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Conserved domains on  [gi|17568967|ref|NP_509146|]
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SCP2 domain-containing protein [Caenorhabditis elegans]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143243)

SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to Dictyostelium discoideum peroxisomal multifunctional enzyme A, that acts on the peroxisomal beta-oxidation pathway for fatty acids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 3-252 5.86e-160

(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: 451.01  E-value: 5.86e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIVK 82
Cdd:cd05353   1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANY 162
Cdd:cd05353  81 TAIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 163 AAAKSALIGLSNSLAQEGAKYNILANTLVPTAGSRLTETVMPQNLVDALKPDYVTPLVTYMVHDSFEESGKVFEAGAGWY 242
Cdd:cd05353 161 SAAKLGLLGLSNTLAIEGAKYNITCNTIAPAAGSRMTETVMPEDLFDALKPEYVAPLVLYLCHESCEVTGGLFEVGAGWI 240

                       250
                ....*....|
gi 17568967 243 GTIQYYKSKG 252
Cdd:cd05353 241 GKLRWERSGG 250
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 325-429 6.45e-20

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


:

Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 84.23  E-value: 6.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   325 FQEMADGVKADPTAVKTLK-SIVLYIITDGKnelGKFTLDFKSASPSVYLGDvknGEKANATVTVADSDFVDIAAGKLNA 403
Cdd:pfam02036   1 LNQLLARDPAARELLKKLNgKVIRFDLTDLG---LSLTLDLKDGGGRVLAGD---EGKADVTLSASDSDLLALATGKLNP 74

                          90       100
                  ....*....|....*....|....*.
gi 17568967   404 QKAFMSGKLKVKGNVMLLQKLQTVLE 429
Cdd:pfam02036  75 QKAFMQGKLKIEGDMELAQKLEGLLK 100
 
Name Accession Description Interval E-value
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 3-252 5.86e-160

(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: 451.01  E-value: 5.86e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIVK 82
Cdd:cd05353   1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANY 162
Cdd:cd05353  81 TAIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 163 AAAKSALIGLSNSLAQEGAKYNILANTLVPTAGSRLTETVMPQNLVDALKPDYVTPLVTYMVHDSFEESGKVFEAGAGWY 242
Cdd:cd05353 161 SAAKLGLLGLSNTLAIEGAKYNITCNTIAPAAGSRMTETVMPEDLFDALKPEYVAPLVLYLCHESCEVTGGLFEVGAGWI 240

                       250
                ....*....|
gi 17568967 243 GTIQYYKSKG 252
Cdd:cd05353 241 GKLRWERSGG 250
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 6-240 1.11e-74

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 235.34  E-value: 1.11e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGD---KIVK 82
Cdd:PRK07791   5 DGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIGVGLDGSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDgaaNLVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQ-KYG-----RIVVTSSNAGVHGN 156
Cdd:PRK07791  85 AAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRAEsKAGravdaRIINTSSGAGLQGS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTAGSRLTETVMP-------QNLVDALKPDYVTPLVTYMVH-DSF 228
Cdd:PRK07791 165 VGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAARTRMTETVFAemmakpeEGEFDAMAPENVSPLVVWLGSaESR 244

                        250
                 ....*....|..
gi 17568967  229 EESGKVFEAGAG 240
Cdd:PRK07791 245 DVTGKVFEVEGG 256
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 4-192 4.74e-65

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 208.87  E-value: 4.74e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVEfg 77
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEA---------LEAAAAELRAAGGRAlavaadVTDEAAVE-- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  78 dKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNF 157
Cdd:COG1028  72 -ALVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSP 150

                       170       180       190
                ....*....|....*....|....*....|....*
gi 17568967 158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:COG1028 151 GQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAP 185
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 10-192 2.12e-55

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 183.56  E-value: 2.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    10 AIVTGAGGGLGKTYALELAKRGCKVVVNDlggdrhgtSSSSSMADKVVQEIKSAGGQA------VANYDSVefgDKIVKT 83
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITY--------RSSEEGAEEVVEELKALGVKAlgvvldVSDREDV---KAVVEE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYA 163
Cdd:TIGR01830  70 IEEELGTIDILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYA 149

                         170       180
                  ....*....|....*....|....*....
gi 17568967   164 AAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:TIGR01830 150 ASKAGVIGFTKSLAKELASRNITVNAVAP 178
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-211 6.17e-54

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 178.19  E-value: 6.17e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967     8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVEfgdKIV 81
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEK---------LEAVAKELGALGGKAlfiqgdVTDRAQVK---ALV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:pfam00106  69 EQAVERLGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 17568967   162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPTAgsrlTETVMPQNLVDAL 211
Cdd:pfam00106 149 YSASKAAVIGFTRSLALELAPHGIRVNAVAPGG----VDTDMTKELREDE 194
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 325-429 6.45e-20

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 84.23  E-value: 6.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   325 FQEMADGVKADPTAVKTLK-SIVLYIITDGKnelGKFTLDFKSASPSVYLGDvknGEKANATVTVADSDFVDIAAGKLNA 403
Cdd:pfam02036   1 LNQLLARDPAARELLKKLNgKVIRFDLTDLG---LSLTLDLKDGGGRVLAGD---EGKADVTLSASDSDLLALATGKLNP 74

                          90       100
                  ....*....|....*....|....*.
gi 17568967   404 QKAFMSGKLKVKGNVMLLQKLQTVLE 429
Cdd:pfam02036  75 QKAFMQGKLKIEGDMELAQKLEGLLK 100
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 8-178 2.06e-19

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: 85.23  E-value: 2.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967      8 KVAIVTGAGGGLGKTYALELAKRGCKVVVndLGGdRHGTSSSSsmADKVVQEIKSAGGQA------VANYDSVEfgdKIV 81
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARRLV--LLS-RSGPDAPG--AAALLAELEAAGARVtvvacdVADRDALA---AVL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967     82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAwpymRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:smart00822  73 AAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELT----ADLPLDFFVLFSSIAGVLGSPGQAN 148

                          170
                   ....*....|....*..
gi 17568967    162 YAAAKSALiglsNSLAQ 178
Cdd:smart00822 149 YAAANAFL----DALAE 161
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
323-431 2.49e-19

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 82.65  E-value: 2.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 323 ALFQEMADGVKAdPTAVKTLKSIVLYIITDGKNelGKFTLDFKSASPSVYLGDVkngEKANATVTVADSDFVDIAAGKLN 402
Cdd:COG3255   2 EWAEALCEKLNA-ADAAAGWDGVVQFVITGEGG--GAYYLVIDDGKCTVSEGDD---DDADVTLTASYEDWKKLLTGELD 75

                        90       100
                ....*....|....*....|....*....
gi 17568967 403 AQKAFMSGKLKVKGNVMLLQKLQTVLEKA 431
Cdd:COG3255  76 PMTAFMTGKLKVEGDMGLAMKLMSLFKAL 104
 
Name Accession Description Interval E-value
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 3-252 5.86e-160

(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: 451.01  E-value: 5.86e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIVK 82
Cdd:cd05353   1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANY 162
Cdd:cd05353  81 TAIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 163 AAAKSALIGLSNSLAQEGAKYNILANTLVPTAGSRLTETVMPQNLVDALKPDYVTPLVTYMVHDSFEESGKVFEAGAGWY 242
Cdd:cd05353 161 SAAKLGLLGLSNTLAIEGAKYNITCNTIAPAAGSRMTETVMPEDLFDALKPEYVAPLVLYLCHESCEVTGGLFEVGAGWI 240

                       250
                ....*....|
gi 17568967 243 GTIQYYKSKG 252
Cdd:cd05353 241 GKLRWERSGG 250
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 6-240 1.11e-74

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 235.34  E-value: 1.11e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGD---KIVK 82
Cdd:PRK07791   5 DGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIGVGLDGSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDgaaNLVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQ-KYG-----RIVVTSSNAGVHGN 156
Cdd:PRK07791  85 AAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRAEsKAGravdaRIINTSSGAGLQGS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTAGSRLTETVMP-------QNLVDALKPDYVTPLVTYMVH-DSF 228
Cdd:PRK07791 165 VGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAARTRMTETVFAemmakpeEGEFDAMAPENVSPLVVWLGSaESR 244

                        250
                 ....*....|..
gi 17568967  229 EESGKVFEAGAG 240
Cdd:PRK07791 245 DVTGKVFEVEGG 256
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 4-192 4.74e-65

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 208.87  E-value: 4.74e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVEfg 77
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEA---------LEAAAAELRAAGGRAlavaadVTDEAAVE-- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  78 dKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNF 157
Cdd:COG1028  72 -ALVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSP 150

                       170       180       190
                ....*....|....*....|....*....|....*
gi 17568967 158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:COG1028 151 GQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAP 185
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-223 3.19e-62

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 201.58  E-value: 3.19e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLrfDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgTSSSSSMADKVVQEIKSAGGQA------VANYDSV 74
Cdd:PRK05557   1 MSL--EGKVALVTGASRGIGRAIAERLAAQGANVVIN--------YASSEAGAEALVAEIGALGGKAlavqgdVSDAESV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   75 efgDKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH 154
Cdd:PRK05557  71 ---ERAVDEAKAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLM 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17568967  155 GNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGsrLTETVMpqnlVDALKPDYVTPLVTYM 223
Cdd:PRK05557 148 GNPGQANYAASKAGVIGFTKSLARELASRGITVNAVAP--G--FIETDM----TDALPEDVKEAILAQI 208
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-235 5.16e-62

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 203.09  E-value: 5.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsSSSSMADKVVQEIKSAGGQAVANYDSV---EFG 77
Cdd:PRK07792   6 NTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDV--------ASALDASDVLDEIRAAGAKAVAVAGDIsqrATA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 DKIVKTAiDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQK-------YGRIVVTSSN 150
Cdd:PRK07792  78 DELVATA-VGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAkaaggpvYGRIVNTSSE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  151 AGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTAGSRLTETV------MPQNLVDALKPDYVTPLVTYMV 224
Cdd:PRK07792 157 AGLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICPRARTAMTADVfgdapdVEAGGIDPLSPEHVVPLVQFLA 236

                        250
                 ....*....|..
gi 17568967  225 HDSFEE-SGKVF 235
Cdd:PRK07792 237 SPAAAEvNGQVF 248
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 8-192 6.11e-61

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: 198.16  E-value: 6.11e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVEfgdKIV 81
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEA---------AAETVEEIKALGGNAaaleadVSDREAVE---ALV 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:cd05333  69 EKVEAEFGPVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQAN 148

                       170       180       190
                ....*....|....*....|....*....|.
gi 17568967 162 YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05333 149 YAASKAGVIGFTKSLAKELASRGITVNAVAP 179
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
4-192 3.34e-59

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 193.84  E-value: 3.34e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDlggdrhgtsSSSSMADKVVQEIKSAGGQA------VANYDSVEfg 77
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYD---------SNEEAAEALAAELRAAGGEArvlvfdVSDEAAVR-- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 dKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNF 157
Cdd:PRK05653  71 -ALIEAAVEAFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNP 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17568967  158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK05653 150 GQTNYSAAKAGVIGFTKALALELASRGITVNAVAP 184
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 10-192 2.12e-55

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 183.56  E-value: 2.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    10 AIVTGAGGGLGKTYALELAKRGCKVVVNDlggdrhgtSSSSSMADKVVQEIKSAGGQA------VANYDSVefgDKIVKT 83
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITY--------RSSEEGAEEVVEELKALGVKAlgvvldVSDREDV---KAVVEE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYA 163
Cdd:TIGR01830  70 IEEELGTIDILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYA 149

                         170       180
                  ....*....|....*....|....*....
gi 17568967   164 AAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:TIGR01830 150 ASKAGVIGFTKSLAKELASRNITVNAVAP 178
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-211 6.17e-54

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 178.19  E-value: 6.17e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967     8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVEfgdKIV 81
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEK---------LEAVAKELGALGGKAlfiqgdVTDRAQVK---ALV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:pfam00106  69 EQAVERLGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 17568967   162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPTAgsrlTETVMPQNLVDAL 211
Cdd:pfam00106 149 YSASKAAVIGFTRSLALELAPHGIRVNAVAPGG----VDTDMTKELREDE 194
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 10-192 4.26e-52

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: 174.78  E-value: 4.26e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  10 AIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVqEIKSAGGQA------VANYDSVEfgdKIVKT 83
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEA---------LAELA-AIEALGGNAvavqadVSDEEDVE---ALVEE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYA 163
Cdd:cd05233  68 ALEEFGRLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYA 147

                       170       180
                ....*....|....*....|....*....
gi 17568967 164 AAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05233 148 ASKAALEGLTRSLALELAPYGIRVNAVAP 176
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-219 6.93e-52

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 174.67  E-value: 6.93e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgTSSSSSMADKVVQEIKSAGGQA------VANYDSVEfg 77
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVH--------YRSDEEAAEELVEAVEALGRRAqavqadVTDKAALE-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 dKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNF 157
Cdd:PRK12825  73 -AAVAAAVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWP 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17568967  158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP--TAGSRLTETVMPQnlvdALKPDYVTPL 219
Cdd:PRK12825 152 GRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPgdIDTDMKEATIEEA----REAKDAETPL 211
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-216 2.38e-49

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 168.12  E-value: 2.38e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   1 MSLRfdGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSV 74
Cdd:COG0300   1 MSLT--GKTVLITGASSGIGRALARALAARGARVVLVARDAER---------LEALAAELRAAGARVevvaldVTDPDAV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  75 EfgdKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH 154
Cdd:COG0300  70 A---ALAEAVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLR 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17568967 155 GNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA-GSRLTETVMPQNLVDALKPDYV 216
Cdd:COG0300 147 GLPGMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPvDTPFTARAGAPAGRPLLSPEEV 209
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-226 1.38e-46

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: 160.73  E-value: 1.38e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   1 MSLRfdGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIksaGGQA------VANYDSV 74
Cdd:COG4221   1 MSDK--GKVALITGASSGIGAATARALAAAGARVVLAARRAER---------LEALAAEL---GGRAlavpldVTDEAAV 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  75 EfgdKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH 154
Cdd:COG4221  67 E---AAVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLR 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 155 GNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP-TAGSRLTETVMPQNL---------VDALKPDYVTPLVTYMV 224
Cdd:COG4221 144 PYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPgAVDTEFLDSVFDGDAeaaaavyegLEPLTPEDVAEAVLFAL 223


                ..
gi 17568967 225 HD 226
Cdd:COG4221 224 TQ 225
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
 8-226 4.48e-45

acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.


Pssm-ID: 273823 [Multi-domain]  Cd Length: 242  Bit Score: 156.83  E-value: 4.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967     8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGgdrhgtssSSSMADKVVQEIKSAGGQA------VANYDSVEfgdKIV 81
Cdd:TIGR01829   1 RIALVTGGMGGIGTAICQRLAKDGYRVAANCGP--------NEERAEAWLQEQGALGFDFrvvegdVSSFESCK---AAV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:TIGR01829  70 AKVEAELGPVDVLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTN 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17568967   162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTETV--MPQNLVDAL----------KPDYVTPLVTYMVHD 226
Cdd:TIGR01829 150 YSAAKAGMIGFTKALAQEGATKGVTVNTISP--GYIATDMVmaMREDVLNSIvaqipvkrlgRPEEIAAAVAFLASE 224
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-194 4.98e-44

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 154.23  E-value: 4.98e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVN-DLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVEf 76
Cdd:PRK05565   2 KLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEA---------AQELLEEIKEEGGDAiavkadVSSEEDVE- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 gdKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGN 156
Cdd:PRK05565  72 --NLVEQIVEKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGA 149

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PRK05565 150 SCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGA 187
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 6-241 1.14e-43

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 153.34  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHgtsssSSMADKVVQEIKSAGGQA-VANYDSVEFGD--KIVK 82
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRG-----RAEADAVAAGIEAAGGKAlGLAFDVRDFAAtrAALD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAA-WPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:PRK12827  80 AGVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAAlPPMIRARRGGRIVNIASVAGVRGNRGQVN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPTA-GSRLTETVMP----QNLVDA---LKPDYVTPLVTYMVHDSFEE-SG 232
Cdd:PRK12827 160 YAASKAGLIGLTKTLANELAPRGITVNAVAPGAiNTPMADNAAPtehlLNPVPVqrlGEPDEVAALVAFLVSDAASYvTG 239


                 ....*....
gi 17568967  233 KVFEAGAGW 241
Cdd:PRK12827 240 QVIPVDGGF 248
FabG-like PRK07231
SDR family oxidoreductase;
3-203 1.44e-43

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 153.06  E-value: 1.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIkSAGGQAV---ANYDSVEFGDK 79
Cdd:PRK07231   1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEA---------AERVAAEI-LAGGRAIavaADVSDEADVEA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 IVKTAIDNFGRIDIVINNAGI-LRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:PRK07231  71 AVAAALERFGSVDILVNNAGTtHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17568967  159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTAG-SRLTETVM 203
Cdd:PRK07231 151 LGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVeTGLLEAFM 196
PRK12826 PRK12826
SDR family oxidoreductase;
4-210 5.04e-43

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 151.61  E-value: 5.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVEfg 77
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDD---------AAATAELVEAAGGKArarqvdVRDRAALK-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 dKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH-GN 156
Cdd:PRK12826  72 -AAVAAGVEDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvGY 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTAgsrlTETVMPQNLVDA 210
Cdd:PRK12826 151 PGLAHYAASKAGLVGFTRALALELAARNITVNSVHPGG----VDTPMAGNLGDA 200
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 4-207 1.60e-41

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 147.46  E-value: 1.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgTSSSSSMADKVVQEIKSAGGQAVA---NYDSVEFGDKI 80
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVIN--------YNSSKEAAENLVNELGKEGHDVYAvqaDVSKVEDANRL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:PRK12935  75 VEEAVNHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQT 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17568967  161 NYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTETVM--PQNL 207
Cdd:PRK12935 155 NYSAAKAGMLGFTKSLALELAKTNVTVNAICP--GFIDTEMVAevPEEV 201
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
8-227 4.62e-41

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 146.06  E-value: 4.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGdrhgtSSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIVKTAIDN 87
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSG-----NDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   88 FGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAAAKS 167
Cdd:PRK12824  78 EGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17568967  168 ALIGLSNSLAQEGAKYNILANTLVPtaGSRLTETV--MPQNLVDALK----------PDYVTPLVTYMVHDS 227
Cdd:PRK12824 158 GMIGFTKALASEGARYGITVNCIAP--GYIATPMVeqMGPEVLQSIVnqipmkrlgtPEEIAAAVAFLVSEA 227
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 4-211 4.13e-39

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 141.56  E-value: 4.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQAV---ANYDSVEFGDKI 80
Cdd:PRK12429   1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEA---------AAAAAEALQKAGGKAIgvaMDVTDEEAINAG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGI-----LRDVSFLKmteldWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHG 155
Cdd:PRK12429  72 IDYAVETFGGVDILVNNAGIqhvapIEDFPTEK-----WKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVG 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17568967  156 NFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTETVmpQNLVDAL 211
Cdd:PRK12429 147 SAGKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICP--GYVDTPLV--RKQIPDL 198
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 7-192 3.57e-38

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: 138.56  E-value: 3.57e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgTSSSSSMADKVVQEIKSAGGQAV---ANYDSVEFGDKIVKT 83
Cdd:cd05362   3 GKVALVTGASRGIGRAIAKRLARDGASVVVN--------YASSKAAAEEVVAEIEAAGGKAIavqADVSDPSQVARLFDA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIVVTSSNAGVHGNFGQANYA 163
Cdd:cd05362  75 AEKAFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG--GRIINISSSLTAAYTPNYGAYA 152

                       170       180
                ....*....|....*....|....*....
gi 17568967 164 AAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05362 153 GSKAAVEAFTRVLAKELGGRGITVNAVAP 181
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 6-194 1.22e-37

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: 137.51  E-value: 1.22e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIVK--- 82
Cdd:cd05358   2 KGKVALVTGASSGIGKAIAIRLATAGANVVVN--------YRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVAlfq 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQK-YGRIVVTSSnagVHGNF---G 158
Cdd:cd05358  74 SAIKEFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKiKGKIINMSS---VHEKIpwpG 150

