYAYTGS--PF-QV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTeqTSGMD-----AKIRDFQASSIPMGRFSEPHEQADPAVLLLS 241
Cdd:cd05369  153 HSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPT--TEGMErlapsGKSEKKMIERVPLGRLGTPEEIANLALFLLS 230
                        250
                 ....*....|....*.
gi 388856966 242 DKASYLTGSVIRPDGG 257
Cdd:cd05369  231 DAASYINGTTLVVDGG 246
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
5-260 1.63e-53

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 173.46  E-value: 1.63e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSEIYNqeglnkpLT 164
Cdd:PRK05557  81 FGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRS--GRIINISSVVGLMGN-------PG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKA 244
Cdd:PRK05557 152 QANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEA 231
                        250
                 ....*....|....*.
gi 388856966 245 SYLTGSVIRPDGGFTI 260
Cdd:PRK05557 232 AYITGQTLHVNGGMVM 247
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
10-257 4.09e-53

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: 172.35  E-value: 4.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEvAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEE-IKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEIYNqeglnkpLTQVFYN 169
Cdd:cd05333   80 ILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKR--RSGRIINISSVVGLIGN-------PGQANYA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 170 SSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLTG 249
Cdd:cd05333  151 ASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITG 230

                 ....*...
gi 388856966 250 SVIRPDGG 257
Cdd:cd05333  231 QVLHVNGG 238
FabG-like PRK07231
SDR family oxidoreductase;
6-261 1.60e-52

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 171.17  E-value: 1.60e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQCRA--YQCDVGDAELVKKTLKQAQD 83
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRN----EEAAERVAAEILAGGRAiaVAADVSDEADVEAAVAAALE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVS-VVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeIYNQEGLnkp 162
Cdd:PRK07231  78 RFGSVDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEG--GGAIVNVASTAG-LRPRPGL--- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 ltqVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTS----GMDAKIRDFQASSIPMGRFSEPHEQADPAVL 238
Cdd:PRK07231 152 ---GWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEafmgEPTPENRAKFLATIPLGRLGTPEDIANAALF 228
                        250       260
                 ....*....|....*....|...
gi 388856966 239 LLSDKASYLTGSVIRPDGGFTIW 261
Cdd:PRK07231 229 LASDEASWITGVTLVVDGGRCVG 251
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-260 6.14e-52

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 169.25  E-value: 6.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK05565   2 KLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSseiynqeGLNKPLTQ 165
Cdd:PRK05565  82 GKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKR--KSGVIVNISSIW-------GLIGASCE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKAS 245
Cdd:PRK05565 153 VLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDAS 232
                        250
                 ....*....|....*
gi 388856966 246 YLTGSVIRPDGGFTI 260
Cdd:PRK05565 233 YITGQIITVDGGWTC 247
PRK06114 PRK06114
SDR family oxidoreductase;
2-261 1.80e-51

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 168.42  E-value: 1.80e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   2 PFVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQA 81
Cdd:PRK06114   1 PQLFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVART 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  82 QDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYNQEglnk 161
Cdd:PRK06114  81 EAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENG--GGSIVNIASMSGIIVNRG---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 162 pLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTS--GMDAKIRDFQaSSIPMGRFSEPHEQADPAVLL 239
Cdd:PRK06114 155 -LLQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTrpEMVHQTKLFE-EQTPMQRMAKVDEMVGPAVFL 232
                        250       260
                 ....*....|....*....|..
gi 388856966 240 LSDKASYLTGSVIRPDGGFTIW 261
Cdd:PRK06114 233 LSDAASFCTGVDLLVDGGFVCW 254
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
18-259 1.06e-50

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: 165.68  E-value: 1.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   18 NRGIGLAMSKAVANAGANVAIFYRShPKAQEAAAEVAKEFGVqcRAYQCDVGDAELVKKTLKQAQDELGQVTGLLANAGV 97
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLN-EALAKRVEELAEELGA--AVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   98 S--VVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIEsgfkKGSIVITSSMSSEIYNqeglnkPLTQVfYNSSKGAV 175
Cdd:pfam13561  82 ApkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE----GGSIVNLSSIGAERVV------PNYNA-YGAAKAAL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  176 TNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDA--KIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLTGSVIR 253
Cdd:pfam13561 151 EALTRYLAVELGPRGIRVNAISPGPIKTLAASGIPGfdELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLY 230

                  ....*.
gi 388856966  254 PDGGFT 259
Cdd:pfam13561 231 VDGGYT 236
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
7-261 2.68e-50

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: 165.25  E-value: 2.68e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSEIynqeglnkPL-TQ 165
Cdd:cd05358   81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSK-IKGKIINMSSVHEKI--------PWpGH 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT----EQTSgmDAKIRDFQASSIPMGRFSEPHEQADPAVLLLS 241
Cdd:cd05358  152 VNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTpinaEAWD--DPEQRADLLSLIPMGRIGEPEEIAAAAAWLAS 229
                        250       260
                 ....*....|....*....|
gi 388856966 242 DKASYLTGSVIRPDGGFTIW 261
Cdd:cd05358  230 DEASYVTGTTLFVDGGMTLY 249
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
6-261 4.40e-50

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 165.12  E-value: 4.40e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHL-EALGIDALWIAADVADEADIERLAEETLERF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMsseiynqEGL--NKP- 162
Cdd:PRK08213  88 GHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPR-GYGRIINVASV-------AGLggNPPe 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 -LTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLS 241
Cdd:PRK08213 160 vMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERLGEDLLAHTPLGRLGDDEDLKGAALLLAS 239
                        250       260
                 ....*....|....*....|
gi 388856966 242 DKASYLTGSVIRPDGGFTIW 261
Cdd:PRK08213 240 DASKHITGQILAVDGGVSAV 259
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-257 4.00e-49

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 162.35  E-value: 4.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSmsseiynQEGLNKPLTQ 165
Cdd:PRK12825  83 GRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRG--GRIVNISS-------VAGLPGWPGR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKAS 245
Cdd:PRK12825 154 SNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASD 233
                        250
                 ....*....|..
gi 388856966 246 YLTGSVIRPDGG 257
Cdd:PRK12825 234 YITGQVIEVTGG 245
PRK12826 PRK12826
SDR family oxidoreductase;
6-259 9.19e-49

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 161.24  E-value: 9.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGvQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGG-KARARQVDVRDRAALKAAVAAGVEDF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSseiynqeGLNKPLT- 164
Cdd:PRK12826  82 GRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGG--GRIVLTSSVA-------GPRVGYPg 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM-DAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:PRK12826 153 LAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLgDAQWAEAIAAAIPLGRLGEPEDIAAAVLFLASDE 232
                        250
                 ....*....|....*.
gi 388856966 244 ASYLTGSVIRPDGGFT 259
Cdd:PRK12826 233 ARYITGQTLPVDGGAT 248
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
9-260 9.83e-48

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: 158.98  E-value: 9.83e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASEL-RAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSEiynQEGLNKPLTqvfy 168
Cdd:cd05344   80 DILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGW--GRIVNISSLTVK---EPEPNLVLS---- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 169 NSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQT-----------SGMDAKIRDFQASSIPMGRFSEPHEQADPAV 237
Cdd:cd05344  151 NVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVrrllearaekeGISVEEAEKEVASQIPLGRVGKPEELAALIA 230
                        250       260
                 ....*....|....*....|...
gi 388856966 238 LLLSDKASYLTGSVIRPDGGFTI 260
Cdd:cd05344  231 FLASEKASYITGQAILVDGGLTR 253
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
10-218 1.52e-47

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 156.62  E-value: 1.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKEL-GALGGKALFIQGDVTDRAQVKALVEQAVERLGRLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   90 GLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSseiynqeGLNKPLTQVFYN 169
Cdd:pfam00106  80 ILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKG--SGGRIVNISSVA-------GLVPYPGGSAYS 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 388856966  170 SSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEqtsgMDAKIRDFQA 218
Cdd:pfam00106 151 ASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTD----MTKELREDEG 195
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
6-261 3.25e-44

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 149.88  E-value: 3.25e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK08936   4 DLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSEIynqeglnkPL-T 164
Cdd:PRK08936  84 GTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHD-IKGNIINMSSVHEQI--------PWpL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT----EQTSgmDAKIRDFQASSIPMGRFSEPHEQADPAVLLL 240
Cdd:PRK08936 155 FVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTpinaEKFA--DPKQRADVESMIPMGYIGKPEEIAAVAAWLA 232
                        250       260
                 ....*....|....*....|.
gi 388856966 241 SDKASYLTGSVIRPDGGFTIW 261
Cdd:PRK08936 233 SSEASYVTGITLFADGGMTLY 253
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
7-219 4.58e-44

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 149.25  E-value: 4.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA-GARVEVVALDVTDPDAVAALAEAVLARFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYNqeglnkPLTQV 166
Cdd:COG0300   82 PIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARG--RGRIVNVSSVAGLRGL------PGMAA 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 388856966 167 fYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQAS 219
Cdd:COG0300  154 -YAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLLS 205
PRK05867 PRK05867
SDR family oxidoreductase;
4-259 1.37e-43

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 148.26  E-value: 1.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   4 VIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKeFGVQCRAYQCDVGDAELVKKTLKQAQD 83
Cdd:PRK05867   4 LFDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGT-SGGKVVPVCCDVSQHQQVTSMLDQVTA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSEIynqegLNKPL 163
Cdd:PRK05867  83 ELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQG-QGGVIINTASMSGHI-----INVPQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 TQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQaSSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:PRK05867 157 QVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQPLWE-PKIPLGRLGRPEELAGLYLYLASEA 235
                        250
                 ....*....|....*.
gi 388856966 244 ASYLTGSVIRPDGGFT 259
Cdd:PRK05867 236 SSYMTGSDIVIDGGYT 251
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
8-254 1.40e-43

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: 147.64  E-value: 1.40e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQ 87
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARR----AERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeIYNQEGLNkpltqvF 167
Cdd:COG4221   80 LDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARG--SGHIVNISSIAG-LRPYPGGA------V 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 168 YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYL 247
Cdd:COG4221  151 YAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQPAHVN 230

                 ....*...
gi 388856966 248 TGSV-IRP 254
Cdd:COG4221  231 VNELvLRP 238
PRK06841 PRK06841
short chain dehydrogenase; Provisional
6-260 3.69e-42

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 144.42  E-value: 3.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVakefGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLL----GGNAKGLVCDVSDSQSVEAAVAAVISAF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIynqeGLNKpltQ 165
Cdd:PRK06841  88 GRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAG--GGKIVNLASQAGVV----ALER---H 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-------QTSGMDAKIRdfqassIPMGRFSEPHEQADPAVL 238
Cdd:PRK06841 159 VAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTElgkkawaGEKGERAKKL------IPAGRFAYPEEIAAAALF 232
                        250       260
                 ....*....|....*....|..
gi 388856966 239 LLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK06841 233 LASDAAAMITGENLVIDGGYTI 254
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
7-260 8.36e-42

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 143.79  E-value: 8.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDIS-PEIEKLADELCGR-GHRCTAVVADVRDPASVAAAIKRAKEKEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSEIYNQEGlnkpltQV 166
Cdd:PRK08226  82 RIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKD--GRIVMMSSVTGDMVADPG------ET 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM---------DAKIRDFqASSIPMGRFSEPHEQADPAV 237
Cdd:PRK08226 154 AYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIarqsnpedpESVLTEM-AKAIPLRRLADPLEVGELAA 232
                        250       260
                 ....*....|....*....|...
gi 388856966 238 LLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK08226 233 FLASDESSYLTGTQNVIDGGSTL 255
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
6-257 4.02e-41

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 142.12  E-value: 4.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVaIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK07097   7 SLKGKIALITGASYGIGFAIAKAYAKAGATI-VFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYNQeglnkplTQ 165
Cdd:PRK07097  86 GVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKG--HGKIINICSMMSELGRE-------TV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTsgmdAKIRDFQA------------SSIPMGRFSEPHEQA 233
Cdd:PRK07097 157 SAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQT----APLRELQAdgsrhpfdqfiiAKTPAARWGDPEDLA 232
                        250       260
                 ....*....|....*....|....
gi 388856966 234 DPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK07097 233 GPAVFLASDASNFVNGHILYVDGG 256
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
14-260 1.41e-40

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: 140.18  E-value: 1.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  14 VTGGNRGIGLAMSKAVANAGANVAI-FYRSHPKAQEAAAEVAkEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGLL 92
Cdd:cd05359    3 VTGGSRGIGKAIALRLAERGADVVInYRKSKDAAAEVAAEIE-ELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  93 ANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYNQeglnkplTQVFYNSSK 172
Cdd:cd05359   82 SNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERG--GGRIVAISSLGSIRALP-------NYLAVGTAK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 173 GAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLTGS 250
Cdd:cd05359  153 AALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFpnREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQ 232
                        250
                 ....*....|
gi 388856966 251 VIRPDGGFTI 260
Cdd:cd05359  233 TLVVDGGLSI 242
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-257 6.19e-40

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 138.55  E-value: 6.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAEC-GALGTEVRGYAANVTDEEDVEATFAQIAEDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAG-------VSVVKPAVE--LTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSeiYNQ 156
Cdd:PRK08217  81 GQLNGLINNAGilrdgllVKAKDGKVTskMSLEQFQSVIDVNLTGVFLCGREAAAKMIESG-SKGVIINISSIAR--AGN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 157 EGlnkpltQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPA 236
Cdd:PRK08217 158 MG------QTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEALERLEKMIPVGRLGEPEEIAHTV 231
                        250       260
                 ....*....|....*....|.
gi 388856966 237 VLLLSDkaSYLTGSVIRPDGG 257
Cdd:PRK08217 232 RFIIEN--DYVTGRVLEIDGG 250
PRK06947 PRK06947
SDR family oxidoreductase;
10-257 6.52e-40

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 138.40  E-value: 6.52e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAG-VSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVA-QLWIESGFKKGSIVITSSMSSEiynqegLNKPLTQVF 167
Cdd:PRK06947  83 ALVNNAGiVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAArRLSTDRGGRGGAIVNVSSIASR------LGSPNEYVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 168 YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-QTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASY 246
Cdd:PRK06947 157 YAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEiHASGGQPGRAARLGAQTPLGRAGEADEVAETIVWLLSDAASY 236
                        250
                 ....*....|.
gi 388856966 247 LTGSVIRPDGG 257
Cdd:PRK06947 237 VTGALLDVGGG 247
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
8-257 1.49e-39

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: 137.81  E-value: 1.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAaevakEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQ 87
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVA-----KLGDNCRFVPVDVTSEKDVKAALALAKAKFGR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSVV------KPAVELTSDDFRYVYDTNVLGVFN----SAKAVAQLWIESGFKKGSIVITSSMSSeiynQE 157
Cdd:cd05371   76 LDIVVNCAGIAVAaktynkKGQQPHSLELFQRVINVNLIGTFNvirlAAGAMGKNEPDQGGERGVIINTASVAA----FE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 158 GlnkPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPM-GRFSEPHEQADPA 236
Cdd:cd05371  152 G---QIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPFpSRLGDPAEYAHLV 228
                        250       260
                 ....*....|....*....|.
gi 388856966 237 VLLLSDkaSYLTGSVIRPDGG 257
Cdd:cd05371  229 QHIIEN--PYLNGEVIRLDGA 247
PRK07677 PRK07677
short chain dehydrogenase; Provisional
9-257 2.05e-39

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 137.12  E-value: 2.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEI-EQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVitsSMSSEIYNQEGLNkpltQVFY 168
Cdd:PRK07677  80 DALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKG-IKGNII---NMVATYAWDAGPG----VIHS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 169 NSSKGAVTNLGKCLAAEWA-QHGIRVNILEPGfcNTEQTSGMDAKIRDFQAS-----SIPMGRFSEPHEQADPAVLLLSD 242
Cdd:PRK07677 152 AAAKAGVLAMTRTLAVEWGrKYGIRVNAIAPG--PIERTGGADKLWESEEAAkrtiqSVPLGRLGTPEEIAGLAYFLLSD 229
                        250
                 ....*....|....*
gi 388856966 243 KASYLTGSVIRPDGG 257
Cdd:PRK07677 230 EAAYINGTCITMDGG 244
PRK07060 PRK07060
short chain dehydrogenase; Provisional
1-260 1.40e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 134.84  E-value: 1.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   1 MPFVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRshpkAQEAAAEVAKEFGvqCRAYQCDVGDAElvkkTLKQ 80
Cdd:PRK07060   1 MNMAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAAR----NAAALDRLAGETG--CEPLRLDVGDDA----AIRA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  81 AQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSmsseiynQEGLN 160
Cdd:PRK07060  71 ALAAAGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAG-RGGSIVNVSS-------QAALV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 161 KPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE--QTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVL 238
Cdd:PRK07060 143 GLPDHLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPmaAEAWSDPQKSGPMLAAIPLGRFAEVDDVAAPILF 222
                        250       260
                 ....*....|....*....|..
gi 388856966 239 LLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK07060 223 LLSDAASMVSGVSLPVDGGYTA 244
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
1-261 3.16e-38

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 135.03  E-value: 3.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   1 MPFVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQ 80
Cdd:PRK08277   2 MPNLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEI-KAAGGEALAVKADVLDKESLEQARQQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  81 AQDELGQVTGLLANAG---------------VSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVI 145
Cdd:PRK08277  81 ILEDFGPCDILINGAGgnhpkattdnefhelIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGR--KGGNIIN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 146 TSSMSSEIynqeglnkPLTQVF-YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM----DAKIRDfQASS 220
Cdd:PRK08277 159 ISSMNAFT--------PLTKVPaYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALlfneDGSLTE-RANK 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 388856966 221 I----PMGRFSEPHEQADPAVLLLSDKAS-YLTGSVIRPDGGFTIW 261
Cdd:PRK08277 230 IlahtPMGRFGKPEELLGTLLWLADEKASsFVTGVVLPVDGGFSAY 275
PRK06138 PRK06138
SDR family oxidoreductase;
6-261 5.81e-38

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 133.74  E-value: 5.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKefGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA--GGRAFARQGDVGSAEAVEALVDFVAARW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeiYNQEGLNKPltq 165
Cdd:PRK06138  80 GRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQG--GGSIVNTASQLA--LAGGRGRAA--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 vfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRD---FQASS---IPMGRFSEPHEQADPAVLL 239
Cdd:PRK06138 153 --YVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADpeaLREALrarHPMNRFGTAEEVAQAALFL 230
                        250       260
                 ....*....|....*....|..
gi 388856966 240 LSDKASYLTGSVIRPDGGFTIW 261
Cdd:PRK06138 231 ASDESSFATGTTLVVDGGWLAA 252
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
7-259 6.76e-38

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: 133.34  E-value: 6.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHpKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:cd05329    4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQ-KELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLAN-AGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSseiynqeGLNKPLTQ 165
Cdd:cd05329   83 GKLNILVNnAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASG--NGNIVFISSVA-------GVIAVPSG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:cd05329  154 APYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPViqQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPA 233
                        250
                 ....*....|....*.
gi 388856966 244 ASYLTGSVIRPDGGFT 259
Cdd:cd05329  234 ASYITGQIIAVDGGLT 249
PRK12939 PRK12939
short chain dehydrogenase; Provisional
7-258 4.00e-37

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 131.25  E-value: 4.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK12939   5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAA-GGRAHAIAADLADPASVQRFFDAAAAALG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeiynqeGLNKPLTQV 166
Cdd:PRK12939  84 GLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSG--RGRIVNLASDTA------LWGAPKLGA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 167 fYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIR-DFQASSIPMGRFSEPHEQADPAVLLLSDKAS 245
Cdd:PRK12939 156 -YVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADERhAYYLKGRALERLQVPDDVAGAVLFLLSDAAR 234
                        250
                 ....*....|...
gi 388856966 246 YLTGSVIRPDGGF 258
Cdd:PRK12939 235 FVTGQLLPVNGGF 247
PRK09730 PRK09730
SDR family oxidoreductase;
13-257 4.08e-37

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 131.13  E-value: 4.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  13 VVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGLL 92
Cdd:PRK09730   5 LVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLAALV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  93 ANAGVSVVKPAVE-LTSDDFRYVYDTNVLGVFNSAK-AVAQLWIESGFKKGSIVITSSMSSEiynqegLNKPLTQVFYNS 170
Cdd:PRK09730  85 NNAGILFTQCTVEnLTAERINRVLSTNVTGYFLCCReAVKRMALKHGGSGGAIVNVSSAASR------LGAPGEYVDYAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 171 SKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-QTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLTG 249
Cdd:PRK09730 159 SKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEmHASGGEPGRVDRVKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTG 238

                 ....*...
gi 388856966 250 SVIRPDGG 257
Cdd:PRK09730 239 SFIDLAGG 246
PRK06484 PRK06484
short chain dehydrogenase; Validated
9-259 5.77e-37

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 136.52  E-value: 5.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRD----AEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRL 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAG-VSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLwiesgFKKGSIVITSSMSSEIYNQEGLNKpltqvf 167
Cdd:PRK06484 345 DVLVNNAGiAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARL-----MSQGGVIVNLGSIASLLALPPRNA------ 413
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 168 YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT------EQTSGMD-AKIRdfqaSSIPMGRFSEPHEQADPAVLLL 240
Cdd:PRK06484 414 YCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETpavlalKASGRADfDSIR----RRIPLGRLGDPEEVAEAIAFLA 489
                        250
                 ....*....|....*....
gi 388856966 241 SDKASYLTGSVIRPDGGFT 259
Cdd:PRK06484 490 SPAASYVNGATLTVDGGWT 508
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
5-258 1.70e-36

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: 130.27  E-value: 1.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:cd08935    1 FSLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEI-TALGGRAIALAADVLDRASLERAREEIVAQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAG--------------VSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMS 150
Cdd:cd08935   80 FGTVDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQ--KGGSIINISSMN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 151 SEIynqeglnkPLTQV-FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM----DAKIRDFQASSI---P 222
Cdd:cd08935  158 AFS--------PLTKVpAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLlinpDGSYTDRSNKILgrtP 229
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 388856966 223 MGRFSEPHEQADPAVLLLSDKAS-YLTGSVIRPDGGF 258
Cdd:cd08935  230 MGRFGKPEELLGALLFLASEKASsFVTGVVIPVDGGF 266
PRK09242 PRK09242
SDR family oxidoreductase;
7-261 2.08e-36

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 129.48  E-value: 2.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEF-GVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFpEREVHGLAADVSDDEDRRAILDWVEDHW 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYNQEGlnkpltq 165
Cdd:PRK09242  87 DGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHA--SSAIVNIGSVSGLTHVRSG------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:PRK09242 158 APYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPlsDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPA 237
                        250
                 ....*....|....*...
gi 388856966 244 ASYLTGSVIRPDGGFTIW 261
Cdd:PRK09242 238 ASYITGQCIAVDGGFLRY 255
PRK06123 PRK06123
SDR family oxidoreductase;
12-257 2.52e-36

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 129.13  E-value: 2.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGL 91
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRLDAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  92 LANAGVSVVKPAVE-LTSDDFRYVYDTNVLGVFNSAK-AVAQLWIESGFKKGSIVITSSMSSEiynqegLNKPLTQVFYN 169
Cdd:PRK06123  85 VNNAGILEAQMRLEqMDAARLTRIFATNVVGSFLCAReAVKRMSTRHGGRGGAIVNVSSMAAR------LGSPGEYIDYA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 170 SSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-QTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLT 248
Cdd:PRK06123 159 ASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEiHASGGEPGRVDRVKAGIPMGRGGTAEEVARAILWLLSDEASYTT 238

