NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1444445608|ref|XP_025884593|]
View 

secoisolariciresinol dehydrogenase-like [Solanum lycopersicum]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 17-119 1.41e-23

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 cd05326:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 249  Bit Score: 91.75  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMATESYIDLPHTYKASKNALW-------TQLREK------------AKKWF 77
Cdd:cd05326   112 NVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLgltrsaaTELGEHgirvncvspygvATPLL 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1444445608  78 GDG---------------GNLEGVLLHEQDVENGVLYLASDDSKYVSGLNFIIHGGF 119
Cdd:cd05326   192 TAGfgvedeaieeavrgaANLKGTALRPEDIAAAVLYLASDDSRYVSGQNLVVDGGL 248
 
Name Accession Description Interval E-value
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 17-119 1.41e-23

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: 91.75  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMATESYIDLPHTYKASKNALW-------TQLREK------------AKKWF 77
Cdd:cd05326   112 NVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLgltrsaaTELGEHgirvncvspygvATPLL 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1444445608  78 GDG---------------GNLEGVLLHEQDVENGVLYLASDDSKYVSGLNFIIHGGF 119
Cdd:cd05326   192 TAGfgvedeaieeavrgaANLKGTALRPEDIAAAVLYLASDDSRYVSGQNLVVDGGL 248
PLN02253 PLN02253
xanthoxin dehydrogenase
 17-126 7.57e-23

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 90.27  E-value: 7.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMATESYIDLPHTYKASKNALWTQLREKA----------------------- 73
Cdd:PLN02253  127 NVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSKHAVLGLTRSVAaelgkhgirvncvspyavptala 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  74 -----------------KKWFGDGGNLEGVLLHEQDVENGVLYLASDDSKYVSGLNFIIHGGFRTTNVAL 126
Cdd:PLN02253  207 lahlpedertedalagfRAFAGKNANLKGVELTVDDVANAVLFLASDEARYISGLNLMIDGGFTCTNHSL 276
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 17-120 5.24e-11

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: 58.26  E-value: 5.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMAT-ESYIDLPHtYKASKNALWTQLREKAKKWFGDG-------------GN 82
Cdd:COG1028   114 NLKGPFLLTRAALPHMRERGGGRIVNISSIAGlRGSPGQAA-YAASKAAVVGLTRSLALELAPRGirvnavapgpidtPM 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1444445608  83 LEGVLLHEQDVE------------------NGVLYLASDDSKYVSGLNFIIHGGFR 120
Cdd:COG1028   193 TRALLGAEEVREalaariplgrlgtpeevaAAVLFLASDAASYITGQVLAVDGGLT 248
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 17-119 1.20e-06

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: 45.88  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMipANKGVIIFTASMATESYIDLPHTYKASKNAL--WT-----QLREK---------------AK 74
Cdd:pfam13561 104 NLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALeaLTrylavELGPRgirvnaispgpiktlAA 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1444445608  75 KWFGDGGNLEGVLLHE---------QDVENGVLYLASDDSKYVSGLNFIIHGGF 119
Cdd:pfam13561 182 SGIPGFDELLAAAEARaplgrlgtpEEVANAAAFLASDLASYITGQVLYVDGGY 235
 
Name Accession Description Interval E-value
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 17-119 1.41e-23

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: 91.75  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMATESYIDLPHTYKASKNALW-------TQLREK------------AKKWF 77
Cdd:cd05326   112 NVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLgltrsaaTELGEHgirvncvspygvATPLL 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1444445608  78 GDG---------------GNLEGVLLHEQDVENGVLYLASDDSKYVSGLNFIIHGGF 119
Cdd:cd05326   192 TAGfgvedeaieeavrgaANLKGTALRPEDIAAAVLYLASDDSRYVSGQNLVVDGGL 248
PLN02253 PLN02253
xanthoxin dehydrogenase
 17-126 7.57e-23

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 90.27  E-value: 7.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMATESYIDLPHTYKASKNALWTQLREKA----------------------- 73
Cdd:PLN02253  127 NVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSKHAVLGLTRSVAaelgkhgirvncvspyavptala 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  74 -----------------KKWFGDGGNLEGVLLHEQDVENGVLYLASDDSKYVSGLNFIIHGGFRTTNVAL 126
Cdd:PLN02253  207 lahlpedertedalagfRAFAGKNANLKGVELTVDDVANAVLFLASDEARYISGLNLMIDGGFTCTNHSL 276
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 17-120 5.24e-11