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17568967 159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:cd05358 151 HVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGA 186
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
4-192 1.67e-37

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 137.24  E-value: 1.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssmADKVVQEIKSAGGQA------VANYDSVEfg 77
Cdd:PRK08226   3 KLTGKTALITGALQGIGEGIARVFARHGANLILLDISPE----------IEKLADELCGRGHRCtavvadVRDPASVA-- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 dKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAG-VHGN 156
Cdd:PRK08226  71 -AAIKRAKEKEGRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVAD 149

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK08226 150 PGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICP 185
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-193 3.19e-37

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 135.97  E-value: 3.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRfdGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA------VANYDSV 74
Cdd:PRK07666   3 QSLQ--GKNALITGAGRGIGRAVAIALAKEGVNVGL---------LARTEENLKAVAEEVEAYGVKVviatadVSDYEEV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   75 EFGDKIVKTaidNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH 154
Cdd:PRK07666  72 TAAIEQLKN---ELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQK 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 17568967  155 GNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPT 193
Cdd:PRK07666 149 GAAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPS 187
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 7-192 2.62e-36

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: 133.94  E-value: 2.62e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHgtsssssmaDKVVQEIKSAGGQA---VANYDSVEFGDKIVKT 83
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENL---------ERAASELRAGGAGVlavVADLTDPEDIDRLVEK 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH--GNFGQAN 161
Cdd:cd05344  72 AGDAFGRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEpePNLVLSN 151

                       170       180       190
                ....*....|....*....|....*....|.
gi 17568967 162 yaAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05344 152 --VARAGLIGLVKTLSRELAPDGVTVNSVLP 180
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 8-215 1.35e-35

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: 131.58  E-value: 1.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVVvndlGGDRHgtsssssmADKVVQEIKSAGGQA------VANYDSVEfgdKIV 81
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVI----ATARN--------PDKLESLGELLNDNLevleldVTDEESIK---AAV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:cd05374  66 KEVIERFGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGP 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17568967 162 YAAAKSALIGLSNSLAQEGAKYNILANTLVP-TAGSRLTETVMPQNLVDALKPDY 215
Cdd:cd05374 146 YCASKAALEALSESLRLELAPFGIKVTIIEPgPVRTGFADNAAGSALEDPEISPY 200
PRK07774 PRK07774
SDR family oxidoreductase;
4-211 2.26e-35

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 131.02  E-value: 2.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKSAGGQA------VANYDSVEfg 77
Cdd:PRK07774   3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAE---------GAERVAKQIVADGGTAiavqvdVSDPDSAK-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 dKIVKTAIDNFGRIDIVINNAGILRDV---SFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAG-V 153
Cdd:PRK07774  72 -AMADATVSAFGGIDYLVNNAAIYGGMkldLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAwL 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17568967  154 HGNFgqanYAAAKSALIGLSNSLAQEGAKYNILANTLVP-TAGSRLTETVMPQNLVDAL 211
Cdd:PRK07774 151 YSNF----YGLAKVGLNGLTQQLARELGGMNIRVNAIAPgPIDTEATRTVTPKEFVADM 205
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 7-217 7.80e-35

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: 129.82  E-value: 7.80e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlgGDRHGTSSSSSMADKVVQ-------EIKSAGGQAVANYDSVEFGDK 79
Cdd:cd05338   3 GKVAFVTGASRGIGRAIALRLAKAGATVVV----AAKTASEGDNGSAKSLPGtieetaeEIEAAGGQALPIVVDVRDEDQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  80 I---VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGN 156
Cdd:cd05338  79 VralVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17568967 157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPtagSRLTETVMPQNLV------DALKPDYVT 217
Cdd:cd05338 159 RGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWP---STAIETPAATELSggsdpaRARSPEILS 222
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 6-192 1.73e-34

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 128.94  E-value: 1.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVEfgdK 79
Cdd:PRK12939   6 AGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAE---------ARELAAALEAAGGRAhaiaadLADPASVQ---R 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 IVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQ 159
Cdd:PRK12939  74 FFDAAAAALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKL 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 17568967  160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK12939 154 GAYVASKGAVIGMTRSLARELGGRGITVNAIAP 186
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-192 1.75e-34

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 129.25  E-value: 1.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSV 74
Cdd:PRK13394   1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDG---------ANAVADEINKAGGKAigvamdVTNEDAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   75 EFGdkiVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYM-RDQKYGRIVVTSSNAGV 153
Cdd:PRK13394  72 NAG---IDKVAERFGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSH 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 17568967  154 HGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK13394 149 EASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 187
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 7-192 4.67e-34

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: 127.88  E-value: 4.67e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssMADKVVQEIKSAGGQAVA------NYDSVEfgdKI 80
Cdd:cd05366   2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEE--------AAKSTIQEISEAGYNAVAvgadvtDKDDVE---AL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKY-GRIVVTSSNAGVHGNFGQ 159
Cdd:cd05366  71 IDQAVEKFGSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHgGKIINASSIAGVQGFPNL 150

                       170       180       190
                ....*....|....*....|....*....|...
gi 17568967 160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05366 151 GAYSASKFAVRGLTQTAAQELAPKGITVNAYAP 183
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 7-192 2.00e-33

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: 125.93  E-value: 2.00e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVefgDKI 80
Cdd:cd05347   5 GKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEK---------AEEAQQLIEKEGVEAtaftcdVSDEEAI---KAA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:cd05347  73 VEAIEEDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVP 152

                       170       180       190
                ....*....|....*....|....*....|..
gi 17568967 161 NYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05347 153 AYAASKGGVAGLTKALATEWARHGIQVNAIAP 184
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 4-195 7.20e-33

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: 124.42  E-value: 7.20e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIksaGGQAVANYDSVEFGDKI--- 80
Cdd:cd05345   2 RLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADG---------AERVAADI---GEAAIAIQADVTKRADVeam 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 VKTAIDNFGRIDIVINNAGIL-RDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQ 159
Cdd:cd05345  70 VEAALSKFGRLDILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGL 149

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17568967 160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTAG 195
Cdd:cd05345 150 TWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAG 185
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 18-192 8.58e-33

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: 123.69  E-value: 8.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    18 GLGKTYALELAKRGCKVVVNDLGGDrhgtsssssmADKVVQEIKSAGGQA-----VANYDSVEfgdKIVKTAIDNFGRID 92
Cdd:pfam13561   7 GIGWAIARALAEEGAEVVLTDLNEA----------LAKRVEELAEELGAAvlpcdVTDEEQVE---ALVAAAVEKFGRLD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    93 IVINNAGILRDV--SFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIVVTSSNAGVHGNFGQANYAAAKSALI 170
Cdd:pfam13561  74 ILVNNAGFAPKLkgPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALE 151

                         170       180
                  ....*....|....*....|..
gi 17568967   171 GLSNSLAQEGAKYNILANTLVP 192
Cdd:pfam13561 152 ALTRYLAVELGPRGIRVNAISP 173
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 3-193 1.01e-32

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 124.00  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsssssmaDKVVQEIKSA--GGQA------VANYDSV 74
Cdd:PRK06841  11 FDLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDR--------------SEDVAEVAAQllGGNAkglvcdVSDSQSV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   75 EfgdKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH 154
Cdd:PRK06841  77 E---AAVAAVISAFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVV 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 17568967  155 GNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPT 193
Cdd:PRK06841 154 ALERHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPT 192
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 4-192 1.90e-32

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: 123.33  E-value: 1.90e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGgDRHGTSSSSSMADKVVQEIKSAggqaVANYDSVEfgdKIVKT 83
Cdd:cd05326   1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADID-DDAGQAVAAELGDPDISFVHCD----VTVEADVR---AAVDT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  84 AIDNFGRIDIVINNAGIL--RDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:cd05326  73 AVARFGRLDIMFNNAGVLgaPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHA 152

                       170       180       190
                ....*....|....*....|....*....|.
gi 17568967 162 YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05326 153 YTASKHAVLGLTRSAATELGEHGIRVNCVSP 183
PRK06138 PRK06138
SDR family oxidoreductase;
3-194 2.31e-32

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 123.34  E-value: 2.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKsAGGQAVANydSVEFGD-KIV 81
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAE---------AAERVAAAIA-AGGRAFAR--QGDVGSaEAV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDN----FGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNF 157
Cdd:PRK06138  69 EALVDFvaarWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGR 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17568967  158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PRK06138 149 GRAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGT 185
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 10-194 4.38e-32

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: 122.08  E-value: 4.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  10 AIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsSSSSMADKVVQEIKSAGGQAV---ANYDSVEFGDKIVKTAID 86
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYR--------KSKDAAAEVAAEIEELGGKAVvvrADVSQPQDVEEMFAAVKE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  87 NFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAAAK 166
Cdd:cd05359  73 RFGRLDVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAK 152

                       170       180
                ....*....|....*....|....*...
gi 17568967 167 SALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:cd05359 153 AALEALVRYLAVELGPRGIRVNAVSPGV 180
PRK06172 PRK06172
SDR family oxidoreductase;
1-194 6.13e-32

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 122.17  E-value: 6.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSV 74
Cdd:PRK06172   1 MSMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAG---------GEETVALIREAGGEAlfvacdVTRDAEV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   75 EfgdKIVKTAIDNFGRIDIVINNAGILRDVSFL-KMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGV 153
Cdd:PRK06172  72 K---ALVEQTIAAYGRLDYAFNNAGIEIEQGRLaEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGL 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17568967  154 HGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PRK06172 149 GAAPKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAV 189
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
8-220 1.14e-31

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 121.27  E-value: 1.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhGTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKiVKTAIDN 87
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVVA--------GCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDS-TKAAFDK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   88 F----GRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYA 163
Cdd:PRK12938  75 VkaevGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17568967  164 AAKSALIGLSNSLAQEGAKYNILANTLVPtagsrlteTVMPQNLVDALKPDYVTPLV 220
Cdd:PRK12938 155 TAKAGIHGFTMSLAQEVATKGVTVNTVSP--------GYIGTDMVKAIRPDVLEKIV 203
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
5-198 1.43e-31

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 127.27  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA-----VANYDSVEfgdK 79
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEA---------AEAAAAELGGPDRALgvacdVTDEAAVQ---A 487

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 IVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQK-YGRIVVTSSNAGVHGNFG 158
Cdd:PRK08324 488 AFEEAALAFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIASKNAVNPGPN 567

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17568967  159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA---GSRL 198
Cdd:PRK08324 568 FGAYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAvvrGSGI 610
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 8-217 2.05e-31

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: 119.78  E-value: 2.05e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVVvndLGGDRHGTSSSSSMADKVVQEIksaggqavaNYDSVEFGD--KIVKTAI 85
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVS---LGLRNPEDLAALSASGGDVEAV---------PYDARDPEDarALVDALR 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  86 DNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAAA 165
Cdd:cd08932  69 DRFGRIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSAS 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17568967 166 KSALIGLSNSLAQEGAKYNILANTLVPTAgsrlTETVMPQ--NLVDALKPDYVT 217
Cdd:cd08932 149 KFALRALAHALRQEGWDHGVRVSAVCPGF----VDTPMAQglTLVGAFPPEEMI 198
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 5-239 3.43e-31

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 120.16  E-value: 3.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlgGDRHGTSSSSSMADkvVQEIKSAGGQA-VANYDSVefgDKIVKT 83
Cdd:PRK12829   9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHV----CDVSEAALAATAAR--LPGAKVTATVAdVADPAQV---ERVFDT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGI-LRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGR-IVVTSSNAGVHGNFGQAN 161
Cdd:PRK12829  80 AVERFGGLDVLVNNAGIaGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGvIIALSSVAGRLGYPGRTP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17568967  162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPTAGSRLTETVMPQNLVDALKPDYVTPLVTYMVHDSFEESGKVFEAGA 239
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLGIGLDEMEQEYLEKISLGRMVEPEDIAA 237
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-192 4.33e-31

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 119.84  E-value: 4.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCkvvvnDLGGDRHGTSssssmADKVVQEIKSAGGQAV---ANYDSVEFGDKI 80
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGA-----DIIITTHGTN-----WDETRRLIEKEGRKVTfvqVDLTKPESAEKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:PRK06935  82 VKEALEEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVP 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17568967  161 NYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK06935 162 AYTASKHGVAGLTKAFANELAAYNIQVNAIAP 193
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 5-192 4.46e-31

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 119.52  E-value: 4.46e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIksaGGQAVANydSVEFGDK----- 79
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGG---------AAQAVVAQI---AGGALAL--RVDVTDEqqvaa 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  80 IVKTAIDNFGRIDIVINNAGILRDVSFLKMTEL-DWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:cd08944  67 LFERAVEEFGGLDLLVNNAGAMHLTPAIIDTDLaVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPG 146

                       170       180       190
                ....*....|....*....|....*....|....
gi 17568967 159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd08944 147 YGAYGASKAAIRNLTRTLAAELRHAGIRCNALAP 180
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 2-192 3.93e-30

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: 117.05  E-value: 3.93e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtssSSSMADKVVQEIKSAGG-QA------VANYDSV 74
Cdd:cd05352   3 LFSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYN---------SAPRAEEKAEELAKKYGvKTkaykcdVSSQESV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  75 EfgdKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH 154
Cdd:cd05352  74 E---KTFKQIQKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTI 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17568967 155 GNFGQ--ANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05352 151 VNRPQpqAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISP 190
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-218 7.30e-30

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 116.05  E-value: 7.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVqeiksAGGQAVANYDSVEfgdKI 80
Cdd:PRK12828   1 MEHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALR-----IGGIDLVDPQAAR---RA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:PRK12828  73 VDEVNRQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17568967  161 NYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTETvMPQNLVDALKPDYVTP 218
Cdd:PRK12828 153 AYAAAKAGVARLTEALAAELLDRGITVNAVLP--SIIDTPP-NRADMPDADFSRWVTP 207
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 4-192 9.14e-30

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 116.18  E-value: 9.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlGGDRHGTsssssmADKVVQEIKSAGGQAVA---NYDSVEFGDKI 80
Cdd:PRK07478   3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVV---GARRQAE------LDQLVAEIRAEGGEAVAlagDVRDEAYAKAL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDV-SFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNF-G 158
Cdd:PRK07478  74 VALAVERFGGLDIAFNNAGTLGEMgPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGFpG 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 17568967  159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07478 154 MAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLP 187
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 7-185 2.24e-29

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: 2.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKS---AGGQAV-------ANYDSVEf 76
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVII---------VARSESKLEEAVEEIEAeanASGQKVsyisadlSDYEEVE- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  77 gdKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGN 156
Cdd:cd08939  71 --QAFAQAVEKGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGI 148

                       170       180
                ....*....|....*....|....*....
gi 17568967 157 FGQANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:cd08939 149 YGYSAYCPSKFALRGLAESLRQELKPYNI 177
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 7-212 3.48e-29

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 114.24  E-value: 3.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrHGTSSS--SSMADKVVQEIKSAGGQaVANYDSVE-FGDKivkt 83
Cdd:PRK12936   6 GRKALVTGASGGIGEEIARLLHAQGAIVGL-------HGTRVEklEALAAELGERVKIFPAN-LSDRDEVKaLGQK---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYA 163
Cdd:PRK12936  74 AEADLEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYC 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17568967  164 AAKSALIGLSNSLAQEGAKYNILANTLVPTagsrLTETVMPQNLVDALK 212
Cdd:PRK12936 154 ASKAGMIGFSKSLAQEIATRNVTVNCVAPG----FIESAMTGKLNDKQK 198
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 8-192 4.08e-29

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: 114.09  E-value: 4.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsSSSSMADKVVQEiksAGGQAVANYDSVEFGDKI---VKTA 84
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVVNYY--------RSTESAEAVAAE---AGERAIAIQADVRDRDQVqamIEEA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  85 IDNFGRIDIVINNAgiLRDVSFL-----KMTELDWDLI---FKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGN 156
Cdd:cd05349  70 KNHFGPVDTIVNNA--LIDFPFDpdqrkTFDTIDWEDYqqqLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPV 147

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17568967 157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05349 148 VPYHDYTTAKAALLGFTRNMAKELGPYGITVNMVSG 183
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 9-216 6.97e-29

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: 113.49  E-value: 6.97e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   9 VAIVTGAGGGLGKTYALELAKRGCKVVVNDLggDRHGtsssssmADKVVQEIKSAGGQA------VANYDSVEfgdKIVK 82
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDI--NEKG-------AEETANNVRKAGGKVhyykcdVSKREEVY---EAAK 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANY 162
Cdd:cd05339  69 KIKKEVGDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADY 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17568967 163 AAAKSALIGLSNSLAQE---GAKYNILANTLVPTagsrLTETVMPQN-------LVDALKPDYV 216
Cdd:cd05339 149 CASKAAAVGFHESLRLElkaYGKPGIKTTLVCPY----FINTGMFQGvktprplLAPILEPEYV 208
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-192 7.24e-29

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 117.63  E-value: 7.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtSSSSSMADKVVQEIksaGGQAVAnYD--SVEFGDKIVKT 83
Cdd:PRK08261 209 AGKVALVTGAARGIGAAIAEVLARDGAHVVCLDV-------PAAGEALAAVANRV---GGTALA-LDitAPDAPARIAEH 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKA--AWPYMRDQkyGRIVVTSSNAGVHGNFGQAN 161
Cdd:PRK08261 278 LAERHGGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEAllAAGALGDG--GRIVGVSSISGIAGNRGQTN 355

                        170       180       190
                 ....*....|....*....|....*....|.
gi 17568967  162 YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK08261 356 YAASKAGVIGLVQALAPLLAERGITINAVAP 386
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 5-204 7.92e-29

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: 113.45  E-value: 7.92e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA-------VANYDSVEfg 77
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVL---------SARREERLEEVKSECLELGAPSphvvpldMSDLEDAE-- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  78 dKIVKTAIDNFGRIDIVINNAGI-LRdvSFLKMTELDWDL-IFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHG 155
Cdd:cd05332  70 -QVVEEALKLFGGLDILINNAGIsMR--SLFHDTSIDVDRkIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIG 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17568967 156 NFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTETVMP 204
Cdd:cd05332 147 VPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCP--GLIDTNIAMN 193
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 3-185 9.48e-29

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 113.57  E-value: 9.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsSSSSMADKVVQEIKSAggqaVANYDSVEfgdKIVK 82
Cdd:PRK06171   5 LNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADI--------HGGDGQHENYQFVPTD----VSSAEEVN---HTVA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   83 TAIDNFGRIDIVINNAGI-----LRDV----SFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGV 153
Cdd:PRK06171  70 EIIEKFGRIDGLVNNAGIniprlLVDEkdpaGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGL 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17568967  154 HGNFGQANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK06171 150 EGSEGQSCYAATKAALNSFTRSWAKELGKHNI 181
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 7-192 1.39e-28

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 112.53  E-value: 1.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgTSSSSSMADKVVQEIKSAGGQAVA-NYDSVEFGD--KIVKT 83
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVN--------YAGSAAAADELVAEIEAAGGRAIAvQADVADAAAvtRLFDA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIVVTSSNAGVHGNFGQANYA 163
Cdd:PRK12937  77 AETAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG--GRIINLSTSVIALPLPGYGPYA 154

                        170       180
                 ....*....|....*....|....*....
gi 17568967  164 AAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK12937 155 ASKAAVEGLVHVLANELRGRGITVNAVAP 183
PRK06181 PRK06181
SDR family oxidoreductase;
7-179 1.50e-28

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 113.15  E-value: 1.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVEfgdKI 80
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETR---------LASLAQELADHGGEAlvvptdVSDAEACE---RL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDW-DLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHGNFGQ 159
Cdd:PRK06181  69 IEAAVARFGGIDILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTR 147

                        170       180
                 ....*....|....*....|
gi 17568967  160 ANYAAAKSALIGLSNSLAQE 179
Cdd:PRK06181 148 SGYAASKHALHGFFDSLRIE 167
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 6-192 6.37e-28

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: 110.64  E-value: 6.37e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGgdrhgtsssssmaDKVVQEIKSAGGQAVANYDSVEFGDkiVKTAI 85
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDIN-------------EEKLKELERGPGITTRVLDVTDKEQ--VAALA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  86 DNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAG-VHGNFGQANYAA 164
Cdd:cd05368  66 KEEGRIDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYST 145