                 ....*....
gi 388856966 249 GSVIRPDGG 257
Cdd:PRK06123 239 GTFIDVSGG 247
PRK07576 PRK07576
short chain dehydrogenase; Provisional
1-257 2.77e-36

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 129.30  E-value: 2.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   1 MPFVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQ 80
Cdd:PRK07576   1 MTTMFDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQL-QQAGPEGLGVSADVRDYAAVEAAFAQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  81 AQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkkGSIV-ITSSmsseiynQEGL 159
Cdd:PRK07576  80 IADEFGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG---ASIIqISAP-------QAFV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 160 NKPLtQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFcnTEQTSGM-----DAKIRDFQASSIPMGRFSEPHEQAD 234
Cdd:PRK07576 150 PMPM-QAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGP--IAGTEGMarlapSPELQAAVAQSVPLKRNGTKQDIAN 226
                        250       260
                 ....*....|....*....|...
gi 388856966 235 PAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK07576 227 AALFLASDMASYITGVVLPVDGG 249
PRK06124 PRK06124
SDR family oxidoreductase;
6-260 3.51e-36

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 129.06  E-value: 3.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK06124   8 SLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAA-GGAAEALAFDIADEEAVAAAFARIDAEH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSEIYNQeglnkplTQ 165
Cdd:PRK06124  87 GRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGY--GRIIAITSIAGQVARA-------GD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:PRK06124 158 AVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMaaDPAVGPWLAQRTPLGRWGRPEEIAGAAVFLASPA 237
                        250
                 ....*....|....*..
gi 388856966 244 ASYLTGSVIRPDGGFTI 260
Cdd:PRK06124 238 ASYVNGHVLAVDGGYSV 254
PRK07063 PRK07063
SDR family oxidoreductase;
7-257 4.04e-36

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 129.02  E-value: 4.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEF-GVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVaGARVLAVPADVTDAASVAAAVAAAEEAF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIV-ITSSMSSEIynqeglnkpLT 164
Cdd:PRK07063  85 GPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERG--RGSIVnIASTHAFKI---------IP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVF-YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASS------IPMGRFSEPHEQADPAV 237
Cdd:PRK07063 154 GCFpYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPAAARaetlalQPMKRIGRPEEVAMTAV 233
                        250       260
                 ....*....|....*....|
gi 388856966 238 LLLSDKASYLTGSVIRPDGG 257
Cdd:PRK07063 234 FLASDEAPFINATCITIDGG 253
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
7-260 7.42e-36

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: 127.89  E-value: 7.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkEFGVQCRAyqcDVGDAELVKKTLKQAQDELG 86
Cdd:cd05345    3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIG-EAAIAIQA---DVTKRADVEAMVEAALSKFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVV-KPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkkGSIVITSSMSSEIYNQEGLnkpltq 165
Cdd:cd05345   79 RLDILVNNAGITHRnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQG---GGVIINIASTAGLRPRPGL------ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT--------EQTSGMDAKIRdfqaSSIPMGRFSEPHEQADPAV 237
Cdd:cd05345  150 TWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETpllsmfmgEDTPENRAKFR----ATIPLGRLSTPDDIANAAL 225
                        250       260
                 ....*....|....*....|...
gi 388856966 238 LLLSDKASYLTGSVIRPDGGFTI 260
Cdd:cd05345  226 YLASDEASFITGVALEVDGGRCI 248
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
7-260 1.61e-35

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: 127.79  E-value: 1.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRS--HPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:cd05355   24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPeeEDDAEETKKLIEEE-GRKCLLIPGDLGDESFCRDLVKEVVKE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVE-LTSDDFRYVYDTNVLGVFNSAKAVAQLwiesgFKKGSIVITSSmSSEIYnqeglnKPL 163
Cdd:cd05355  103 FGKLDILVNNAAYQHPQESIEdITTEQLEKTFRTNIFSMFYLTKAALPH-----LKKGSSIINTT-SVTAY------KGS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 TQVF-YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-QTSGMDA-KIRDFqASSIPMGRFSEPHEQADPAVLLL 240
Cdd:cd05355  171 PHLLdYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPlIPSSFPEeKVSEF-GSQVPMGRAGQPAEVAPAYVFLA 249
                        250       260
                 ....*....|....*....|
gi 388856966 241 SDKASYLTGSVIRPDGGFTI 260
Cdd:cd05355  250 SQDSSYVTGQVLHVNGGEII 269
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
10-260 2.27e-35

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: 126.80  E-value: 2.27e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPkaqEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRST---ESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVV------KPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVitsSMSSEIYnqEGLNKPL 163
Cdd:cd05349   78 TIVNNALIDFPfdpdqrKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGS--GRVI---NIGTNLF--QNPVVPY 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 TQvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAK-IRDFQASSIPMGRFSEPHEQADPAVLLLSD 242
Cdd:cd05349  151 HD--YTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAATPKeVFDAIAQTTPLGKVTTPQDIADAVLFFASP 228
                        250
                 ....*....|....*...
gi 388856966 243 KASYLTGSVIRPDGGFTI 260
Cdd:cd05349  229 WARAVTGQNLVVDGGLVM 246
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
9-257 3.35e-35

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: 126.34  E-value: 3.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSeiynQEGLnkPLTQVfY 168
Cdd:cd05366   82 DVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLG-HGGKIINASSIAG----VQGF--PNLGA-Y 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 169 NSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKI-----------RDFQASSIPMGRFSEPHEQADPAV 237
Cdd:cd05366  154 SASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVgeiagkpegegFAEFSSSIPLGRLSEPEDVAGLVS 233
                        250       260
                 ....*....|....*....|
gi 388856966 238 LLLSDKASYLTGSVIRPDGG 257
Cdd:cd05366  234 FLASEDSDYITGQTILVDGG 253
PRK06500 PRK06500
SDR family oxidoreductase;
7-257 5.02e-35

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 125.84  E-value: 5.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRD----PASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLwiesgFKKG-SIVITSSMSSEIynqeGLnkPLTQ 165
Cdd:PRK06500  80 RLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPL-----LANPaSIVLNGSINAHI----GM--PNSS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT----------EQTSGMDAKIRdfqaSSIPMGRFSEPHEQADP 235
Cdd:PRK06500 149 V-YAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTplygklglpeATLDAVAAQIQ----ALVPLGRFGTPEEIAKA 223
                        250       260
                 ....*....|....*....|..
gi 388856966 236 AVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK06500 224 VLYLASDESAFIVGSEIIVDGG 245
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
5-259 6.17e-35

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: 125.57  E-value: 6.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:cd05341    1 NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDIL----DEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIynqeGLnkPLT 164
Cdd:cd05341   77 FGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAG--GGSIINMSSIEGLV----GD--PAL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVfYNSSKGAVTNLGKCLAAEWAQH--GIRVNILEPGFCNTEQTSGM-DAKIRDFQASSIPMGRFSEPHEQADPAVLLLS 241
Cdd:cd05341  149 AA-YNASKGAVRGLTKSAALECATQgyGIRVNSVHPGYIYTPMTDELlIAQGEMGNYPNTPMGRAGEPDEIAYAVVYLAS 227
                        250
                 ....*....|....*...
gi 388856966 242 DKASYLTGSVIRPDGGFT 259
Cdd:cd05341  228 DESSFVTGSELVVDGGYT 245
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-258 1.39e-34

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 124.85  E-value: 1.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANvaIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGAD--IIITTHGTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSeiyNQEGLNKPLtq 165
Cdd:PRK06935  90 GKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGS--GKIINIASMLS---FQGGKFVPA-- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 vfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTsgmdAKIRDFQA------SSIPMGRFSEPHEQADPAVLL 239
Cdd:PRK06935 163 --YTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANT----APIRADKNrndeilKRIPAGRWGEPDDLMGAAVFL 236
                        250
                 ....*....|....*....
gi 388856966 240 LSDKASYLTGSVIRPDGGF 258
Cdd:PRK06935 237 ASRASDYVNGHILAVDGGW 255
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
8-257 6.01e-34

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: 122.83  E-value: 6.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQ 87
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSV---VKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSM------SSEIYNQEG 158
Cdd:cd08930   81 IDILINNAYPSPkvwGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQG--KGSIINIASIygviapDFRIYENTQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 159 LNKPLTqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGfcnteqtsgmdaKIRDFQAS--------SIPMGRFSEPH 230
Cdd:cd08930  159 MYSPVE---YSVIKAGIIHLTKYLAKYYADTGIRVNAISPG------------GILNNQPSeflekytkKCPLKRMLNPE 223
                        250       260
                 ....*....|....*....|....*..
gi 388856966 231 EQADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:cd08930  224 DLRGAIIFLLSDASSYVTGQNLVIDGG 250
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
13-258 7.79e-34

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 122.57  E-value: 7.79e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  13 VVTGGNRGIGLAMSKAVANAGANVAIFYRShpkAQEAAAEVAKEFGV---QCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:PRK12824   6 LVTGAKRGIGSAIARELLNDGYRVIATYFS---GNDCAKDWFEEYGFtedQVRLKELDVTDTEECAEALAEIEEEEGPVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNsakaVAQLWIESGFKKGS--IVITSSMSseiynqeGLNKPLTQVF 167
Cdd:PRK12824  83 ILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFN----VTQPLFAAMCEQGYgrIINISSVN-------GLKGQFGQTN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 168 YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYL 247
Cdd:PRK12824 152 YSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFI 231
                        250
                 ....*....|.
gi 388856966 248 TGSVIRPDGGF 258
Cdd:PRK12824 232 TGETISINGGL 242
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
6-259 1.66e-33

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 122.18  E-value: 1.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAqEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK07523   7 DLTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKL-AAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEiynqegLNKPlTQ 165
Cdd:PRK07523  86 GPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARG--AGKIINIASVQSA------LARP-GI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:PRK07523 157 APYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALvaDPEFSAWLEKRTPAGRWGKVEELVGACVFLASDA 236
                        250
                 ....*....|....*.
gi 388856966 244 ASYLTGSVIRPDGGFT 259
Cdd:PRK07523 237 SSFVNGHVLYVDGGIT 252
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
5-258 7.46e-33

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: 119.88  E-value: 7.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkefGVQcrAYQCDVGDAELVKKTLKQAqde 84
Cdd:cd05351    3 LDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECP---GIE--PVCVDLSDWDATEEALGSV--- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 lGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFKkGSIVITSSMSSEiynqeglnKPLT 164
Cdd:cd05351   75 -GPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVP-GSIVNVSSQASQ--------RALT 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 -QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE--QTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLS 241
Cdd:cd05351  145 nHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDmgRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILFLLS 224
                        250
                 ....*....|....*..
gi 388856966 242 DKASYLTGSVIRPDGGF 258
Cdd:cd05351  225 DKSSMTTGSTLPVDGGF 241
PRK12827 PRK12827
short chain dehydrogenase; Provisional
7-258 1.86e-32

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 119.05  E-value: 1.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQ---CRAYQCDVGDAELVKKTLKQAQD 83
Cdd:PRK12827   4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEAAggkALGLAFDVRDFAATRAALDAGVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSEIYNQEGLNkpl 163
Cdd:PRK12827  84 EFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRAR-RGGRIVNIASVAGVRGNRGQVN--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 tqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSgmDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:PRK12827 160 ----YAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMAD--NAAPTEHLLNPVPVQRLGEPDEVAALVAFLVSDA 233
                        250
                 ....*....|....*
gi 388856966 244 ASYLTGSVIRPDGGF 258
Cdd:PRK12827 234 ASYVTGQVIPVDGGF 248
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
2-259 2.50e-32

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 118.83  E-value: 2.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   2 PFVIDLKGQTIVVTGGNRGIGLAMSKAvanaganvaiFYrshpkaqEAAAEVA-------KEFGVQCRAYQCDVGDAELV 74
Cdd:PRK08220   1 MNAMDFSGKTVWVTGAAQGIGYAVALA----------FV-------EAGAKVIgfdqaflTQEDYPFATFVLDVSDAAAV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  75 KKTLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSeiy 154
Cdd:PRK08220  64 AQVCQRLLAETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQ--RSGAIVTVGSNAA--- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 155 nqeglNKPLTQV-FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-------QTSGMDAKIRDFQAS---SIPM 223
Cdd:PRK08220 139 -----HVPRIGMaAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDmqrtlwvDEDGEQQVIAGFPEQfklGIPL 213
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 388856966 224 GRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK08220 214 GKIARPQEIANAVLFLASDLASHITLQDIVVDGGAT 249
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-260 2.58e-32

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 118.91  E-value: 2.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVVKPA--VELTSDDFRYVYDTNVLGVFNSAKAVAQLWI----ESGFKKGSIVITSSMSSEIYNQEGLNkpl 163
Cdd:PRK12745  83 CLVNNAGVGVKVRGdlLDLTPESFDRVLAINLRGPFFLTQAVAKRMLaqpePEELPHRSIVFVSSVNAIMVSPNRGE--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 tqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRD-FQASSIPMGRFSEPHEQADPAVLLLSD 242
Cdd:PRK12745 160 ----YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAKYDAlIAKGLVPMPRWGEPEDVARAVAALASG 235
                        250
                 ....*....|....*...
gi 388856966 243 KASYLTGSVIRPDGGFTI 260
Cdd:PRK12745 236 DLPYSTGQAIHVDGGLSI 253
PRK08589 PRK08589
SDR family oxidoreductase;
7-257 3.06e-32

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 119.11  E-value: 3.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHpKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAE-AVSETVDKI-KSNGGKAKAYHVDISDEQQVKDFASEIKEQFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAV-ELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkkGSIVITSSMSseiynqeGLNKPLTQ 165
Cdd:PRK08589  82 RVDVLFNNAGVDNAAGRIhEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQG---GSIINTSSFS-------GQAADLYR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT---EQTSG-----MDAKIRDFQASSIPMGRFSEPHEQADPAV 237
Cdd:PRK08589 152 SGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETplvDKLTGtsedeAGKTFRENQKWMTPLGRLGKPEEVAKLVV 231
                        250       260
                 ....*....|....*....|
gi 388856966 238 LLLSDKASYLTGSVIRPDGG 257
Cdd:PRK08589 232 FLASDDSSFITGETIRIDGG 251
PRK07035 PRK07035
SDR family oxidoreductase;
6-260 3.14e-32

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 118.58  E-value: 3.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK07035   5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAA-GGKAEALACHIGEMEQIDALFAHIRERH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVS-VVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSseiynqeGLNKPLT 164
Cdd:PRK07035  84 GRLDILVNNAAANpYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQG--GGSIVNVASVN-------GVSPGDF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVLLLSD 242
Cdd:PRK07035 155 QGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALfkNDAILKQALAHIPLRRHAEPSEMAGAVLYLASD 234
                        250
                 ....*....|....*...
gi 388856966 243 KASYLTGSVIRPDGGFTI 260
Cdd:PRK07035 235 ASSYTTGECLNVDGGYLS 252
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
11-260 3.47e-32

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: 118.72  E-value: 3.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHP-KAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDdQATEVVAEVLAA-GRRAIYFQADIGELSDHEALLDQAWEDFGRLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVVKPA--VELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFKK----GSIVITSSMSSEIYNQEglnkpl 163
Cdd:cd05337   82 CLVNNAGIAVRPRGdlLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRFdgphRSIIFVTSINAYLVSPN------ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 tQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRD-FQASSIPMGRFSEPHEQADPAVLLLSD 242
Cdd:cd05337  156 -RGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDElIAAGLVPIRRWGQPEDIAKAVRTLASG 234
                        250
                 ....*....|....*...
gi 388856966 243 KASYLTGSVIRPDGGFTI 260
Cdd:cd05337  235 LLPYSTGQPINIDGGLSM 252
PRK06701 PRK06701
short chain dehydrogenase; Provisional
7-260 5.57e-32

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 118.98  E-value: 5.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRS-HPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDeHEDANETKQRVEKE-GVKCLLIPGDVSDEAFCKDAVEETVREL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVE-LTSDDFRYVYDTNVLGVFNSAKAvAQLWIESGfkkGSIVITSSmsseIYNQEGlNKPLt 164
Cdd:PRK06701 123 GRLDILVNNAAFQYPQQSLEdITAEQLDKTFKTNIYSYFHMTKA-ALPHLKQG---SAIINTGS----ITGYEG-NETL- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 qVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-QTSGMDA-KIRDFQASSiPMGRFSEPHEQADPAVLLLSD 242
Cdd:PRK06701 193 -IDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPlIPSDFDEeKVSQFGSNT-PMQRPGQPEELAPAYVFLASP 270
                        250
                 ....*....|....*...
gi 388856966 243 KASYLTGSVIRPDGGFTI 260
Cdd:PRK06701 271 DSSYITGQMLHVNGGVIV 288
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
7-257 7.37e-32

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: 117.59  E-value: 7.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAyqcDVGDAELVKKTLKQAQDELG 86
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGG-ALALRV---DVTDEQQVAALFERAVEEFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTS-DDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSseiynqeGLNKPLTQ 165
Cdd:cd08944   77 GLDLLVNNAGAMHLTPAIIDTDlAVWDQTMAINLRGTFLCCRHAAPRMIARG--GGSIVNLSSIA-------GQSGDPGY 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTsgmDAKIRDFQASSIPMG----------RFSEPHEQADP 235
Cdd:cd08944  148 GAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLL---LAKLAGFEGALGPGGfhllihqlqgRLGRPEDVAAA 224
                        250       260
                 ....*....|....*....|..
gi 388856966 236 AVLLLSDKASYLTGSVIRPDGG 257
Cdd:cd08944  225 VVFLLSDDASFITGQVLCVDGG 246
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
7-259 1.04e-31

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: 116.99  E-value: 1.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkAQEAAAEVAKEF---GVQCRAYQCDVGDAELVKKTLKQAQD 83
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYAS---SKAAAEEVVAEIeaaGGKAIAVQADVSDPSQVARLFDAAEK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLwIESGfkkGSIVITSSMSSEIYnqeglnKPL 163
Cdd:cd05362   78 AFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKR-LRDG---GRIINISSSLTAAY------TPN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 TQVfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQ-TSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSD 242
Cdd:cd05362  148 YGA-YAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMfYAGKTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASP 226
                        250
                 ....*....|....*..
gi 388856966 243 KASYLTGSVIRPDGGFT 259
Cdd:cd05362  227 DGRWVNGQVIRANGGYV 243
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
7-260 1.14e-31

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 117.13  E-value: 1.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAI-FYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVnYARSRKAAEETAEEI-EALGRKALAVKANVGDVEKIKEMFAQIDEEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSS----EIYNQEGLnk 161
Cdd:PRK08063  81 GRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVG--GGKIISLSSLGSirylENYTTVGV-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 162 pltqvfynsSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTS---GMDAKIRDFQASSiPMGRFSEPHEQADPAVL 238
Cdd:PRK08063 157 ---------SKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKhfpNREELLEDARAKT-PAGRMVEPEDVANAVLF 226
                        250       260
                 ....*....|....*....|..
gi 388856966 239 LLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK08063 227 LCSPEADMIRGQTIIVDGGRSL 248
PRK06484 PRK06484
short chain dehydrogenase; Validated
8-259 1.42e-31

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 121.49  E-value: 1.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKavanaganvaIFYRSH------PKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQA 81
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQ----------RFARAGdqvvvaDRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  82 QDELGQVTGLLANAGVS--VVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQlWIESGFKKGSIVITSSMSseiynqeGL 159
Cdd:PRK06484  74 HREFGRIDVLVNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALR-LMIEQGHGAAIVNVASGA-------GL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 160 NKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM-DAKIRDFQA--SSIPMGRFSEPHEQADPA 236
Cdd:PRK06484 146 VALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELeRAGKLDPSAvrSRIPLGRLGRPEEIAEAV 225
                        250       260
                 ....*....|....*....|...
gi 388856966 237 VLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK06484 226 FFLASDQASYITGSTLVVDGGWT 248
PRK12743 PRK12743
SDR family oxidoreductase;
10-260 1.51e-31

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 117.06  E-value: 1.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIV-ITSSmsseiynQEGLNKPlTQVFY 168
Cdd:PRK12743  83 VLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQG-QGGRIInITSV-------HEHTPLP-GASAY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 169 NSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLT 248
Cdd:PRK12743 154 TAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPGIPLGRPGDTHEIASLVAWLCSEGASYTT 233
                        250
                 ....*....|..
gi 388856966 249 GSVIRPDGGFTI 260
Cdd:PRK12743 234 GQSLIVDGGFML 245
PRK12829 PRK12829
short chain dehydrogenase; Provisional
6-258 1.75e-31

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 117.08  E-value: 1.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkefGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK12829   8 PLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLP---GAKVTATVADVADPAQVERVFDTAVERF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVE-LTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSEiynqegLNKPLt 164
Cdd:PRK12829  85 GGLDVLVNNAGIAGPTGGIDeITPEQWEQTLAVNLNGQFYFARAAVPLLKASG-HGGVIIALSSVAGR------LGYPG- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDA-----------KIRDFQASSIPMGRFSEPHEQA 233
Cdd:PRK12829 157 RTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEaraqqlgigldEMEQEYLEKISLGRMVEPEDIA 236
                        250       260
                 ....*....|....*....|....*
gi 388856966 234 DPAVLLLSDKASYLTGSVIRPDGGF 258
Cdd:PRK12829 237 ATALFLASPAARYITGQAISVDGNV 261
PRK06172 PRK06172
SDR family oxidoreductase;
6-259 1.84e-31

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 116.77  E-value: 1.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK06172   4 TFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALI-REAGGEALFVACDVTRDAEVKALVEQTIAAY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAV-ELTSDDFRYVYDTNVLGVFNSAK-AVAQLWIESGfkkGSIVITSSMSseiynqeGLNKPL 163
Cdd:PRK06172  83 GRLDYAFNNAGIEIEQGRLaEGSEAEFDAIMGVNVKGVWLCMKyQIPLMLAQGG---GAIVNTASVA-------GLGAAP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 TQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT---EQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLL 240
Cdd:PRK06172 153 KMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTdmfRRAYEADPRKAEFAAAMHPVGRIGKVEEVASAVLYLC 232
                        250
                 ....*....|....*....
gi 388856966 241 SDKASYLTGSVIRPDGGFT 259
Cdd:PRK06172 233 SDGASFTTGHALMVDGGAT 251
PRK06057 PRK06057
short chain dehydrogenase; Provisional
7-259 1.92e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 116.75  E-value: 1.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFgvqcraYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLF------VPTDVTDEDAVNALFDTAAETYG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTS--DDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEiynqegLNKPLT 164
Cdd:PRK06057  79 SVDIAFNNAGISPPEDDSILNTglDAWQRVQDVNLTSVYLCCKAALPHMVRQG--KGSIINTASFVAV------MGSATS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASS---IPMGRFSEPHEQADPAVLLLS 241
Cdd:PRK06057 151 QISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKDPERAARRlvhVPMGRFAEPEEIAAAVAFLAS 230
                        250
                 ....*....|....*...
gi 388856966 242 DKASYLTGSVIRPDGGFT 259
Cdd:PRK06057 231 DDASFITASTFLVDGGIS 248
PRK06949 PRK06949
SDR family oxidoreductase;
1-258 5.47e-31

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 115.63  E-value: 5.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   1 MPFVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGvQCRAYQCDVGDAELVKKTLKQ 80
Cdd:PRK06949   1 MGRSINLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGG-AAHVVSLDVTDYQSIKAAVAH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  81 AQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIE------SGFKKGSIVITSSMSseiy 154
Cdd:PRK06949  80 AETEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIArakgagNTKPGGRIINIASVA---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 155 nqeGLnKPLTQV-FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE------QTSGMDAKIrdfqaSSIPMGRFS 227
Cdd:PRK06949 156 ---GL-RVLPQIgLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEinhhhwETEQGQKLV-----SMLPRKRVG 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 388856966 228 EPHEQADPAVLLLSDKASYLTGSVIRPDGGF 258
Cdd:PRK06949 227 KPEDLDGLLLLLAADESQFINGAIISADDGF 257
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
7-257 6.13e-31