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: 58.26  E-value: 5.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMAT-ESYIDLPHtYKASKNALWTQLREKAKKWFGDG-------------GN 82
Cdd:COG1028   114 NLKGPFLLTRAALPHMRERGGGRIVNISSIAGlRGSPGQAA-YAASKAAVVGLTRSLALELAPRGirvnavapgpidtPM 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1444445608  83 LEGVLLHEQDVE------------------NGVLYLASDDSKYVSGLNFIIHGGFR 120
Cdd:COG1028   193 TRALLGAEEVREalaariplgrlgtpeevaAAVLFLASDAASYITGQVLAVDGGLT 248
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 17-118 4.62e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 49.94  E-value: 4.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARV-MIPANKGVIIFTASMA--TESYIDLPHT--YKASKNALWTQLREKAKKW--------------- 76
Cdd:PRK08213  120 NVRGLFLLSQAVAKRsMIPRGYGRIINVASVAglGGNPPEVMDTiaYNTSKGAVINFTRALAAEWgphgirvnaiapgff 199

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444445608  77 ------------------------FGDGGNLEGVllheqdvengVLYLASDDSKYVSGLNFIIHGG 118
Cdd:PRK08213  200 ptkmtrgtlerlgedllahtplgrLGDDEDLKGA----------ALLLASDASKHITGQILAVDGG 255
FabG-like PRK07231
SDR family oxidoreductase;
17-118 4.69e-08

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 49.83  E-value: 4.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMATESYIDLPHTYKASKNALWTQLREKAKKW-------------FGDGGNL 83
Cdd:PRK07231  113 NVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLTKALAAELgpdkirvnavapvVVETGLL 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1444445608  84 E--------------------GVLLHEQDVENGVLYLASDDSKYVSGLNFIIHGG 118
Cdd:PRK07231  193 EafmgeptpenrakflatiplGRLGTPEDIANAALFLASDEASWITGVTLVVDGG 247
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 17-119 4.15e-07

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: 47.33  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMAteSYI-DLPHT---YKASKNALWTQLREKAKKWFGDGGNLEGVL----- 87
Cdd:cd05352   117 NLNGVFNCAQAAAKIFKKQGKGSLIITASMS--GTIvNRPQPqaaYNASKAAVIHLAKSLAVEWAKYFIRVNSISpgyid 194

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1444445608  88 ----------LHE--------------QDVENGVLYLASDDSKYVSGLNFIIHGGF 119
Cdd:cd05352   195 tdltdfvdkeLRKkwesyiplkrialpEELVGAYLYLASDASSYTTGSDLIIDGGY 250
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 7-120 5.28e-07

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: 46.99  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608   7 FLVLYQIphnNVVGGFFFAKHAARVMIPAN-KGVIIFTASMA-TESYIDLPHtYKASKNAL--WTQ-------------- 68
Cdd:cd05366   104 LKKVYAV---NVFGVLFGIQAAARQFKKLGhGGKIINASSIAgVQGFPNLGA-YSASKFAVrgLTQtaaqelapkgitvn 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444445608  69 -----------LREKAKKWFGDGGNLEGVLLHE-------------QDVENGVLYLASDDSKYVSGLNFIIHGGFR 120
Cdd:cd05366   180 ayapgivktemWDYIDEEVGEIAGKPEGEGFAEfsssiplgrlsepEDVAGLVSFLASEDSDYITGQTILVDGGMV 255
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 17-119 1.20e-06

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: 45.88  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMipANKGVIIFTASMATESYIDLPHTYKASKNAL--WT-----QLREK---------------AK 74
Cdd:pfam13561 104 NLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALeaLTrylavELGPRgirvnaispgpiktlAA 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1444445608  75 KWFGDGGNLEGVLLHE---------QDVENGVLYLASDDSKYVSGLNFIIHGGF 119
Cdd:pfam13561 182 SGIPGFDELLAAAEARaplgrlgtpEEVANAAAFLASDLASYITGQVLYVDGGY 235
PRK07069 PRK07069
short chain dehydrogenase; Validated
 17-118 1.70e-06