                       170       180
                ....*....|....*....|....*...
gi 17568967 165 AKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05368 146 TKAAVIGLTKSVAADFAQQGIRCNAICP 173
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 7-239 8.26e-28

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: 111.00  E-value: 8.26e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGgdrhgtsssSSMADKVVQEIKSA--GGQAVA-NYD---SVEFGDkI 80
Cdd:cd08940   2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFG---------DAAEIEAVRAGLAAkhGVKVLYhGADlskPAAIED-M 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:cd08940  72 VAYAQRQFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKS 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 161 NYAAAKSALIGLSNSLAQEGAKYNILANtlvptagsrltetvmpqnlvdALKPDYV-TPLVTYMVHDSFEESGKVFEAGA 239
Cdd:cd08940 152 AYVAAKHGVVGLTKVVALETAGTGVTCN---------------------AICPGWVlTPLVEKQISALAQKNGVPQEQAA 210
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 8-212 9.88e-28

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: 110.08  E-value: 9.88e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVVVndlgGDRHgtssSSSMADKVVQEIKSAGG----QA-VANYDSVEfgdKIVK 82
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAI----LDRN----ENPGAAAELQAINPKVKatfvQCdVTSWEQLA---AAFK 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNAGILRDVSFLKMTEL--DWDLIFKVHVKGAYAVTKAAWPYMRDQKY---GRIVVTSSNAGVHGNF 157
Cdd:cd05323  70 KAIEKFGRVDILINNAGILDEKSYLFAGKLppPWEKTIDVNLTGVINTTYLALHYMDKNKGgkgGVIVNIGSVAGLYPAP 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17568967 158 GQANYAAAKSALIGLSNSLAQEG-AKYNILANTLVPTagsrLTETVMPQNLVDALK 212
Cdd:cd05323 150 QFPVYSASKHGVVGFTRSLADLLeYKTGVRVNAICPG----FTNTPLLPDLVAKEA 201
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-214 1.05e-27

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 110.44  E-value: 1.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRfdGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtssSSSMADKVVQEIKSAGGQA------VANYDSV 74
Cdd:PRK08217   1 MDLK--DKVIVITGGAQGLGRAMAEYLAQKGAKLALIDL---------NQEKLEEAVAECGALGTEVrgyaanVTDEEDV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   75 EfgdKIVKTAIDNFGRIDIVINNAGILRDVSFLK---------MTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIV 145
Cdd:PRK08217  70 E---ATFAQIAEDFGQLNGLINNAGILRDGLLVKakdgkvtskMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSKGVI 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17568967  146 VTSSNAGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTagsrLTETVMpqnlVDALKPD 214
Cdd:PRK08217 147 INISSIARAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPG----VIETEM----TAAMKPE 207
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 7-219 1.78e-27

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 110.12  E-value: 1.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQAVANYDSVEFGD-----KIV 81
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEK---------AANVAQEINAEYGEGMAYGFGADATSeqsvlALS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNFGRIDIVINNAGILRDVsflKMTEL---DWDLIFKVHVKGAYAVTKAAWPYM-RDQKYGRIVVTSSNAGVHGNF 157
Cdd:PRK12384  73 RGVDEIFGRVDLLVYNAGIAKAA---FITDFqlgDFDRSLQVNLVGYFLCAREFSRLMiRDGIQGRIIQINSKSGKVGSK 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17568967  158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLvptagsrltetvMPQNLVDA-----LKPDYVTPL 219
Cdd:PRK12384 150 HNSGYSAAKFGGVGLTQSLALDLAEYGITVHSL------------MLGNLLKSpmfqsLLPQYAKKL 204
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-207 2.07e-27

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 109.59  E-value: 2.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsssssmadkvvQEIKSAGGQA------VANYDSV 74
Cdd:PRK08220   2 NAMDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQ------------------AFLTQEDYPFatfvldVSDAAAV 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   75 efgDKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH 154
Cdd:PRK08220  64 ---AQVCQRLLAETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHV 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17568967  155 GNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSrlTETVMPQNL 207
Cdd:PRK08220 141 PRIGMAAYGASKAALTSLAKCVGLELAPYGVRCNVVSP--GS--TDTDMQRTL 189
kduD TIGR01832
2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase ...
 7-192 4.88e-27

2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase (also called 2-keto-3-deoxygluconate oxidoreductase), a member of the family of short-chain-alcohol dehydrogenases (pfam00106). This protein has been characterized in Erwinia chrysanthemi as an enzyme of pectin degradation. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 188170 [Multi-domain]  Cd Length: 248  Bit Score: 108.31  E-value: 4.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967     7 GKVAIVTGAGGGLGKTYALELAKRGCKVVvndlggdrhGTSSSSsmADKVVQEIKSAGGQA---VANYDSVEFGDKIVKT 83
Cdd:TIGR01832   5 GKVALVTGANTGLGQGIAVGLAEAGADIV---------GAGRSE--PSETQQQVEALGRRFlslTADLSDIEAIKALVDS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQ-KYGRIVVTSSNAGVHGNFGQANY 162
Cdd:TIGR01832  74 AVEEFGHIDILVNNAGIIRRADAEEFSEKDWDDVMNVNLKSVFFLTQAAAKHFLKQgRGGKIINIASMLSFQGGIRVPSY 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 17568967   163 AAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:TIGR01832 154 TASKHAVAGLTKLLANEWAAKGINVNAIAP 183
PRK05650 PRK05650
SDR family oxidoreductase;
12-192 2.61e-26

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 107.05  E-value: 2.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   12 VTGAGGGLGKTYALELAKRGCKVV---VNDLGGDrhgtsssssmadKVVQEIKSAGGQA------VANYDSVE-FGDKIV 81
Cdd:PRK05650   5 ITGAASGLGRAIALRWAREGWRLAladVNEEGGE------------ETLKLLREAGGDGfyqrcdVRDYSQLTaLAQACE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KtaidNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:PRK05650  73 E----KWGGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSS 148

                        170       180       190
                 ....*....|....*....|....*....|.
gi 17568967  162 YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK05650 149 YNVAKAGVVALSETLLVELADDEIGVHVVCP 179
PRK07063 PRK07063
SDR family oxidoreductase;
1-192 4.82e-26

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 105.90  E-value: 4.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQAVANYDSVEFGDK- 79
Cdd:PRK07063   1 MMNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAAL---------AERAAAAIARDVAGARVLAVPADVTDAa 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 ----IVKTAIDNFGRIDIVINNAGI--LRDVsfLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGV 153
Cdd:PRK07063  72 svaaAVAAAEEAFGPLDVLVNNAGInvFADP--LAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAF 149

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 17568967  154 HGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07063 150 KIIPGCFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAP 188
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 2-194 5.31e-26

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 105.70  E-value: 5.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKSAGGQAVA---NYDSVEFGD 78
Cdd:PRK06113   6 NLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINAD---------AANHVVDEIQQLGGQAFAcrcDITSEQELS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KIVKTAIDNFGRIDIVINNAGILRDVSF-LKMTELDWdlIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNF 157
Cdd:PRK06113  77 ALADFALSKLGKVDILVNNAGGGGPKPFdMPMADFRR--AYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNI 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17568967  158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PRK06113 155 NMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGA 191
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 9-194 6.60e-26

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: 105.34  E-value: 6.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   9 VAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQAVA---NYDSVEFGDKIVKTAI 85
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEG---------AEAVAAAIQQAGGQAIGlecNVTSEQDLEAVVKATV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  86 DNFGRIDIVINNAGILRDVSF-LKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAA 164
Cdd:cd05365  72 SQFGGITILVNNAGGGGPKPFdMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGS 151

                       170       180       190
                ....*....|....*....|....*....|
gi 17568967 165 AKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:cd05365 152 SKAAVNHMTRNLAFDLGPKGIRVNAVAPGA 181
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 7-194 7.55e-26

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 105.58  E-value: 7.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsSSSSMADKVVQEIKSAGGQAVANYDSVEFGD---KIVKT 83
Cdd:PRK08936   7 GKVVVITGGSTGLGRAMAVRFGKEKAKVVINYR--------SDEEEANDVAEEIKKAGGEAIAVKGDVTVESdvvNLIQT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQ-KYGRIVVTSSnagVHGNFGQ--- 159
Cdd:PRK08936  79 AVKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSS---VHEQIPWplf 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17568967  160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PRK08936 156 VHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGA 190
PRK12743 PRK12743
SDR family oxidoreductase;
8-194 1.03e-25

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 105.12  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCkvvvnDLGGDRHgtsSSSSMADKVVQEIKSAGGQAVA---NYDSVEFGDKIVKTA 84
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGF-----DIGITWH---SDEEGAKETAEEVRSHGVRAEIrqlDLSDLPEGAQALDKL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   85 IDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQ-KYGRIVVTSSnagVHGNF---GQA 160
Cdd:PRK12743  75 IQRLGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITS---VHEHTplpGAS 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 17568967  161 NYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PRK12743 152 AYTAAKHALGGLTKAMALELVEHGILVNAVAPGA 185
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
7-192 1.08e-25

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 104.81  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKSAGGQAVANYDSVEFGDKI---VKT 83
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEE---------TAQAAADKLSKDGGKAIAVKADVSDRDQVfaaVRQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKY-GRIVVTSSNAGVHGNFGQANY 162
Cdd:PRK08643  73 VVDTFGDLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHgGKIINATSQAGVVGNPELAVY 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 17568967  163 AAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK08643 153 SSTKFAVRGLTQTAARDLASEGITVNAYAP 182
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 6-192 2.28e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 104.37  E-value: 2.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDlggdrhgtsSSSSMADKVVQEIKSAGGQA------VANYDSVefgDK 79
Cdd:PRK07097   9 KGKIALITGASYGIGFAIAKAYAKAGATIVFND---------INQELVDKGLAAYRELGIEAhgyvcdVTDEDGV---QA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 IVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQ 159
Cdd:PRK07097  77 MVSQIEKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETV 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 17568967  160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07097 157 SAYAAAKGGLKMLTKNIASEYGEANIQCNGIGP 189
PRK08589 PRK08589
SDR family oxidoreductase;
4-262 3.20e-25

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 104.09  E-value: 3.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsssSSMADKVVQEIKSAGGQA------VANYDSV-EF 76
Cdd:PRK08589   3 RLENKVAVITGASTGIGQASAIALAQEGAYVLAVDI----------AEAVSETVDKIKSNGGKAkayhvdISDEQQVkDF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 GDKIVKTaidnFGRIDIVINNAGILRDVSFLKMTELD-WDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHG 155
Cdd:PRK08589  73 ASEIKEQ----FGRVDVLFNNAGVDNAAGRIHEYPVDvFDKIMAVDMRGTFLMTKMLLPLMMEQG-GSIINTSSFSGQAA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  156 NFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTagsrlteTVMpqnlvdalkpdyvTPLVTYMVHDSFEESGKVF 235
Cdd:PRK08589 148 DLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPG-------TIE-------------TPLVDKLTGTSEDEAGKTF 207

                        250       260       270
                 ....*....|....*....|....*....|
gi 17568967  236 EAGAGW---YGTIQYYKSKGKVISHASADD 262
Cdd:PRK08589 208 RENQKWmtpLGRLGKPEEVAKLVVFLASDD 237
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 1-192 4.64e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 103.27  E-value: 4.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhGTSSSSSMADKVVQeiksaggQAVANYDSVEfgdKI 80
Cdd:PRK06057   1 LSQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEA-GKAAADEVGGLFVP-------TDVTDEDAVN---AL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGIL--RDVSFLKmTELD-WDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGN- 156
Cdd:PRK06057  70 FDTAAETYGSVDIAFNNAGISppEDDSILN-TGLDaWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSa 148

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK06057 149 TSQISYTASKGGVLAMSRELGVQFARQGIRVNALCP 184
PRK06114 PRK06114
SDR family oxidoreductase;
2-192 7.07e-25

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 102.55  E-value: 7.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrHGTSSSssmadkvVQEIKSAGGQAV---ANYDSVEFGD 78
Cdd:PRK06114   3 LFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTD-DGLAET-------AEHIEAAGRRAIqiaADVTSKADLR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:PRK06114  75 AAVARTEAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRG 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 17568967  159 --QANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK06114 155 llQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISP 190
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
4-192 7.36e-25

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 102.80  E-value: 7.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhGTSSSSSMADKVVqeiksAGGQAVANYDSVefgDKIVKT 83
Cdd:PRK07067   3 RLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPAR-ARLAALEIGPAAI-----AVSLDVTRQDSI---DRIVAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQ-KYGRIVVTSSNAGVHGNFGQANY 162
Cdd:PRK07067  74 AVERFGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGEALVSHY 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 17568967  163 AAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07067 154 CATKAAVISYTQSAALALIRHGINVNAIAP 183
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 2-192 8.76e-25

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: 102.76  E-value: 8.76e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtssssSMADKVVQEIKSAGGQAVA---NYDSVEFGD 78
Cdd:cd05355  21 SGKLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEE-------DDAEETKKLIEEEGRKCLLipgDLGDESFCR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  79 KIVKTAIDNFGRIDIVINNAGILRDV-SFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMrdQKYGRIVVTSSNAGVHGNF 157
Cdd:cd05355  94 DLVKEVVKEFGKLDILVNNAAYQHPQeSIEDITTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGSP 171

                       170       180       190
                ....*....|....*....|....*....|....*
gi 17568967 158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05355 172 HLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAP 206
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 7-202 9.65e-25

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: 102.09  E-value: 9.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssmADKVVQEIKSAGGQAVANYDSVEFGDKI---VKT 83
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPE----------IAEKVAEAAQGGPRALGVQCDVTSEAQVqsaFEQ 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKY-GRIVVTSSNAGVHGNFGQANY 162
Cdd:cd08943  71 AVLEFGGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIgGNIVFNASKNAVAPGPNAAAY 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17568967 163 AAAKSALIGLSNSLAQEGAKYNILANTLVPTA---GSRLTETV 202
Cdd:cd08943 151 SAAKAAEAHLARCLALEGGEDGIRVNTVNPDAvfrGSKIWEGV 193
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 7-202 1.06e-24

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: 102.52  E-value: 1.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggDRHGTSSsssmADKVVQEIKSAGGQAVANY----DSVEFGDKIVK 82
Cdd:cd09763   3 GKIALVTGASRGIGRGIALQLGEAGATVYIT----GRTILPQ----LPGTAEEIEARGGKCIPVRcdhsDDDEVEALFER 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNA-------GILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHG 155
Cdd:cd09763  75 VAREQQGRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEY 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17568967 156 NFGQAnYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTETV 202
Cdd:cd09763 155 LFNVA-YGVGKAAIDRMAADMAHELKPHGVAVVSLWP--GFVRTELV 198
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-192 1.46e-24

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 101.91  E-value: 1.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVvndlgGDRHgtssssSMADKVVQEIKSAGGQ---AVANYDSVEFGDKIV 81
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIV-----GVGV------AEAPETQAQVEALGRKfhfITADLIQQKDIDSIV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKA-AWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:PRK12481  75 SQAVEVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAvAKQFVKQGNGGKIINIASMLSFQGGIRVP 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17568967  161 NYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK12481 155 SYTASKSAVMGLTRALATELSQYNINVNAIAP 186
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 6-179 1.51e-24

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: 101.46  E-value: 1.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA---VANYDSVEFGDKIVK 82
Cdd:cd08934   2 QGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDR---------LEALADELEAEGGKAlvlELDVTDEQQVDAAVE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANY 162
Cdd:cd08934  73 RTVEALGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVY 152

                       170
                ....*....|....*..
gi 17568967 163 AAAKSALIGLSNSLAQE 179
Cdd:cd08934 153 NATKFGVNAFSEGLRQE 169
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 5-192 3.06e-24

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: 100.74  E-value: 3.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQAVA-------NYDSVEfg 77
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAI---------AGRKPEVLEAAAEEISSATGGRAHpiqcdvrDPEAVE-- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  78 dKIVKTAIDNFGRIDIVINNAGilrdVSFL----KMTELDWDLIFKVHVKGAYAVTKAAWPY-MRDQKYGRIVVTSSNAG 152
Cdd:cd05369  70 -AAVDETLKEFGKIDILINNAA----GNFLapaeSLSPNGFKTVIDIDLNGTFNTTKAVGKRlIEAKHGGSILNISATYA 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17568967 153 VHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05369 145 YTGSPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAP 184
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 10-207 3.21e-24

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 100.62  E-value: 3.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  10 AIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtSSSSSMADKVVQEIKSAGgqaVANYDSVefgDKIVKTAIDNFG 89
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDL-------PFVLLLEYGDPLRLTPLD---VADAAAV---REVCSRLLAEHG 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  90 RIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAAAKSAL 169
Cdd:cd05331  68 PIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAAL 147

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17568967 170 IGLSNSLAQEGAKYNILANTLVPtaGSrlTETVMPQNL 207
Cdd:cd05331 148 ASLSKCLGLELAPYGVRCNVVSP--GS--TDTAMQRTL 181
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 5-192 5.74e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 100.03  E-value: 5.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQAVA------NYDSVEfgd 78
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVL---------AARTAERLDEVAAEIDDLGRRALAvptditDEDQCA--- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KIVKTAIDNFGRIDIVINNAgiLRDVSFLKMTELDWDLI---FKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHG 155
Cdd:PRK07890  71 NLVALALERFGRVDALVNNA--FRVPSMKPLADADFAHWravIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHS 147

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17568967  156 NFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07890 148 QPKYGAYKMAKGALLAASQSLATELGPQGIRVNSVAP 184
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 7-185 5.80e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 100.50  E-value: 5.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVV--------VNDLgGDRHGtsssssmaDKVVQ-----EIKSAGGQAVAnyds 73
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVatardtatLADL-AEKYG--------DRLLPlaldvTDRAAVFAAVE---- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   74 vefgdkivkTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGV 153
Cdd:PRK08263  70 ---------TAVEHFGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGI 140

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17568967  154 HGNFGQANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK08263 141 SAFPMSGIYHASKWALEGMSEALAQEVAEFGI 172
PRK07831 PRK07831
SDR family oxidoreductase;
6-193 5.96e-24

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 100.11  E-value: 5.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGG-GLGKTYALELAKRGCKVVVNDLGGDRHGTSssssmadkvVQEIKSAGG-----QAVANYDSVEFGDK 79
Cdd:PRK07831  16 AGKVVLVTAAAGtGIGSATARRALEEGARVVISDIHERRLGET---------ADELAAELGlgrveAVVCDVTSEAQVDA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 IVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVtsSNAGVHG---N 156
Cdd:PRK07831  87 LIDAAVERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIV--NNASVLGwraQ 164

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPT 193
Cdd:PRK07831 165 HGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPS 201
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 5-194 7.28e-24

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 99.90  E-value: 7.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhGTSSSSSMADKVVQEIKSAggQAVANYDSVEFGDKIVKTA 84
Cdd:cd05330   1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEE--GLEAAKAALLEIAPDAEVL--LIKADVSDEAQVEAYVDAT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  85 IDNFGRIDIVINNAGIL-RDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYA 163
Cdd:cd05330  77 VEQFGRIDGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYA 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 17568967 164 AAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:cd05330 157 AAKHGVVGLTRNSAVEYGQYGIRINAIAPGA 187
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-192 7.48e-24

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 100.02  E-value: 7.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FD--GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA------VANYDSVEf 76
Cdd:PRK08213   8 FDlsGKTALVTGGSRGLGLQIAEALGEAGARVVL---------SARKAEELEEAAAHLEALGIDAlwiaadVADEADIE- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 gdKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKA-AWPYMRDQKYGRIVVTSSNAGVHG 155
Cdd:PRK08213  78 --RLAEETLERFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAvAKRSMIPRGYGRIINVASVAGLGG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17568967  156 N----FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK08213 156 NppevMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAP 196
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 5-192 8.00e-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: 99.79  E-value: 8.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA------VANYDSVEFGD 78
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLAL---------TGRDAERLEETRQSCLQAGVSEkkillvVADLTEEEGQD 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  79 KIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHGNFG 158
Cdd:cd05364  72 RIISTTLAKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPG 150