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 115.51  E-value: 6.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRshpkAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADI----KPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVitsSMSSeiynQEGLNKPLTQV 166
Cdd:PRK07067  80 GIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQG-RGGKII---NMAS----QAGRRGEALVS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQ-----------ASSIPMGRFSEPHEQADP 235
Cdd:PRK07067 152 HYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQVDALFARYEnrppgekkrlvGEAVPLGRMGVPDDLTGM 231
                        250       260
                 ....*....|....*....|..
gi 388856966 236 AVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK07067 232 ALFLASADADYIVAQTYNVDGG 253
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
9-206 7.88e-31

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: 114.66  E-value: 7.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEV---AKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIeaeANASGQKVSYISADLSDYEEVEQAFAQAVEKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEI----YNQeglnk 161
Cdd:cd08939   81 GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQ--RPGHIVFVSSQAALVgiygYSA----- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 388856966 162 pltqvfYNSSKGAVTNLGKCLAAEWAQHGIRV------NILEPGFCNTEQT 206
Cdd:cd08939  154 ------YCPSKFALRGLAESLRQELKPYNIRVsvvyppDTDTPGFEEENKT 198
PRK12828 PRK12828
short chain dehydrogenase; Provisional
6-257 1.56e-30

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 113.74  E-value: 1.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkefGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVP---ADALRIGGIDLVDPQAARRAVDEVNRQF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSseiynqeGLNKPLTQ 165
Cdd:PRK12828  81 GRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASG--GGRIVNIGAGA-------ALKAGPGM 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTsgmdakirdfqASSIPMGRFS---EPHEQADPAVLLLSD 242
Cdd:PRK12828 152 GAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPN-----------RADMPDADFSrwvTPEQIAAVIAFLLSD 220
                        250
                 ....*....|....*
gi 388856966 243 KASYLTGSVIRPDGG 257
Cdd:PRK12828 221 EAQAITGASIPVDGG 235
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-259 2.40e-30

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 113.65  E-value: 2.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRshpKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK08642   1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYH---QSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQ-VTGLLANAGVSVV------KPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVitsSMSSEIYNqe 157
Cdd:PRK08642  78 FGKpITTVVNNALADFSfdgdarKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGF--GRII---NIGTNLFQ-- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 158 glNKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAK-IRDFQASSIPMGRFSEPHEQADPA 236
Cdd:PRK08642 151 --NPVVPYHDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAATPDeVFDLIAATTPLRKVTTPQEFADAV 228
                        250       260
                 ....*....|....*....|...
gi 388856966 237 VLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK08642 229 LFFASPWARAVTGQNLVVDGGLV 251
PRK12937 PRK12937
short chain dehydrogenase; Provisional
7-258 6.68e-30

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 112.14  E-value: 6.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQlWIESGfkkGSIVITSSmsseiyNQEGLNKPlTQV 166
Cdd:PRK12937  83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAAR-HLGQG---GRIINLST------SVIALPLP-GYG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-QTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKAS 245
Cdd:PRK12937 152 PYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATElFFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGA 231
                        250
                 ....*....|...
gi 388856966 246 YLTGSVIRPDGGF 258
Cdd:PRK12937 232 WVNGQVLRVNGGF 244
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
7-259 1.60e-29

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 111.52  E-value: 1.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKA-GGKAIGVAMDVTDEEAINAGIDYAVETFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSEIYNQEglnkpltQV 166
Cdd:PRK12429  81 GVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGG--GRIINMASVHGLVGSAG-------KA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE----------QTSGMDAK--IRDFQASSIPMGRFSEPHEQAD 234
Cdd:PRK12429 152 AYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPlvrkqipdlaKERGISEEevLEDVLLPLVPQKRFTTVEEIAD 231
                        250       260
                 ....*....|....*....|....*
gi 388856966 235 PAVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK12429 232 YALFLASFAAKGVTGQAWVVDGGWT 256
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
11-204 2.71e-29

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: 110.78  E-value: 2.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAvanaganvaiFYRS---------HPKAQEAAAEvakEFGVQCRAYQCDVGDAELVKKTLKQA 81
Cdd:cd05374    2 VVLITGCSSGIGLALALA----------LAAQgyrviatarNPDKLESLGE---LLNDNLEVLELDVTDEESIKAAVKEV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  82 QDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSseiynqeGLNK 161
Cdd:cd05374   69 IERFGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQG--SGRIVNVSSVA-------GLVP 139
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 388856966 162 PLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:cd05374  140 TPFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTG 182
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
7-259 7.16e-29

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: 109.85  E-value: 7.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKavanaganvaIFYRSHPK------AQEAAAEVAKEFGVQCRAY-QCDVGDAELVKKTLK 79
Cdd:cd05326    2 LDGKVAIITGGASGIGEATAR----------LFAKHGARvviadiDDDAGQAVAAELGDPDISFvHCDVTVEADVRAAVD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  80 QAQDELGQVTGLLANAGVSVVKPA--VELTSDDFRYVYDTNVLGVFNSAKAVAQLWIesGFKKGSIVITSSMSseiynqe 157
Cdd:cd05326   72 TAVARFGRLDIMFNNAGVLGAPCYsiLETSLEEFERVLDVNVYGAFLGTKHAARVMI--PAKKGSIVSVASVA------- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 158 GLNKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE---QTSGMD-AKIRD-FQASSIPMGRFSEPHEQ 232
Cdd:cd05326  143 GVVGGLGPHAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPlltAGFGVEdEAIEEaVRGAANLKGTALRPEDI 222
                        250       260
                 ....*....|....*....|....*..
gi 388856966 233 ADPAVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:cd05326  223 AAAVLYLASDDSRYVSGQNLVVDGGLT 249
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
4-258 9.30e-29

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 109.32  E-value: 9.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   4 VIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQD 83
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSmsseIYNQEGlnkPL 163
Cdd:PRK12935  81 HFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEA--EEGRIISISS----IIGQAG---GF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 TQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:PRK12935 152 GQTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRDG 231
                        250
                 ....*....|....*
gi 388856966 244 AsYLTGSVIRPDGGF 258
Cdd:PRK12935 232 A-YITGQQLNINGGL 245
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
7-260 1.12e-28

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 109.66  E-value: 1.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERS----AEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGV-----SVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkkGSIVITSSMSSEIYNQEGlnk 161
Cdd:PRK06200  80 KLDCFVGNAGIwdyntSLVDIPAETLDTAFDEIFNVNVKGYLLGAKAALPALKASG---GSMIFTLSNSSFYPGGGG--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 162 pltqVFYNSSKGAVTNLGKCLAAEWAQHgIRVNILEPGFCNTE----QTSGMDAK-------IRDFQASSIPMGRFSEPH 230
Cdd:PRK06200 154 ----PLYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDlrgpASLGQGETsisdspgLADMIAAITPLQFAPQPE 228
                        250       260       270
                 ....*....|....*....|....*....|.
gi 388856966 231 EQADPAVLLLSDKAS-YLTGSVIRPDGGFTI 260
Cdd:PRK06200 229 DHTGPYVLLASRRNSrALTGVVINADGGLGI 259
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-257 1.13e-28

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 109.49  E-value: 1.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQcrAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNS----AENEAKELREKGVF--TIKCDVGNRDQVKKSKEVVEKEFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLG-VFNSAKAVAQLWIEsgfKKGSIVITSSMSSEIYNQEGlnkpltQ 165
Cdd:PRK06463  79 RVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGaIYTTYEFLPLLKLS---KNGAIVNIASNAGIGTAAEG------T 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDA-----KIRDFQASSIPMGRFSEPHEQADPAVLLL 240
Cdd:PRK06463 150 TFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSqeeaeKLRELFRNKTVLKTTGKPEDIANIVLFLA 229
                        250
                 ....*....|....*..
gi 388856966 241 SDKASYLTGSVIRPDGG 257
Cdd:PRK06463 230 SDDARYITGQVIVADGG 246
PRK07856 PRK07856
SDR family oxidoreductase;
5-257 1.53e-28

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 108.87  E-value: 1.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPkaqEAAAEVAKEFgvqcraYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK07856   2 LDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAP---ETVDGRPAEF------HAADVRDPDQVAALVDAIVER 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAV-----AQlwiESGfkkGSIVITSSMSseiynqeGL 159
Cdd:PRK07856  73 HGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAAnavmqQQ---PGG---GSIVNIGSVS-------GR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 160 N-KPLTQVfYNSSKGAVTNLGKCLAAEWAQHgIRVNILEPGFCNTEQTS---GMDAKIRDFqASSIPMGRFSEPHEQADP 235
Cdd:PRK07856 140 RpSPGTAA-YGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQSElhyGDAEGIAAV-AATVPLGRLATPADIAWA 216
                        250       260
                 ....*....|....*....|..
gi 388856966 236 AVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK07856 217 CLFLASDLASYVSGANLEVHGG 238
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
11-216 1.95e-28

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: 108.48  E-value: 1.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTG 90
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNV-RKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  91 LLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEIYnqeglnkPLTQVFYNS 170
Cdd:cd05339   80 LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLER--NHGHIVTIASVAGLIS-------PAGLADYCA 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 388856966 171 SKGAVTNLGKCLAAE--WAQH-GIRVNILEPGFCNTEQTSGMDAKIRDF 216
Cdd:cd05339  151 SKAAAVGFHESLRLElkAYGKpGIKTTLVCPYFINTGMFQGVKTPRPLL 199
PRK07478 PRK07478
short chain dehydrogenase; Provisional
7-260 4.22e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 107.71  E-value: 4.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGvQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGG-EAVALAGDVRDEAYAKALVALAVERFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAG-VSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSS----------MSSeiyn 155
Cdd:PRK07478  83 GLDIAFNNAGtLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARG--GGSLIFTSTfvghtagfpgMAA---- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 156 qeglnkpltqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQA 233
Cdd:PRK07478 157 ------------YAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMgdTPEALAFVAGLHALKRMAQPEEIA 224
                        250       260
                 ....*....|....*....|....*..
gi 388856966 234 DPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK07478 225 QAALFLASDAASFVTGTALLVDGGVSI 251
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
6-260 4.82e-28

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: 107.82  E-value: 4.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:cd05348    1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRS----AEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGV-----SVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfkKGSIVITSSMSSEIYNQEGln 160
Cdd:cd05348   77 GKLDCFIGNAGIwdystSLVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYAT---EGSVIFTVSNAGFYPGGGG-- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 161 kpltqVFYNSSKGAVTNLGKCLAAEWAQHgIRVNILEPGFCNT----------EQTSGMDAKIRDFQASSIPMGRFSEPH 230
Cdd:cd05348  152 -----PLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTdlrgpaslgqGETSISTPPLDDMLKSILPLGFAPEPE 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 388856966 231 EQADPAVLLLS-DKASYLTGSVIRPDGGFTI 260
Cdd:cd05348  226 DYTGAYVFLASrGDNRPATGTVINYDGGMGV 256
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
13-257 5.21e-28

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: 107.27  E-value: 5.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  13 VVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGLL 92
Cdd:cd05365    3 IVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQA-GGQAIGLECNVTSEQDLEAVVKATVSQFGGITILV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  93 ANAGVSVVKP-AVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSEiynqeglNKPLTQVFYNSS 171
Cdd:cd05365   82 NNAGGGGPKPfDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGG--GAILNISSMSSE-------NKNVRIAAYGSS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 172 KGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQ-TSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLTGS 250
Cdd:cd05365  153 KAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDAlASVLTPEIERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQ 232

                 ....*..
gi 388856966 251 VIRPDGG 257
Cdd:cd05365  233 VLTVSGG 239
PRK08628 PRK08628
SDR family oxidoreductase;
5-259 7.16e-28

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 107.35  E-value: 7.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKefGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK08628   3 LNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEELRAL--QPRAEFVQVDLTDDAQCRDAVEQTVAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGV--SVvkpAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfkKGSIVITSSMSSeIYNQEGLNKp 162
Cdd:PRK08628  81 FGRIDGLVNNAGVndGV---GLEAGREAFVASLERNLIHYYVMAHYCLPHLKAS---RGAIVNISSKTA-LTGQGGTSG- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 ltqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQ----TSGMD------AKIrdfqASSIPMG-RFSEPHE 231
Cdd:PRK08628 153 -----YAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLyenwIATFDdpeaklAAI----TAKIPLGhRMTTAEE 223
                        250       260
                 ....*....|....*....|....*...
gi 388856966 232 QADPAVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK08628 224 IADTAVFLLSERSSHTTGQWLFVDGGYV 251
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
6-257 7.98e-28

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: 106.80  E-value: 7.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKeFGvQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:cd08942    3 SVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSA-YG-ECIAIPADLSSEEGIEALVARVAERS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFKK--------GSIVITSSMSSEIYNqe 157
Cdd:cd08942   81 DRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATAEnparviniGSIAGIVVSGLENYS-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 158 glnkpltqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADP 235
Cdd:cd08942  159 ----------YGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLlnDPAALEAEEKSIPLGRWGRPEDMAGL 228
                        250       260
                 ....*....|....*....|..
gi 388856966 236 AVLLLSDKASYLTGSVIRPDGG 257
Cdd:cd08942  229 AIMLASRAGAYLTGAVIPVDGG 250
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
7-257 8.53e-28

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 111.48  E-value: 8.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQCRAY--QCDVGDAELVKKTLKQAQDE 84
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLD----EEAAEAAAAELGGPDRALgvACDVTDEAAVQAAFEEAALA 495
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSmsseiynQEGLNKPLT 164
Cdd:PRK08324 496 FGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQG-LGGSIVFIAS-------KNAVNPGPN 567
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEP-------GFCNTE------QTSGMD-AKIRDFQASSIPMGRFSEPH 230
Cdd:PRK08324 568 FGAYGAAKAAELHLVRQLALELGPDGIRVNGVNPdavvrgsGIWTGEwiearaAAYGLSeEELEEFYRARNLLKREVTPE 647
                        250       260
                 ....*....|....*....|....*..
gi 388856966 231 EQADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK08324 648 DVAEAVVFLASGLLSKTTGAIITVDGG 674
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
1-257 1.22e-27

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 106.76  E-value: 1.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   1 MPFVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQ 80
Cdd:PRK08085   1 MNDLFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQE-GIKAHAAPFNVTHKQEVEAAIEH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  81 AQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEIYNQegln 160
Cdd:PRK08085  80 IEKDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKR--QAGKIINICSMQSELGRD---- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 161 kplTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVL 238
Cdd:PRK08085 154 ---TITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALveDEAFTAWLCKRTPAARWGDPQELIGAAVF 230
                        250
                 ....*....|....*....
gi 388856966 239 LLSDKASYLTGSVIRPDGG 257
Cdd:PRK08085 231 LSSKASDFVNGHLLFVDGG 249
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
5-259 1.23e-27

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 107.02  E-value: 1.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAvanaganvaiFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK06171   5 LNLQGKIIIVTGGSSGIGLAIVKE----------LLANGANVVNADIHGGDGQHENYQFVPTDVSSAEEVNHTVAEIIEK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAV---------ELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVitsSMSSEiyn 155
Cdd:PRK06171  75 FGRIDGLVNNAGINIPRLLVdekdpagkyELNEAAFDKMFNINQKGVFLMSQAVARQMVKQ--HDGVIV---NMSSE--- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 156 qEGLNKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRV-----NILEP-GFCNTEQTSGM----DAKIRDFQA-----SS 220
Cdd:PRK06171 147 -AGLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVvgvapGILEAtGLRTPEYEEALaytrGITVEQLRAgytktST 225
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 388856966 221 IPMGRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK06171 226 IPLGRSGKLSEVADLVCYLLSDRASYITGVTTNIAGGKT 264
PRK07062 PRK07062
SDR family oxidoreductase;
5-258 1.90e-27

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 106.28  E-value: 1.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEF-GVQCRAYQCDVGDAELVKKTLKQAQD 83
Cdd:PRK07062   4 IQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFpGARLLAARCDVLDEADVAAFAAAVEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeiynqegLNKPL 163
Cdd:PRK07062  84 RFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASA--AASIVCVNSLLA-------LQPEP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 TQVFYNSSKGAVTNLGKCLAAEWAQHGIRVN-----ILEPG-----FcNTEQTSGMD-----AKIRdfQASSIPMGRFSE 228
Cdd:PRK07062 155 HMVATSAARAGLLNLVKSLATELAPKGVRVNsillgLVESGqwrrrY-EARADPGQSweawtAALA--RKKGIPLGRLGR 231
                        250       260       270
                 ....*....|....*....|....*....|
gi 388856966 229 PHEQADPAVLLLSDKASYLTGSVIRPDGGF 258
Cdd:PRK07062 232 PDEAARALFFLASPLSSYTTGSHIDVSGGF 261
PRK07774 PRK07774
SDR family oxidoreductase;
6-260 4.54e-27

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 104.83  E-value: 4.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK07774   3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVAD-GGTAIAVQVDVSDPDSAKAMADATVSAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANA---GVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYnqeglnkp 162
Cdd:PRK07774  82 GGIDYLVNNAaiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRG--GGAIVNQSSTAAWLY-------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 ltQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAK-IRDFQASSIPMGRFSEPHEQADPAVLLLS 241
Cdd:PRK07774 152 --SNFYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKeFVADMVKGIPLSRMGTPEDLVGMCLFLLS 229
                        250
                 ....*....|....*....
gi 388856966 242 DKASYLTGSVIRPDGGFTI 260
Cdd:PRK07774 230 DEASWITGQIFNVDGGQII 248
PRK06198 PRK06198
short chain dehydrogenase; Provisional
6-252 7.38e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 104.70  E-value: 7.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK06198   3 RLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSEIynqeglnkplTQ 165
Cdd:PRK06198  83 GRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRK-AEGTIVNIGSMSAHG----------GQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VF---YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-------QTSGMDAKIRDFQASSIPMGRFSEPHEQADP 235
Cdd:PRK06198 152 PFlaaYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEgedriqrEFHGAPDDWLEKAAATQPFGRLLDPDEVARA 231
                        250
                 ....*....|....*..
gi 388856966 236 AVLLLSDKASYLTGSVI 252
Cdd:PRK06198 232 VAFLLSDESGLMTGSVI 248
PRK07825 PRK07825
short chain dehydrogenase; Provisional
5-208 1.02e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 104.64  E-value: 1.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkefgvQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK07825   1 DDLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELG-----LVVGGPLDVTDPASFAAFLDAVEAD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYnqeglnkPLT 164
Cdd:PRK07825  76 LGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRG--RGHVVNVASLAGKIP-------VPG 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSG 208
Cdd:PRK07825 147 MATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAG 190
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-258 1.59e-26

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 103.45  E-value: 1.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSkaVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK12481   5 DLNGKVAIITGCNTGLGQGMA--IGLAKAGADIVGVGVAEAPETQAQV-EALGRKFHFITADLIQQKDIDSIVSQAVEVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSeiyNQEGLNKPltq 165
Cdd:PRK12481  82 GHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQG-NGGKIINIASMLS---FQGGIRVP--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 vFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQA--SSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:PRK12481 155 -SYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRADTARNEAilERIPASRWGTPDDLAGPAIFLSSSA 233
                        250
                 ....*....|....*
gi 388856966 244 ASYLTGSVIRPDGGF 258
Cdd:PRK12481 234 SDYVTGYTLAVDGGW 248
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-260 3.66e-26

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 102.35  E-value: 3.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKavanaganvaIFyrshpkaQEAAAEVakeFGVQC----------RAYQCDVGDAelvk 75
Cdd:PRK06550   2 EFMTKTVLITGAASGIGLAQAR----------AF-------LAQGAQV---YGVDKqdkpdlsgnfHFLQLDLSDD---- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  76 ktLKQAQDELGQVTGLLANAGV-SVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIY 154
Cdd:PRK06550  58 --LEPLFDWVPSVDILCNTAGIlDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERK--SGIIINMCSIASFVA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 155 NQEGlnkpltqVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSG--MDAKIRDFQASSIPMGRFSEPHEQ 232
Cdd:PRK06550 134 GGGG-------AAYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAAdfEPGGLADWVARETPIKRWAEPEEV 206
                        250       260
                 ....*....|....*....|....*...
gi 388856966 233 ADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK06550 207 AELTLFLASGKADYMQGTIVPIDGGWTL 234
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
12-260 3.79e-26

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: 102.55  E-value: 3.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGanvaifyrSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGL 91
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAG--------ATVIALDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDAL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  92 LANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeiynqeglNKPLTQV-FYNS 170
Cdd:cd05331   73 VNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRR--TGAIVTVASNAA--------HVPRISMaAYGA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 171 SKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM-------DAKIRDFQAS---SIPMGRFSEPHEQADPAVLLL 240
Cdd:cd05331  143 SKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTLwhdedgaAQVIAGVPEQfrlGIPLGKIAQPADIANAVLFLA 222
                        250       260
                 ....*....|....*....|
gi 388856966 241 SDKASYLTGSVIRPDGGFTI 260
Cdd:cd05331  223 SDQAGHITMHDLVVDGGATL 242
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
8-260 5.34e-26

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: 101.78  E-value: 5.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAevakefGVQCRAYQCDVGDAELVKKTLKqaqdELGQ 87
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELER------GPGITTRVLDVTDKEQVAALAK----EEGR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEIYNQEGlnkpltQVF 167
Cdd:cd05368   71 IDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLAR--KDGSIINMSSVASSIKGVPN------RFV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 168 YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT-------EQTSGMDAKIRDFqASSIPMGRFSEPHEQADPAVLLL 240
Cdd:cd05368  143 YSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTpsleeriQAQPDPEEALKAF-AARQPLGRLATPEEVAALAVYLA 221
                        250       260
                 ....*....|....*....|
gi 388856966 241 SDKASYLTGSVIRPDGGFTI 260
Cdd:cd05368  222 SDESAYVTGTAVVIDGGWSL 241
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-258 1.27e-25

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 101.10  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAyqcDVGDAELVKKTLKQAQDEL 85
Cdd:PRK08993   7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPTETIEQVTALGRRFLSLTA---DLRKIDGIPALLERAVAEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSeiyNQEGLNKPltq 165
Cdd:PRK08993  84 GHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQG-NGGKIINIASMLS---FQGGIRVP--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 vFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAkirDFQASS-----IPMGRFSEPHEQADPAVLLL 240
Cdd:PRK08993 157 -SYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRA---DEQRSAeildrIPAGRWGLPSDLMGPVVFLA 232
                        250
                 ....*....|....*...
gi 388856966 241 SDKASYLTGSVIRPDGGF 258
Cdd:PRK08993 233 SSASDYINGYTIAVDGGW 250
PRK06398 PRK06398
aldose dehydrogenase; Validated
6-260 1.65e-25

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 101.06  E-value: 1.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKaqeaaaEVAKEFgvqcraYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK06398   3 GLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS------YNDVDY------FKVDVSNKEQVIKGIDYVISKY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYNQEGlnkpltq 165
Cdd:PRK06398  71 GRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQD--KGVIINIASVQSFAVTRNA------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQhGIRVNILEPGFCNT-------EQTSGMDA-----KIRDFqASSIPMGRFSEPHEQA 233
Cdd:PRK06398 142 AAYVTSKHAVLGLTRSIAVDYAP-TIRCVAVCPGSIRTpllewaaELEVGKDPehverKIREW-GEMHPMKRVGKPEEVA 219
                        250       260
                 ....*....|....*....|....*..
gi 388856966 234 DPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK06398 220 YVVAFLASDLASFITGECVTVDGGLRA 246
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
7-257 1.69e-25