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 45.47  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMAteSYIDLPH--TYKASKNALW---------------------------- 66
Cdd:PRK07069  110 NVESIFLGCKHALPYLRASQPASIVNISSVA--AFKAEPDytAYNASKAAVAsltksialdcarrgldvrcnsihptfir 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  67 TQLREKAKKWFGDGGNLE--------GVLLHEQDVENGVLYLASDDSKYVSGLNFIIHGG 118
Cdd:PRK07069  188 TGIVDPIFQRLGEEEATRklargvplGRLGEPDDVAHAVLYLASDESRFVTGAELVIDGG 247
PRK07856 PRK07856
SDR family oxidoreductase;
17-118 4.97e-06

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 44.15  E-value: 4.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIP-ANKGVIIFTASMateSYID-LPHT--YKASKNALWTQLREKAKKW---------------- 76
Cdd:PRK07856  106 NLLAPLLVAQAANAVMQQqPGGGSIVNIGSV---SGRRpSPGTaaYGAAKAGLLNLTRSLAVEWapkvrvnavvvglvrt 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1444445608  77 ------FGDGGNLEGV--------LLHEQDVENGVLYLASDDSKYVSGLNFIIHGG 118
Cdd:PRK07856  183 eqselhYGDAEGIAAVaatvplgrLATPADIAWACLFLASDLASYVSGANLEVHGG 238
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 17-118 8.43e-06

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 43.50  E-value: 8.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMATESYIDLPHTYKASKNALWTQLREKAKKWFGDG-------------GNL 83
Cdd:cd05347   113 NLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVAGLTKALATEWARHGiqvnaiapgyfatEMT 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1444445608  84 EGVLLHE------------------QDVENGVLYLASDDSKYVSGLNFIIHGG 118
Cdd:cd05347   193 EAVVADPefnddilkripagrwgqpEDLVGAAVFLASDASDYVNGQIIFVDGG 245
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 17-119 3.34e-05

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: 41.99  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASmaTESYIDLP--HTYKASKNA----------------------------LW 66
Cdd:cd05341   110 NLTGVFLGTRAVIPPMKEAGGGSIINMSS--IEGLVGDPalAAYNASKGAvrgltksaalecatqgygirvnsvhpgyIY 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1444445608  67 TQLREKAKKWFGDGGNLEGVLL----HEQDVENGVLYLASDDSKYVSGLNFIIHGGF 119
Cdd:cd05341   188 TPMTDELLIAQGEMGNYPNTPMgragEPDEIAYAVVYLASDESSFVTGSELVVDGGY 244
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 17-47 7.00e-05

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: 40.83  E-value: 7.00e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMA 47
Cdd:cd05373   108 AAFGGFLAAREAAKRMLARGRGTIIFTGATA 138
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 17-65 8.13e-05

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: 40.55  E-value: 8.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMA-TESYIDLPHtYKASKNAL 65
Cdd:COG4221   110 NVKGVLYVTRAALPAMRARGSGHIVNISSIAgLRPYPGGAV-YAATKAAV 158
PRK12826 PRK12826
SDR family oxidoreductase;
17-119 1.54e-04

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 39.90  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMA--TESYIDLPHtYKASKNALWTQLREKAKKWFGDG-------------- 80
Cdd:PRK12826  114 NLTGTFLLTQAALPALIRAGGGRIVLTSSVAgpRVGYPGLAH-YAASKAGLVGFTRALALELAARNitvnsvhpggvdtp 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1444445608  81 --GNLEGVLLHEQ--------------DVENGVLYLASDDSKYVSGLNFIIHGGF 119
Cdd:PRK12826  193 maGNLGDAQWAEAiaaaiplgrlgepeDIAAAVLFLASDEARYITGQTLPVDGGA 247
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 17-118 2.81e-04

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: 39.10  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIpANKGVIIFTASmaTESYIDLPHT--YKASKNAL-----------------------WTQLRE 71
Cdd:cd09761   106 NLTGPYELSRYCRDELI-KNKGRIINIAS--TRAFQSEPDSeaYAASKGGLvalthalamslgpdirvncispgWINTTE 182

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1444445608  72 KAKKWFGDGGNLEgvllHEQ----------DVENGVLYLASDDSKYVSGLNFIIHGG 118
Cdd:cd09761   183 QQEFTAAPLTQED----HAQhpagrvgtpkDIANLVLFLCQQDAGFITGETFIVDGG 235
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 17-118 2.95e-04