                       170       180       190
                ....*....|....*....|....*....|....
gi 17568967 159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05364 151 VLYYCISKAALDQFTRCTALELAPKGVRVNSVSP 184
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 6-187 1.13e-23

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: 102.45  E-value: 1.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   6 DGKVAIVTGAGGGLGKTYALELAKR-GCKVVVndLGgdRHGTSSSSSMADKVVQEIKSAGGQA------VANYDSVEfgd 78
Cdd:cd08953 204 PGGVYLVTGGAGGIGRALARALARRyGARLVL--LG--RSPLPPEEEWKAQTLAALEALGARVlyisadVTDAAAVR--- 276

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  79 KIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAwpymRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:cd08953 277 RLLEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQAL----ADEPLDFFVLFSSVSAFFGGAG 352

                       170       180
                ....*....|....*....|....*....
gi 17568967 159 QANYAAAKSALIGLSNSLAQEGAKYNILA 187
Cdd:cd08953 353 QADYAAANAFLDAFAAYLRQRGPQGRVLS 381
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 4-226 1.16e-23

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: 98.99  E-value: 1.16e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKSAG---GQAVANYDSVEfgdKI 80
Cdd:cd05341   2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDE---------EGQAAAAELGDAArffHLDVTDEDGWT---AV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:cd05341  70 VDTAREAFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALA 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 161 NYAAAKSALIGLSNSLAQEGAK--YNILANTLVPTagsrLTETVMPQNLVDAL---------------KPDYVTPLVTYM 223
Cdd:cd05341 150 AYNASKGAVRGLTKSAALECATqgYGIRVNSVHPG----YIYTPMTDELLIAQgemgnypntpmgragEPDEIAYAVVYL 225


                ...
gi 17568967 224 VHD 226
Cdd:cd05341 226 ASD 228
PRK07814 PRK07814
SDR family oxidoreductase;
4-200 1.82e-23

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 99.08  E-value: 1.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA---VANYDSVEFGDKI 80
Cdd:PRK07814   7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVLI---------AARTESQLDEVAEQIRAAGRRAhvvAADLAHPEATAGL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYM-RDQKYGRIVVTSSNAGVHGNFGQ 159
Cdd:PRK07814  78 AGQAVEAFGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMlEHSGGGSVINISSTMGRLAGRGF 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17568967  160 ANYAAAKSALIGLSNSLAQEGAKyNILANTLVPtaGSRLTE 200
Cdd:PRK07814 158 AAYGTAKAALAHYTRLAALDLCP-RIRVNAIAP--GSILTS 195
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
2-192 2.17e-23

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 98.41  E-value: 2.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtssssSMADKVVQEIKSAGGQAV---ANYDSVEFGD 78
Cdd:PRK08993   5 AFSLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINI-----------VEPTETIEQVTALGRRFLsltADLRKIDGIP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKA-AWPYMRDQKYGRIVVTSSNAGVHGNF 157
Cdd:PRK08993  74 ALLERAVAEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAaAKHFIAQGNGGKIINIASMLSFQGGI 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17568967  158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK08993 154 RVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAP 188
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 7-192 2.42e-23

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: 98.84  E-value: 2.42e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndLGGDRhgtssssSMADKVVQEIKSAGGQA--------VANYDSVEfgd 78
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVII--ACRNE-------EKGEEAAAEIKKETGNAkveviqldLSSLASVR--- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  79 KIVKTAIDNFGRIDIVINNAGILRdvSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:cd05327  69 QFAEEFLARFPRLDILINNAGIMA--PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPID 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17568967 159 QAN--------------YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05327 147 FNDldlennkeyspykaYGQSKLANILFTRELARRLEGTGVTVNALHP 194
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 7-237 6.06e-23

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 96.87  E-value: 6.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrHGTSSSSSMAdkVVQEIKSAGGQAVA------------NYDsv 74
Cdd:PRK08945  12 DRIILVTGAGDGIGREAALTYARHGATVIL-------LGRTEEKLEA--VYDEIEAAGGPQPAiipldlltatpqNYQ-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   75 EFGDKIVKtaidNFGRIDIVINNAGILRDVS-FLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGV 153
Cdd:PRK08945  81 QLADTIEE----QFGRLDGVLHNAGLLGELGpMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  154 HGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTAgsrlTETVM-----PQNLVDALK-PDYVTPLVTY-MVHD 226
Cdd:PRK08945 157 QGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGG----TRTAMrasafPGEDPQKLKtPEDIMPLYLYlMGDD 232

                        250
                 ....*....|.
gi 17568967  227 SFEESGKVFEA 237
Cdd:PRK08945 233 SRRKNGQSFDA 243
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
4-200 6.30e-23

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 97.10  E-value: 6.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgTSSSSSMADKVVQEIKSAGGQAV---ANYDSVEFGDKI 80
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVN--------YARSRKAAEETAEEIEALGRKALavkANVGDVEKIKEM 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNA--GILRDVsfLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSnAGVHGNFg 158
Cdd:PRK08063  73 FAQIDEEFGRLDVFVNNAasGVLRPA--MELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSS-LGSIRYL- 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 17568967  159 qANYAA---AKSALIGLSNSLAQEGAKYNILANTLvpTAGSRLTE 200
Cdd:PRK08063 149 -ENYTTvgvSKAALEALTRYLAVELAPKGIAVNAV--SGGAVDTD 190
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 4-205 6.58e-23

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: 97.13  E-value: 6.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA---VANYDSVEFGDKI 80
Cdd:cd05329   3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYT---------CARNQKELDECLTEWREKGFKVegsVCDVSSRSERQEL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 VKTAIDNF-GRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQ 159
Cdd:cd05329  74 MDTVASHFgGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17568967 160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVP-TAGSRLTETVMPQ 205
Cdd:cd05329 154 APYGATKGALNQLTRSLACEWAKDNIRVNAVAPwVIATPLVEPVIQQ 200
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 7-192 8.04e-23

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: 96.52  E-value: 8.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGqAVANYDSVEFGDKI-----V 81
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVIL---------ISRTQEKLDAVAKEIEEKYG-VETKTIAADFSAGDdiyerI 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  82 KTAIDNFgRIDIVINNAGILRD--VSFLKMTE-LDWDLIfKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:cd05356  71 EKELEGL-DIGILVNNVGISHSipEYFLETPEdELQDII-NVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPL 148

                       170       180       190
                ....*....|....*....|....*....|....
gi 17568967 159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05356 149 LATYSASKAFLDFFSRALYEEYKSQGIDVQSLLP 182
PRK08278 PRK08278
SDR family oxidoreductase;
1-192 1.13e-22

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 96.90  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRfdGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRH----GTSSSssmadkVVQEIKSAGGQAVA------N 70
Cdd:PRK08278   2 MSLS--GKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHpklpGTIHT------AAEEIEAAGGQALPlvgdvrD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   71 YDSVEfgdKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSS- 149
Cdd:PRK08278  74 EDQVA---AAVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPp 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 17568967  150 -NAGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK08278 151 lNLDPKWFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK07326 PRK07326
SDR family oxidoreductase;
5-200 1.68e-22

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 95.46  E-value: 1.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGG-----QAVANYDSVEfgdK 79
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAI---------TARDQKELEEAAAELNNKGNvlglaADVRDEADVQ---R 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 IVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHGNFGQ 159
Cdd:PRK07326  72 AVDAIVAAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTNFFAGG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17568967  160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTE 200
Cdd:PRK07326 151 AAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMP--GSVATH 189
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 4-194 2.70e-22

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: 95.67  E-value: 2.70e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsssSSMADKVVQEIKSAGGQAVA-NYDSVEFGD--KI 80
Cdd:cd08937   1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDR----------SELVHEVLAEILAAGDAAHVhTADLETYAGaqGV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDwDLIFKVH--VKGAYAVTKAAWPYMRDQKYGRIVVTSSNA--GVHgn 156
Cdd:cd08937  71 VRAAVERFGRVDVLINNVGGTIWAKPYEHYEEE-QIEAEIRrsLFPTLWCCRAVLPHMLERQQGVIVNVSSIAtrGIY-- 147

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17568967 157 fgQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:cd08937 148 --RIPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGG 183
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 4-232 2.71e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 95.46  E-value: 2.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhGTSSSSSMADKVVQEIKSAGGQAV---ANYDSVEFGDKI 80
Cdd:PRK06198   3 RLDGKVALVTGGTQGLGAAIARAFAERGAAGLV--------ICGRNAEKGEAQAAELEALGAKAVfvqADLSDVEDCRRV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKY-GRIV-VTSSNAgvHGnfG 158
Cdd:PRK06198  75 VAAADEAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVnIGSMSA--HG--G 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  159 Q---ANYAAAKSALIGLSNSLAQEGAKYNILANTLVP----TAGSRLTETVM---PQNLVDA----------LKPDYVTP 218
Cdd:PRK06198 151 QpflAAYCASKGALATLTRNAAYALLRNRIRVNGLNIgwmaTEGEDRIQREFhgaPDDWLEKaaatqpfgrlLDPDEVAR 230

                        250
                 ....*....|....
gi 17568967  219 LVTYMVHDsfeESG 232
Cdd:PRK06198 231 AVAFLLSD---ESG 241
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 7-192 3.19e-22

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: 95.05  E-value: 3.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGgdrhgtsssssmADKVVQEIKSAGGQA-----VANYDSVEfgdKIV 81
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLP------------NSPGETVAKLGDNCRfvpvdVTSEKDVK---AAL 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  82 KTAIDNFGRIDIVINNAGI---LRDVSFLKMTEL---DWDLIFKVHVKGAYAVTKAAWPYMR------DQKYGRIVVTSS 149
Cdd:cd05371  67 ALAKAKFGRLDIVVNCAGIavaAKTYNKKGQQPHsleLFQRVINVNLIGTFNVIRLAAGAMGknepdqGGERGVIINTAS 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17568967 150 NAGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05371 147 VAAFEGQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAP 189
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 9-182 3.32e-22

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: 94.76  E-value: 3.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   9 VAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA------VANYDSVEfgdKIVK 82
Cdd:cd05360   2 VVVITGASSGIGRATALAFAERGAKVVL---------AARSAEALHELAREVRELGGEAiavvadVADAAQVE---RAAD 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANY 162
Cdd:cd05360  70 TAVERFGRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAY 149

                       170       180
                ....*....|....*....|
gi 17568967 163 AAAKSALIGLSNSLAQEGAK 182
Cdd:cd05360 150 SASKHAVRGFTESLRAELAH 169
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 7-192 3.60e-22

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: 95.30  E-value: 3.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQ---AVANYDSVEFGDKIVKT 83
Cdd:cd08936  10 NKVALVTASTDGIGLAIARRLAQDGAHVVV---------SSRKQQNVDRAVATLQGEGLSvtgTVCHVGKAEDRERLVAT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  84 AIDNFGRIDIVINNAGI-LRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANY 162
Cdd:cd08936  81 AVNLHGGVDILVSNAAVnPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPY 160

                       170       180       190
                ....*....|....*....|....*....|
gi 17568967 163 AAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd08936 161 NVSKTALLGLTKNLAPELAPRNIRVNCLAP 190
PRK05855 PRK05855
SDR family oxidoreductase;
4-192 4.08e-22

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 98.90  E-value: 4.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggDRHGtsssssmADKVVQEIKSAGGQA------VANYDSVE-F 76
Cdd:PRK05855 312 PFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDI--DEAA-------AERTAELIRAAGAVAhayrvdVSDADAMEaF 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 GDKIVKTAidnfGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQ-KYGRIVVTSSNAGvhg 155
Cdd:PRK05855 383 AEWVRAEH----GVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAA--- 455

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17568967  156 nFGQAN----YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK05855 456 -YAPSRslpaYATSKAAVLMLSECLRAELAAAGIGVTAICP 495
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 8-222 5.61e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 94.97  E-value: 5.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVvndlggdrhGTSSSSSMAdkvvqeiKSAGGQA-----VANYDSVEFGdkiVK 82
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVF---------GTSRNPARA-------APIPGVElleldVTDDASVQAA---VD 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   83 TAIDNFGRIDIVINNAGilrdVSFLKMTE----LDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:PRK06179  66 EVIARAGRIDVLVNNAG----VGLAGAAEessiAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPY 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17568967  159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTagsrLTETVMPQNlvdALKPDyvTPLVTY 222
Cdd:PRK06179 142 MALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPA----YTKTNFDAN---APEPD--SPLAEY 196
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 1-192 9.90e-22

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 93.86  E-value: 9.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDlggdrhgtssSSSMADKVVQEIKSAGGQA---VANYDSVEFG 77
Cdd:PRK12823   2 MNQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVD----------RSELVHEVAAELRAAGGEAlalTADLETYAGA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 DKIVKTAIDNFGRIDIVINNAG---------------ILRDVSFLKMTELdWdlifkvhvkgayaVTKAAWPYMRDQKYG 142
Cdd:PRK12823  72 QAAMAAAVEAFGRIDVLINNVGgtiwakpfeeyeeeqIEAEIRRSLFPTL-W-------------CCRAVLPHMLAQGGG 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17568967  143 RIVVTSSNA--GVHgnfgQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK12823 138 AIVNVSSIAtrGIN----RVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAP 185
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-211 1.59e-21

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 93.25  E-value: 1.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRfdGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGtsssssmaDKVVQEIKSAGGQAV---ANYDSVEFG 77
Cdd:PRK06077   2 YSLK--DKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEM--------NETLKMVKENGGEGIgvlADVSTREGC 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 DKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIVVTSSNAGVHGNF 157
Cdd:PRK06077  72 ETLAKATIDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREG--GAIVNIASVAGIRPAY 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17568967  158 GQANYAAAKSALIGLSNSLAQEGAKyNILANTLVPTagsrLTETVMPQNLVDAL 211
Cdd:PRK06077 150 GLSIYGAMKAAVINLTKYLALELAP-KIRVNAIAPG----FVKTKLGESLFKVL 198
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 4-194 1.67e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 93.47  E-value: 1.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKSAGGQA--VANYDSVEfgdKIV 81
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEA---------LAKETAAELGLVVGGPldVTDPASFA---AFL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:PRK07825  70 DAVEADLGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMAT 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 17568967  162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PRK07825 150 YCASKHAVVGFTDAARLELRGTGVHVSVVLPSF 182
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 6-209 1.71e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 93.28  E-value: 1.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQAVANYDSVEFGDKiVKTAI 85
Cdd:PRK08085   8 AGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAER---------AELAVAKLRQEGIKAHAAPFNVTHKQE-VEAAI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   86 D----NFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:PRK08085  78 EhiekDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITP 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17568967  162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTEtvMPQNLVD 209
Cdd:PRK08085 158 YAASKGAVKMLTRGMCVELARHNIQVNGIAP--GYFKTE--MTKALVE 201
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-188 2.28e-21

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 92.85  E-value: 2.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgTSSSSSMADKVVQEIksaGGQAVA------NYDSVef 76
Cdd:PRK08642   1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVVVN--------YHQSEDAAEALADEL---GDRAIAlqadvtDREQV-- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 gDKIVKTAIDNFGR-IDIVINNAgiLRDVSF-----LKMTELDWDLI---FKVHVKGAYAVTKAAWPYMRDQKYGRIVvt 147
Cdd:PRK08642  68 -QAMFATATEHFGKpITTVVNNA--LADFSFdgdarKKADDITWEDFqqqLEGSVKGALNTIQAALPGMREQGFGRII-- 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17568967  148 ssNAGVhgNFGQA------NYAAAKSALIGLSNSLAQEGAKYNILAN 188
Cdd:PRK08642 143 --NIGT--NLFQNpvvpyhDYTTAKAALLGLTRNLAAELGPYGITVN 185
PRK07454 PRK07454
SDR family oxidoreductase;
8-194 2.47e-21

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 92.33  E-value: 2.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQAV------ANYDSVEFGdkiV 81
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLAL---------VARSQDALEALAAELRSTGVKAAaysidlSNPEAIAPG---I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:PRK07454  75 AELLEQFGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGA 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 17568967  162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PRK07454 155 YCVSKAALAAFTKCLAEEERSHGIRVCTITLGA 187
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-192 2.67e-21

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 92.54  E-value: 2.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGgdrhgtsssssmADKVVQEIKSAGGQA----VANYDSVEF 76
Cdd:PRK06463   1 YSMRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNS------------AENEAKELREKGVFTikcdVGNRDQVKK 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 GDKIVKtaiDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGV-HG 155
Cdd:PRK06463  69 SKEVVE---KEFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTA 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17568967  156 NFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK06463 146 AEGTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAP 182
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 7-237 2.83e-21

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: 92.25  E-value: 2.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrHGTSSSSsmADKVVQEIKSAGGQA----VANYD--SVEFGDKI 80
Cdd:cd05340   4 DRIILVTGASDGIGREAALTYARYGATVIL-------LGRNEEK--LRQVADHINEEGGRQpqwfILDLLtcTSENCQQL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 VKTAIDNFGRIDIVINNAGILRDVSFL-KMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNagvHGNFGQ 159
Cdd:cd05340  75 AQRIAVNYPRLDGVLHNAGLLGDVCPLsEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSS---VGRQGR 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 160 AN---YAAAKSALIGLSNSLAQEGAKYNILANTLVPTAgsrlTETVM---------PQNLVdalKPDYVTPLVTY-MVHD 226
Cdd:cd05340 152 ANwgaYAVSKFATEGL*QVLADEYQQRNLRVNCINPGG----TRTAMrasafptedPQKLK---TPADIMPLYLWlMGDD 224

                       250
                ....*....|.
gi 17568967 227 SFEESGKVFEA 237
Cdd:cd05340 225 SRRKTGMTFDA 235
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 7-192 4.59e-21

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: 92.01  E-value: 4.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEIKSAggQAVANYDSVEfgdKIVKTAID 86
Cdd:cd08930   2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALE--LDITSKESIK---ELIESYLE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  87 NFGRIDIVINNAGI---LRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHG----NFGQ 159
Cdd:cd08930  77 KFGRIDILINNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIApdfrIYEN 156

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17568967 160 AN------YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd08930 157 TQmyspveYSVIKAGIIHLTKYLAKYYADTGIRVNAISP 195
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 6-185 4.84e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 92.29  E-value: 4.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVvndlggdrhGTSSSssmADKVVQEIKSAGGQA------VANYDSVefgDK 79
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVV---------GTVRS---EAARADFEALHPDRAlarlldVTDFDAI---DA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 IVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQ 159
Cdd:PRK06180  68 VVADAEATFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGI 147

                        170       180
                 ....*....|....*....|....*.
gi 17568967  160 ANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK06180 148 GYYCGSKFALEGISESLAKEVAPFGI 173
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 8-192 5.26e-21

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 91.18  E-value: 5.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrHGTSSSSSmADKVVQEIKSAGGQAV---ANYDSVEFGDKIVKTA 84
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVV-------HYNRSEAE-AQRLKDELNALRNSAVlvqADLSDFAACADLVAAA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  85 IDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIV-VTSSNAGvHGNFGQANYA 163
Cdd:cd05357  73 FRAFGRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIInIIDAMTD-RPLTGYFAYC 151

                       170       180
                ....*....|....*....|....*....
gi 17568967 164 AAKSALIGLSNSLAQEGAKyNILANTLVP 192
Cdd:cd05357 152 MSKAALEGLTRSAALELAP-NIRVNGIAP 179
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-193 7.41e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 91.31  E-value: 7.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgtsssssmADKVVQEIKSAGGQAVANYDSVEFGDKI 80
Cdd:PRK07060   3 MAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVA----------------AARNAAALDRLAGETGCEPLRLDVGDDA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 -VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYM-RDQKYGRIVVTSSNAGVHGNFG 158
Cdd:PRK07060  67 aIRAALAAAGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMiAAGRGGSIVNVSSQAALVGLPD 146