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: 101.06  E-value: 1.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEF-GVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIApDAEVLLIKADVSDEAQVEAYVDATVEQF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVK-PAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSseiynqeGLNKPLT 164
Cdd:cd05330   81 GRIDGFFNNAGIEGKQnLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGS--GMIVNTASVG-------GIRGVGN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT-------EQTSGMDAKIRDFQASSI-PMGRFSEPHEQADPA 236
Cdd:cd05330  152 QSGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTpmvegslKQLGPENPEEAGEEFVSVnPMKRFGEPEEVAAVV 231
                        250       260
                 ....*....|....*....|.
gi 388856966 237 VLLLSDKASYLTGSVIRPDGG 257
Cdd:cd05330  232 AFLLSDDAGYVNAAVVPIDGG 252
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
8-257 2.91e-25

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 100.19  E-value: 2.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGvQCRAYQCDVGDAELVKKTLKQAQDELGQ 87
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGG-KAIAVKADVSDRDQVFAAVRQVVDTFGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVF-NSAKAVAQlwiesgFKK----GSIVITSSMSSEIYNQEglnkp 162
Cdd:PRK08643  80 LNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIwGIQAAQEA------FKKlghgGKIINATSQAGVVGNPE----- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 LTqvFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRD------------FqASSIPMGRFSEPH 230
Cdd:PRK08643 149 LA--VYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVGEnagkpdewgmeqF-AKDITLGRLSEPE 225
                        250       260
                 ....*....|....*....|....*..
gi 388856966 231 EQADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK08643 226 DVANCVSFLAGPDSDYITGQTIIVDGG 252
PRK06128 PRK06128
SDR family oxidoreductase;
7-257 3.32e-25

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 101.09  E-value: 3.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRshPKAQEAAAEVA---KEFGVQCRAYQCDVGDAELVKKTLKQAQD 83
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNYL--PEEEQDAAEVVqliQAEGRKAVALPGDLKDEAFCRQLVERAVK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSV-VKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLwIESGfkkGSIVITSSMSSeiYNQEGlnkp 162
Cdd:PRK06128 131 ELGGLDILVNIAGKQTaVKDIADITTEQFDATFKTNVYAMFWLCKAAIPH-LPPG---ASIINTGSIQS--YQPSP---- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 lTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPG-FCNTEQTSG--MDAKIRDFqASSIPMGRFSEPHEQADPAVLL 239
Cdd:PRK06128 201 -TLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGpVWTPLQPSGgqPPEKIPDF-GSETPMKRPGQPVEMAPLYVLL 278
                        250
                 ....*....|....*...
gi 388856966 240 LSDKASYLTGSVIRPDGG 257
Cdd:PRK06128 279 ASQESSYVTGEVFGVTGG 296
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
8-259 3.93e-25

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: 99.83  E-value: 3.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAA-AEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVrAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMsseiynqEGLNKPLTQV 166
Cdd:cd08940   81 GVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGW--GRIINIASV-------HGLVASANKS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE----------QTSGM--DAKIRDFQASSIPMGRFSEPHEQAD 234
Cdd:cd08940  152 AYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPlvekqisalaQKNGVpqEQAARELLLEKQPSKQFVTPEQLGD 231
                        250       260
                 ....*....|....*....|....*
gi 388856966 235 PAVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:cd08940  232 TAVFLASDAASQITGTAVSVDGGWT 256
PRK07577 PRK07577
SDR family oxidoreductase;
7-257 6.37e-25

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 99.03  E-value: 6.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaqeAAAEVAKEFgvqcraYQCDVGDAELVKKTLKQAQDElG 86
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIARS------AIDDFPGEL------FACDLADIEQTAATLAQINEI-H 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVlgvfNSAKAVAQLWIESGFKKGSIVITSSMSSEIYNQeglnkpLTQV 166
Cdd:PRK07577  68 PVDAIVNNVGIALPQPLGKIDLAALQDVYDLNV----RAAVQVTQAFLEGMKLREQGRIVNICSRAIFGA------LDRT 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE---QTS--GMDAKiRDFQASsIPMGRFSEPHEQADPAVLLLS 241
Cdd:PRK07577 138 SYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETElfrQTRpvGSEEE-KRVLAS-IPMRRLGTPEEVAAAIAFLLS 215
                        250
                 ....*....|....*.
gi 388856966 242 DKASYLTGSVIRPDGG 257
Cdd:PRK07577 216 DDAGFITGQVLGVDGG 231
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
7-257 1.34e-24

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 98.38  E-value: 1.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIfyrSHPKAQ--EAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVV---SDINADaaNHVVDEIQQLGGQAFACRCDITSEQELSALADFALSK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPaVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEiynqeglNKPLT 164
Cdd:PRK06113  86 LGKVDILVNNAGGGGPKP-FDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNG--GGVILTITSMAAE-------NKNIN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQ-TSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:PRK06113 156 MTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDAlKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPA 235
                        250
                 ....*....|....
gi 388856966 244 ASYLTGSVIRPDGG 257
Cdd:PRK06113 236 ASWVSGQILTVSGG 249
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
7-257 1.38e-24

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: 98.25  E-value: 1.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQC---DVGDAELVKKTLKQAQD 83
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSC-LQAGVSEKKILLvvaDLTEEEGQDRIISTTLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfkKGSIVITSSMSSeiynqeGLNKPl 163
Cdd:cd05364   80 KFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT---KGEIVNVSSVAG------GRSFP- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 TQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE--QTSGMD----AKIRDFQASSIPMGRFSEPHEQADPAV 237
Cdd:cd05364  150 GVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGfhRRMGMPeeqyIKFLSRAKETHPLGRPGTVDEVAEAIA 229
                        250       260
                 ....*....|....*....|
gi 388856966 238 LLLSDKASYLTGSVIRPDGG 257
Cdd:cd05364  230 FLASDASSFITGQLLPVDGG 249
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-204 1.52e-24

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 97.84  E-value: 1.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK07666   4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEV-EAYGVKVVIATADVSDYEEVTAAIEQLKNEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSseiynqeGLNKPLTQ 165
Cdd:PRK07666  83 GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIER--QSGDIINISSTA-------GQKGAAVT 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:PRK07666 154 SAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATD 192
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-258 2.31e-24

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 97.84  E-value: 2.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNR--GIGLAMSKAVANAGANvaIF---YRSHPKAQEAAAE------VAKE---FGVQCRAYQCDVGDAE 72
Cdd:PRK12748   3 LMKKIALVTGASRlnGIGAAVCRRLAAKGID--IFftyWSPYDKTMPWGMHdkepvlLKEEiesYGVRCEHMEIDLSQPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  73 LVKKTLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVlgvfNSAKAVAQLWIE--SGFKKGSIVITSS-- 148
Cdd:PRK12748  81 APNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNV----RATMLLSSAFAKqyDGKAGGRIINLTSgq 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 149 ----MSSEIYnqeglnkpltqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTeqtSGMDAKIRDFQASSIPMG 224
Cdd:PRK12748 157 slgpMPDELA-------------YAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT---GWITEELKHHLVPKFPQG 220
                        250       260       270
                 ....*....|....*....|....*....|....
gi 388856966 225 RFSEPHEQADPAVLLLSDKASYLTGSVIRPDGGF 258
Cdd:PRK12748 221 RVGEPVDAARLIAFLVSEEAKWITGQVIHSEGGF 254
PRK07326 PRK07326
SDR family oxidoreductase;
7-214 2.91e-24

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 97.00  E-value: 2.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVqcRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNV--LGLAADVRDEADVQRAVDAIVAAFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkkGSIVITSSMSSeiynqeglnkplTQV 166
Cdd:PRK07326  82 GLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG---GYIINISSLAG------------TNF 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 388856966 167 F-----YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE----QTSGMDA-KIR 214
Cdd:PRK07326 147 FaggaaYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHfnghTPSEKDAwKIQ 204
PRK07985 PRK07985
SDR family oxidoreductase;
7-257 2.92e-24

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 98.53  E-value: 2.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRshPKAQEAAAEVAK---EFGVQCRAYQCDVGDAELVKKTLKQAQD 83
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYL--PVEEEDAQDVKKiieECGRKAVLLPGDLSDEKFARSLVHEAHK 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSVVKPAV-ELTSDDFRYVYDTNVLGVFNSAKAVAQLwiesgFKKGSIVITSSmSSEIYnqeglnKP 162
Cdd:PRK07985 125 ALGGLDIMALVAGKQVAIPDIaDLTSEQFQKTFAINVFALFWLTQEAIPL-----LPKGASIITTS-SIQAY------QP 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 LTQVF-YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-QTSG--MDAKIRDFqASSIPMGRFSEPHEQADPAVL 238
Cdd:PRK07985 193 SPHLLdYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAlQISGgqTQDKIPQF-GQQTPMKRAGQPAELAPVYVY 271
                        250
                 ....*....|....*....
gi 388856966 239 LLSDKASYLTGSVIRPDGG 257
Cdd:PRK07985 272 LASQESSYVTAEVHGVCGG 290
PRK07069 PRK07069
short chain dehydrogenase; Validated
46-257 4.41e-24

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 97.09  E-value: 4.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  46 AQEAAAEVAKEFGVQCR-AYQCDVGDAELVKKTLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFN 124
Cdd:PRK07069  37 LDAFAAEINAAHGEGVAfAAVQDVTDEAQWQALLAQAADAMGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 125 SAKAVAQLWIESGfkKGSIVITSSMSSEIYNQeglnkplTQVFYNSSKGAVTNLGKCLAAEWAQHG--IRVNILEPGFCN 202
Cdd:PRK07069 117 GCKHALPYLRASQ--PASIVNISSVAAFKAEP-------DYTAYNASKAAVASLTKSIALDCARRGldVRCNSIHPTFIR 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 203 TEQTSGMDAKIRDFQAS-----SIPMGRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK07069 188 TGIVDPIFQRLGEEEATrklarGVPLGRLGEPDDVAHAVLYLASDESRFVTGAELVIDGG 247
PRK07890 PRK07890
short chain dehydrogenase; Provisional
7-257 9.34e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 96.18  E-value: 9.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEID-DLGRRALAVPTDITDEDQCANLVALALERFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANA-GVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkkGSIVITSSMSseiynqegLNKP-LT 164
Cdd:PRK07890  82 RVDALVNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG---GSIVMINSMV--------LRHSqPK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPG----------FCNTEQTSGMDAK-IRDFQASSIPMGRFSEPHEQA 233
Cdd:PRK07890 151 YGAYKMAKGALLAASQSLATELGPQGIRVNSVAPGyiwgdplkgyFRHQAGKYGVTVEqIYAETAANSDLKRLPTDDEVA 230
                        250       260
                 ....*....|....*....|....
gi 388856966 234 DPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK07890 231 SAVLFLASDLARAITGQTLDVNCG 254
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-258 1.38e-23

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 96.01  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNR--GIGLAMSKAVANAGANvaIFY-------RSHPKAQEAA-----AEVAKEFGVQCRAYQCDVGDAE 72
Cdd:PRK12859   4 LKNKVAVVTGVSRldGIGAAICKELAEAGAD--IFFtywtaydKEMPWGVDQDeqiqlQEELLKNGVKVSSMELDLTQND 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  73 LVKKTLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQlwiesGFKKGS----IVITSS 148
Cdd:PRK12859  82 APKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFAR-----GFDKKSggriINMTSG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 149 msseiynqEGLNKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTeqtSGMDAKIRDFQASSIPMGRFSE 228
Cdd:PRK12859 157 --------QFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDT---GWMTEEIKQGLLPMFPFGRIGE 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 388856966 229 PHEQADPAVLLLSDKASYLTGSVIRPDGGF 258
Cdd:PRK12859 226 PKDAARLIKFLASEEAEWITGQIIHSEGGF 255
PRK05872 PRK05872
short chain dehydrogenase; Provisional
1-211 1.99e-23

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 96.19  E-value: 1.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   1 MPFVIDLKGQTIVVTGGNRGIGLAMSKavanaganvaifyRSHPKA---------QEAAAEVAKEFGVQCRAY--QCDVG 69
Cdd:PRK05872   1 GPPMTSLAGKVVVVTGAARGIGAELAR-------------RLHARGaklalvdleEAELAALAAELGGDDRVLtvVADVT 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  70 DAELVKKTLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfkKGSIVITSSM 149
Cdd:PRK05872  68 DLAAMQAAAEEAVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIER---RGYVLQVSSL 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388856966 150 SSeIYNQEGLNKpltqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDA 211
Cdd:PRK05872 145 AA-FAAAPGMAA------YCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDADA 199
PRK08416 PRK08416
enoyl-ACP reductase;
7-259 2.04e-23

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 95.61  E-value: 2.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPK-AQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK08416   6 MKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEeANKIAEDLEQKYGIKAKAYPLNILEPETYKELFKKIDEDF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANA---GVSVV---KPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIY--NQE 157
Cdd:PRK08416  86 DRVDFFISNAiisGRAVVggyTKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVG--GGSIISLSSTGNLVYieNYA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 158 GlnkpltqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMD--AKIRDFQASSIPMGRFSEPHEQADP 235
Cdd:PRK08416 164 G---------HGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTnyEEVKAKTEELSPLNRMGQPEDLAGA 234
                        250       260
                 ....*....|....*....|....
gi 388856966 236 AVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK08416 235 CLFLCSEKASWLTGQTIVVDGGTT 258
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
11-257 2.15e-23

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: 94.65  E-value: 2.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIFYR-SHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:cd05357    2 VALVTGAAKRIGRAIAEALAAEGYRVVVHYNrSEAEAQRLKDELNAL-RNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIV-ITSSMsseiynqegLNKPLTQVF- 167
Cdd:cd05357   81 VLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSR--NGSIInIIDAM---------TDRPLTGYFa 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 168 YNSSKGAVTNLGKCLAAEWAQHgIRVNILEPGFCNTEQtsGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKasYL 247
Cdd:cd05357  150 YCMSKAALEGLTRSAALELAPN-IRVNGIAPGLILLPE--DMDAEYRENALRKVPLKRRPSAEEIADAVIFLLDSN--YI 224
                        250
                 ....*....|
gi 388856966 248 TGSVIRPDGG 257
Cdd:cd05357  225 TGQIIKVDGG 234
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
8-257 4.97e-23

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 94.33  E-value: 4.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFG-VQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGeGMAYGFGADATSEQSVLALSRGVDEIFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFKkGSIVITSSMSSEI---YNQEglnkpl 163
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIQ-GRIIQINSKSGKVgskHNSG------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 tqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPG-FCNTEQTSGM-----------DAKIRDFQASSIPMGRFSEPHE 231
Cdd:PRK12384 154 ----YSAAKFGGVGLTQSLALDLAEYGITVHSLMLGnLLKSPMFQSLlpqyakklgikPDEVEQYYIDKVPLKRGCDYQD 229
                        250       260
                 ....*....|....*....|....*.
gi 388856966 232 QADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK12384 230 VLNMLLFYASPKASYCTGQSINVTGG 255
PRK08265 PRK08265
short chain dehydrogenase; Provisional
5-260 5.48e-23

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 94.31  E-value: 5.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRshpkAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK08265   2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDI----DADNGAAVAASLGERARFIATDITDDAAIERAVATVVAR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTgLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkkGSIVITSSMSSEiYNQEGlnkplt 164
Cdd:PRK08265  78 FGRVD-ILVNLACTYLDDGLASSRADWLAALDVNLVSAAMLAQAAHPHLARGG---GAIVNFTSISAK-FAQTG------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT----EQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLL 240
Cdd:PRK08265 147 RWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSrvmdELSGGDRAKADRVAAPFHLLGRVGDPEEVAQVVAFLC 226
                        250       260
                 ....*....|....*....|
gi 388856966 241 SDKASYLTGSVIRPDGGFTI 260
Cdd:PRK08265 227 SDAASFVTGADYAVDGGYSA 246
PRK06523 PRK06523
short chain dehydrogenase; Provisional
1-257 9.20e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 93.82  E-value: 9.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   1 MPFVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkefgvqcrayQCDVGDAELVKKTLKQ 80
Cdd:PRK06523   1 MSFFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSRPDDLPEGVEFV----------AADLTTAEGCAAVARA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  81 AQDELGQVTGLLANAGVSVVkPA---VELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIynqe 157
Cdd:PRK06523  71 VLERLGGVDILVHVLGGSSA-PAggfAALTDEEWQDELNLNLLAAVRLDRALLPGMIARG--SGVIIHVTSIQRRL---- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 158 glnkPLTQVF--YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEqtsGMDAKIRDFQASS--------------- 220
Cdd:PRK06523 144 ----PLPESTtaYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE---AAVALAERLAEAAgtdyegakqiimdsl 216
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 388856966 221 --IPMGRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK06523 217 ggIPLGRPAEPEEVAELIAFLASDRAASITGTEYVIDGG 255
PRK07831 PRK07831
SDR family oxidoreductase;
7-252 1.35e-22

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 93.17  E-value: 1.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGG-NRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGV-QCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK07831  15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGLgRVEAVVCDVTSEAQVDALIDAAVER 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSseiynqeGLNKPLT 164
Cdd:PRK07831  95 LGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARG-HGGVIVNNASVL-------GWRAQHG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPG-----FCNTEQTSGMDAKIRDFQAssipMGRFSEPHEQADPAVLL 239
Cdd:PRK07831 167 QAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSiamhpFLAKVTSAELLDELAAREA----FGRAAEPWEVANVIAFL 242
                        250
                 ....*....|...
gi 388856966 240 LSDKASYLTGSVI 252
Cdd:PRK07831 243 ASDYSSYLTGEVV 255
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
8-257 3.16e-22

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: 92.14  E-value: 3.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQ 87
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkKGSIVITSSMSSEI---YNQEglnkplt 164
Cdd:cd05322   81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGI-QGRIIQINSKSGKVgskHNSG------- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 qvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPG-FCNTEQTSGM-----------DAKIRDFQASSIPMGRFSEPHEQ 232
Cdd:cd05322  153 ---YSAAKFGGVGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQSLlpqyakklgikESEVEQYYIDKVPLKRGCDYQDV 229
                        250       260
                 ....*....|....*....|....*
gi 388856966 233 ADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:cd05322  230 LNMLLFYASPKASYCTGQSINITGG 254
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
7-257 3.17e-22

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: 92.30  E-value: 3.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFyrshPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIA----DINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVitsSMSSeiynQEGLNKPLTQV 166
Cdd:cd05363   77 SIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQG-RGGKII---NMAS----QAGRRGEALVG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQ-----------ASSIPMGRFSEPHEQADP 235
Cdd:cd05363  149 VYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKFARYEnrprgekkrlvGEAVPFGRMGRAEDLTGM 228
                        250       260
                 ....*....|....*....|..
gi 388856966 236 AVLLLSDKASYLTGSVIRPDGG 257
Cdd:cd05363  229 AIFLASTDADYIVAQTYNVDGG 250
PRK05875 PRK05875
short chain dehydrogenase; Provisional
7-257 4.59e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 92.17  E-value: 4.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEV-AKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIeALKGAGAVRYEPADVTDEDQVARAVDAATAWH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVS-VVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIV-ITSSMSSEIYNQEGLnkpl 163
Cdd:PRK05875  85 GRLHGVVHCAGGSeTIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGG--GGSFVgISSIAASNTHRWFGA---- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 tqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVLLLS 241
Cdd:PRK05875 159 ----YGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPIteSPELSADYRACTPLPRVGEVEDVANLAMFLLS 234
                        250
                 ....*....|....*.
gi 388856966 242 DKASYLTGSVIRPDGG 257
Cdd:PRK05875 235 DAASWITGQVINVDGG 250
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
12-210 4.88e-22

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: 91.24  E-value: 4.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGvQCRAYQCDVGDAELVKKTLKQAQDELGQVTGL 91
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNP-SVEVEILDVTDEERNQLVIAELEAELGGLDLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  92 LANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIynqeGLNkplTQVFYNSS 171
Cdd:cd05350   80 IINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKG--RGHLVLISSVAALR----GLP---GAAAYSAS 150
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 388856966 172 KGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMD 210
Cdd:cd05350  151 KAALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANMF 189
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
4-260 5.73e-22

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 91.13  E-value: 5.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   4 VIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIfyrsHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQD 83
Cdd:PRK12936   1 MFDLSGRKALVTGASGGIGEEIARLLHAQGAIVGL----HGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSEIYNQeglnkpl 163
Cdd:PRK12936  77 DLEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRY--GRIINITSVVGVTGNP------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 TQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:PRK12936 148 GQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLASSE 227
                        250
                 ....*....|....*..
gi 388856966 244 ASYLTGSVIRPDGGFTI 260
Cdd:PRK12936 228 AAYVTGQTIHVNGGMAM 244
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
14-258 5.81e-22

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 91.23  E-value: 5.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  14 VTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGLLA 93
Cdd:PRK12938   8 VTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDVLVN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  94 NAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSeiynQEGlnkPLTQVFYNSSKG 173
Cdd:PRK12938  88 NAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGW--GRIINISSVNG----QKG---QFGQTNYSTAKA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 174 AVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLTGSVIR 253
Cdd:PRK12938 159 GIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGADFS 238

                 ....*
gi 388856966 254 PDGGF 258
Cdd:PRK12938 239 LNGGL 243
PRK07814 PRK07814
SDR family oxidoreductase;
7-259 8.40e-22

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 91.38  E-value: 8.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIR-AAGRRAHVVAADLAHPEATAGLAGQAVEAFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIE-SGfkKGSIV-ITSSMSSeiYNQEGLnkplt 164
Cdd:PRK07814  87 RLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEhSG--GGSVInISSTMGR--LAGRGF----- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 qVFYNSSKGAVTNLGKCLAAEWAQHgIRVNILEPGFCNTEQTSGMDA--KIRDFQASSIPMGRFSEPHEQADPAVLLLSD 242
Cdd:PRK07814 158 -AAYGTAKAALAHYTRLAALDLCPR-IRVNAIAPGSILTSALEVVAAndELRAPMEKATPLRRLGDPEDIAAAAVYLASP 235
                        250
                 ....*....|....*..
gi 388856966 243 KASYLTGSVIRPDGGFT 259
Cdd:PRK07814 236 AGSYLTGKTLEVDGGLT 252
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
11-252 3.28e-21

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: 88.57  E-value: 3.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFgvqcrAYQCDVGDAELVKKTLKQAQDELGQVTG 90
Cdd:cd08932    2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGGDVE-----AVPYDARDPEDARALVDALRDRFGRIDV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  91 LLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeiynqeGLNKPLTQVfYNS 170
Cdd:cd08932   77 LVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAG--SGRVVFLNSLSG------KRVLAGNAG-YSA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 171 SKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEqtsgMDAKIRDFQAssIPMGRFSEPHEQADPAVLLLSDKASYLTGS 250
Cdd:cd08932  148 SKFALRALAHALRQEGWDHGVRVSAVCPGFVDTP----MAQGLTLVGA--FPPEEMIQPKDIANLVRMVIELPENITSVA 221

                 ..
gi 388856966 251 VI 252
Cdd:cd08932  222 VL 223
PLN02253 PLN02253
xanthoxin dehydrogenase
7-259 5.79e-21