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 39.05  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMATEsyIDLPHT--YKASKNAL----------------------------- 65
Cdd:PRK05565  114 NLTGVMLLTRYALPYMIKRKSGVIVNISSIWGL--IGASCEvlYSASKGAVnaftkalakelapsgirvnavapgaidte 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1444445608  66 -WTQLREKAKKWFGDGGNLeGVLLHEQDVENGVLYLASDDSKYVSGLNFIIHGG 118
Cdd:PRK05565  192 mWSSFSEEDKEGLAEEIPL-GRLGKPEEIAKVVLFLASDDASYITGQIITVDGG 244
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 17-118 5.42e-04

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: 38.47  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMA----------TESYIDLPHTYKASKNALWTQLREKAKKWFGDG------ 80
Cdd:cd08930   114 NLGGAFLCSQAFIKLFKKQGKGSIINIASIYgviapdfriyENTQMYSPVEYSVIKAGIIHLTKYLAKYYADTGirvnai 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1444445608  81 --------------GNLE-----GVLLHEQDVENGVLYLASDDSKYVSGLNFIIHGG 118
Cdd:cd08930   194 spggilnnqpseflEKYTkkcplKRMLNPEDLRGAIIFLLSDASSYVTGQNLVIDGG 250
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
17-71 1.06e-03

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 37.54  E-value: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMAteSYIDLPH--TYKASKNAL--WTQ-LRE 71
Cdd:COG0300   113 NVFGPVRLTRALLPLMRARGRGRIVNVSSVA--GLRGLPGmaAYAASKAALegFSEsLRA 170
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 17-65 1.50e-03

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 36.82  E-value: 1.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1444445608  17 NVVGGFFFAKHAARVMIPANKGVIIFTASMAT-ESYIDLPHtYKASKNAL 65
Cdd:pfam00106 108 NLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGlVPYPGGSA-YSASKAAV 156
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
91-120 1.90e-03

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 36.63  E-value: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1444445608  91 QDVENGVLYLASDDSKYVSGLNFIIHGGFR 120
Cdd:PRK08643  225 EDVANCVSFLAGPDSDYITGQTIIVDGGMV 254
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 91-118 2.02e-03

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 36.61  E-value: 2.02e-03
                          10        20
                  ....*....|....*....|....*...
gi 1444445608  91 QDVENGVLYLASDDSKYVSGLNFIIHGG 118
Cdd:PRK08642  222 QEFADAVLFFASPWARAVTGQNLVVDGG 249
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 91-118 6.56e-03

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: 35.13  E-value: 6.56e-03
                          10        20
                  ....*....|....*....|....*...
gi 1444445608  91 QDVENGVLYLASDDSKYVSGLNFIIHGG 118
Cdd:cd05349   216 QDIADAVLFFASPWARAVTGQNLVVDGG 243
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 17-41 7.33e-03

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 35.01  E-value: 7.33e-03
                          10        20
                  ....*....|....*....|....*.
gi 1444445608  17 NVVGGFFFAKHAARVMIPAN-KGVII 41
Cdd:PRK12384  112 NLVGYFLCAREFSRLMIRDGiQGRII 137
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 91-119 8.11e-03

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 34.78  E-value: 8.11e-03
                          10        20
                  ....*....|....*....|....*....
gi 1444445608  91 QDVENGVLYLASDDSKYVSGLNFIIHGGF 119
Cdd:PRK05557  217 EEIASAVAFLASDEAAYITGQTLHVNGGM 245
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 71-118 8.59e-03

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 34.76  E-value: 8.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1444445608  71 EKAKKWFGDGGNLEGVLLHEqDVENGVLYLASDDSKYVSGLNFIIHGG 118
Cdd:PRK06463  200 EKLRELFRNKTVLKTTGKPE-DIANIVLFLASDDARYITGQVIVADGG 246
PRK08589 PRK08589
SDR family oxidoreductase;
35-118 9.08e-03

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 34.75  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444445608  35 ANKGVIIFTASMATE-------------SYIDLPHTYK---ASKNALWTQLREkAKKWFGDGGNLEgvllHEQDVENGVL 98
Cdd:PRK08589  157 AKGAVINFTKSIAIEygrdgiranaiapGTIETPLVDKltgTSEDEAGKTFRE-NQKWMTPLGRLG----KPEEVAKLVV 231

                          90       100
                  ....*....|....*....|
gi 1444445608  99 YLASDDSKYVSGLNFIIHGG 118
Cdd:PRK08589  232 FLASDDSSFITGETIRIDGG 251
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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