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17568967  159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVPT 193
Cdd:PRK07060 147 HLAYCASKAALDAITRVLCVELGPHGIRVNSVNPT 181
PRK06484 PRK06484
short chain dehydrogenase; Validated
 7-214 1.98e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 93.38  E-value: 1.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEIKSAGGQAVanydsvefgDKIVKTAID 86
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQI---------REGFEQLHR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   87 NFGRIDIVINNAGIL-RDVSFLKMTEL-DWDLIFKVHVKGAYAVTKAAWPYMRDQKYGR-IVVTSSNAGVHGNFGQANYA 163
Cdd:PRK06484  76 EFGRIDVLVNNAGVTdPTMTATLDTTLeEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17568967  164 AAKSALIGLSNSLAQEGAKYNILANTLVPTagsrLTETVMPQNLVDALKPD 214
Cdd:PRK06484 156 ASKAAVISLTRSLACEWAAKGIRVNAVLPG----YVRTQMVAELERAGKLD 202
PRK07035 PRK07035
SDR family oxidoreductase;
6-201 3.13e-20

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 89.69  E-value: 3.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgtsSSSSMAD--KVVQEIKSAGGQAVA---NYDSVEFGDKI 80
Cdd:PRK07035   7 TGKIALVTGASRGIGEAIAKLLAQQGAHVIV-----------SSRKLDGcqAVADAIVAAGGKAEAlacHIGEMEQIDAL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELD-WDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQ 159
Cdd:PRK07035  76 FAHIRERHGRLDILVNNAAANPYFGHILDTDLGaFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQ 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 17568967  160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTagsrLTET 201
Cdd:PRK07035 156 GIYSITKAAVISMTKAFAKECAPFGIRVNALLPG----LTDT 193
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 1-193 4.76e-20

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: 88.68  E-value: 4.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVvndlggdrhGTSSSSSMADKVVQE---IKSAGGQaVANYDSVEFg 77
Cdd:cd05351   1 MELDFAGKRALVTGAGKGIGRATVKALAKAGARVV---------AVSRTQADLDSLVREcpgIEPVCVD-LSDWDATEE- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  78 dkivktAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKY-GRIVVTSSNAGVHGN 156
Cdd:cd05351  70 ------ALGSVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQRAL 143

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17568967 157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPT 193
Cdd:cd05351 144 TNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPT 180
PRK06182 PRK06182
short chain dehydrogenase; Validated
 8-185 5.15e-20

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 89.25  E-value: 5.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVvvndLGGDRHgtsssssmADKVvQEIKSAGGQA----VANYDSVEfgdKIVKT 83
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTV----YGAARR--------VDKM-EDLASLGVHPlsldVTDEASIK---AAVDT 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGI-----LRDVSflkMTELDWDliFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAG-VHGNF 157
Cdd:PRK06182  68 IIAEEGRIDVLVNNAGYgsygaIEDVP---IDEARRQ--FEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGkIYTPL 142

                        170       180
                 ....*....|....*....|....*...
gi 17568967  158 GqANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK06182 143 G-AWYHATKFALEGFSDALRLEVAPFGI 169
PRK08628 PRK08628
SDR family oxidoreductase;
1-192 5.91e-20

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 88.86  E-value: 5.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDlggdrhgtssSSSMADKVVQEIKSAGGQA------VANYDSV 74
Cdd:PRK08628   1 MDLNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFG----------RSAPDDEFAEELRALQPRAefvqvdLTDDAQC 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   75 EfgdKIVKTAIDNFGRIDIVINNAGILRDVS-------FLKMTELDWdlifkVHVkgaYAVTKAAWPYMRDQKyGRIVVT 147
Cdd:PRK08628  71 R---DAVEQTVAKFGRIDGLVNNAGVNDGVGleagreaFVASLERNL-----IHY---YVMAHYCLPHLKASR-GAIVNI 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 17568967  148 SSNAGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK08628 139 SSKTALTGQGGTSGYAAAKGAQLALTREWAVALAKDGVRVNAVIP 183
PRK06914 PRK06914
SDR family oxidoreductase;
7-185 6.04e-20

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 89.31  E-value: 6.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVvndlggdrhGTSSSSSMADKVVQEIKSAGGQA--------VANYDSVEFGD 78
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAKKGYLVI---------ATMRNPEKQENLLSQATQLNLQQnikvqqldVTDQNSIHNFQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KIVKTaidnFGRIDIVINNAG-----ILRDVSflkMTEldWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGV 153
Cdd:PRK06914  74 LVLKE----IGRIDLLVNNAGyanggFVEEIP---VEE--YRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGR 144

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17568967  154 HGNFGQANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK06914 145 VGFPGLSPYVSSKYALEGFSESLRLELKPFGI 176
PRK06194 PRK06194
hypothetical protein; Provisional
 4-234 6.11e-20

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 89.30  E-value: 6.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKSAGGQA------VANYDSVEfg 77
Cdd:PRK06194   3 DFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQD---------ALDRAVAELRAQGAEVlgvrtdVSDAAQVE-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 dKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYM-----RDQKY-GRIVVTSSNA 151
Cdd:PRK06194  72 -ALADAALERFGAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMlaaaeKDPAYeGHIVNTASMA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  152 GVHGNFGQANYAAAKSALIGLSNSL--------AQEGAkyNILANTLVPTaGSRLTETVMPQNLVDALKPdyVTP-LVTY 222
Cdd:PRK06194 151 GLLAPPAMGIYNVSKHAVVSLTETLyqdlslvtDQVGA--SVLCPYFVPT-GIWQSERNRPADLANTAPP--TRSqLIAQ 225

                        250
                 ....*....|..
gi 17568967  223 MVHDSFEESGKV 234
Cdd:PRK06194 226 AMSQKAVGSGKV 237
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
 325-429 6.45e-20

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 84.23  E-value: 6.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   325 FQEMADGVKADPTAVKTLK-SIVLYIITDGKnelGKFTLDFKSASPSVYLGDvknGEKANATVTVADSDFVDIAAGKLNA 403
Cdd:pfam02036   1 LNQLLARDPAARELLKKLNgKVIRFDLTDLG---LSLTLDLKDGGGRVLAGD---EGKADVTLSASDSDLLALATGKLNP 74

                          90       100
                  ....*....|....*....|....*.
gi 17568967   404 QKAFMSGKLKVKGNVMLLQKLQTVLE 429
Cdd:pfam02036  75 QKAFMQGKLKIEGDMELAQKLEGLLK 100
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 8-192 6.98e-20

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: 87.68  E-value: 6.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGC-KVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA------VANYDSVE-FGDK 79
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPgTVIL---------TARDVERGQAAVEKLRAEGLSVrfhqldVTDDASIEaAADF 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  80 IVKtaidNFGRIDIVINNAGILRDV-SFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVhgnfG 158
Cdd:cd05324  72 VEE----KYGGLDILVNNAGIAFKGfDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGS----L 143

                       170       180       190
                ....*....|....*....|....*....|....
gi 17568967 159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05324 144 TSAYGVSKAALNALTRILAKELKETGIKVNACCP 177
PRK06124 PRK06124
SDR family oxidoreductase;
6-201 8.91e-20

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 88.23  E-value: 8.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQAVA---NYDSVEFGDKIVK 82
Cdd:PRK06124  10 AGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAAT---------LEAAVAALRAAGGAAEAlafDIADEEAVAAAFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   83 TAIDNFGRIDIVINNAGI--------LRDVSFLKMTELDwdlifkvhVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH 154
Cdd:PRK06124  81 RIDAEHGRLDILVNNVGArdrrplaeLDDAAIRALLETD--------LVAPILLSRLAAQRMKRQGYGRIIAITSIAGQV 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17568967  155 GNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTET 201
Cdd:PRK06124 153 ARAGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAP--GYFATET 197
PRK07201 PRK07201
SDR family oxidoreductase;
7-179 9.02e-20

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 91.94  E-value: 9.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA------VANYDSVefgDKI 80
Cdd:PRK07201 371 GKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEA---------LDELVAEIRAKGGTAhaytcdLTDSAAV---DHT 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAG--ILRDV--SFLKMTelDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSnAGVHGN 156
Cdd:PRK07201 439 VKDILAEHGHVDYLVNNAGrsIRRSVenSTDRFH--DYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSS-IGVQTN 515

                        170       180
                 ....*....|....*....|....*.
gi 17568967  157 ---FgqANYAAAKSALIGLSNSLAQE 179
Cdd:PRK07201 516 aprF--SAYVASKAALDAFSDVAASE 539
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-194 1.17e-19

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 87.33  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsssssmadkvvQEIKSAGGQAvaNYDSVEFGDKiVKTA 84
Cdd:PRK06550   3 FMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDK------------------QDKPDLSGNF--HFLQLDLSDD-LEPL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   85 IDNFGRIDIVINNAGILRDV-SFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYA 163
Cdd:PRK06550  62 FDWVPSVDILCNTAGILDDYkPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYT 141

                        170       180       190
                 ....*....|....*....|....*....|.
gi 17568967  164 AAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PRK06550 142 ASKHALAGFTKQLALDYAKDGIQVFGIAPGA 172
PLN02253 PLN02253
xanthoxin dehydrogenase
 2-194 1.81e-19

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 87.96  E-value: 1.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsssssmADKVVQEI-KSAGGQAVANY--DSVEFGD 78
Cdd:PLN02253  13 SQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDL-------------QDDLGQNVcDSLGGEPNVCFfhCDVTVED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KI---VKTAIDNFGRIDIVINNAGI-------LRDVSFlkmteLDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTS 148
Cdd:PLN02253  80 DVsraVDFTVDKFGTLDIMVNNAGLtgppcpdIRNVEL-----SEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLC 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17568967  149 SNAGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PLN02253 155 SVASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYA 200
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 8-178 2.06e-19

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: 85.23  E-value: 2.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967      8 KVAIVTGAGGGLGKTYALELAKRGCKVVVndLGGdRHGTSSSSsmADKVVQEIKSAGGQA------VANYDSVEfgdKIV 81
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARRLV--LLS-RSGPDAPG--AAALLAELEAAGARVtvvacdVADRDALA---AVL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967     82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAwpymRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:smart00822  73 AAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELT----ADLPLDFFVLFSSIAGVLGSPGQAN 148

                          170
                   ....*....|....*..
gi 17568967    162 YAAAKSALiglsNSLAQ 178
Cdd:smart00822 149 YAAANAFL----DALAE 161
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 10-192 2.16e-19

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: 85.65  E-value: 2.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  10 AIVTGAGGGLGKTYALELAKRG-CKVVVNDlggdrhgtsssssmadkvvqeiksaggqavanydsvefgdkivktaidnf 88
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGsPKVLVVS-------------------------------------------------- 30

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  89 gRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAAAKSA 168
Cdd:cd02266  31 -RRDVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAA 109

                       170       180
                ....*....|....*....|....
gi 17568967 169 LIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd02266 110 LDGLAQQWASEGWGNGLPATAVAC 133
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
323-431 2.49e-19

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 82.65  E-value: 2.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 323 ALFQEMADGVKAdPTAVKTLKSIVLYIITDGKNelGKFTLDFKSASPSVYLGDVkngEKANATVTVADSDFVDIAAGKLN 402
Cdd:COG3255   2 EWAEALCEKLNA-ADAAAGWDGVVQFVITGEGG--GAYYLVIDDGKCTVSEGDD---DDADVTLTASYEDWKKLLTGELD 75

                        90       100
                ....*....|....*....|....*....
gi 17568967 403 AQKAFMSGKLKVKGNVMLLQKLQTVLEKA 431
Cdd:COG3255  76 PMTAFMTGKLKVEGDMGLAMKLMSLFKAL 104
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 5-192 3.35e-19

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 86.93  E-value: 3.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggDRHGTSSSssmadkvVQEIKSAGGQAVANYDSVEFGDKIVKTA 84
Cdd:PRK05876   4 FPGRGAVITGGASGIGLATGTEFARRGARVVLGDV--DKPGLRQA-------VNHLRAEGFDVHGVMCDVRHREEVTHLA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   85 IDNF---GRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKY-GRIVVTSSNAGVHGNFGQA 160
Cdd:PRK05876  75 DEAFrllGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTgGHVVFTASFAGLVPNAGLG 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17568967  161 NYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK05876 155 AYGVAKYGVVGLAETLAREVTADGIGVSVLCP 186
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-176 3.65e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 88.05  E-value: 3.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndLGGDRHGTsssssmaDKVVQEIKSAGGQA------VANYDSV 74
Cdd:PRK07109   2 MLKPIGRQVVVITGASAGVGRATARAFARRGAKVVL--LARGEEGL-------EALAAEIRAAGGEAlavvadVADAEAV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   75 EfgdKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVH 154
Cdd:PRK07109  73 Q---AAADRAEEELGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYR 149

                        170       180
                 ....*....|....*....|..
gi 17568967  155 GNFGQANYAAAKSALIGLSNSL 176
Cdd:PRK07109 150 SIPLQSAYCAAKHAIRGFTDSL 171
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 7-219 4.78e-19

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: 86.36  E-value: 4.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA----VANYDSVEFGDKIVK 82
Cdd:cd05322   2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSEN---------AEKVADEINAEYGEKaygfGADATNEQSVIALSK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYM-RDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:cd05322  73 GVDEIFKRVDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMiRDGIQGRIIQINSKSGKVGSKHNSG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17568967 162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPtagSRLTETVMPQNLVdalkPDYVTPL 219
Cdd:cd05322 153 YSAAKFGGVGLTQSLALDLAEHGITVNSLML---GNLLKSPMFQSLL----PQYAKKL 203
PRK05867 PRK05867
SDR family oxidoreductase;
5-204 5.02e-19

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 86.24  E-value: 5.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FD--GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlgGDRHgtsssSSMADKVVQEIKSAGGQAVANYDSVEFGDKI-- 80
Cdd:PRK05867   5 FDlhGKRALITGASTGIGKRVALAYVEAGAQVAI----AARH-----LDALEKLADEIGTSGGKVVPVCCDVSQHQQVts 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 -VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQ-KYGRIVVTSSNAGVHGNFG 158
Cdd:PRK05867  76 mLDQVTAELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIINVP 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17568967  159 Q--ANYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTETVMP 204
Cdd:PRK05867 156 QqvSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSP--GYILTELVEP 201
PRK07069 PRK07069
short chain dehydrogenase; Validated
 10-193 6.49e-19

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 85.92  E-value: 6.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   10 AIVTGAGGGLGKTYALELAKRGCKVVVNDLGgdrhgtssSSSMADKVVQEIKSAGGQAVA-----NYDSVEFGDKIVKTA 84
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDIN--------DAAGLDAFAAEINAAHGEGVAfaavqDVTDEAQWQALLAQA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   85 IDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAA 164
Cdd:PRK07069  74 ADAMGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNA 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 17568967  165 AKSALIGLSNSLAQEGAK--YNILANTLVPT 193
Cdd:PRK07069 154 SKAAVASLTKSIALDCARrgLDVRCNSIHPT 184
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 9-178 1.30e-18

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 84.82  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   9 VAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsSSSSMADKVVQEIKSAGGQAV---ANYDSVEFGDKIVKTAI 85
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINDL--------PDDDQATEVVAEVLAAGRRAIyfqADIGELSDHEALLDQAW 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  86 DNFGRIDIVINNAGI----LRDVsfLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQK------YGRIV-VTSSNAG-V 153
Cdd:cd05337  75 EDFGRLDCLVNNAGIavrpRGDL--LDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPdrfdgpHRSIIfVTSINAYlV 152

                       170       180
                ....*....|....*....|....*
gi 17568967 154 HGNFGQanYAAAKSALIGLSNSLAQ 178
Cdd:cd05337 153 SPNRGE--YCISKAGLSMATRLLAY 175
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 5-192 1.30e-18

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: 84.98  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSsssmadkvvQEIKSAGGQAVANYDSVEFGDKIVKTA 84
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATA---------AEIGPAACAISLDVTDQASIDRCVAAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  85 IDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQ-KYGRIVVTSSNAGVHGNFGQANYA 163
Cdd:cd05363  72 VDRWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYC 151

                       170       180
                ....*....|....*....|....*....
gi 17568967 164 AAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05363 152 ATKAAVISLTQSAGLNLIRHGINVNAIAP 180
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-177 2.36e-18

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 84.11  E-value: 2.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsssSSMADKVVQEIKSAggqaVANYDSVEFG-DKIVKt 83
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDI----------KEPSYNDVDYFKVD----VSNKEQVIKGiDYVIS- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 aidNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYA 163
Cdd:PRK06398  69 ---KYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYV 145

                        170
                 ....*....|....
gi 17568967  164 AAKSALIGLSNSLA 177
Cdd:PRK06398 146 TSKHAVLGLTRSIA 159
PRK09242 PRK09242
SDR family oxidoreductase;
4-203 3.48e-18

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 83.64  E-value: 3.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSA--GGQA---VANYDSVEFGD 78
Cdd:PRK09242   6 RLDGQTALITGASKGIGLAIAREFLGLGADVLI---------VARDADALAQARDELAEEfpEREVhglAADVSDDEDRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:PRK09242  77 AILDWVEDHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRS 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17568967  159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA-GSRLTETVM 203
Cdd:PRK09242 157 GAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYiRTPLTSGPL 202
PRK07577 PRK07577
SDR family oxidoreductase;
8-192 4.61e-18

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 82.85  E-value: 4.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVV--NDLGGDRHGTSSSSSMADKvvqeiksagGQAVAnydsvefgdkiVKTAI 85
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGiaRSAIDDFPGELFACDLADI---------EQTAA-----------TLAQI 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   86 DNFGRIDIVINNAGIlrdVSFLKMTELDWDLIFKV---HVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAgVHGNFGQANY 162
Cdd:PRK07577  64 NEIHPVDAIVNNVGI---ALPQPLGKIDLAALQDVydlNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-IFGALDRTSY 139

                        170       180       190
                 ....*....|....*....|....*....|
gi 17568967  163 AAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07577 140 SAAKSALVGCTRTWALELAEYGITVNAVAP 169
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 11-180 5.98e-18

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: 81.07  E-value: 5.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    11 IVTGAGGGLGKTYALELAKRGCKVVVndLGGDRHGtssSSSMADKVVQEIKSAGGQA------VANYDSVEfgdKIVKTA 84
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARHLV--LLSRSAA---PRPDAQALIAELEARGVEVvvvacdVSDPDAVA---ALLAEI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    85 IDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAwpymRDQKYGRIVVTSSNAGVHGNFGQANYAA 164
Cdd:pfam08659  76 KAEGPPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEAT----PDEPLDFFVLFSSIAGLLGSPGQANYAA 151

                         170
                  ....*....|....*.
gi 17568967   165 AKSALIGLSNSLAQEG 180
Cdd:pfam08659 152 ANAFLDALAEYRRSQG 167
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 5-197 6.23e-18

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 86.12  E-value: 6.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQAVANYDSV------EFGD 78
Cdd:COG3347 423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEA---------AEAAAAELGGGYGADAVDATDVdvtaeaAVAA 493

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  79 KIVKTAIDnFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQK-YGRIVVTSSNAGVHGNF 157
Cdd:COG3347 494 AFGFAGLD-IGGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGlGGSSVFAVSKNAAAAAY 572

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17568967 158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTAGSR 197
Cdd:COG3347 573 GAAAAATAKAAAQHLLRALAAEGGANGINANRVNPDAVLD 612
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 10-192 6.59e-18

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: 82.76  E-value: 6.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  10 AIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKS-AGGQAVANYDSVEFgdKIVKTAI--- 85
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDR---------LDELKAELLNpNPSVEVEILDVTDE--ERNQLVIael 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  86 -DNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAA 164
Cdd:cd05350  70 eAELGGLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSA 149

                       170       180
                ....*....|....*....|....*...
gi 17568967 165 AKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05350 150 SKAALSSLAESLRYDVKKRGIRVTVINP 177
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 4-192 1.02e-17

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 82.36  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQAVANYDSVEFGDKIVKT 83
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADN---------GAAVAASLGERARFIATDITDDAAIERAVAT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGILRDVSFlKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSnagVHGNFGQAN-- 161
Cdd:PRK08265  74 VVARFGRVDILVNLACTYLDDGL-ASSRADWLAALDVNLVSAAMLAQAAHPHLARGG-GAIVNFTS---ISAKFAQTGrw 148