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 89.11  E-value: 5.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKavanaganvaIFYRSHPKA------QEAAAEVAKEFGVQCRA--YQCDVGDAELVKKTL 78
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVR----------LFHKHGAKVcivdlqDDLGQNVCDSLGGEPNVcfFHCDVTVEDDVSRAV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  79 KQAQDELGQVTGLLANAGVSVVK----PAVELTsdDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEIy 154
Cdd:PLN02253  86 DFTVDKFGTLDIMVNNAGLTGPPcpdiRNVELS--EFEKVFDVNVKGVFLGMKHAARIMIPL--KKGSIVSLCSVASAI- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 155 nqeGLNKPLTqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT----------EQTSGMDAKIRDFQASSIPM- 223
Cdd:PLN02253 161 ---GGLGPHA---YTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTalalahlpedERTEDALAGFRAFAGKNANLk 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 388856966 224 GRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PLN02253 235 GVELTVDDVANAVLFLASDEARYISGLNLMIDGGFT 270
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
7-257 9.40e-21

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: 88.35  E-value: 9.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHpKAQEAAAEVaKEFGVQCRAYQCDV---GDAELVkktLKQAQD 83
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSE-LVHEVLAEI-LAAGDAAHVHTADLetyAGAQGV---VRAAVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSVV-KPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSSEiynqeGLNKp 162
Cdd:cd08937   77 RFGRVDVLINNVGGTIWaKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQ--GVIVNVSSIATR-----GIYR- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 ltqVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT-------------EQTSGMDAKIRDFQASSIPMGRFSEP 229
Cdd:cd08937  149 ---IPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEApprkiprnaapmsEQEKVWYQRIVDQTLDSSLMGRYGTI 225
                        250       260
                 ....*....|....*....|....*...
gi 388856966 230 HEQADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:cd08937  226 DEQVRAILFLASDEASYITGTVLPVGGG 253
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
9-259 1.04e-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: 88.02  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFyrshPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFA----DIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFKKGSIVITSSMSSEiynqeglnkPLTQVfY 168
Cdd:cd09761   77 DVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSE---------PDSEA-Y 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 169 NSSKGAVTNLGKCLAAEWAQHgIRVNILEPGFCNT-EQTSGMDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYL 247
Cdd:cd09761  147 AASKGGLVALTHALAMSLGPD-IRVNCISPGWINTtEQQEFTAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFI 225
                        250
                 ....*....|..
gi 388856966 248 TGSVIRPDGGFT 259
Cdd:cd09761  226 TGETFIVDGGMT 237
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
11-258 1.18e-20

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: 87.93  E-value: 1.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAvanaganvaifyrshpkAQEAAAEVakeFGVQCRA--YQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:cd05328    1 TIVITGAASGIGAATAEL-----------------LEDAGHTV---IGIDLREadVIADLSTPEGRAAAIADVLARCSGV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 -TGLLANAGVSVVKPAVEltsddfryVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEIYNQEG--LNKPLTQ 165
Cdd:cd05328   61 lDGLVNCAGVGGTTVAGL--------VLKVNYFGLRALMEALLPRLRKG--HGPAAVVVSSIAGAGWAQDKleLAKALAA 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VF------------------YNSSKGAVTNLGKCLAAEW-AQHGIRVNILEPGFCNT------EQTSGMDAKIRDFQAss 220
Cdd:cd05328  131 GTearavalaehagqpgylaYAGSKEALTVWTRRRAATWlYGAGVRVNTVAPGPVETpilqafLQDPRGGESVDAFVT-- 208
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 388856966 221 iPMGRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGGF 258
Cdd:cd05328  209 -PMGRRAEPDEIAPVIAFLASDAASWINGANLFVDGGL 245
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
8-257 1.73e-20

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 87.59  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQ 87
Cdd:cd08933    8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTKEEDIKTLISVTVERFGR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSVV-KPAVELTSDDFRYVYDTNVLGVFNSAK-AVAQLWIesgfKKGSIVITSSMSSEIYNQEGlnkpltq 165
Cdd:cd08933   88 IDCLVNNAGWHPPhQTTDETSAQEFRDLLNLNLISYFLASKyALPHLRK----SQGNIINLSSLVGSIGQKQA------- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQAS------SIPMGRFSEPHEQADPAVLL 239
Cdd:cd08933  157 APYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATikegelAQLLGRMGTEAESGLAALFL 236
                        250
                 ....*....|....*...
gi 388856966 240 LSDkASYLTGSVIRPDGG 257
Cdd:cd08933  237 AAE-ATFCTGIDLLLSGG 253
PRK06194 PRK06194
hypothetical protein; Provisional
6-203 2.30e-20

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 87.76  E-value: 2.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK06194   3 DFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAEL-RAQGAEVLGVRTDVSDAAQVEALADAALERF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFK----KGSIVITSSMSSeiynqeGLNK 161
Cdd:PRK06194  82 GAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEKdpayEGHIVNTASMAG------LLAP 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 388856966 162 PLTQVfYNSSKGAVTNLGKCLAAEWAQHG--IRVNILEPGFCNT 203
Cdd:PRK06194 156 PAMGI-YNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPT 198
PRK05855 PRK05855
SDR family oxidoreductase;
9-211 3.89e-20

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 89.27  E-value: 3.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIR-AAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVP 393
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMS----SEIYNQeglnkplt 164
Cdd:PRK05855 394 DIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERG-TGGHIVNVASAAayapSRSLPA-------- 464
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 388856966 165 qvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTS-----GMDA 211
Cdd:PRK05855 465 ---YATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVAttrfaGADA 513
PRK12742 PRK12742
SDR family oxidoreductase;
6-258 5.67e-20

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 85.58  E-value: 5.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkAQEAAAEVAKEFGVQcrAYQCDVGDAELVKKTLKQAqdel 85
Cdd:PRK12742   3 AFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAG---SKDAAERLAQETGAT--AVQTDSADRDAVIDVVRKS---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfkkGSIVITSSMSSEIYNQEGLNKpltq 165
Cdd:PRK12742  74 GALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG----GRIIIIGSVNGDRMPVAGMAA---- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 vfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGmDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDKAS 245
Cdd:PRK12742 146 --YAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDANPA-NGPMKDMMHSFMAIKRHGRPEEVAGMVAWLAGPEAS 222
                        250
                 ....*....|...
gi 388856966 246 YLTGSVIRPDGGF 258
Cdd:PRK12742 223 FVTGAMHTIDGAF 235
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
9-257 5.76e-20

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 85.91  E-value: 5.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFyRSHPKAQEAAAEVAkEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVA-DIDPEIAEKVAEAA-QGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSmsseiynQEGLNKPLTQVFY 168
Cdd:cd08943   79 DIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQG-IGGNIVFNAS-------KNAVAPGPNAAAY 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 169 NSSKGAVTNLGKCLAAEWAQHGIRVNILEP-GFCNTEQTSGM----------DAKIRDFQASSIpMGRFSEPHEQADPAV 237
Cdd:cd08943  151 SAAKAAEAHLARCLALEGGEDGIRVNTVNPdAVFRGSKIWEGvwraarakayGLLEEEYRTRNL-LKREVLPEDVAEAVV 229
                        250       260
                 ....*....|....*....|
gi 388856966 238 LLLSDKASYLTGSVIRPDGG 257
Cdd:cd08943  230 AMASEDFGKTTGAIVTVDGG 249
PRK09135 PRK09135
pteridine reductase; Provisional
4-257 6.78e-20

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 85.75  E-value: 6.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   4 VIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkAQEAAAEVAKEFGVQC----RAYQCDVGDAELVKKTLK 79
Cdd:PRK09135   1 MMTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHR---SAAEADALAAELNALRpgsaAALQADLLDPDALPELVA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  80 QAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfkKGSIV-ITssmssEIYNQeg 158
Cdd:PRK09135  78 ACVAAFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQ---RGAIVnIT-----DIHAE-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 159 lnKPLTQ-VFYNSSKGAVTNLGKCLAAEWAQHgIRVN------ILEPgfcntEQTSGMDAKIRDFQASSIPMGRFSEPHE 231
Cdd:PRK09135 148 --RPLKGyPVYCAAKAALEMLTRSLALELAPE-VRVNavapgaILWP-----EDGNSFDEEARQAILARTPLKRIGTPED 219
                        250       260
                 ....*....|....*....|....*.
gi 388856966 232 QADpAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK09135 220 IAE-AVRFLLADASFITGQILAVDGG 244
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
6-259 9.63e-20

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 85.72  E-value: 9.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKA-GGKAIGVAMDVTNEDAVNAGIDKVAERF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVItsSMSSeIYNQEGlnKPLTQ 165
Cdd:PRK13394  83 GSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKD--DRGGVVI--YMGS-VHSHEA--SPLKS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 VfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT------------EQTSGMDAKIRDFQASSIPMGRFSEPHEQA 233
Cdd:PRK13394 156 A-YVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTplvdkqipeqakELGISEEEVVKKVMLGKTVDGVFTTVEDVA 234
                        250       260
                 ....*....|....*....|....*.
gi 388856966 234 DPAVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK13394 235 QTVLFLSSFPSAALTGQSFVVSHGWF 260
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
7-236 2.14e-19

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: 84.13  E-value: 2.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAE-GGKALVLELDVTDEQQVDAAVERTVEALG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVaqLWIESGFKKGSIVITSSMSSEIynqeglNKPlTQV 166
Cdd:cd08934   80 RLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAA--LPHHLLRNKGTIVNISSVAGRV------AVR-NSA 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSgmdaKIRDFQASSIPMGRFS--EPHEQADPA 236
Cdd:cd08934  151 VYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRD----HITHTITKEAYEERIStiRKLQAEDIA 218
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
10-204 2.43e-19

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: 84.25  E-value: 2.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFRDID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSV-VKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMS-SEIYnqEGLNkpltqvF 167
Cdd:cd05346   81 ILVNNAGLALgLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARN--QGHIINLGSIAgRYPY--AGGN------V 150
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 388856966 168 YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:cd05346  151 YCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETE 187
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
13-257 3.52e-19

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 83.50  E-value: 3.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  13 VVTGGNRGIGLAMSKAVANAGANVAIFYRsHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGLL 92
Cdd:cd05323    4 IITGGASGIGLATAKLLLKKGAKVAILDR-NENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDILI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  93 ANAGVSVVKPAVELT--SDDFRYVYDTNVLGVFNSAKAVAQLWIES-GFKKGSIVITSSMSseiynqeGLNKPLTQVFYN 169
Cdd:cd05323   83 NNAGILDEKSYLFAGklPPPWEKTIDVNLTGVINTTYLALHYMDKNkGGKGGVIVNIGSVA-------GLYPAPQFPVYS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 170 SSKGAVTNLGKCLA-AEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDFQASSIpmgrFSEPHEQADPAVLLLSDKASylT 248
Cdd:cd05323  156 ASKHGVVGFTRSLAdLLEYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAP----TQSPEVVAKAIVYLIEDDEK--N 229

                 ....*....
gi 388856966 249 GSVIRPDGG 257
Cdd:cd05323  230 GAIWIVDGG 238
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
8-257 4.20e-19

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 83.84  E-value: 4.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELGQ 87
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELRAA-GGEALALTADLETYAGAQAAMAAAVEAFGR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSV-VKPAVELTSDDF-----RYVYDTnvlgvFNSAKAVAQLWIESGfkKGSIVITSSMSSEiynqeGLNK 161
Cdd:PRK12823  85 IDVLINNVGGTIwAKPFEEYEEEQIeaeirRSLFPT-----LWCCRAVLPHMLAQG--GGAIVNVSSIATR-----GINR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 162 pltqVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFC---------NTEQTSGMDAK----IRDFQASSIPMGRFSE 228
Cdd:PRK12823 153 ----VPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTeapprrvprNAAPQSEQEKAwyqqIVDQTLDSSLMKRYGT 228
                        250       260
                 ....*....|....*....|....*....
gi 388856966 229 PHEQADPAVLLLSDKASYLTGSVIrPDGG 257
Cdd:PRK12823 229 IDEQVAAILFLASDEASYITGTVL-PVGG 256
PRK07074 PRK07074
SDR family oxidoreductase;
10-259 4.33e-19

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 83.67  E-value: 4.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVqcrAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFV---PVACDLTDAASLAAALANAAAERGPVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSseiynqeGLNkpltqVF-- 167
Cdd:PRK07074  80 VLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRS--RGAVVNIGSVN-------GMA-----ALgh 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 168 --YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGfcnTEQTSGMDAKIRD----FQASS--IPMGRFSEPHEQADPAVLL 239
Cdd:PRK07074 146 paYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPG---TVKTQAWEARVAAnpqvFEELKkwYPLQDFATPDDVANAVLFL 222
                        250       260
                 ....*....|....*....|
gi 388856966 240 LSDKASYLTGSVIRPDGGFT 259
Cdd:PRK07074 223 ASPAARAITGVCLPVDGGLT 242
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
7-257 7.20e-19

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: 82.97  E-value: 7.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:cd08936    8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGE-GLSVTGTVCHVGKAEDRERLVATAVNLHG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVS-VVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeiYNQEGLNKPltq 165
Cdd:cd08936   87 GVDILVSNAAVNpFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRG--GGSVVIVSSVAA--FHPFPGLGP--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 166 vfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSG--MDAKIRDFQASSIPMGRFSEPHEQADPAVLLLSDK 243
Cdd:cd08936  160 --YNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSAlwMDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSED 237
                        250
                 ....*....|....
gi 388856966 244 ASYLTGSVIRPDGG 257
Cdd:cd08936  238 ASYITGETVVVGGG 251
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
12-204 8.25e-19

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: 82.34  E-value: 8.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGANVAI-FYRSHPKAQEAAAEVAKEFGVqcRAYQCDVGDaelvkkTLKQAQDELGQVTG 90
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNTVIaTCRDPSAATELAALGASHSRL--HILELDVTD------EIAESAEAVAERLG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  91 ------LLANAGV-SVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLwIESGFKKGSIVITSSMSSeIynqeGLNKPL 163
Cdd:cd05325   73 dagldvLINNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPL-LLKGARAKIINISSRVGS-I----GDNTSG 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 388856966 164 TQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:cd05325  147 GWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTD 187
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
7-204 1.35e-18

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 82.25  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEIynqeGLnkPLTqV 166
Cdd:cd05332   81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIER--SQGSIVVVSSIAGKI----GV--PFR-T 151
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:cd05332  152 AYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTN 189
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
11-208 1.67e-18

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: 81.51  E-value: 1.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIF-YRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:cd05324    2 VALVTGANRGIGFEIVRQLAKSGPGTVILtARDVERGQAAVEKLRAE-GLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSV-VKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIV-ITSSMSSeiynqeglnkplTQVF 167
Cdd:cd05324   81 ILVNNAGIAFkGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKS--PAGRIVnVSSGLGS------------LTSA 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 388856966 168 YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSG 208
Cdd:cd05324  147 YGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGG 187
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
10-205 6.10e-18

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: 80.12  E-value: 6.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:cd05360    1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREV-RELGGEAIAVVADVADAAQVERAADTAVERFGRID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEiynqegLNKPLtQVFYN 169
Cdd:cd05360   80 TWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRG--GGALINVGSLLGY------RSAPL-QAAYS 150
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 388856966 170 SSKGAVTNLGKCLAAEWAQHG--IRVNILEPGFCNTEQ 205
Cdd:cd05360  151 ASKHAVRGFTESLRAELAHDGapISVTLVQPTAMNTPF 188
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-257 8.17e-18

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 80.15  E-value: 8.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK06077   3 SLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVVKPAveLTSDDfRYV---YDTNVLGVFNSAKAVAQLwIESGfkkGSIVITSSMSSeIYNQEGLNkp 162
Cdd:PRK06077  83 GVADILVNNAGLGLFSPF--LNVDD-KLIdkhISTDFKSVIYCSQELAKE-MREG---GAIVNIASVAG-IRPAYGLS-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 163 ltqvFYNSSKGAVTNLGKCLAAEWAQHgIRVNILEPGFCNTE------QTSGMDAKirDFQASSIPMGRFSEPHEQADPA 236
Cdd:PRK06077 153 ----IYGAMKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKlgeslfKVLGMSEK--EFAEKFTLMGKILDPEEVAEFV 225
                        250       260
                 ....*....|....*....|.
gi 388856966 237 VLLLsdKASYLTGSVIRPDGG 257
Cdd:PRK06077 226 AAIL--KIESITGQVFVLDSG 244
PRK07109 PRK07109
short chain dehydrogenase; Provisional
7-205 2.18e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 79.97  E-value: 2.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEI-RAAGGEALAVVADVADAEAVQAAADRAEEELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIynqeGLnkPLtQV 166
Cdd:PRK07109  85 PIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRD--RGAIIQVGSALAYR----SI--PL-QS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHG--IRVNILEPGFCNTEQ 205
Cdd:PRK07109 156 AYCAAKHAIRGFTDSLRCELLHDGspVSVTMVQPPAVNTPQ 196
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
10-257 3.92e-17

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: 78.35  E-value: 3.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:cd08945    4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREA-GVEADGRTCDVRSVPEIEALVAAAVARYGPID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFKKGSIVITSSMSseiynqeGLNKPLTQVFYN 169
Cdd:cd08945   83 VLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAGGMLERGTGRIINIASTG-------GKQGVVHAAPYS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 170 SSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEqtsgMDAKIRDFQA---------------SSIPMGRFSEPHEQAD 234
Cdd:cd08945  156 ASKHGVVGFTKALGLELARTGITVNAVCPGFVETP----MAASVREHYAdiwevsteeafdritARVPLGRYVTPEEVAG 231
                        250       260
                 ....*....|....*....|...
gi 388856966 235 PAVLLLSDKASYLTGSVIRPDGG 257
Cdd:cd08945  232 MVAYLIGDGAAAVTAQALNVCGG 254
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
11-253 4.19e-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: 78.10  E-value: 4.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVA--IFYRSHPKAQEAAAEVakEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVvvLLARSEEPLQELKEEL--RPGLRVTTVKADLSDAAGVEQLLEAIRKLDGER 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSV-VKPAVELTSDDFRYVYDTNvlgvFNSAKAVAQLWIESG---FKKGSIVITSSMSSeiynqeglNKPL- 163
Cdd:cd05367   79 DLLINNAGSLGpVSKIEFIDLDELQKYFDLN----LTSPVCLTSTLLRAFkkrGLKKTVVNVSSGAA--------VNPFk 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 TQVFYNSSKGAVTNLGKCLAAEwaQHGIRVNILEPGFCNTEqtsgMDAKIRDFQASSIPMGRFSEPHEQA---DPAV--- 237
Cdd:cd05367  147 GWGLYCSSKAARDMFFRVLAAE--EPDVRVLSYAPGVVDTD----MQREIRETSADPETRSRFRSLKEKGellDPEQsae 220
                        250
                 ....*....|....*...
gi 388856966 238 --LLLSDKASYLTGSVIR 253
Cdd:cd05367  221 klANLLEKDKFESGAHVD 238
PRK07454 PRK07454
SDR family oxidoreductase;
10-204 5.52e-17

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 77.69  E-value: 5.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEvAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVT 89
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAE-LRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEiynqeglnkpltQVF-- 167
Cdd:PRK07454  86 VLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARG--GGLIINVSSIAAR------------NAFpq 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 388856966 168 ---YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:PRK07454 152 wgaYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTP 191
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
12-211 6.03e-17

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: 77.11  E-value: 6.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfgvQCRAYQCDVGDaelvKKTLKQAQDELGQVTG- 90
Cdd:cd08931    3 IFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAE---NVVAGALDVTD----RAAWAAALADFAAATGg 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  91 ----LLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLwiesgFKK--GSIVITSSMSSEIYNQEGLnkplt 164
Cdd:cd08931   76 rldaLFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPY-----LKAtpGARVINTASSSAIYGQPDL----- 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 388856966 165 qVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDA 211
Cdd:cd08931  146 -AVYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGET 191
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
13-254 1.22e-16

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: 76.39  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  13 VVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEV-AKEFGVQCrayqcDVGDAELVKKTLKQAQDELGQVTGL 91
Cdd:cd08929    4 LVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQElEGVLGLAG-----DVRDEADVRRAVDAMEEAFGGLDAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  92 LANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSA-KAVAQLWIESGfkkGSIVITSSMSseiynqeGLNKPLTQVFYNS 170
Cdd:cd08929   79 VNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIhKAAPALLRRGG---GTIVNVGSLA-------GKNAFKGGAAYNA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 171 SKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTeqtsgmdakirDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLTGS 250
Cdd:cd08929  149 SKFGLLGLSEAAMLDLREANIRVVNVMPGSVDT-----------GFAGSPEGQAWKLAPEDVAQAVLFALEMPARALVSR 217

                 ....*
gi 388856966 251 V-IRP 254
Cdd:cd08929  218 IeLRP 222
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
7-205 1.41e-16

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: 76.46  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDV--GDAELVKKTLKQAQDE 84
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLltCTSENCQQLAQRIAVN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAG-VSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSmsseiynQEGLNKPL 163
Cdd:cd05340   82 YPRLDGVLHNAGlLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKS--DAGSLVFTSS-------SVGRQGRA 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 388856966 164 TQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQ 205
Cdd:cd05340  153 NWGAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAM 194
PRK07041 PRK07041
SDR family oxidoreductase;
13-260 1.58e-16

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 76.23  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  13 VVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVqcRAYQCDVGDAELVKKTLKqaqdELGQVTGLL 92
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPV--RTAALDITDEAAVDAFFA----EAGPFDHVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  93 ANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAqlwIESGfkkGSIVITSSMSSEiynqeglnKPL-TQVFYNSS 171
Cdd:PRK07041  75 ITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAAR---IAPG---GSLTFVSGFAAV--------RPSaSGVLQGAI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 172 KGAVTNLGKCLAAEWAQhgIRVNILEPGFCNTEQTSGM--DAKIRDFQ--ASSIPMGRFSEPHEQADPAVLLLSDkaSYL 247
Cdd:PRK07041 141 NAALEALARGLALELAP--VRVNTVSPGLVDTPLWSKLagDAREAMFAaaAERLPARRVGQPEDVANAILFLAAN--GFT 216
                        250
                 ....*....|...
gi 388856966 248 TGSVIRPDGGFTI 260
Cdd:PRK07041 217 TGSTVLVDGGHAI 229
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
7-211 2.27e-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: 75.91  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVaiFYRShPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDelg 86
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAKK--VYAA-VRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD--- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 qVTGLLANAGVSvvKPAVELTSDDF---RYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeIYNQEGLNKpl 163
Cdd:cd05354   75 -VDVVINNAGVL--KPATLLEEGALealKQEMDVNVFGLLRLAQAFAPVLKANG--GGAIVNLNSVAS-LKNFPAMGT-- 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 388856966 164 tqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDA 211
Cdd:cd05354  147 ----YSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAGG 190
PRK06125 PRK06125
short chain dehydrogenase; Provisional
5-257 3.76e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 75.85  E-value: 3.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAqde 84
Cdd:PRK06125   3 LHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVHALDLSSPEAREQLAAEA--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 lGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNsakaVAQLWIESGFKKGSIVITSsmsseIYNQEGLNKPLT 164
Cdd:PRK06125  80 -GDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYID----LTRLAYPRMKARGSGVIVN-----VIGAAGENPDAD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTS-----------GMDAKIRDFQASsIPMGRFSEPHEQA 233
Cdd:PRK06125 150 YICGSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLtllkgraraelGDESRWQELLAG-LPLGRPATPEEVA 228
                        250       260
                 ....*....|....*....|....
gi 388856966 234 DPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK06125 229 DLVAFLASPRSGYTSGTVVTVDGG 252
PRK09291 PRK09291
SDR family oxidoreductase;
9-235 5.64e-16