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17568967  162 -YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK08265 149 lYPASKAAIRQLTRSMAMDLAPDGIRVNSVSP 180
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 6-192 1.13e-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: 82.20  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSssssmadkvVQEIKSAGGQA---VANYDSVEFGDKIVK 82
Cdd:cd08945   2 DSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATT---------VKELREAGVEAdgrTCDVRSVPEIEALVA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  83 TAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKA--AWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:cd08945  73 AAVARYGPIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEvlKAGGMLERGTGRIINIASTGGKQGVVHAA 152

                       170       180       190
                ....*....|....*....|....*....|..
gi 17568967 161 NYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd08945 153 PYSASKHGVVGFTKALGLELARTGITVNAVCP 184
PRK06123 PRK06123
SDR family oxidoreductase;
8-184 1.18e-17

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 82.13  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdRHGTSssssmADKVVQEIKSAGGQAVANYDSVEFGDKIVK--TAI 85
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLNYL---RNRDA-----AEAVVQAIRRQGGEALAVAADVADEADVLRlfEAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   86 D-NFGRIDIVINNAGIL-RDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGR---IVVTSSNAGVHGNFGQ- 159
Cdd:PRK06123  75 DrELGRLDALVNNAGILeAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSPGEy 154

                        170       180
                 ....*....|....*....|....*....
gi 17568967  160 ANYAAAKSAL----IGLSNSLAQEGAKYN 184
Cdd:PRK06123 155 IDYAASKGAIdtmtIGLAKEVAAEGIRVN 183
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 6-181 1.24e-17

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 82.31  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGktyaLELAKR----GCKVVVNDLggdrhgtssSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIV 81
Cdd:PRK06200   5 HGQVALITGGGSGIG----RALVERflaeGARVAVLER---------SAEKLASLRQRFGDHVLVVEGDVTSYADNQRAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNFGRIDIVINNAGILrDVsFLKMTELDWDLI-------FKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVH 154
Cdd:PRK06200  72 DQTVDAFGKLDCFVGNAGIW-DY-NTSLVDIPAETLdtafdeiFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFY 148

                        170       180
                 ....*....|....*....|....*..
gi 17568967  155 GNFGQANYAAAKSALIGLSNSLAQEGA 181
Cdd:PRK06200 149 PGGGGPLYTASKHAVVGLVRQLAYELA 175
PRK06949 PRK06949
SDR family oxidoreductase;
2-192 1.29e-17

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 82.12  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgtssSSSMADKVVQ---EIKSAGGQA------VANYD 72
Cdd:PRK06949   4 SINLEGKVALVTGASSGLGARFAQVLAQAGAKVVL------------ASRRVERLKElraEIEAEGGAAhvvsldVTDYQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   73 SVEFGdkiVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYM--------RDQKYGRI 144
Cdd:PRK06949  72 SIKAA---VAHAETEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMiarakgagNTKPGGRI 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17568967  145 VVTSSNAG--VHGNFGQanYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK06949 149 INIASVAGlrVLPQIGL--YCMSKAAVVHMTRAMALEWGRHGINVNAICP 196
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 5-192 1.59e-17

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 82.26  E-value: 1.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQAVA------NYDSVEfgd 78
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEK---------AEAVVAEIKAAGGEALAvkadvlDKESLE--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KIVKTAIDNFGRIDIVINNAG---------------ILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGR 143
Cdd:PRK08277  76 QARQQILEDFGPCDILINGAGgnhpkattdnefhelIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGN 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17568967  144 IVVTSSNAGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK08277 156 IINISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAP 204
PRK07074 PRK07074
SDR family oxidoreductase;
8-192 1.82e-17

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 81.74  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKSAGGQAVA-NYDSVEFGDKIVKTAID 86
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAA---------ALAAFADALGDARFVPVAcDLTDAASLAAALANAAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   87 NFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGnFGQANYAAAK 166
Cdd:PRK07074  74 ERGPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAA-LGHPAYSAAK 152

                        170       180
                 ....*....|....*....|....*.
gi 17568967  167 SALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07074 153 AGLIHYTKLLAVEYGRFGIRANAVAP 178
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 7-192 2.76e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 81.62  E-value: 2.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggDRHGTSSSSSMAdkVVQEiksaGGQAV---ANYDSVEFGDKIVKT 83
Cdd:PRK06701  46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYL--DEHEDANETKQR--VEKE----GVKCLlipGDVSDEAFCKDAVEE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGILRDVSFLK-MTELDWDLIFKVHVKGAYAVTKAAWPYMRdqKYGRIVVTSSNAGVHGNFGQANY 162
Cdd:PRK06701 118 TVRELGRLDILVNNAAFQYPQQSLEdITAEQLDKTFKTNIYSYFHMTKAALPHLK--QGSAIINTGSITGYEGNETLIDY 195

                        170       180       190
                 ....*....|....*....|....*....|
gi 17568967  163 AAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK06701 196 SATKGAIHAFTRSLAQSLVQKGIRVNAVAP 225
PRK06128 PRK06128
SDR family oxidoreductase;
4-192 3.11e-17

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 81.83  E-value: 3.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtSSSSSMADKVVQEIKSAGGQAVA---NYDSVEFGDKI 80
Cdd:PRK06128  52 RLQGRKALITGADSGIGRATAIAFAREGADIALNYL-------PEEEQDAAEVVQLIQAEGRKAVAlpgDLKDEAFCRQL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAG---ILRDVSflKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIVVTSSNAGVHGNF 157
Cdd:PRK06128 125 VERAVKELGGLDILVNIAGkqtAVKDIA--DITTEQFDATFKTNVYAMFWLCKAAIPHLPPG--ASIINTGSIQSYQPSP 200

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17568967  158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK06128 201 TLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAP 235
PRK08267 PRK08267
SDR family oxidoreductase;
12-185 3.79e-17

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 80.75  E-value: 3.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   12 VTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKSAGGQA----VANYDSVEfgdkivkTAIDN 87
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEA---------GLAALAAELGAGNAWTgaldVTDRAAWD-------AALAD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   88 F-----GRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANY 162
Cdd:PRK08267  70 FaaatgGRLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVY 149

                        170       180
                 ....*....|....*....|...
gi 17568967  163 AAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK08267 150 SATKFAVRGLTEALDLEWRRHGI 172
PRK07832 PRK07832
SDR family oxidoreductase;
8-202 4.05e-17

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 80.86  E-value: 4.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA-------VANYDSV-EFGDK 79
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADG---------LAQTVADARALGGTVpehraldISDYDAVaAFAAD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 IVKTaidnFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYM-RDQKYGRIVVTSSNAGVHGNFG 158
Cdd:PRK07832  72 IHAA----HGSMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMvAAGRGGHLVNVSSAAGLVALPW 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 17568967  159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA-GSRLTETV 202
Cdd:PRK07832 148 HAAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAvKTPLVNTV 192
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 5-192 1.15e-16

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: 79.81  E-value: 1.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQAVANYDSVEFGDKIVKTA 84
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEK---------GDKVAKEITALGGRAIALAADVLDRASLERAR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  85 ---IDNFGRIDIVINNAG--------------ILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVT 147
Cdd:cd08935  74 eeiVAQFGTVDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINI 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17568967 148 SSNAGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd08935 154 SSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAP 198
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 5-192 1.58e-16

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: 78.64  E-value: 1.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRH----GTSSSSSmadkvvQEIKSAGGQAVANYDSVEFGDKI 80
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHpklpGTIYTAA------EEIEAAGGKALPCIVDIRDEDQV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 ---VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSS----NA-- 151
Cdd:cd09762  75 raaVEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPplnlNPkw 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17568967 152 -GVHGNFGQANYAAAKSALiglsnSLAQEGAKYNILANTLVP 192
Cdd:cd09762 155 fKNHTAYTMAKYGMSMCVL-----GMAEEFKPGGIAVNALWP 191
PRK06947 PRK06947
SDR family oxidoreductase;
6-193 2.19e-16

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 78.31  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGgdrhgtssSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIV---K 82
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVGINYAR--------DAAAAEETADAVRAAGGRACVVAGDVANEADVIamfD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   83 TAIDNFGRIDIVINNAGI------LRDVSFLKMTEldwdlIFKVHVKGAYAVTKAAWPYMRDQKYGR---IVVTSSNAGV 153
Cdd:PRK06947  73 AVQSAFGRLDALVNNAGIvapsmpLADMDAARLRR-----MFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASR 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 17568967  154 HGN-FGQANYAAAKSAL----IGLSNSLAQEGAKYNILANTLVPT 193
Cdd:PRK06947 148 LGSpNEYVDYAGSKGAVdtltLGLAKELGPHGVRVNAVRPGLIET 192
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 8-192 4.24e-16

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: 4.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsSSSSMADKVVQEIKSAGGQAVANYDSVEfgdkivkTAIDN 87
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDED-----GLAALAAELGAENVVAGALDVTDRAAWA-------AALAD 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  88 F-----GRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANY 162
Cdd:cd08931  69 FaaatgGRLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVY 148

                       170       180       190
                ....*....|....*....|....*....|
gi 17568967 163 AAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd08931 149 SATKFAVRGLTEALDVEWARHGIRVADVWP 178
PRK12744 PRK12744
SDR family oxidoreductase;
7-192 5.56e-16

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 77.47  E-value: 5.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdRHGTSSSSSM-ADKVVQEIKSAGGQAVA------NYDSVEfgdK 79
Cdd:PRK12744   8 GKVVLIAGGAKNLGGLIARDLAAQGAKAVA------IHYNSAASKAdAEETVAAVKAAGAKAVAfqadltTAAAVE---K 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 IVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIV--VTSSNAGVHGnf 157
Cdd:PRK12744  79 LFDDAKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDN--GKIVtlVTSLLGAFTP-- 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17568967  158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK12744 155 FYSAYAGSKAPVEHFTRAASKEFGARGISVTAVGP 189
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 4-192 6.09e-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: 77.17  E-value: 6.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVvndlggdrhGTSSSSSMADKVVQEIKSAGGQAVANYD---SVEfgDKI 80
Cdd:cd05343   3 RWRGRVALVTGASVGIGAAVARALVQHGMKVV---------GCARRVDKIEALAAECQSAGYPTLFPYQcdlSNE--EQI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 VK--TAI-DNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKY--GRIVVTSSNAG--- 152
Cdd:cd05343  72 LSmfSAIrTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSMSGhrv 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17568967 153 VHGNFGQAnYAAAKSALIGLSNSLAQE--GAKYNILANTLVP 192
Cdd:cd05343 152 PPVSVFHF-YAATKHAVTALTEGLRQElrEAKTHIRATSISP 192
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 4-181 1.07e-15

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: 76.62  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmadkvVQEIKSAGGQAV----ANYDSVEFGDK 79
Cdd:cd05348   1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEK-------------VAELRADFGDAVvgveGDVRSLADNER 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  80 IVKTAIDNFGRIDIVINNAGI------LRDVSFLKMTELdWDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGV 153
Cdd:cd05348  68 AVARCVERFGKLDCFIGNAGIwdystsLVDIPEEKLDEA-FDELFHINVKGYILGAKAALPALYATE-GSVIFTVSNAGF 145

                       170       180
                ....*....|....*....|....*...
gi 17568967 154 HGNFGQANYAAAKSALIGLSNSLAQEGA 181
Cdd:cd05348 146 YPGGGGPLYTASKHAVVGLVKQLAYELA 173
PRK08219 PRK08219
SDR family oxidoreductase;
8-179 1.20e-15

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 75.74  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAkRGCKVVVndlggdrHGTSSSSsmADKVVQEIKSAGGQAV--ANYDSVEfgdkivkTAI 85
Cdd:PRK08219   4 PTALITGASRGIGAAIARELA-PTHTLLL-------GGRPAER--LDELAAELPGATPFPVdlTDPEAIA-------AAV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   86 DNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHGNFGQANYAAA 165
Cdd:PRK08219  67 EQLGRLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAAS 145

                        170
                 ....*....|....
gi 17568967  166 KSALIGLSNSLAQE 179
Cdd:PRK08219 146 KFALRALADALREE 159
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 7-192 1.68e-15

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: 75.69  E-value: 1.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggDRHGTSSSSSMADKVVQEIKSAggqaVANYDSVEFgdkIVKTAID 86
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADI--DEERGADFAEAEGPNLFFVHGD----VADETLVKF---VVYAMLE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  87 NFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHGNFGQANYAAAK 166
Cdd:cd09761  72 KLGRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAASK 150

                       170       180
                ....*....|....*....|....*.
gi 17568967 167 SALIGLSNSLAQEGAKYnILANTLVP 192
Cdd:cd09761 151 GGLVALTHALAMSLGPD-IRVNCISP 175
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 7-192 2.65e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 75.49  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA------VANYDSVEfgdKI 80
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVI---------TGRTKEKLEEAKLEIEQFPGQVltvqmdVRNPEDVQ---KM 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPY-MRDQKYGRIVVTSSNAGVHGNFGQ 159
Cdd:PRK07677  69 VEQIDEKFGRIDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYwIEKGIKGNIINMVATYAWDAGPGV 148

                        170       180       190
                 ....*....|....*....|....*....|....
gi 17568967  160 ANYAAAKSALIGLSNSLAQE-GAKYNILANTLVP 192
Cdd:PRK07677 149 IHSAAAKAGVLAMTRTLAVEwGRKYGIRVNAIAP 182
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 9-179 3.80e-15

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: 74.73  E-value: 3.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   9 VAIVTGAGGGLGKTYALELAKRGCKVVvndLGGDRHGTsssssmADKV-VQEIKSAGGQAVA------NYDSVEfgdKIV 81
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVA---LAARREAK------LEALlVDIIRDAGGSAKAvptdarDEDEVI---ALF 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:cd05373  69 DLIEEEIGPLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAA 148

                       170
                ....*....|....*...
gi 17568967 162 YAAAKSALIGLSNSLAQE 179
Cdd:cd05373 149 FAGAKFALRALAQSMARE 166
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 6-183 4.22e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 75.39  E-value: 4.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEiksaggqAVANYDSVEFGDKIVKTAI 85
Cdd:PRK05872   8 AGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLT-------VVADVTDLAAMQAAAEEAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   86 DNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHGNFGQANYAAA 165
Cdd:PRK05872  81 ERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPGMAAYCAS 159

                        170
                 ....*....|....*...
gi 17568967  166 KSALIGLSNSLAQEGAKY 183
Cdd:PRK05872 160 KAGVEAFANALRLEVAHH 177
PRK09730 PRK09730
SDR family oxidoreductase;
8-192 4.44e-15

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 74.50  E-value: 4.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgtsSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIVK--TAI 85
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQ--------QNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAmfTAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   86 D-NFGRIDIVINNAGILRDVSFLK-MTELDWDLIFKVHVKGAYAVTKAAWPYMRDQ---KYGRIVVTSSNAGVHGNFGQ- 159
Cdd:PRK09730  74 DqHDEPLAALVNNAGILFTQCTVEnLTAERINRVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPGEy 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 17568967  160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK09730 154 VDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRP 186
PRK12746 PRK12746
SDR family oxidoreductase;
5-192 4.56e-15

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 74.69  E-value: 4.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgTSSSSSMADKVVQEIKSAGGQAV---ANYDSVEFGDKIV 81
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIH--------YGRNKQAADETIREIESNGGKAFlieADLNSIDGVKKLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNF------GRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIVVTSSNAGVHG 155
Cdd:PRK12746  76 EQLKNELqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAEVRLG 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17568967  156 NFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK12746 154 FTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMP 190
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 1-192 4.77e-15

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: 74.88  E-value: 4.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGgdrhgtsssSSMADKVVQEIKSAG-GQAV---ANYDSVEF 76
Cdd:cd08933   3 SGLRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARG---------EAAGQALESELNRAGpGSCKfvpCDVTKEED 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  77 GDKIVKTAIDNFGRIDIVINNAGI------LRDVS---FLKMTELdwDLIfkvhvkGAYAVTKAAWPYMRdQKYGRIVVT 147
Cdd:cd08933  74 IKTLISVTVERFGRIDCLVNNAGWhpphqtTDETSaqeFRDLLNL--NLI------SYFLASKYALPHLR-KSQGNIINL 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17568967 148 SSNAGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd08933 145 SSLVGSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRVNCISP 189
PRK09072 PRK09072
SDR family oxidoreductase;
3-211 5.24e-15

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 74.59  E-value: 5.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrHGTSSSSsmADKVVQEIKSAGGQAVANYD-SVEFGDKIV 81
Cdd:PRK09072   1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLL-------VGRNAEK--LEALAARLPYPGRHRWVVADlTSEAGREAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:PRK09072  72 LARAREMGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYAS 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17568967  162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPtagsRLTETVMPQNLVDAL 211
Cdd:PRK09072 152 YCASKFALRGFSEALRRELADTGVRVLYLAP----RATRTAMNSEAVQAL 197
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-185 6.82e-15

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 74.23  E-value: 6.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssSSMADkVVQEIKSAGGQAVA---NYDSVEFGDKIVKTA 84
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDD-------EELAA-TQQELRALGVEVIFfpaDVADLSAHEAMLDAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   85 IDNFGRIDIVINNAGI--LRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQK------YGRIV-VTSSNAGVhG 155
Cdd:PRK12745  75 QAAWGRIDCLVNNAGVgvKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPepeelpHRSIVfVSSVNAIM-V 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 17568967  156 NFGQANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK12745 154 SPNRGEYCISKAGLSMAAQLFAARLAEEGI 183
PRK07775 PRK07775
SDR family oxidoreductase;
10-179 9.34e-15

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 74.02  E-value: 9.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   10 AIVTGAGGGLGKTYALELAKRGCKVVvndLGGDRhgTSSSSSMADKvvqeIKSAGGQAVANY------DSVefgDKIVKT 83
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVA---LGARR--VEKCEELVDK----IRADGGEAVAFPldvtdpDSV---KSFVAQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGilrDVSFLKMTELDWDLI---FKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:PRK07775  81 AEEALGEIEVLVSGAG---DTYFGKLHEISTEQFesqVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMG 157

                        170
                 ....*....|....*....
gi 17568967  161 NYAAAKSALIGLSNSLAQE 179
Cdd:PRK07775 158 AYGAAKAGLEAMVTNLQME 176
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 7-193 3.26e-14

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 71.59  E-value: 3.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggdrhgTSSSSSMADKVVQeiksaggqavANYDSVEFGDKIVKTAID 86
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDL------AENEEADASIIVL----------DSDSFTEQAKQVVASVAR 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  87 NFGRIDIVINNAG-----ILRDVSFLKmtelDWDLIFKVHVKGAYAVTKAAWPYMRdqKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:cd05334  65 LSGKVDALICVAGgwaggSAKSKSFVK----NWDLMWKQNLWTSFIASHLATKHLL--SGGLLVLTGAKAALEPTPGMIG 138

                       170       180       190
                ....*....|....*....|....*....|....
gi 17568967 162 YAAAKSALIGLSNSLAQE--GAKYNILANTLVPT 193
Cdd:cd05334 139 YGAAKAAVHQLTQSLAAEnsGLPAGSTANAILPV 172
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 8-185 3.29e-14

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: 71.93  E-value: 3.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVVvndLGGDRhgtsssssmADKVvQEIKSAGGQAVANYD---SVEFGDKI-VKT 83
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLI---LTGRR---------AERL-QELADELGAKFPVKVlplQLDVSDREsIEA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  84 AIDN----FGRIDIVINNAGILRDV-SFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:cd05346  68 ALENlpeeFRDIDILVNNAGLALGLdPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAG 147

                       170       180
                ....*....|....*....|....*..
gi 17568967 159 QANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:cd05346 148 GNVYCATKAAVRQFSLNLRKDLIGTGI 174
PRK07856 PRK07856
SDR family oxidoreductase;
2-201 4.78e-14

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 71.50  E-value: 4.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlGGDRHGTSSSSSMADKVVQEIKSAggqavanyDSVefgDKIV 81
Cdd:PRK07856   1 NLDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVV---CGRRAPETVDGRPAEFHAADVRDP--------DQV---AALV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKY-GRIVVTSSNAGVHGNFGQA 160
Cdd:PRK07856  67 DAIVERHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNIGSVSGRRPSPGTA 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17568967  161 NYAAAKSALIGLSNSLAQEGAKyNILANTLVPtaGSRLTET 201
Cdd:PRK07856 147 AYGAAKAGLLNLTRSLAVEWAP-KVRVNAVVV--GLVRTEQ 184
PRK09135 PRK09135
pteridine reductase; Provisional
 6-181 6.04e-14