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 75.03  E-value: 5.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGN----RGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEvakefGVQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK09291   2 SKTILITGAGsgfgREVALRLARKGHNVIAGVQIAPQVTALRAEAARR-----GLALRVEKLDLTDAIDRAQAAEWDVDV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LgqvtglLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSseiynqeGLNKPLT 164
Cdd:PRK09291  77 L------LNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVAR--GKGKVVFTSSMA-------GLITGPF 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE-QTSGMDAKIR--DFQASSIPMGRFSEPHEQADP 235
Cdd:PRK09291 142 TGAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTGfNDTMAETPKRwyDPARNFTDPEDLAFPLEQFDP 215
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
7-222 5.80e-16

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: 74.86  E-value: 5.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:cd05343    4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFKKGSIVITSSMSSEIYNQEGLNKpltqv 166
Cdd:cd05343   84 GVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDGHIININSMSGHRVPPVSVFH----- 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388856966 167 FYNSSKGAVTNLGKCLAAE--WAQHGIRVNILEPGFCNTE---QTSGMDAKIRDFQASSIP 222
Cdd:cd05343  159 FYAATKHAVTALTEGLRQElrEAKTHIRATSISPGLVETEfafKLHDNDPEKAAATYESIP 219
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-257 1.29e-15

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 74.03  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVqcRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNI--HYVVGDVSSTESARNVIEKAAKVLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAG------VSVVKPAVELTSDDFRY-VYDTNVLGVFnsakavaqlwiesgFKKGS-IVITSSMSseiynqeG 158
Cdd:PRK05786  81 AIDGLVVTVGgyvedtVEEFSGLEEMLTNHIKIpLYAVNASLRF--------------LKEGSsIVLVSSMS-------G 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 159 LNKPL-TQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMD-AKIRDFQASSIPmgrfsePHEQADPA 236
Cdd:PRK05786 140 IYKASpDQLSYAVAKAGLAKAVEILASELLGRGIRVNGIAPTTISGDFEPERNwKKLRKLGDDMAP------PEDFAKVI 213
                        250       260
                 ....*....|....*....|.
gi 388856966 237 VLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK05786 214 IWLLTDEADWVDGVVIPVDGG 234
PRK12746 PRK12746
SDR family oxidoreductase;
6-260 4.18e-15

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 72.76  E-value: 4.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFY-RSHPKAQEAAAEVAKEFGvQCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK12746   3 NLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYgRNKQAADETIREIESNGG-KAFLIEADLNSIDGVKKLVEQLKNE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 L------GQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWiesgFKKGSIVITSSMSSEIynqeG 158
Cdd:PRK12746  82 LqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL----RAEGRVINISSAEVRL----G 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 159 LNKPLTqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPA 236
Cdd:PRK12746 154 FTGSIA---YGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLldDPEIRNFATNSSVFGRIGQVEDIADAV 230
                        250       260
                 ....*....|....*....|....
gi 388856966 237 VLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK12746 231 AFLASSDSRWVTGQIIDVSGGFCL 254
PRK08264 PRK08264
SDR family oxidoreductase;
5-211 4.28e-15

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 72.23  E-value: 4.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAmskavanaganvaiFYRS--HPKAQE--AAA---EVAKEFGVQCRAYQCDVGDAELVKKT 77
Cdd:PRK08264   2 MDIKGKVVLVTGANRGIGRA--------------FVEQllARGAAKvyAAArdpESVTDLGPRVVPLQLDVTDPASVAAA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  78 LKQAQDelgqVTGLLANAGVSVVKPAVELTS-DDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeIYNQ 156
Cdd:PRK08264  68 AEAASD----VTILVNNAGIFRTGSLLLEGDeDALRAEMETNYFGPLAMARAFAPVLAANG--GGAIVNVLSVLS-WVNF 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 388856966 157 EGLNKpltqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDA 211
Cdd:PRK08264 141 PNLGT------YSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGLDA 189
PRK05876 PRK05876
short chain dehydrogenase; Provisional
9-220 5.37e-15

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 72.68  E-value: 5.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAE-GFDVHGVMCDVRHREEVTHLADEAFRLLGHV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSSEIYNQeGLNKpltqvfY 168
Cdd:PRK05876  85 DVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQG-TGGHVVFTASFAGLVPNA-GLGA------Y 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 388856966 169 NSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDaKIR--DFQASS 220
Cdd:PRK05876 157 GVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNLVANSE-RIRgaACAQSS 209
PRK08267 PRK08267
SDR family oxidoreductase;
10-203 5.88e-15

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 72.28  E-value: 5.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAvanaganvaiFYRSHPK------AQEAAAEVAKEFGV-QCRAYQCDVGDAELVKKTLKQ-A 81
Cdd:PRK08267   2 KSIFITGAASGIGRATALL----------FAAEGWRvgaydiNEAGLAALAAELGAgNAWTGALDVTDRAAWDAALADfA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  82 QDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAvAQLWIESgfKKGSIVITSSMSSEIYNQEGLnk 161
Cdd:PRK08267  72 AATGGRLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHA-ALPYLKA--TPGARVINTSSASAIYGQPGL-- 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 388856966 162 pltqVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT 203
Cdd:PRK08267 147 ----AVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDT 184
PRK06180 PRK06180
short chain dehydrogenase; Provisional
9-199 3.33e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 70.33  E-value: 3.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:PRK06180   4 MKTWLITGVSSGFGRALAQAALAAGHRVVGTVRS----EAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAV-----AQlwiesgfKKGSIVITSSMSSEIYNqEGLNkpl 163
Cdd:PRK06180  80 DVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVlpgmrAR-------RRGHIVNITSMGGLITM-PGIG--- 148
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 388856966 164 tqvFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPG 199
Cdd:PRK06180 149 ---YYCGSKFALEGISESLAKEVAPFGIHVTAVEPG 181
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
7-253 3.52e-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: 70.17  E-value: 3.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQ-AQDEL 85
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERvAREQQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANA-------GVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYnqeg 158
Cdd:cd09763   81 GRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAG--KGLIVIISSTGGLEY---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 159 lnkpLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQ-TSGMDAKIRDFQASSIPMGRFSEPHEQADPAV 237
Cdd:cd09763  155 ----LFNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELvLEMPEDDEGSWHAKERDAFLNGETTEYSGRCV 230
                        250
                 ....*....|....*...
gi 388856966 238 LLLSD--KASYLTGSVIR 253
Cdd:cd09763  231 VALAAdpDLMELSGRVLI 248
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
7-199 3.71e-14

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: 70.11  E-value: 3.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQ-----------EAAAEVAKEFGVQCRAYQCDVGDAELVK 75
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDngsakslpgtiEETAEEIEAAGGQALPIVVDVRDEDQVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  76 KTLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVitsSMSSEIYN 155
Cdd:cd05338   81 ALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAG--QGHIL---NISPPLSL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 388856966 156 QEGLNKpltqVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPG 199
Cdd:cd05338  156 RPARGD----VAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPS 195
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
9-260 4.43e-14

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: 69.92  E-value: 4.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTG--GNRGIGLAMSKAVANAGANVAIFYRShPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:cd05372    1 GKRILITGiaNDRSIAWGIAKALHEAGAELAFTYQP-EALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGL---LANA-GVSVVKPAVELTSDDFRYVYDtnvlgvfNSAKAVAQLwiESGFKK-----GSIV----ITSSMSSEI 153
Cdd:cd05372   80 KLDGLvhsIAFApKVQLKGPFLDTSRKGFLKALD-------ISAYSLVSL--AKAALPimnpgGSIVtlsyLGSERVVPG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 154 YNQEGLNKpltqvfynSSKGAVTnlgKCLAAEWAQHGIRVNILEPGFCNTEQTSG---MDaKIRDFQASSIPMGRFSEPH 230
Cdd:cd05372  151 YNVMGVAK--------AALESSV---RYLAYELGRKGIRVNAISAGPIKTLAASGitgFD-KMLEYSEQRAPLGRNVTAE 218
                        250       260       270
                 ....*....|....*....|....*....|
gi 388856966 231 EQADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:cd05372  219 EVGNTAAFLLSDLSSGITGEIIYVDGGYHI 248
PRK08251 PRK08251
SDR family oxidoreductase;
10-215 6.09e-14

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 69.19  E-value: 6.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEF-GVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYpGIKVAVAALDVNDHDQVFEVFAEFRDELGGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeiynQEGLNKPLTQvfY 168
Cdd:PRK08251  83 DRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQG--SGHLVLISSVSA----VRGLPGVKAA--Y 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 388856966 169 NSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEqtsgMDAKIRD 215
Cdd:PRK08251 155 AASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSE----MNAKAKS 197
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
9-249 7.60e-14

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: 69.18  E-value: 7.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFG---VQCRayQCDVGDAELVKKTLKQAQDEL 85
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGnakVEVI--QLDLSSLASVRQFAEEFLARF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGVSVvkPAVELTSDDFRYVYDTNVLGVFnsakAVAQLWIESgFKKGS---IVITSSMSS-------EIYN 155
Cdd:cd05327   79 PRLDILINNAGIMA--PPRRLTKDGFELQFAVNYLGHF----LLTNLLLPV-LKASApsrIVNVSSIAHragpidfNDLD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 156 QEGLNKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTsgmdAKIRDFQASSIPMGRFSE--PHEQA 233
Cdd:cd05327  152 LENNKEYSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELL----RRNGSFFLLYKLLRPFLKksPEQGA 227
                        250
                 ....*....|....*..
gi 388856966 234 DPAV-LLLSDKASYLTG 249
Cdd:cd05327  228 QTALyAATSPELEGVSG 244
PRK06181 PRK06181
SDR family oxidoreductase;
9-204 1.01e-13

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 68.85  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELA-DHGGEALVVPTDVSDAEACERLIEAAVARFGGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  89 TGLLANAGVSVVKPAVELTSDD-FRYVYDTNVLG-VFNSAKAVAQLwIESgfkKGSIVITSSMSseiynqeGLNKPLTQV 166
Cdd:PRK06181  80 DILVNNAGITMWSRFDELTDLSvFERVMRVNYLGaVYCTHAALPHL-KAS---RGQIVVVSSLA-------GLTGVPTRS 148
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 388856966 167 FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:PRK06181 149 GYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATD 186
PRK08263 PRK08263
short chain dehydrogenase; Provisional
48-242 1.83e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 68.53  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  48 EAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAK 127
Cdd:PRK08263  38 ATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 128 AVAQLWIESGfkKGSIVITSSMSseiynqeGLNK-PLTQVfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPG------- 199
Cdd:PRK08263 118 AVLPYLREQR--SGHIIQISSIG-------GISAfPMSGI-YHASKWALEGMSEALAQEVAEFGIKVTLVEPGgystdwa 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 388856966 200 FCNTEQTSGMDA--KIRD--FQASSIPMGRfSEPHEQAdPAVLLLSD 242
Cdd:PRK08263 188 GTSAKRATPLDAydTLREelAEQWSERSVD-GDPEAAA-EALLKLVD 232
PRK05650 PRK05650
SDR family oxidoreductase;
10-203 1.92e-13

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 68.14  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGvqcRAY--QCDVGDAELVKKTLKQAQDELGQ 87
Cdd:PRK05650   1 NRVMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGG---DGFyqRCDVRDYSQLTALAQACEEKWGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSseiynqeGLNKPLTQVF 167
Cdd:PRK05650  78 IDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQK--SGRIVNIASMA-------GLMQGPAMSS 148
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 388856966 168 YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT 203
Cdd:PRK05650 149 YNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQT 184
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
5-260 2.41e-13

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 67.83  E-value: 2.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTG--GNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQ 82
Cdd:PRK08594   3 LSLEGKTYVVMGvaNKRSIAWGIARSLHNAGAKLVFTYAGERLEKEVRELADTLEGQESLLLPCDVTSDEEITACFETIK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  83 DELGQVTGL---LANAGVSVVKPA-VELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkkgSIVITSSMSSEI----Y 154
Cdd:PRK08594  83 EEVGVIHGVahcIAFANKEDLRGEfLETSRDGFLLAQNISAYSLTAVAREAKKLMTEGG----SIVTLTYLGGERvvqnY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 155 NQEGLNKPltqvfynSSKGAVtnlgKCLAAEWAQHGIRVNILEPGFCNT---EQTSGMDAKIRDFQASSiPMGRFSEPHE 231
Cdd:PRK08594 159 NVMGVAKA-------SLEASV----KYLANDLGKDGIRVNAISAGPIRTlsaKGVGGFNSILKEIEERA-PLRRTTTQEE 226
                        250       260
                 ....*....|....*....|....*....
gi 388856966 232 QADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK08594 227 VGDTAAFLFSDLSRGVTGENIHVDSGYHI 255
PRK06940 PRK06940
short chain dehydrogenase; Provisional
48-259 3.71e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 67.35  E-value: 3.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  48 EAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQdELGQVTGLLANAGVSVVKPAVE--LTSDdfryVYDTNVLgvfns 125
Cdd:PRK06940  38 EAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQ-TLGPVTGLVHTAGVSPSQASPEaiLKVD----LYGTALV----- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 126 AKAVAQLwIESGfkkGSIVITSSMSS--------EIYNQ-------EGLNKPLTQV--------FYNSSKGAvtNLGKCL 182
Cdd:PRK06940 108 LEEFGKV-IAPG---GAGVVIASQSGhrlpaltaEQERAlattpteELLSLPFLQPdaiedslhAYQIAKRA--NALRVM 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 183 AA--EWAQHGIRVNILEPGFCNT-----EQTSGMDAKIRDFQASSiPMGRFSEPHEQADPAVLLLSDKASYLTGSVIRPD 255
Cdd:PRK06940 182 AEavKWGERGARINSISPGIISTplaqdELNGPRGDGYRNMFAKS-PAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVD 260

                 ....
gi 388856966 256 GGFT 259
Cdd:PRK06940 261 GGAT 264
PRK07201 PRK07201
SDR family oxidoreductase;
7-191 5.72e-13

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 68.05  E-value: 5.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVaKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK07201 369 LVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEI-RAKGGTAHAYTCDLTDSAAVDHTVKDILAEHG 447
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTGLLANAGVSvVKPAVELTSD---DFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMsseiynqeGL--NK 161
Cdd:PRK07201 448 HVDYLVNNAGRS-IRRSVENSTDrfhDYERTMAVNYFGAVRLILGLLPHMRERRF--GHVVNVSSI--------GVqtNA 516
                        170       180       190
                 ....*....|....*....|....*....|..
gi 388856966 162 PLtqvF--YNSSKGAVTNLGKCLAAEWAQHGI 191
Cdd:PRK07201 517 PR---FsaYVASKAALDAFSDVAASETLSDGI 545
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
11-193 1.05e-12

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: 65.87  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTG 90
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  91 LLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSeIYNQEGLNKpltqvfYNS 170
Cdd:cd05373   81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARG--RGTIIFTGATAS-LRGRAGFAA------FAG 151
                        170       180
                 ....*....|....*....|...
gi 388856966 171 SKGAVTNLGKCLAAEWAQHGIRV 193
Cdd:cd05373  152 AKFALRALAQSMARELGPKGIHV 174
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-214 1.29e-12

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 66.78  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKavanaganvaIFYR--SH------PKAQEAAAEVAKEFGvqCRAYQCDVGDAELVKKTL 78
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAE----------VLARdgAHvvcldvPAAGEALAAVANRVG--GTALALDITAPDAPARIA 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  79 KQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLgvfnSAKAVAQLWIESGFKK--GSIVITSSMSseiynq 156
Cdd:PRK08261 276 EHLAERHGGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLL----APLRITEALLAAGALGdgGRIVGVSSIS------ 345
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 388856966 157 eGLNKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIR 214
Cdd:PRK08261 346 -GIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMTAAIPFATR 402
PRK09186 PRK09186
flagellin modification protein A; Provisional
7-260 1.33e-12

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 65.78  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRA-YQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSlVELDITDQESLEEFLSKSAEKY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANA---GVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSS------EIYNQ 156
Cdd:PRK09186  82 GKIDGAVNCAyprNKDYGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGG--GNLVNISSIYGvvapkfEIYEG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 157 EGLNKPltqVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIRDfQASSIPMgrfSEPHEQADPA 236
Cdd:PRK09186 160 TSMTSP---VEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQPEAFLNAYKK-CCNGKGM---LDPDDICGTL 232
                        250       260
                 ....*....|....*....|....
gi 388856966 237 VLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK09186 233 VFLLSDQSKYITGQNIIVDDGFSL 256
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
6-258 1.43e-12

(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: 65.42  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAI-----FYRSHPKAQEAAAEVAKEF---GVQCRAYQCDVGDAELVKKT 77
Cdd:cd05353    2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggDRKGSGKSSSAADKVVDEIkaaGGKAVANYDSVEDGEKIVKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  78 lkqAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSmSSEIYNQE 157
Cdd:cd05353   82 ---AIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQ--KFGRIINTSS-AAGLYGNF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 158 GlnkpltQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGfcnteQTSGMDAKIrdfqassIPMGRFSEPH-EQADPA 236
Cdd:cd05353  156 G------QANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA-----AGSRMTETV-------MPEDLFDALKpEYVAPL 217
                        250       260
                 ....*....|....*....|..
gi 388856966 237 VLLLSDKASYLTGSVIRPDGGF 258
Cdd:cd05353  218 VLYLCHESCEVTGGLFEVGAGW 239
PRK08339 PRK08339
short chain dehydrogenase; Provisional
5-257 3.23e-12

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 64.88  E-value: 3.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDe 84
Cdd:PRK08339   4 IDLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTKREDLERTVKELKN- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFkkGSIVITSSMSseiynqegLNKPLT 164
Cdd:PRK08339  83 IGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGF--GRIIYSTSVA--------IKEPIP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 165 QV-FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE------------QTSGMDAKIRDFqASSIPMGRFSEPHE 231
Cdd:PRK08339 153 NIaLSNVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTDrviqlaqdrakrEGKSVEEALQEY-AKPIPLGRLGEPEE 231
                        250       260
                 ....*....|....*....|....*.
gi 388856966 232 QADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK08339 232 IGYLVAFLASDLGSYINGAMIPVDGG 257
PRK05866 PRK05866
SDR family oxidoreductase;
5-196 4.74e-12

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 64.38  E-value: 4.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVqCRAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK05866  36 VDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGD-AMAVPCDLSDLDAVDALVADVEKR 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVVKPAVElTSDDFRYVYDTNVLGVFNSAK---AVAQLWIESGfkKGSI--VITSSMSSEIynqegl 159
Cdd:PRK05866 115 IGGVDILINNAGRSIRRPLAE-SLDRWHDVERTMVLNYYAPLRlirGLAPGMLERG--DGHIinVATWGVLSEA------ 185
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 388856966 160 nKPLTQVfYNSSKGAVTNLGKCLAAEWAQHGIRVNIL 196
Cdd:PRK05866 186 -SPLFSV-YNASKAALSAVSRVIETEWGDRGVHSTTL 220
PRK06179 PRK06179
short chain dehydrogenase; Provisional
8-203 6.93e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 63.77  E-value: 6.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGanvaifYR-----SHPKAQEAAAEVakEFGVqcrayqCDVGDAELVKKTLKQAQ 82
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAG------YRvfgtsRNPARAAPIPGV--ELLE------LDVTDDASVQAAVDEVI 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  83 DELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAV-----AQlwiesgfKKGSIVITSSMSSEI---Y 154
Cdd:PRK06179  69 ARAGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVlphmrAQ-------GSGRIINISSVLGFLpapY 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 388856966 155 NqeglnkpltqVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT 203
Cdd:PRK06179 142 M----------ALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKT 180
PRK08278 PRK08278
SDR family oxidoreductase;
6-249 7.91e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 63.77  E-value: 7.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRS---HPKAQ----EAAAEVaKEFGVQCRAYQCDVGDAELVKKTL 78
Cdd:PRK08278   3 SLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTaepHPKLPgtihTAAEEI-EAAGGQALPLVGDVRDEDQVAAAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  79 KQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkkGSIVITSS----MSSEIY 154
Cdd:PRK08278  82 AKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSE---NPHILTLSpplnLDPKWF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 155 NQEglnkpltqVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPgfcnteQTSGMDAKIRDFQASSIPMGRFSEPHEQAD 234
Cdd:PRK08278 159 APH--------TAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP------RTTIATAAVRNLLGGDEAMRRSRTPEIMAD 224
                        250
                 ....*....|....*
gi 388856966 235 PAVLLLSDKASYLTG 249
Cdd:PRK08278 225 AAYEILSRPAREFTG 239
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
6-260 8.74e-12

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: 63.12  E-value: 8.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTG--GNRGIGLAMSKAVANAGANVAIFYRShPKAQEAAAEVAKEFGVqCRAYQCDVGDAELVKKTLKQAQD 83
Cdd:COG0623    2 LLKGKRGLITGvaNDRSIAWGIAKALHEEGAELAFTYQG-EALKKRVEPLAEELGS-ALVLPCDVTDDEQIDALFDEIKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLL---ANAGVS-VVKPAVELTSDDFRYVYDTnvlgvfnSA---KAVAQLwiesgFKK-----GSIVITSSMSS 151
Cdd:COG0623   80 KWGKLDFLVhsiAFAPKEeLGGRFLDTSREGFLLAMDI-------SAyslVALAKA-----AEPlmnegGSIVTLTYLGA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 152 E----IYNQEGLNKpltqvfynSSKGAVTnlgKCLAAEWAQHGIRVNILEPGFCNTEQTSGMD--AKIRDFQASSIPMGR 225
Cdd:COG0623  148 ErvvpNYNVMGVAK--------AALEASV---RYLAADLGPKGIRVNAISAGPIKTLAASGIPgfDKLLDYAEERAPLGR 216
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 388856966 226 FSEPHEQADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:COG0623  217 NVTIEEVGNAAAFLLSDLASGITGEIIYVDGGYHI 251
PRK12747 PRK12747
short chain dehydrogenase; Provisional
7-257 2.04e-11

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 62.40  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELG 86
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTG------LLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFnsakAVAQLWIESGFKKGSIVITSSMSSEIYNQEGln 160
Cdd:PRK12747  82 NRTGstkfdiLINNAGIGPGAFIEETTEQFFDRMVSVNAKAPF----FIIQQALSRLRDNSRIINISSAATRISLPDF-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 161 kpltqVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--DAKIRDFQASSIPMGRFSEPHEQADPAVL 238
Cdd:PRK12747 156 -----IAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELlsDPMMKQYATTISAFNRLGEVEDIADTAAF 230
                        250
                 ....*....|....*....
gi 388856966 239 LLSDKASYLTGSVIRPDGG 257
Cdd:PRK12747 231 LASPDSRWVTGQLIDVSGG 249
PRK06182 PRK06182
short chain dehydrogenase; Validated
11-204 2.26e-11

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 62.28  E-value: 2.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAevakeFGVQCRAYqcDVGDAELVKKTLKQAQDELGQVTG 90
Cdd:PRK06182   5 VALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLAS-----LGVHPLSL--DVTDEASIKAAVDTIIAEEGRIDV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  91 LLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAV-----AQlwiesgfKKGSIVITSSMSSEIYNQEGlnkpltq 165
Cdd:PRK06182  78 LVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVlphmrAQ-------RSGRIINISSMGGKIYTPLG------- 143
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 388856966 166 VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:PRK06182 144 AWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTE 182
PRK06482 PRK06482
SDR family oxidoreductase;
49-211 2.52e-11

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 62.44  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  49 AAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKA 128
Cdd:PRK06482  38 ALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 129 -VAQLWIESGfkkGSIVITSSMSSEI-YNQEGLnkpltqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQT 206
Cdd:PRK06482 118 aLPHLRRQGG---GRIVQVSSEGGQIaYPGFSL--------YHATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFG 186