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 71.11  E-value: 6.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrHGTSSSSSmADKVVQEIKSAGGQAVA-------NYDSVEfgd 78
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAI-------HYHRSAAE-ADALAAELNALRPGSAAalqadllDPDALP--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KIVKTAIDNFGRIDIVINNAGilrdvSFL-----KMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVvtsSNAGV 153
Cdd:PRK09135  74 ELVAACVAAFGRLDALVNNAS-----SFYptplgSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQR-GAIV---NITDI 144

                        170       180       190
                 ....*....|....*....|....*....|.
gi 17568967  154 HGNFGQANYA---AAKSALIGLSNSLAQEGA 181
Cdd:PRK09135 145 HAERPLKGYPvycAAKAALEMLTRSLALELA 175
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 9-187 8.23e-14

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: 70.78  E-value: 8.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   9 VAIVTGAGGGLGKTYALELAKRGCKVVVNDLG---GDRHGTSSSSSMADKVVqeiksaggQAVANYDSVEFGDKIVKTAI 85
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPSVVVLLArseEPLQELKEELRPGLRVT--------TVKADLSDAAGVEQLLEAIR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  86 DNFGRIDIVINNAGILRDVSFLKMTELD-WDLIFKVHVKGAYAVTKAAWPYMRDQKY-GRIVVTSSNAGVHGNFGQANYA 163
Cdd:cd05367  73 KLDGERDLLINNAGSLGPVSKIEFIDLDeLQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYC 152

                       170       180
                ....*....|....*....|....
gi 17568967 164 AAKSALIGLSNSLAQEGAKYNILA 187
Cdd:cd05367 153 SSKAARDMFFRVLAAEEPDVRVLS 176
PRK05866 PRK05866
SDR family oxidoreductase;
4-190 1.34e-13

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 70.93  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    4 RFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKSAGGQAVA------NYDSVefg 77
Cdd:PRK05866  37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARRED---------LLDAVADRITRAGGDAMAvpcdlsDLDAV--- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 DKIVKTAIDNFGRIDIVINNAG--ILRDVSflkmTELD-WDLIFKVHVKGAYA---VTKAAWPYMRDQKYGRIVVTSS-- 149
Cdd:PRK05866 105 DALVADVEKRIGGVDILINNAGrsIRRPLA----ESLDrWHDVERTMVLNYYAplrLIRGLAPGMLERGDGHIINVATwg 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 17568967  150 -NAGVHGNFGQanYAAAKSALIGLSNSLAQEGAKYNILANTL 190
Cdd:PRK05866 181 vLSEASPLFSV--YNASKAALSAVSRVIETEWGDRGVHSTTL 220
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 1-169 1.48e-13

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: 69.64  E-value: 1.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   1 MSLrfDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA--VANYDSVEfgd 78
Cdd:cd05370   1 MKL--TGNTVLITGGTSGIGLALARKFLEAGNTVII---------TGRREERLAEAKKELPNIHTIVldVGDAESVE--- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  79 KIVKTAIDNFGRIDIVINNAGILRDVSFLK--------MTELDWDLIFKVHvkgayaVTKAAWPYMRDQKYGRIVVTSSN 150
Cdd:cd05370  67 ALAEALLSEYPNLDILINNAGIQRPIDLRDpasdldkaDTEIDTNLIGPIR------LIKAFLPHLKKQPEATIVNVSSG 140

                       170
                ....*....|....*....
gi 17568967 151 AGVHGNFGQANYAAAKSAL 169
Cdd:cd05370 141 LAFVPMAANPVYCATKAAL 159
PRK07985 PRK07985
SDR family oxidoreductase;
2-192 1.68e-13

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 70.79  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGtsssssmADKVVQEIKSAGGQAV---ANYDSVEFGD 78
Cdd:PRK07985  44 SGRLKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEED-------AQDVKKIIEECGRKAVllpGDLSDEKFAR 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KIVKTAIDNFGRIDIVINNAGILRDVSFLK-MTELDWDLIFKVHVKGAYAVTKAAWPYMrdQKYGRIVVTSSNAGVHGNF 157
Cdd:PRK07985 117 SLVHEAHKALGGLDIMALVAGKQVAIPDIAdLTSEQFQKTFAINVFALFWLTQEAIPLL--PKGASIITTSSIQAYQPSP 194

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17568967  158 GQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07985 195 HLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAP 229
PRK06484 PRK06484
short chain dehydrogenase; Validated
 6-192 1.87e-13

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 72.19  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRH-------GTSSSSSMAD-KVVQEIKSAGGQAVANYdsvefg 77
Cdd:PRK06484 268 SPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAkklaealGDEHLSVQADiTDEAAVESAFAQIQARW------ 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 dkivktaidnfGRIDIVINNAGILRdvSFLKMTE---LDWDLIFKVHVKGAYAVTKAAWPYMRdqKYGRIVVTSSNAGvH 154
Cdd:PRK06484 342 -----------GRLDVLVNNAGIAE--VFKPSLEqsaEDFTRVYDVNLSGAFACARAAARLMS--QGGVIVNLGSIAS-L 405

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 17568967  155 GNFGQAN-YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK06484 406 LALPPRNaYCASKAAVTMLSRSLACEWAPAGIRVNTVAP 444
PRK06500 PRK06500
SDR family oxidoreductase;
1-192 2.44e-13

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 69.60  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSlRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhGTSSSSSMADKvvqeiKSAGGQAV---ANYDSVEFG 77
Cdd:PRK06500   1 MS-RLQGKTALITGGTSGIGLETARQFLAEGARVAIT-------GRDPASLEAAR-----AELGESALvirADAGDVAAQ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 DKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIVV-TSSNAGVhgn 156
Cdd:PRK06500  68 KALAQALAEAFGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANP--ASIVLnGSINAHI--- 142

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 17568967  157 fGQAN---YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK06500 143 -GMPNssvYAASKAALLSLAKTLSGELLPRGIRVNAVSP 180
PRK06720 PRK06720
hypothetical protein; Provisional
 1-117 3.78e-13

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 67.30  E-value: 3.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLggDRHGTSSSssmadkvVQEIKSAGGQAV-ANYDSVEFGD- 78
Cdd:PRK06720  10 MKMKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDI--DQESGQAT-------VEEITNLGGEALfVSYDMEKQGDw 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 17568967   79 -KIVKTAIDNFGRIDIVINNAGILR-DVSFLKMTELDWDLI 117
Cdd:PRK06720  81 qRVISITLNAFSRIDMLFQNAGLYKiDSIFSRQQENDSNVL 121
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 1-226 3.96e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 69.16  E-value: 3.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDlggdRHGTSSSSSMADKVVQEIKSAGGqavanydsvefGDKI 80
Cdd:PRK06523   3 FFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTTA----RSRPDDLPEGVEFVAADLTTAEG-----------CAAV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDVS--FLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGV---HG 155
Cdd:PRK06523  68 ARAVLERLGGVDILVHVLGGSSAPAggFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRlplPE 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  156 NFgqANYAAAKSALIGLSNSLAQEGAKYNILANTLVP-----TAGSRLTETVM----------PQNLVDAL--------- 211
Cdd:PRK06523 148 ST--TAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPgwietEAAVALAERLAeaagtdyegaKQIIMDSLggiplgrpa 225

                        250
                 ....*....|....*
gi 17568967  212 KPDYVTPLVTYMVHD 226
Cdd:PRK06523 226 EPEEVAELIAFLASD 240
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 8-192 1.09e-12

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: 67.15  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIVKTAIDN 87
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHAEGYRVGI---------CARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  88 FGRIDIVINNAGI--LRDVSflKMTELDWDL-IFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHGNFGQANYAA 164
Cdd:cd08929  72 FGGLDALVNNAGVgvMKPVE--ELTPEEWRLvLDTNLTGAFYCIHKAAPALLRRGG-GTIVNVGSLAGKNAFKGGAAYNA 148

                       170       180
                ....*....|....*....|....*...
gi 17568967 165 AKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd08929 149 SKFGLLGLSEAAMLDLREANIRVVNVMP 176
PRK09134 PRK09134
SDR family oxidoreductase;
8-123 1.90e-12

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 66.87  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrHgTSSSSSMADKVVQEIKSAGGQAVA------NYDSVEfgdKIV 81
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVAV-------H-YNRSRDEAEALAAEIRALGRRAVAlqadlaDEAEVR---ALV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 17568967   82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVK 123
Cdd:PRK09134  79 ARASAALGPITLLVNNASLFEYDSAASFTRASWDRHMATNLR 120
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 10-192 4.63e-12

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: 65.39  E-value: 4.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  10 AIVTGAGGGLGKTYALELAKRGCKVVV-----NDLGGDRHGTSSSSSMADKVVQEIKSAGGQAVANydsvefgdkiVKTA 84
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIatcrdPSAATELAALGASHSRLHILELDVTDEIAESAEA----------VAER 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  85 IDNfGRIDIVINNAGILRDVSFLK-MTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGN---FGQA 160
Cdd:cd05325  71 LGD-AGLDVLINNAGILHSYGPASeVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGDntsGGWY 149

                       170       180       190
                ....*....|....*....|....*....|..
gi 17568967 161 NYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05325 150 SYRASKAALNMLTKSLAVELKRDGITVVSLHP 181
PRK09291 PRK09291
SDR family oxidoreductase;
7-194 5.86e-12

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 65.40  E-value: 5.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVvndlggdrhGTSSSSSMADKVVQEIKSAGGQ-AVANYDSVEFGDKIVKTAI 85
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVI---------AGVQIAPQVTALRAEAARRGLAlRVEKLDLTDAIDRAQAAEW 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   86 DnfgrIDIVINNAGILRDVSflkMTELDWDLI---FKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAG-VHGNFGQAn 161
Cdd:PRK09291  73 D----VDVLLNNAGIGEAGA---VVDIPVELVrelFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGlITGPFTGA- 144

                        170       180       190
                 ....*....|....*....|....*....|...
gi 17568967  162 YAAAKSALIGLSNSLAQEGAKYNILANTLVPTA 194
Cdd:PRK09291 145 YCASKHALEAIAEAMHAELKPFGIQVATVNPGP 177
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 5-237 1.04e-11

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: 64.35  E-value: 1.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVV---VNDLGGDRHGTSSSSSMADKVVQEiksaggqaVANYDSvefgdkiV 81
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKKVyaaVRDPGSAAHLVAKYGDKVVPLRLD--------VTDPES-------I 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  82 KTAIDNFGRIDIVINNAGILRDVSFLKMTELDWD-LIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:cd05354  66 KAAAAQAKDVDVVINNAGVLKPATLLEEGALEALkQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMG 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 161 NYAAAKSALIGLSNSLAQEGAKYNILANTLVP-------TAGSRLTE---TVMPQNLVDALKPDYVTPLVTYM---VHDS 227
Cdd:cd05354 146 TYSASKSAAYSLTQGLRAELAAQGTLVLSVHPgpidtrmAAGAGGPKespETVAEAVLKALKAGEFHVFPDEMakqVKEA 225

                       250
                ....*....|
gi 17568967 228 FEESGKVFEA 237
Cdd:cd05354 226 YQSFPKNVVA 235
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 7-192 1.31e-11

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 64.33  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgTSSSSSMADKVVQEIKSAGGQAV---ANYDSVEfGDKIVKT 83
Cdd:PRK12747   4 GKVALVTGASRGIGRAIAKRLANDGALVAIH--------YGNRKEEAEETVYEIQSNGGSAFsigANLESLH-GVEALYS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDN-------FGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKygRIVVTSSNAGVHGN 156
Cdd:PRK12747  75 SLDNelqnrtgSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNS--RIINISSAATRISL 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK12747 153 PDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILP 188
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 9-192 1.33e-11

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: 64.13  E-value: 1.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   9 VAIVTGAGGGLGKTYALELAKRGCKVVVNDlggdrhgtSSSSSMADKVVQEIKSAGGQAVANYDSVEfgdkIVKTAIDNF 88
Cdd:cd05361   3 IALVTHARHFAGPASAEALTEDGYTVVCHD--------ASFADAAERQAFESENPGTKALSEQKPEE----LVDAVLQAG 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  89 GRIDIVINNAGILRDVSFL-KMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAAAKS 167
Cdd:cd05361  71 GAIDVLVSNDYIPRPMNPIdGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARA 150

                       170       180
                ....*....|....*....|....*
gi 17568967 168 ALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd05361 151 AAVALAESLAKELSRDNILVYAIGP 175
PRK07806 PRK07806
SDR family oxidoreductase;
6-151 1.37e-11

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 64.36  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGdrhgtsssSSMADKVVQEIKSAGGQAV---ANYDSVEFGDKIVK 82
Cdd:PRK07806   5 PGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQK--------APRANKVVAEIEAAGGRASavgADLTDEESVAALMD 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   83 TAIDNFGRIDIVINNAgilrdvSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIV-VTSSNA 151
Cdd:PRK07806  77 TAREEFGGLDALVLNA------SGGMESGMDEDYAMRLNRDAQRNLARAALPLMPAG--SRVVfVTSHQA 138
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 7-192 1.63e-11

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 64.04  E-value: 1.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGG-QAV-ANYDSVEFGDKIVKTA 84
Cdd:cd08942   6 GKIVLVTGGSRGIGRMIAQGFLEAGARVII---------SARKAEACADAAEELSAYGEcIAIpADLSSEEGIEALVARV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  85 IDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMR----DQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:cd08942  77 AERSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRaaatAENPARVINIGSIAGIVVSGLEN 156

                       170       180       190
                ....*....|....*....|....*....|...
gi 17568967 161 -NYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd08942 157 ySYGASKAAVHQLTRKLAKELAGEHITVNAIAP 189
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 1-192 2.94e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 63.63  E-value: 2.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLR-FD--GKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA-VANYDSVEf 76
Cdd:PRK07523   1 MSLNlFDltGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAK---------LAAAAESLKGQGLSAhALAFDVTD- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 gDKIVKTAIDNF----GRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAG 152
Cdd:PRK07523  71 -HDAVRAAIDAFeaeiGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQS 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 17568967  153 VHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07523 150 ALARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAP 189
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 3-192 3.16e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 63.44  E-value: 3.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgtSSSSSMADKVVQEIKSAGGQA------VANYDSVEF 76
Cdd:PRK07576   5 FDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVA---------SRSQEKVDAAVAQLQQAGPEGlgvsadVRDYAAVEA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 GdkiVKTAIDNFGRIDIVINNAGILRDVSFLKMTE------LDWDLIfkvhvkGAYAVTKAAWPYMRDQKYGRIVVTSSN 150
Cdd:PRK07576  76 A---FAQIADEFGPIDVLVSGAAGNFPAPAAGMSAngfktvVDIDLL------GTFNVLKAAYPLLRRPGASIIQISAPQ 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 17568967  151 AGVHGNFgQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07576 147 AFVPMPM-QAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVP 187
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 1-185 3.96e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 63.14  E-value: 3.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQAVA----NYDSVEF 76
Cdd:PRK06125   1 MDLHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHL---------VARDADALEALAADLRAAHGVDVAvhalDLSSPEA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 GDKIVKTAidnfGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGN 156
Cdd:PRK06125  72 REQLAAEA----GDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPD 147

                        170       180
                 ....*....|....*....|....*....
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK06125 148 ADYICGSAGNAALMAFTRALGGKSLDDGV 176
PRK12742 PRK12742
SDR family oxidoreductase;
5-192 4.69e-11

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 62.47  E-value: 4.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    5 FDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGgdrhgtssSSSMADKVVQEIKSAGGQA-VANYDSVefgdkivKT 83
Cdd:PRK12742   4 FTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAG--------SKDAAERLAQETGATAVQTdSADRDAV-------ID 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIVVTSSNAGVHGNF-GQANY 162
Cdd:PRK12742  69 VVRKSGALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG--GRIIIIGSVNGDRMPVaGMAAY 146

                        170       180       190
                 ....*....|....*....|....*....|
gi 17568967  163 AAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK12742 147 AASKSALQGMARGLARDFGPRGITINVVQP 176
PRK06139 PRK06139
SDR family oxidoreductase;
1-183 6.17e-11

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 63.20  E-value: 6.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDrhgtsssssMADKVVQEIKSAGGQAVANYDSVEFGDKI 80
Cdd:PRK06139   1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEE---------ALQAVAEECRALGAEVLVVPTDVTDADQV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 ---VKTAIDNFGRIDIVINNAGIlRDVSFLKMTELD-------WDLIFkvHVKGAYAVTkaawPYMRDQKYGRIVVTSSN 150
Cdd:PRK06139  72 kalATQAASFGGRIDVWVNNVGV-GAVGRFEETPIEaheqviqTNLIG--YMRDAHAAL----PIFKKQGHGIFINMISL 144

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17568967  151 agvhGNFGQANYAAAKSA----LIGLSNSLAQEGAKY 183
Cdd:PRK06139 145 ----GGFAAQPYAAAYSAskfgLRGFSEALRGELADH 177
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 11-174 9.37e-11

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: 63.07  E-value: 9.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  11 IVTGAGGGLGKTYALELAKRGCKVVVndLGGdRHGTSSSssmADKVVQEIKSAGGQAVanydsVEFGDKIVKTAI-DNFG 89
Cdd:cd08955 153 LITGGLGGLGLLVAEWLVERGARHLV--LTG-RRAPSAA---ARQAIAALEEAGAEVV-----VLAADVSDRDALaAALA 221

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  90 RIDI-------VINNAGILRDVSFLKMtelDWDLIFKV---HVKGAYAVTKAAwpymRDQKYGRIVVTSSNAGVHGNFGQ 159
Cdd:cd08955 222 QIRAslpplrgVIHAAGVLDDGVLANQ---DWERFRKVlapKVQGAWNLHQLT----QDLPLDFFVLFSSVASLLGSPGQ 294

                       170
                ....*....|....*
gi 17568967 160 ANYAAAKSALIGLSN 174
Cdd:cd08955 295 ANYAAANAFLDALAH 309
PRK08264 PRK08264
SDR family oxidoreductase;
7-185 1.21e-10

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 61.44  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlGGDRHgTSSSSSMADKVV---------QEIKSAGGQAvanydsvefG 77
Cdd:PRK08264   6 GKVVLVTGANRGIGRAFVEQLLARGAAKVY---AAARD-PESVTDLGPRVVplqldvtdpASVAAAAEAA---------S 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   78 DkivktaidnfgrIDIVINNAGILRDVSFLKMTELD-WDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGN 156
Cdd:PRK08264  73 D------------VTILVNNAGIFRTGSLLLEGDEDaLRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNF 140

                        170       180
                 ....*....|....*....|....*....
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK08264 141 PNLGTYSASKAAAWSLTQALRAELAPQGT 169
PRK06196 PRK06196
oxidoreductase; Provisional
 6-149 2.43e-10

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 61.24  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIK--SAGGQAVANYDSV-EFGDKIVK 82
Cdd:PRK06196  25 SGKTAIVTGGYSGLGLETTRALAQAGAHVIV---------PARRPDVAREALAGIDgvEVVMLDLADLESVrAFAERFLD 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17568967   83 TAidnfGRIDIVINNAGILrdVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSS 149
Cdd:PRK06196  96 SG----RRIDILINNAGVM--ACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSS 156
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 11-172 2.70e-10

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: 61.63  E-value: 2.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  11 IVTGAGGGLGKTYALELAKRGCKVVVndLGGdRHGtssSSSMADKVVQEIKSAGGQAVAnyDSVEFGD----KIVKTAID 86
Cdd:cd05274 154 LITGGLGGLGLLVARWLAARGARHLV--LLS-RRG---PAPRAAARAALLRAGGARVSV--VRCDVTDpaalAALLAELA 225

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  87 NFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTkAAWPyMRDQKYgrIVVTSSNAGVHGNFGQANYAAAK 166
Cdd:cd05274 226 AGGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLH-ELTP-DLPLDF--FVLFSSVAALLGGAGQAAYAAAN 301