                 ....*
gi 388856966 207 SGMDA 211
Cdd:PRK06482 187 AGLDR 191
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
11-124 3.41e-11

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: 60.27  E-value: 3.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   11 TIVVTGGNRGIGLAMSKAVANAGANVAIFY-RSHPKAQEAAAEVA--KEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQ 87
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARHLVLLsRSAAPRPDAQALIAelEARGVEVVVVACDVSDPDAVAALLAEIKAEGPP 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 388856966   88 VTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFN 124
Cdd:pfam08659  82 IRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWN 118
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
5-212 3.72e-11

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: 61.17  E-value: 3.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVakeFGVQcrAYQCDVGDAELVKKTLKQAQDE 84
Cdd:cd05370    1 MKLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKEL---PNIH--TIVLDVGDAESVEALAEALLSE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGV----SVVKPAVELtsDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSmsseiynqeGL- 159
Cdd:cd05370   76 YPNLDILINNAGIqrpiDLRDPASDL--DKADTEIDTNLIGPIRLIKAFLPHLKKQ--PEATIVNVSS---------GLa 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 388856966 160 NKPLTQV-FYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAK 212
Cdd:cd05370  143 FVPMAANpVYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNP 196
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
8-153 5.33e-11

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: 62.00  E-value: 5.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGLAMSKAVANAGANVAIFY--RSHPKAQEAAAEVAKEF---GVQCRAYQCDVGDAELVKKTLKQAQ 82
Cdd:cd08953  204 PGGVYLVTGGAGGIGRALARALARRYGARLVLLgrSPLPPEEEWKAQTLAALealGARVLYISADVTDAAAVRRLLEKVR 283
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388856966  83 DELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLwiESGFkkgsIVITSSMSSEI 153
Cdd:cd08953  284 ERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADE--PLDF----FVLFSSVSAFF 348
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
7-260 9.91e-11

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 60.22  E-value: 9.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTG--GNRGIGLAMSKAVANAGANVAIFYRSHpKAQEAAAEVAKEFGVQCrAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK06997   4 LAGKRILITGllSNRSIAYGIAKACKREGAELAFTYVGD-RFKDRITEFAAEFGSDL-VFPCDVASDEQIDALFASLGQH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVvKPAVE------LTSDDFRYVYDTNVLGVFNSAKAVAQLWIesgfKKGSIVITSSMSSEI----Y 154
Cdd:PRK06997  82 WDGLDGLVHSIGFAP-REAIAgdfldgLSRENFRIAHDISAYSFPALAKAALPMLS----DDASLLTLSYLGAERvvpnY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 155 NQEGLNKPltqvfynSSKGAVtnlgKCLAAEWAQHGIRVNILEPGFCNTEQTSGMD--AKIRDFQASSIPMGRFSEPHEQ 232
Cdd:PRK06997 157 NTMGLAKA-------SLEASV----RYLAVSLGPKGIRANGISAGPIKTLAASGIKdfGKILDFVESNAPLRRNVTIEEV 225
                        250       260
                 ....*....|....*....|....*...
gi 388856966 233 ADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK06997 226 GNVAAFLLSDLASGVTGEITHVDSGFNA 253
PRK08340 PRK08340
SDR family oxidoreductase;
12-259 1.72e-10

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 59.82  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGANVAIFYRShPKAQEAAAEVAKEFGvQCRAYQCDVGDAELVKKTLKQAQDELGQVTGL 91
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARVVISSRN-EENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELLGGIDAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  92 LANAGVSVVKPAV--ELTSDDFRYVYDTNVLGVFNSAKAVAQLWIEsGFKKGSIVITSSMSseiynqegLNKPLTQ-VFY 168
Cdd:PRK08340  81 VWNAGNVRCEPCMlhEAGYSDWLEAALLHLVAPGYLTTLLIQAWLE-KKMKGVLVYLSSVS--------VKEPMPPlVLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 169 NSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT------------EQTSGMDAKIRDFQASSIPMGRFSEPHEQADPA 236
Cdd:PRK08340 152 DVTRAGLVQLAKGVSRTYGGKGIRAYTVLLGSFDTpgarenlariaeERGVSFEETWEREVLERTPLKRTGRWEELGSLI 231
                        250       260
                 ....*....|....*....|...
gi 388856966 237 VLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK08340 232 AFLLSENAEYMLGSTIVFDGAMT 254
PRK06914 PRK06914
SDR family oxidoreductase;
8-203 2.85e-10

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 59.27  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   8 KGQTIVVTGGNRGIGL----AMSKAVanaganvaifYR-----SHPKAQEAAAEVAKEFGVQCR--AYQCDVGDAELVKk 76
Cdd:PRK06914   2 NKKIAIVTGASSGFGLlttlELAKKG----------YLviatmRNPEKQENLLSQATQLNLQQNikVQQLDVTDQNSIH- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  77 TLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEIyNQ 156
Cdd:PRK06914  71 NFQLVLKEIGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQ--KSGKIINISSISGRV-GF 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 388856966 157 EGLNKpltqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNT 203
Cdd:PRK06914 148 PGLSP------YVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNT 188
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
7-260 8.53e-10

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 57.67  E-value: 8.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTG--GNRGIGLAMSKAVANAGANVAIFYRSHpKAQEAAAEVAKEFGVQCrAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK08690   4 LQGKKILITGmiSERSIAYGIAKACREQGAELAFTYVVD-KLEERVRKMAAELDSEL-VFRCDVASDDEINQVFADLGKH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSVvKPAVE------LTSDDFRYVYDTNVLGVFNSAKAvAQLWIESgfKKGSIVITSSMSS----EIY 154
Cdd:PRK08690  82 WDGLDGLVHSIGFAP-KEALSgdfldsISREAFNTAHEISAYSLPALAKA-ARPMMRG--RNSAIVALSYLGAvraiPNY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 155 NQEGLNKPltqvfynSSKGAVTNLGKCLAAEwaqhGIRVNILEPGFCNTEQTSGMD--AKIRDFQASSIPMGRFSEPHEQ 232
Cdd:PRK08690 158 NVMGMAKA-------SLEAGIRFTAACLGKE----GIRCNGISAGPIKTLAASGIAdfGKLLGHVAAHNPLRRNVTIEEV 226
                        250       260
                 ....*....|....*....|....*...
gi 388856966 233 ADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK08690 227 GNTAAFLLSDLSSGITGEITYVDGGYSI 254
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
13-260 8.92e-10

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: 57.63  E-value: 8.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   13 VVTGGNRGIGLAMSKAVANAGANVAIFY-RSHPKAQEAAAEVAKE---FGVQCRAyqcdvgDAELVKKTLKQAQD----- 83
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYhRSAAAASTLAAELNARrpnSAVTCQA------DLSNSATLFSRCEAiidac 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   84 --ELGQVTGLLANAgvSVVKPAVELTSDDFRYV-----YDTNVLGVFNSaKAVAQLWIESGF---KKGSIVITSSMSSEI 153
Cdd:TIGR02685  79 frAFGRCDVLVNNA--SAFYPTPLLRGDAGEGVgdkksLEVQVAELFGS-NAIAPYFLIKAFaqrQAGTRAEQRSTNLSI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  154 YN--QEGLNKPLTQ-VFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFcnTEQTSGMDAKIRDFQASSIPMGRFSEPH 230
Cdd:TIGR02685 156 VNlcDAMTDQPLLGfTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL--SLLPDAMPFEVQEDYRRKVPLGQREASA 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 388856966  231 EQ-ADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:TIGR02685 234 EQiADVVIFLVSPKAKYITGTCIKVDGGLSL 264
PRK12744 PRK12744
SDR family oxidoreductase;
6-259 2.26e-09

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 56.29  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGG--NRGiGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVA--KEFGVQCRAYQCDVGDAELVKKTLKQA 81
Cdd:PRK12744   5 SLKGKVVLIAGGakNLG-GLIARDLAAQGAKAVAIHYNSAASKADAEETVAavKAAGAKAVAFQADLTTAAAVEKLFDDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  82 QDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNvlgvfnsAKAvAQLWIESGFKK----GSIV--ITSSMsseiyn 155
Cdd:PRK12744  84 KAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVN-------SKS-AFFFIKEAGRHlndnGKIVtlVTSLL------ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 156 qeGLNKPLTQVfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGMDAKIR-DFQASSIPMGRFSEPH---- 230
Cdd:PRK12744 150 --GAFTPFYSA-YAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFFYPQEGAEAvAYHKTAAALSPFSKTGltdi 226
                        250       260
                 ....*....|....*....|....*....
gi 388856966 231 EQADPAVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK12744 227 EDIVPFIRFLVTDGWWITGQTILINGGYT 255
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
13-214 2.27e-09

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 56.07  E-value: 2.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  13 VVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELgQVTGLL 92
Cdd:cd05356    5 VVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERIEKELEGL-DIGILV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  93 ANAGVSVVKPAV--ELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEIynqeglNKPLTQVfYNS 170
Cdd:cd05356   84 NNVGISHSIPEYflETPEDELQDIINVNVMATLKMTRLILPGMVKR--KKGAIVNISSFAGLI------PTPLLAT-YSA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 388856966 171 SKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTsgmdaKIR 214
Cdd:cd05356  155 SKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMS-----KIR 193
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
186-257 2.30e-09

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 56.16  E-value: 2.30e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 388856966 186 WAQHGIRVNILEPGFCNT---EQTSGM--DAKIRDFQAssiPMGRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK12428 156 FGARGIRVNCVAPGPVFTpilGDFRSMlgQERVDSDAK---RMGRPATADEQAAVLVFLCSDAARWINGVNLPVDGG 229
PRK07791 PRK07791
short chain dehydrogenase; Provisional
7-257 3.06e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 56.22  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIG----LAMSKAVANAGAN-VAIFYRSHPKAQEAAAEVAKEF---GVQCRAYQCDVGDAELVKKTL 78
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGrahaLAFAAEGARVVVNdIGVGLDGSASGGSAAQAVVDEIvaaGGEAVANGDDIADWDGAANLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  79 KQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWiESGFKKG-----SIVITSSMSsei 153
Cdd:PRK07791  84 DAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYW-RAESKAGravdaRIINTSSGA--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 154 ynqeGLNKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGfCNTEQTSGMDAKIrdfqASSIPMGRF--SEPHE 231
Cdd:PRK07791 160 ----GLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA-ARTRMTETVFAEM----MAKPEEGEFdaMAPEN 230
                        250       260
                 ....*....|....*....|....*.
gi 388856966 232 QADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK07791 231 VSPLVVWLGSAESRDVTGKVFEVEGG 256
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
11-204 3.39e-09

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: 55.93  E-value: 3.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIFY---RSHPKAQ---EAAAEVAkefGVQCRAYQCDVGDAELVKKTLKQAQDe 84
Cdd:cd09806    2 VVLITGCSSGIGLHLAVRLASDPSKRFKVYatmRDLKKKGrlwEAAGALA---GGTLETLQLDVCDSKSVAAAVERVTE- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 lGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAqlwieSGFKK---GSIVITSSMSseiynqeGLNK 161
Cdd:cd09806   78 -RHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFL-----PDMKRrgsGRILVTSSVG-------GLQG 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 388856966 162 PLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:cd09806  145 LPFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTA 187
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
11-124 4.78e-09

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: 54.41  E-value: 4.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966    11 TIVVTGGNRGIGLA---------------MSkavanaganvaifyRSHPKAQEAAAEVA--KEFGVQCRAYQCDVGDAEL 73
Cdd:smart00822   2 TYLITGGLGGLGRAlarwlaergarrlvlLS--------------RSGPDAPGAAALLAelEAAGARVTVVACDVADRDA 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 388856966    74 VKKTLKQAQDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFN 124
Cdd:smart00822  68 LAAVLAAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWN 118
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
6-122 5.43e-09

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: 55.17  E-value: 5.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEF-GVQcrAYQCDVGDAELVKKTLKQAQDE 84
Cdd:COG3967    2 KLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRR----EEKLEEAAAANpGLH--TIVLDVADPASIAALAEQVTAE 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 388856966  85 LGQVTGLLANAGV----SVVKPAVELtsDDFRYVYDTNVLGV 122
Cdd:COG3967   76 FPDLNVLINNAGImraeDLLDEAEDL--ADAEREITTNLLGP 115
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
65-206 5.78e-09

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: 55.36  E-value: 5.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  65 QCDVGDAELVKKTLKQAQDELGQvTGLLA---NAGVS-VVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfkK 140
Cdd:cd09805   54 QLDVTKPEQIKRAAQWVKEHVGE-KGLWGlvnNAGILgFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRA---K 129
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 388856966 141 GSIVITSSMSSEIYNQEGLNkpltqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQT 206
Cdd:cd09805  130 GRVVNVSSMGGRVPFPAGGA-------YCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGIT 188
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
9-204 1.92e-08

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: 54.01  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFG---VQCRayQCDVGDAELVKKTLKQAQDEL 85
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLnheVIVR--HLDLASLKSIRAFAAEFLAEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  86 GQVTGLLANAGvsVVKPAVELTSDDFRYVYDTNVLGVFnsakAVAQLWIESgFKKGS---IVITSSMSSEI--YNQEGLN 160
Cdd:cd09807   79 DRLDVLINNAG--VMRCPYSKTEDGFEMQFGVNHLGHF----LLTNLLLDL-LKKSApsrIVNVSSLAHKAgkINFDDLN 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 388856966 161 --KPLTQVF-YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:cd09807  152 seKSYNTGFaYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTE 198
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
10-148 2.12e-08

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: 54.06  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFY-RSHPKAQEAAAEVAKEFGvQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:cd09810    2 GTVVITGASSGLGLAAAKALARRGEWHVVMAcRDFLKAEQAAQEVGMPKD-SYSVLHCDLASLDSVRQFVDNFRRTGRPL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388856966  89 TGLLANAGVSVVK-PAVELTSDDFRYVYDTNVLGVFnsakAVAQLWIE----SGFKKGSIVITSS 148
Cdd:cd09810   81 DALVCNAAVYLPTaKEPRFTADGFELTVGVNHLGHF----LLTNLLLEdlqrSENASPRIVIVGS 141
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
12-210 3.39e-08

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: 52.20  E-value: 3.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAvanaganvaifyrshpkAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAqdelGQVTGL 91
Cdd:cd11731    1 IIVIGATGTIGLAVAQL-----------------LSAHGHEVITA-GRSSGDYQVDITDEASIKALFEKV----GHFDAI 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  92 LANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKaVAQLWIESGfkkGSIVITSSMSSEIYNQEGLNKPLTQvfynss 171
Cdd:cd11731   59 VSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVR-HGLPYLNDG---GSITLTSGILAQRPIPGGAAAATVN------ 128
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 388856966 172 kGAVTNLGKCLAAEWAQhGIRVNILEPGFCNTEQTSGMD 210
Cdd:cd11731  129 -GALEGFVRAAAIELPR-GIRINAVSPGVVEESLEAYGD 165
PRK09134 PRK09134
SDR family oxidoreductase;
14-257 3.52e-08

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 53.01  E-value: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  14 VTGGNRGIGLAMSKAVANAGANVAIFY-RSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGLL 92
Cdd:PRK09134  14 VTGAARRIGRAIALDLAAHGFDVAVHYnRSRDEAEALAAEIRAL-GRRAVALQADLADEAEVRALVARASAALGPITLLV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  93 ANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVitssmssEIYNQEGLNkpLTQVF--YNS 170
Cdd:PRK09134  93 NNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPAD--ARGLVV-------NMIDQRVWN--LNPDFlsYTL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 171 SKGAVTNLGKCLAAEWAQHgIRVNILEPG--FCNTEQTSGmdakirDF--QASSIPMGRFSEPHEQADpAVLLLSDKASy 246
Cdd:PRK09134 162 SKAALWTATRTLAQALAPR-IRVNAIGPGptLPSGRQSPE------DFarQHAATPLGRGSTPEEIAA-AVRYLLDAPS- 232
                        250
                 ....*....|.
gi 388856966 247 LTGSVIRPDGG 257
Cdd:PRK09134 233 VTGQMIAVDGG 243
PRK08219 PRK08219
SDR family oxidoreductase;
11-254 3.62e-08

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 52.63  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVaIFYRSHPKAQEAAAEVAKEfgvqcRAYQCDVGDAElvkkTLKQAQDELGQVTG 90
Cdd:PRK08219   5 TALITGASRGIGAAIARELAPTHTLL-LGGRPAERLDELAAELPGA-----TPFPVDLTDPE----AIAAAVEQLGRLDV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  91 LLANAGVSVVKPAVELTSDDFRYVYDTNVLGVfnsAKAVAQLWIESGFKKGSIVITSSMSseiynqeGLNKPLTQVFYNS 170
Cdd:PRK08219  75 LVHNAGVADLGPVAESTVDEWRATLEVNVVAP---AELTRLLLPALRAAHGHVVFINSGA-------GLRANPGWGSYAA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 171 SKGAVTNLGKCLAAEWAQHgIRVNILEPGFCNTEqtsgMDAKIRDFQASSIPMGRFSEPHEQADP--AVLLLSDKASyLT 248
Cdd:PRK08219 145 SKFALRALADALREEEPGN-VRVTSVHPGRTDTD----MQRGLVAQEGGEYDPERYLRPETVAKAvrFAVDAPPDAH-IT 218

                 ....*.
gi 388856966 249 GSVIRP 254
Cdd:PRK08219 219 EVVVRP 224
PRK05717 PRK05717
SDR family oxidoreductase;
1-259 3.95e-08

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 52.97  E-value: 3.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   1 MPFVIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIfyrsHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQ 80
Cdd:PRK05717   2 SEPNPGHNGRVALVTGAARGIGLGIAAWLIAEGWQVVL----ADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  81 AQDELGQVTGLLANAGVSVVK--PAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkkGSIV-ITSSMSSEiynqe 157
Cdd:PRK05717  78 VLGQFGRLDALVCNAAIADPHntTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN---GAIVnLASTRARQ----- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 158 glNKPLTQVfYNSSKGAVTNLGKCLAAEWAQHgIRVNILEPGFCNTEQTSGMDAK-IRDFQASSIPMGRFSEPHEQADPA 236
Cdd:PRK05717 150 --SEPDTEA-YAASKGGLLALTHALAISLGPE-IRVNAVSPGWIDARDPSQRRAEpLSEADHAQHPAGRVGTVEDVAAMV 225
                        250       260
                 ....*....|....*....|...
gi 388856966 237 VLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK05717 226 AWLLSRQAGFVTGQEFVVDGGMT 248
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
71-258 5.22e-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: 52.19  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  71 AELVKKTLKQAqdelGQVTGLLANAGVSVVKPAVELTSD-DFRYVYDTNVLGVFNSAKA-VAQLWIESGfkkGSIV-ITS 147
Cdd:cd05361   60 EELVDAVLQAG----GAIDVLVSNDYIPRPMNPIDGTSEaDIRQAFEALSIFPFALLQAaIAQMKKAGG---GSIIfITS 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 148 SMsseiynqeGLNKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQ---TSGMDA--KIRDFQASSIP 222
Cdd:cd05361  133 AV--------PKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSPTyfpTSDWENnpELRERVKRDVP 204
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 388856966 223 MGRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGGF 258
Cdd:cd05361  205 LGRLGRPDEMGALVAFLASRRADPITGQFFAFAGGY 240
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
5-260 5.49e-08

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 52.41  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTG--GNRGIGLAMSKAVANAGANVAIFY------RSHPKAQEAAAEVAKEFGVQCrayqcDVGDAELVKK 76
Cdd:PRK07370   2 LDLTGKKALVTGiaNNRSIAWGIAQQLHAAGAELGITYlpdekgRFEKKVRELTEPLNPSLFLPC-----DVQDDAQIEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  77 TLKQAQDELGQVTGL---LANAGVS-VVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIEsgfkKGSIVITSSMSSE 152
Cdd:PRK07370  77 TFETIKQKWGKLDILvhcLAFAGKEeLIGDFSATSREGFARALEISAYSLAPLCKAAKPLMSE----GGSIVTLTYLGGV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 153 I----YNQEGLnkpltqvfynsSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTS---GMDAKIRDFQASSiPMGR 225
Cdd:PRK07370 153 RaipnYNVMGV-----------AKAALEASVRYLAAELGPKNIRVNAISAGPIRTLASSavgGILDMIHHVEEKA-PLRR 220
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 388856966 226 FSEPHEQADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK07370 221 TVTQTEVGNTAAFLLSDLASGITGQTIYVDAGYCI 255
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
9-258 8.15e-08

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: 51.83  E-value: 8.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQ-CRAYQCDVGDAELVKKTLKQAQDELGQ 87
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQnIFLHIVDMSDPKQVWEFVEEFKEEGKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSVVKPavELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfkKGSIVITSSmSSEIYNQEGLNKPL---- 163
Cdd:cd09808   81 LHVLINNAGCMVNKR--ELTEDGLEKNFATNTLGTYILTTHLIPVLEKE---EDPRVITVS-SGGMLVQKLNTNNLqser 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 164 -----TQVFYNSSKGAVTnlgkcLAAEWAQH--GIRVNILEPGFCNteqTSGMDAKIRDFQASsipMG-RFSEPHEQADP 235
Cdd:cd09808  155 tafdgTMVYAQNKRQQVI-----MTEQWAKKhpEIHFSVMHPGWAD---TPAVRNSMPDFHAR---FKdRLRSEEQGADT 223
                        250       260
                 ....*....|....*....|...
gi 388856966 236 AVLLLSDKAsyltgSVIRPDGGF 258
Cdd:cd09808  224 VVWLALSSA-----AAKAPSGRF 241
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
12-208 8.66e-08

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 52.00  E-value: 8.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGANVAIFY-----RSHPKAQEAAAEVAKEF---GVQCRAYQCDVGDAELVKKTLKQAQD 83
Cdd:cd08941    4 VLVTGANSGLGLAICERLLAEDDENPELTlilacRNLQRAEAACRALLASHpdaRVVFDYVLVDLSNMVSVFAAAKELKK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAG---------------------------------VSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVA 130
Cdd:cd08941   84 RYPRLDYLYLNAGimpnpgidwigaikevltnplfavtnptykiqaEGLLSQGDKATEDGLGEVFQTNVFGHYYLIRELE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 131 QLWIESGfKKGSIVITSSMSSE--IYNQEGLNKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSG 208
Cdd:cd08941  164 PLLCRSD-GGSQIIWTSSLNASpkYFSLEDIQHLKGPAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTTNLTYG 242
PRK07775 PRK07775
SDR family oxidoreductase;
13-199 1.16e-07

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 51.68  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  13 VVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGvQCRAYQCDVGDAELVKKTLKQAQDELGQVTGLL 92
Cdd:PRK07775  14 LVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGG-EAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  93 ANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMSSEiynqegLNKPLTQVfYNSSK 172
Cdd:PRK07775  93 SGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIER--RRGDLIFVGSDVAL------RQRPHMGA-YGAAK 163
                        170       180
                 ....*....|....*....|....*..
gi 388856966 173 GAVTNLGKCLAAEWAQHGIRVNILEPG 199
Cdd:PRK07775 164 AGLEAMVTNLQMELEGTGVRASIVHPG 190
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
7-212 1.99e-07

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 50.64  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDV--GDAELVKKTLKQAQDE 84
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLDLltATPQNYQQLADTIEEQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGV-SVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSMsseiYNQEGlnkpl 163
Cdd:PRK08945  90 FGRLDGVLHNAGLlGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKS--PAASLVFTSSS----VGRQG----- 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 388856966 164 tQVF---YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTeqtsGMDAK 212
Cdd:PRK08945 159 -RANwgaYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRT----AMRAS 205
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-198 3.26e-07

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 50.55  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIG----LAMSKAVANAGANVaifYRSHPKAQEAAAEVAKEfGVQCRAYQCDVGDAELVKKTLKQA 81
Cdd:PRK07792   9 DLSGKVAVVTGAAAGLGraeaLGLARLGATVVVND---VASALDASDVLDEIRAA-GAKAVAVAGDISQRATADELVATA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  82 qDELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLW-----IESGFKKGSIVITSSmsseiynQ 156
Cdd:PRK07792  85 -VGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWrakakAAGGPVYGRIVNTSS-------E 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 388856966 157 EGLNKPLTQVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEP 198
Cdd:PRK07792 157 AGLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK07806 PRK07806
SDR family oxidoreductase;
6-95 5.87e-07

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 49.33  E-value: 5.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   6 DLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDEL 85
Cdd:PRK07806   3 DLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEF 82
                         90
                 ....*....|
gi 388856966  86 GQVTGLLANA 95
Cdd:PRK07806  83 GGLDALVLNA 92
PRK05693 PRK05693
SDR family oxidoreductase;
11-199 6.08e-07

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 49.40  E-value: 6.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVaifYRSHPKAQEAAAEVAKEFgvqcRAYQCDVGDAELVKKTLKQAQDELGQVTG 90
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEV---WATARKAEDVEALAAAGF----TAVQLDVNDGAALARLAEELEAEHGGLDV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  91 LLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfkKGSIVITSSMSSEiynqegLNKPLTQVfYNS 170
Cdd:PRK05693  76 LINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRS---RGLVVNIGSVSGV------LVTPFAGA-YCA 145
                        170       180
                 ....*....|....*....|....*....
gi 388856966 171 SKGAVTNLGKCLAAEWAQHGIRVNILEPG 199
Cdd:PRK05693 146 SKAAVHALSDALRLELAPFGVQVMEVQPG 174
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
9-199 3.42e-06

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 47.21  E-value: 3.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   9 GQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFG-VQCRAYQCDVGDAELVKKTLKQAQDELGQ 87
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWHkARVEAMTLDLASLRSVQRFAEAFKAKNSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  88 VTGLLANAGVSVVkpAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMS---SEIYNQEG------ 158
Cdd:cd09809   81 LHVLVCNAAVFAL--PWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSA--PARVIVVSSEShrfTDLPDSCGnldfsl 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 388856966 159 LNKPLTQVF----YNSSKGAVTNLGKCLAAEWAQHGIRVNILEPG 199
Cdd:cd09809  157 LSPPKKKYWsmlaYNRAKLCNILFSNELHRRLSPRGITSNSLHPG 201
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
7-108 5.99e-06

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: 46.28  E-value: 5.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRS---HPKAQ----EAAAEVaKEFGVQCRAYQCDVGDAELVKKTLK 79
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTaepHPKLPgtiyTAAEEI-EAAGGKALPCIVDIRDEDQVRAAVE 79
                         90       100
                 ....*....|....*....|....*....
gi 388856966  80 QAQDELGQVTGLLANAGvsvvkpAVELTS 108
Cdd:cd09762   80 KAVEKFGGIDILVNNAS------AISLTG 102
PRK06139 PRK06139
SDR family oxidoreductase;
7-203 7.09e-06

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 46.25  E-value: 7.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKE---FGVQCRAYQCDVGDAELVKKTLKQAQD 83
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARLVLAARD----EEALQAVAEEcraLGAEVLVVPTDVTDADQVKALATQAAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIynqeglnkpl 163
Cdd:PRK06139  81 FGGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQG--HGIFINMISLGGFA---------- 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 388856966 164 TQVF---YNSSKGAVTNLGKCLAAEWAQH-GIRVNILEPGFCNT 203
Cdd:PRK06139 149 AQPYaaaYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDT 192
PRK07024 PRK07024
SDR family oxidoreductase;
10-206 1.00e-05

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 45.69  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKefGVQCRAYQCDVGDAELVKKTlkqAQDELGQVT 89
Cdd:PRK07024   3 LKVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPK--AARVSVYAADVRDADALAAA---AADFIAAHG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 G---LLANAGVSVVKpaveLTS-----DDFRYVYDTNVLGVFNS-----AKAVAQlwiesgfKKGSIVITSSMSSeiynQ 156
Cdd:PRK07024  78 LpdvVIANAGISVGT----LTEeredlAVFREVMDTNYFGMVATfqpfiAPMRAA-------RRGTLVGIASVAG----V 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 388856966 157 EGLnkPLTQVfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQT 206
Cdd:PRK07024 143 RGL--PGAGA-YSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMT 189
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
182-260 1.11e-05

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 45.31  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 182 LAAEWAQHGIRVNILEPGFCNTEQTSGM---DAKIRDFQASSiPMGRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGGF 258
Cdd:PRK07533 176 LAAELGPKGIRVHAISPGPLKTRAASGIddfDALLEDAAERA-PLRRLVDIDDVGAVAAFLASDAARRLTGNTLYIDGGY 254

                 ..
gi 388856966 259 TI 260
Cdd:PRK07533 255 HI 256
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
11-151 1.25e-05

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: 45.84  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAvanaganvaiFYRSH----------PKAQEAAAEVAKE--FGVQCRAYQCDVGDAELVKKTL 78
Cdd:cd05274  152 TYLITGGLGGLGLLVARW----------LAARGarhlvllsrrGPAPRAAARAALLraGGARVSVVRCDVTDPAALAALL 221
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 388856966  79 KQAQdELGQVTGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNsakaVAQLWIESGFKkgSIVITSSMSS 151
Cdd:cd05274  222 AELA-AGGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALN----LHELTPDLPLD--FFVLFSSVAA 287
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
65-257 1.76e-05

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 44.71  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  65 QCDVGDAELVKKTLKQAQDELGQVTGLLanAGVSVVKPAvELTSDdfryVYDTNVLGvFNSAK--------AVAQLWIES 136
Cdd:PRK06079  61 ECDVASDESIERAFATIKERVGKIDGIV--HAIAYAKKE-ELGGN----VTDTSRDG-YALAQdisaysliAVAKYARPL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 137 GFKKGSIVITSSMSSEI----YNQEGLnkpltqvfynsSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTEQTSGM--- 209
Cdd:PRK06079 133 LNPGASIVTLTYFGSERaipnYNVMGI-----------AKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAVTGIkgh 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 388856966 210 -------DAKIRDFQASSIpmgrfsepHEQADPAVLLLSDKASYLTGSVIRPDGG 257
Cdd:PRK06079 202 kdllkesDSRTVDGVGVTI--------EEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
PRK06101 PRK06101
SDR family oxidoreductase;
114-206 1.85e-05

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 44.86  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 114 VYDTNVLGVFNSAKAVaQLWIESGFKkgsIVITSSMSSEiynqegLNKPLTQVfYNSSKGAVTNLGKCLAAEWAQHGIRV 193
Cdd:PRK06101  98 VFNVNVLGVANCIEGI-QPHLSCGHR---VVIVGSIASE------LALPRAEA-YGASKAAVAYFARTLQLDLRPKGIEV 166
                         90
                 ....*....|...
gi 388856966 194 NILEPGFCNTEQT 206
Cdd:PRK06101 167 VTVFPGFVATPLT 179
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
11-124 2.91e-05

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (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 oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses 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-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses 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 the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 44.58  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIFY-RSHPKAQEAAAEVAKE-FGVQCRAYQCDVGDAELVKKTLKQAQDELGQV 88
Cdd:cd08955  151 TYLITGGLGGLGLLVAEWLVERGARHLVLTgRRAPSAAARQAIAALEeAGAEVVVLAADVSDRDALAAALAQIRASLPPL 230
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 388856966  89 TGLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFN 124
Cdd:cd08955  231 RGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWN 266
PRK08703 PRK08703
SDR family oxidoreductase;
7-205 3.01e-05

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 44.15  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDV---GDAELVKKTLKQAQD 83
Cdd:PRK08703   4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAIRFDLmsaEEKEFEQFAATIAEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  84 ELGQVTGLLANAG-VSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIVITSSmsseiynQEGLNKP 162
Cdd:PRK08703  84 TQGKLDGIVHCAGyFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQS--PDASVIFVGE-------SHGETPK 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 388856966 163 LTQVFYNSSKGAVTNLGKCLAAEWAQHG-IRVNILEPGFCNTEQ 205
Cdd:PRK08703 155 AYWGGFGASKAALNYLCKVAADEWERFGnLRANVLVPGPINSPQ 198
PRK06196 PRK06196
oxidoreductase; Provisional
5-133 3.59e-05

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 44.29  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAK-EFGvqcrayQCDVGDAELVKKTLKQAQD 83
Cdd:PRK06196  22 HDLSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDGvEVV------MLDLADLESVRAFAERFLD 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 388856966  84 ELGQVTGLLANAGVSvvkpAVELT--SDDFRYVYDTNVLGVFnsaKAVAQLW 133
Cdd:PRK06196  96 SGRRIDILINNAGVM----ACPETrvGDGWEAQFATNHLGHF---ALVNLLW 140
PRK07984 PRK07984
enoyl-ACP reductase FabI;
7-260 3.59e-05

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 44.12  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTG--GNRGIGLAMSKAVANAGANVAIFYRSHpKAQEAAAEVAKEFGVQCrAYQCDVGDAELVKKTLKQAQDE 84
Cdd:PRK07984   4 LSGKRILVTGvaSKLSIAYGIAQAMHREGAELAFTYQND-KLKGRVEEFAAQLGSDI-VLPCDVAEDASIDAMFAELGKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  85 LGQVTGLLANAGVSvvkPAVEL--------TSDDFRYVYDTNVLGVFNSAKAVAQLwiesgFKKGSIVIT-SSMSSEI-- 153
Cdd:PRK07984  82 WPKFDGFVHSIGFA---PGDQLdgdyvnavTREGFKIAHDISSYSFVAMAKACRSM-----LNPGSALLTlSYLGAERai 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 154 --YNQEGLNKPltqvfynSSKGAVTNLGKCLAAEwaqhGIRVNILEPGFCNTEQTSGmdakIRDFQA------SSIPMGR 225
Cdd:PRK07984 154 pnYNVMGLAKA-------SLEANVRYMANAMGPE----GVRVNAISAGPIRTLAASG----IKDFRKmlahceAVTPIRR 218
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 388856966 226 FSEPHEQADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK07984 219 TVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSI 253
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
53-260 6.06e-05

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 43.19  E-value: 6.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  53 VAKEFGVQcRAYQCDVGDAELVKKTLKQAQDELGQVTgLLANAGVSVVKPA-----VELTSDDFRYVYDTNVLGVFNSAK 127
Cdd:PRK08415  50 IAQELGSD-YVYELDVSKPEHFKSLAESLKKDLGKID-FIVHSVAFAPKEAlegsfLETSKEAFNIAMEISVYSLIELTR 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 128 AVAQLwiesgFKKGSIVITSSMSSEI-----YNQEGLnkpltqvfynsSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCN 202
Cdd:PRK08415 128 ALLPL-----LNDGASVLTLSYLGGVkyvphYNVMGV-----------AKAALESSVRYLAVDLGKKGIRVNAISAGPIK 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388856966 203 TEQTSGmdakIRDFQ------ASSIPMGRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK08415 192 TLAASG----IGDFRmilkwnEINAPLKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVDAGYNI 251
PRK06197 PRK06197
short chain dehydrogenase; Provisional
4-123 8.83e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 43.09  E-value: 8.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   4 VIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEF-----GVQcrayQCDVGDAELVKKTL 78
Cdd:PRK06197  11 IPDQSGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATpgadvTLQ----ELDLTSLASVRAAA 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 388856966  79 KQAQDELGQVTGLLANAGVSVvkPAVELTSDDFRYVYDTNVLGVF 123
Cdd:PRK06197  87 DALRAAYPRIDLLINNAGVMY--TPKQTTADGFELQFGTNHLGHF 129
PRK07832 PRK07832
SDR family oxidoreductase;
13-203 8.87e-05

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 42.72  E-value: 8.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  13 VVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGLL 92
Cdd:PRK07832   4 FVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRALDISDYDAVAAFAADIHAAHGSMDVVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  93 ANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfKKGSIVITSSMSseiynqeGLNKPLTQVFYNSSK 172
Cdd:PRK07832  84 NIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAG-RGGHLVNVSSAA-------GLVALPWHAAYSASK 155
                        170       180       190
                 ....*....|....*....|....*....|.
gi 388856966 173 GAVTNLGKCLAAEWAQHGIRVNILEPGFCNT 203
Cdd:PRK07832 156 FGLRGLSEVLRFDLARHGIGVSVVVPGAVKT 186
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
12-215 1.57e-04

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 41.98  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfgvQCRAYQCDVGDAELVKKTLKQA-----QDELG 86
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYNS---NLTFHSLDLQDVHELETNFNEIlssiqEDNVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  87 QVTgLLANAG-VSVVKPAVELTSDDFRYVYDTNVLgvfnsakavAQLWIESGFKK--------GSIVITSSMSSEiynqe 157
Cdd:PRK06924  81 SIH-LINNAGmVAPIKPIEKAESEELITNVHLNLL---------APMILTSTFMKhtkdwkvdKRVINISSGAAK----- 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388856966 158 glnKPL-TQVFYNSSKGAVTNLGKCLAAEWA--QHGIRVNILEPGFCNTEqtsgMDAKIRD 215
Cdd:PRK06924 146 ---NPYfGWSAYCSSKAGLDMFTQTVATEQEeeEYPVKIVAFSPGVMDTN----MQAQIRS 199
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
41-260 1.91e-04

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 41.66  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  41 RSHPKAQEAAAEVAKEfgvqcrayqCDVGDAELVKKTLKQAQDELGQVTGLLANAGVS----VVKPAVELTSDDFRYVYD 116
Cdd:PRK08159  51 RVEPLAAELGAFVAGH---------CDVTDEASIDAVFETLEKKWGKLDFVVHAIGFSdkdeLTGRYVDTSRDNFTMTMD 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 117 TNVLgvfnSAKAVAQLWIESGFKKGSIVITSSMSSEI----YNQEGLnkpltqvfynsSKGAVTNLGKCLAAEWAQHGIR 192
Cdd:PRK08159 122 ISVY----SFTAVAQRAEKLMTDGGSILTLTYYGAEKvmphYNVMGV-----------AKAALEASVKYLAVDLGPKNIR 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388856966 193 VNILEPGFCNTEQTSGmdakIRDFQ------ASSIPMGRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGGFTI 260
Cdd:PRK08159 187 VNAISAGPIKTLAASG----IGDFRyilkwnEYNAPLRRTVTIEEVGDSALYLLSDLSRGVTGEVHHVDSGYHV 256
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
7-194 2.17e-04

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 42.21  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   7 LKGQTIVVTGGNRGIGLAMSKAVAnaganvaifyrshpkAQ-----------EAAAEVAKEFGvqcRAYQCDVGDAELVK 75
Cdd:COG3347  423 LAGRVALVTGGAGGIGRATAARLA---------------AEgaavvvadldgEAAEAAAAELG---GGYGADAVDATDVD 484
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  76 KTLKQAQDELGQVTGLL--------ANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGFKKGSIVITS 147
Cdd:COG3347  485 VTAEAAVAAAFGFAGLDiggsdigvANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSVFAVS 564
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 388856966 148 SMSseiynqeglnkpltqVFYNSSKGAVTN-------LGKCLAAEWAQHGIRVN 194
Cdd:COG3347  565 KNA---------------AAAAYGAAAAATakaaaqhLLRALAAEGGANGINAN 603
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
182-260 3.04e-04

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 41.27  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 182 LAAEWAQHGIRVNILEPGFCNTEQTSGM-DAK-IRDFQASSIPMGRFSEPHEQADPAVLLLSDKASYLTGSVIRPDGGFT 259
Cdd:PRK06505 173 LAADYGPQGIRVNAISAGPVRTLAGAGIgDARaIFSYQQRNSPLRRTVTIDEVGGSALYLLSDLSSGVTGEIHFVDSGYN 252

                 .
gi 388856966 260 I 260
Cdd:PRK06505 253 I 253
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
14-203 4.68e-04

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: 40.20  E-value: 4.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  14 VTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKefgvqcRAYQCDVGDAELVKKtlkqAQDELGQVTGLLA 93
Cdd:cd11730    3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGA------LARPADVAAELEVWA----LAQELGPLDLLVY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  94 NAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAK-AVAQLwiesgfKKGSIVITSSMSSEIYNQEGLNKpltqvfYNSSK 172
Cdd:cd11730   73 AAGAILGKPLARTKPAAWRRILDANLTGAALVLKhALALL------AAGARLVFLGAYPELVMLPGLSA------YAAAK 140
                        170       180       190
                 ....*....|....*....|....*....|.
gi 388856966 173 GAVTNLGKCLAAEWaqHGIRVNILEPGFCNT 203
Cdd:cd11730  141 AALEAYVEVARKEV--RGLRLTLVRPPAVDT 169
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
94-200 5.19e-04

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: 39.81  E-value: 5.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  94 NAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSSEIYNqeGLNKPltqvfYNSSKG 173
Cdd:cd02266   38 NAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKR--LGRFILISSVAGLFGA--PGLGG-----YAASKA 108
                         90       100
                 ....*....|....*....|....*..
gi 388856966 174 AVTNLGKCLAAEWAQHGIRVNILEPGF 200
Cdd:cd02266  109 ALDGLAQQWASEGWGNGLPATAVACGT 135
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
12-199 6.44e-04

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 40.13  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGANVAIFYRShpkaQEAAAEVAKEFGVQCRAYQCDVGDAELVKKTLKQAQDELGQVTGL 91
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRR----QERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  92 LANAGVSV-VKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESgfKKGSIV-ITSSMSSEIYnqEGLNkpltqvFYN 169
Cdd:PRK10538  79 VNNAGLALgLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVER--NHGHIInIGSTAGSWPY--AGGN------VYG 148
                        170       180       190
                 ....*....|....*....|....*....|
gi 388856966 170 SSKGAVTNLGKCLAAEWAQHGIRVNILEPG 199
Cdd:PRK10538 149 ATKAFVRQFSLNLRTDLHGTAVRVTDIEPG 178
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
11-201 9.68e-04

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 39.96  E-value: 9.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFgvqcraYQCDVGDAELVKKTLKqaqdelgQVTG 90
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEF------VRGDLRDPEALAAALA-------GVDA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  91 LLANAGVSVVkpavelTSDDFRYVYDTNVLGVFNsakaVAQLWIESGFKKgsIVITSSMS-----SEIYNQEGLNKPLTq 165
Cdd:COG0451   68 VVHLAAPAGV------GEEDPDETLEVNVEGTLN----LLEAARAAGVKR--FVYASSSSvygdgEGPIDEDTPLRPVS- 134
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 388856966 166 vFYNSSKGAVTNLgkcLAAEWAQHGIRVNILEPGFC 201
Cdd:COG0451  135 -PYGASKLAAELL---ARAYARRYGLPVTILRPGNV 166
PRK05854 PRK05854
SDR family oxidoreductase;
4-123 1.31e-03

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 39.28  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   4 VIDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEfgvqcrayqcdVGDAELVKKTLK---- 79
Cdd:PRK05854   9 VPDLSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTA-----------VPDAKLSLRALDlssl 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 388856966  80 QAQDELGQ--------VTGLLANAGVsVVKPAVELTSDDFRYVYDTNVLGVF 123
Cdd:PRK05854  78 ASVAALGEqlraegrpIHLLINNAGV-MTPPERQTTADGFELQFGTNHLGHF 128
PRK08017 PRK08017
SDR family oxidoreductase;
10-199 1.60e-03

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 38.91  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  10 QTIVVTGGNRGIGLAMSKAVANAGanvaifYRSHpKAQEAAAEVAKEFGVQCRAYQCDVGDAELVKktlkQAQDELGQVT 89
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRG------YRVL-AACRKPDDVARMNSLGFTGILLDLDDPESVE----RAADEVIALT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 -----GLLANAGVSVVKPAVELTSDDFRYVYDTNVLGVFNSAKAVAQLWIESGfkKGSIVITSSMSseiynqeGLNKPLT 164
Cdd:PRK08017  72 dnrlyGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHG--EGRIVMTSSVM-------GLISTPG 142
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 388856966 165 QVFYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPG 199
Cdd:PRK08017 143 RGAYAASKYALEAWSDALRMELRHSGIKVSLIEPG 177
PRK09072 PRK09072
SDR family oxidoreductase;
5-98 1.91e-03

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 38.77  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966   5 IDLKGQTIVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAkeFGVQCRAYQCDVGDAELVKKTLKQAQdE 84
Cdd:PRK09072   1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLP--YPGRHRWVVADLTSEAGREAVLARAR-E 77
                         90
                 ....*....|....
gi 388856966  85 LGQVTGLLANAGVS 98
Cdd:PRK09072  78 MGGINVLINNAGVN 91
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
171-258 2.64e-03

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 38.38  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966 171 SKGAVTNLGKCLAAEWAQHGIRVNILEPGfcnteqtsgmdaKIRDFQASSIP-MGRFSEPHEQADP-------------- 235
Cdd:PRK07889 161 AKAALESTNRYLARDLGPRGIRVNLVAAG------------PIRTLAAKAIPgFELLEEGWDERAPlgwdvkdptpvara 228
                         90       100
                 ....*....|....*....|...
gi 388856966 236 AVLLLSDKASYLTGSVIRPDGGF 258
Cdd:PRK07889 229 VVALLSDWFPATTGEIVHVDGGA 251
PRK08177 PRK08177
SDR family oxidoreductase;
11-204 3.56e-03

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 37.70  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  11 TIVVTGGNRGIGLAMSKAVANAGANVAIFYRShPKAQEAAAEVAkefgvQCRAYQCDVGDAELVKKTLKQAQdelGQVTG 90
Cdd:PRK08177   3 TALIIGASRGLGLGLVDRLLERGWQVTATVRG-PQQDTALQALP-----GVHIEKLDMNDPASLDQLLQRLQ---GQRFD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  91 LL-ANAGVS--VVKPAVELTSDDFRYVYDTNVLGVFNSAKA-VAQLwiesgfKKGSIVItSSMSSEIYNQE---GLNKPL 163
Cdd:PRK08177  74 LLfVNAGISgpAHQSAADATAAEIGQLFLTNAIAPIRLARRlLGQV------RPGQGVL-AFMSSQLGSVElpdGGEMPL 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 388856966 164 tqvfYNSSKGAVTNLGKCLAAEWAQHGIRVNILEPGFCNTE 204
Cdd:PRK08177 147 ----YKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTD 183
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
12-203 9.00e-03

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: 36.70  E-value: 9.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  12 IVVTGGNRGIGLAMSKAVANAGANVAIFYRSHPKAQEAAAEVAKEFGVQcrayqcdVGDAELVKKTLKQAQD--ELGQVT 89
Cdd:cd08951   10 IFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVL-------IGDLSSLAETRKLADQvnAIGRFD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856966  90 GLLANAGVsvvkpavelTSDDFRYVYDTNVLGVFNS---AKAVAQLWIESgfKKGSIVITSSMsseiynQEGLNKPLTQV 166
Cdd:cd08951   83 AVIHNAGI---------LSGPNRKTPDTGIPAMVAVnvlAPYVLTALIRR--PKRLIYLSSGM------HRGGNASLDDI 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 388856966 167 F-----------YNSSKGAVTNLGKCLAAEWAQhgIRVNILEPGFCNT 203
Cdd:cd08951  146 DwfnrgendspaYSDSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPT 191
 
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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