                ....*.
gi 17568967 167 SALIGL 172
Cdd:cd05274 302 AFLDAL 307
PRK05717 PRK05717
SDR family oxidoreductase;
2-177 3.14e-10

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 60.29  E-value: 3.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssSSMADKVVQEIKSAGGQAVANYDSVEFGdkiV 81
Cdd:PRK05717   5 NPGHNGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRER------GSKVAKALGENAWFIAMDVADEAQVAAG---V 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNFGRIDIVINNAGIlRDVSFLKMTELD---WDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHGNFG 158
Cdd:PRK05717  76 AEVLGQFGRLDALVCNAAI-ADPHNTTLESLSlahWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSEPD 153

                        170
                 ....*....|....*....
gi 17568967  159 QANYAAAKSALIGLSNSLA 177
Cdd:PRK05717 154 TEAYAASKGGLLALTHALA 172
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 8-185 3.19e-10

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 60.55  E-value: 3.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELA---KRGCKVVvndlggdrhgtsssSSMADKVVQE--IKSAGGQAVANYDSVEF---GDK 79
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLAsdpSKRFKVY--------------ATMRDLKKKGrlWEAAGALAGGTLETLQLdvcDSK 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  80 IVKTAIDNF--GRIDIVINNAGI--LRDVSFLKMTELDwdLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHG 155
Cdd:cd09806  67 SVAAAVERVteRHVDVLVCNAGVglLGPLEALSEDAMA--SVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQG 144

                       170       180       190
                ....*....|....*....|....*....|
gi 17568967 156 NFGQANYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:cd09806 145 LPFNDVYCASKFALEGLCESLAVQLLPFNV 174
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 7-192 3.46e-10

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: 60.56  E-value: 3.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVV--NDLGgdrhgtsssssMADKVVQEIKSAGGQA--------VANYDSV-E 75
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMacRDMA-----------KCEEAAAEIRRDTLNHevivrhldLASLKSIrA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  76 FGDKIVKTAidnfGRIDIVINNAGILRDVSFLkmTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHG 155
Cdd:cd09807  70 FAAEFLAEE----DRLDVLINNAGVMRCPYSK--TEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAG 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17568967 156 --NFGQAN----------YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:cd09807 144 kiNFDDLNseksyntgfaYCQSKLANVLFTRELARRLQGTGVTVNALHP 192
PRK08703 PRK08703
SDR family oxidoreductase;
7-192 4.49e-10

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 59.56  E-value: 4.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGG--QAVANYDSVEFGDK----- 79
Cdd:PRK08703   6 DKTILVTGASQGLGEQVAKAYAAAGATVIL---------VARHQKKLEKVYDAIVEAGHpePFAIRFDLMSAEEKefeqf 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   80 IVKTAIDNFGRIDIVINNAGILRDVSFLK-MTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:PRK08703  77 AATIAEATQGKLDGIVHCAGYFYALSPLDfQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAY 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17568967  159 QANYAAAKSALIGLSNSLAQEGAKY-NILANTLVP 192
Cdd:PRK08703 157 WGGFGASKAALNYLCKVAADEWERFgNLRANVLVP 191
PRK06482 PRK06482
SDR family oxidoreductase;
7-185 9.89e-10

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 58.97  E-value: 9.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIVTGAGGGLGKTYALELAKRGCKVV--------VNDLGgDRHGTSSSSSMADkvvqeiksaggqaVANYDSVEfgd 78
Cdd:PRK06482   2 SKTWFITGASSGFGRGMTERLLARGDRVAatvrrpdaLDDLK-ARYGDRLWVLQLD-------------VTDSAAVR--- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 KIVKTAIDNFGRIDIVINNAGI--------LRDVSFLKmtELDWDLIfkvhvkGAYAVTKAAWPYMRDQKYGRIVVTSSN 150
Cdd:PRK06482  65 AVVDRAFAALGRIDVVVSNAGYglfgaaeeLSDAQIRR--QIDTNLI------GSIQVIRAALPHLRRQGGGRIVQVSSE 136

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17568967  151 AG--VHGNFGQanYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK06482 137 GGqiAYPGFSL--YHATKWGIEGFVEAVAQEVAPFGI 171
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-205 4.44e-09

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 57.01  E-value: 4.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRfdGKVAIVTGA--GGGLGKTYALELAKRGCKVVVND-LGGDRHGTSSSSSMADKVVQEIKSAGGQAVA----NYDS 73
Cdd:PRK12748   1 LPLM--KKIALVTGAsrLNGIGAAVCRRLAAKGIDIFFTYwSPYDKTMPWGMHDKEPVLLKEEIESYGVRCEhmeiDLSQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   74 VEFGDKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKA-AWPYMRDQKyGRIVVTSSNAG 152
Cdd:PRK12748  79 PYAPNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAfAKQYDGKAG-GRIINLTSGQS 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17568967  153 VHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPT------AGSRLTETVMPQ 205
Cdd:PRK12748 158 LGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGptdtgwITEELKHHLVPK 216
PRK07024 PRK07024
SDR family oxidoreductase;
7-192 7.72e-09

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 56.09  E-value: 7.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    7 GKVAIvTGAGGGLGKTYALELAKRGCKVvvnDLGGDRhgtsssSSMADKVVQEIKSAGGQAVANYDsVEFGDKIVKTA-- 84
Cdd:PRK07024   3 LKVFI-TGASSGIGQALAREYARQGATL---GLVARR------TDALQAFAARLPKAARVSVYAAD-VRDADALAAAAad 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   85 -IDNFGRIDIVINNAGILRDVsflkMTELDWDL-----IFKVHVKGAYAVTKaawPY---MRDQKYGRIVVTSSNAGVHG 155
Cdd:PRK07024  72 fIAAHGLPDVVIANAGISVGT----LTEEREDLavfreVMDTNYFGMVATFQ---PFiapMRAARRGTLVGIASVAGVRG 144

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17568967  156 NFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK07024 145 LPGAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAP 181
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 6-101 1.54e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 55.80  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVV--VNDLGGDRHGTS---SSSSMADKVVQEIKsaggqaVANYDSvefgdki 80
Cdd:PRK06197  15 SGRVAVVTGANTGLGYETAAALAAKGAHVVlaVRNLDKGKAAAAritAATPGADVTLQELD------LTSLAS------- 81

                         90       100
                 ....*....|....*....|....*
gi 17568967   81 VKTAIDNFG----RIDIVINNAGIL 101
Cdd:PRK06197  82 VRAAADALRaaypRIDLLINNAGVM 106
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 1-192 3.28e-08

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 54.48  E-value: 3.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQAV----ANYDSVEF 76
Cdd:PRK08339   2 LKIDLSGKLAFTTASSKGIGFGVARVLARAGADVIL---------LSRNEENLKKAREKIKSESNVDVsyivADLTKRED 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 GDKIVKTaIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGN 156
Cdd:PRK08339  73 LERTVKE-LKNIGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPI 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK08339 152 PNIALSNVVRISMAGLVRTLAKELGPKGITVNGIMP 187
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
11-156 3.71e-08

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 54.60  E-value: 3.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  11 IVTGAGGGLGKTYALELAKRGCKVVvndlGGDRHgtsssssmadkvvqeikSAGGQAVANYDSVEF--GDKIVKTAIDN- 87
Cdd:COG0451   3 LVTGGAGFIGSHLARRLLARGHEVV----GLDRS-----------------PPGAANLAALPGVEFvrGDLRDPEALAAa 61

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17568967  88 FGRIDIVINNAGILRDvsflkmTELDWDLIFKVHVKGAYAVTKAAwpymRDQKYGRIVVTSSnAGVHGN 156
Cdd:COG0451  62 LAGVDAVVHLAAPAGV------GEEDPDETLEVNVEGTLNLLEAA----RAAGVKRFVYASS-SSVYGD 119
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 7-169 5.17e-08

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: 53.63  E-value: 5.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGGQA--VANYDSVEfgdKIVKTA 84
Cdd:COG3967   5 GNTILITGGTSGIGLALAKRLHARGNTVII---------TGRREEKLEEAAAANPGLHTIVldVADPASIA---ALAEQV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  85 IDNFGRIDIVINNAGILRDVSFLKmTELDWDLI---FKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:COG3967  73 TAEFPDLNVLINNAGIMRAEDLLD-EAEDLADAereITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPT 151


                ....*...
gi 17568967 162 YAAAKSAL 169
Cdd:COG3967 152 YSATKAAL 159
PRK07062 PRK07062
SDR family oxidoreductase;
1-190 6.82e-08

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 53.51  E-value: 6.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhgtsssssmADKVVQEIKSAGGQA--------VANYD 72
Cdd:PRK07062   2 MQIQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEER---------LASAEARLREKFPGArllaarcdVLDEA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   73 SV-EFGDKIVktaiDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNA 151
Cdd:PRK07062  73 DVaAFAAAVE----ARFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLL 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 17568967  152 GVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTL 190
Cdd:PRK07062 149 ALQPEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSI 187
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 2-192 8.23e-08

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 53.72  E-value: 8.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    2 SLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEIKSAggqAVANYDSVEFGDKIV 81
Cdd:PLN02780  48 NLKKYGSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTV---VVDFSGDIDEGVKRI 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNFGrIDIVINNAGILRDVSFLkMTELDWDLI---FKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAG--VHGN 156
Cdd:PLN02780 125 KETIEGLD-VGVLINNVGVSYPYARF-FHEVDEELLknlIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAivIPSD 202

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 17568967  157 FGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PLN02780 203 PLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVP 238
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-192 1.46e-07

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 52.48  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    3 LRFDGKVAIVTGAG--GGLGKTYALELAKRGCKVVVNDLGG-DR---HGTSSSSSMadKVVQEIKSAGgQAVANYD---- 72
Cdd:PRK12859   2 NQLKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTYWTAyDKempWGVDQDEQI--QLQEELLKNG-VKVSSMEldlt 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   73 SVEFGDKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTkAAWPYMRDQKYG-RIVVTSSNA 151
Cdd:PRK12859  79 QNDAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLS-SQFARGFDKKSGgRIINMTSGQ 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17568967  152 GVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK12859 158 FQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINP 198
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 10-179 1.56e-07

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: 51.43  E-value: 1.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  10 AIVTGAGGGLGKTYALELAKRGCKVVvndlggdrhgTSSSSSmadkvvqeiksaGGQAV--ANYDSVefgdkivKTAIDN 87
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVI----------TAGRSS------------GDYQVdiTDEASI-------KALFEK 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  88 FGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIVVTSSNAGVHGNFGQANYAAAKS 167
Cdd:cd11731  52 VGHFDAIVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLNDG--GSITLTSGILAQRPIPGGAAAATVNG 129

                       170
                ....*....|..
gi 17568967 168 ALIGLSNSLAQE 179
Cdd:cd11731 130 ALEGFVRAAAIE 141
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 10-216 2.57e-07

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: 50.98  E-value: 2.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  10 AIVTGAGGGLGKTYALELAKRGCKVvvndLGGDRHGTSSSSSMADkvvqeiksAGGQAVanyDSVEFGDKIVKTAIDNFG 89
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRL----LLSGRDAGALAGLAAE--------VGALAR---PADVAAELEVWALAQELG 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  90 RIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQkyGRIVVTSSNAGVHGNFGQANYAAAKSAL 169
Cdd:cd11730  66 PLDLLVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAG--ARLVFLGAYPELVMLPGLSAYAAAKAAL 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17568967 170 IGLSNSLAQEGAKYNIlANTLVPTAGSRLTETV--MPQNlvdALKPDYV 216
Cdd:cd11730 144 EAYVEVARKEVRGLRL-TLVRPPAVDTGLWAPPgrLPKG---ALSPEDV 188
PRK05693 PRK05693
SDR family oxidoreductase;
8-206 2.99e-07

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 51.72  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVvndlggdrhgtSSSSSMADkvVQEIKSAGGQAV---ANyDSVEFGdKIVKTA 84
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVW-----------ATARKAED--VEALAAAGFTAVqldVN-DGAALA-RLAEEL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   85 IDNFGRIDIVINNAGI-----LRDVSFLKMTELdwdliFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSSNAGVHGNFGQ 159
Cdd:PRK05693  67 EAEHGGLDVLINNAGYgamgpLLDGGVEAMRRQ-----FETNVFAVVGVTRALFPLLRRSR-GLVVNIGSVSGVLVTPFA 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17568967  160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTA--------GSRLTETVMPQN 206
Cdd:PRK05693 141 GAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAiasqfasnASREAEQLLAEQ 195
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 7-180 3.12e-07

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-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); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP 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 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: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 52.45  E-value: 3.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGktyaLELAK----RGCKVVVNDLggdrhgtsSSSSMADKVVQEIKSAGGQAVA-NYDSVEFGDKI- 80
Cdd:cd08954 218 GKSYLITGGSGGLG----LEILKwlvkRGAVENIIIL--------SRSGMKWELELLIREWKSQNIKfHFVSVDVSDVSs 285

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  81 VKTAID------NFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYgrIVVTSSNAGVH 154
Cdd:cd08954 286 LEKAINlilnapKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDY--FVLFSSVSSIR 363

                       170       180
                ....*....|....*....|....*.
gi 17568967 155 GNFGQANYAAAKSALIGLSNSLAQEG 180
Cdd:cd08954 364 GSAGQCNYVCANSVLDSLSRYRKSIG 389
PRK05993 PRK05993
SDR family oxidoreductase;
8-185 9.70e-07

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 50.03  E-value: 9.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVVvndlggdrhgtssSSSMADKVVQEIKSAGGQAVA-NYDSVEFGDKIVKTAID 86
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVF-------------ATCRKEEDVAALEAEGLEAFQlDYAEPESIAALVAQVLE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   87 -NFGRIDIVINN-----AGILRDVSFLKMTELdwdliFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:PRK05993  72 lSGGRLDALFNNgaygqPGAVEDLPTEALRAQ-----FEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRG 146

                        170       180
                 ....*....|....*....|....*
gi 17568967  161 NYAAAKSALIGLSNSLAQEGAKYNI 185
Cdd:PRK05993 147 AYNASKFAIEGLSLTLRMELQGSGI 171
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 7-149 1.58e-06

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: 49.13  E-value: 1.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRgckvvvndlGGDRHGTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGD-----KIV 81
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKR---------GGTVHMVCRNQTRAEEARKEIETESGNQNIFLHIVDMSDpkqvwEFV 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17568967  82 KTAIDNFGRIDIVINNAGILrdVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSS 149
Cdd:cd09808  72 EEFKEEGKKLHVLINNAGCM--VNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSS 137
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 8-223 2.55e-06

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


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 48.81  E-value: 2.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVV--VNDLGGD-----RHGTSSSSsmadKVVQ-------EIKSAggqavANYDS 73
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLagCLTKNGPgakelRRVCSDRL----RTLQldvtkpeQIKRA-----AQWVK 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  74 VEFGDKivktaiDNFGridiVINNAGILrdvSFLKMTEL----DWDLIFKVHVKGAYAVTKAAWPYMRDQKyGRIVVTSS 149
Cdd:cd09805  72 EHVGEK------GLWG----LVNNAGIL---GFGGDEELlpmdDYRKCMEVNLFGTVEVTKAFLPLLRRAK-GRVVNVSS 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 150 NAGVHGNFGQANYAAAKSALIGLSNSLAQE----GAKYNILANTLVPTAGSRLTETV----------MPQNLVDALKPDY 215
Cdd:cd09805 138 MGGRVPFPAGGAYCASKAAVEAFSDSLRRElqpwGVKVSIIEPGNFKTGITGNSELWekqakklwerLPPEVKKDYGEDY 217


                ....*...
gi 17568967 216 VTPLVTYM 223
Cdd:cd09805 218 IDELKNKM 225
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 1-219 3.67e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 48.26  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    1 MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSssssmadkvVQEIKSAGGQAVANYDSVEFGD-- 78
Cdd:PRK05875   1 MQLSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAA---------AEEIEALKGAGAVRYEPADVTDed 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   79 ---KIVKTAIDNFGRIDIVINNAGILRDVSflKMTELD---WDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAG 152
Cdd:PRK05875  72 qvaRAVDAATAWHGRLHGVVHCAGGSETIG--PITQIDsdaWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAA 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17568967  153 --VHGNFGQanYAAAKSALIGLSNSLAQEGAKYNILANTLVPtaGSRLTETVMPQNLVDALKPDYV--TPL 219
Cdd:PRK05875 150 snTHRWFGA--YGVTKSAVDHLMKLAADELGPSWVRVNSIRP--GLIRTDLVAPITESPELSADYRacTPL 216
PRK08017 PRK08017
SDR family oxidoreductase;
8-202 4.91e-06

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 47.77  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVvvndLGGDRHGtsssssmADkvVQEIKSAGGQAVA----NYDSVEFGDKIVKT 83
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRV----LAACRKP-------DD--VARMNSLGFTGILldldDPESVERAADEVIA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   84 AIDNfgRIDIVINNAGI-----LRDVSFLKMTELdwdliFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFG 158
Cdd:PRK08017  70 LTDN--RLYGLFNNAGFgvygpLSTISRQQMEQQ-----FSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPG 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 17568967  159 QANYAAAKSALIGLSNSLAQEGAKYNILANTLVP-TAGSRLTETV 202
Cdd:PRK08017 143 RGAYAASKYALEAWSDALRMELRHSGIKVSLIEPgPIRTRFTDNV 187
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 7-99 7.82e-06

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 47.45  E-value: 7.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGkTYALELAK-RGCKVVvndlggdrhGTSSSSSMADKVvqeiKSAGGQAVANYDSVEFGDKIvkTAI 85
Cdd:COG0604 140 GETVLVHGAAGGVG-SAAVQLAKaLGARVI---------ATASSPEKAELL----RALGADHVIDYREEDFAERV--RAL 203

                        90
                ....*....|....
gi 17568967  86 DNFGRIDIVINNAG 99
Cdd:COG0604 204 TGGRGVDVVLDTVG 217
Alkyl_sulf_C pfam14864
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. ...
 359-431 1.41e-05

Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. Together with the N-terminal catalytic domain, this domain forms a hydrophobic chute and may recruit hydrophobic substrates.


Pssm-ID: 405542 [Multi-domain]  Cd Length: 124  Bit Score: 44.11  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   359 KFTLDFK-SASPSVYLGDVKNG----------EKANATVTVADSDFVDIAAGKLNAQKAFMSGKLKVKGNVMLLQKLQTV 427
Cdd:pfam14864  32 DLTINLVfPDVDEQYRLTLSNGvltyrkgrqaDDADATLTLTRADLLALLLGKATLGKLIAAGKIKVEGDPSALAELLSL 111


                  ....
gi 17568967   428 LEKA 431
Cdd:pfam14864 112 LDTF 115
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 12-129 3.00e-05

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 45.56  E-value: 3.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  12 VTGAGGGLGKTYALELAKRGCKVVVndlggdrHGTSSSSSMAdkVVQEIKSAGGQAVANYDSVEFGDKIVKTaIDNFGRI 91
Cdd:cd08951  12 ITGSSDGLGLAAARTLLHQGHEVVL-------HARSQKRAAD--AKAACPGAAGVLIGDLSSLAETRKLADQ-VNAIGRF 81

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17568967  92 DIVINNAGILRDvSFLKMTELDWDLIFKVHVKGAYAVT 129
Cdd:cd08951  82 DAVIHNAGILSG-PNRKTPDTGIPAMVAVNVLAPYVLT 118
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 11-223 3.84e-05

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 44.79  E-value: 3.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  11 IVTGAGGGLGKTYALELAKRGCKVVVNDLG-GDRHGtsssssmadkvvqEIKSAGGQAVAnydsvefgdkIVKTAIDNFG 89
Cdd:cd05328   3 VITGAASGIGAATAELLEDAGHTVIGIDLReADVIA-------------DLSTPEGRAAA----------IADVLARCSG 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  90 RIDIVINNAGILRDVSFlkmteldwDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNF------------ 157
Cdd:cd05328  60 VLDGLVNCAGVGGTTVA--------GLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAQdklelakalaag 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967 158 ---------------GQANYAAAKSALIGLSNSLA-QEGAKYNILANTLVPTAgsrlTETVMPQNLV-DALKPDYVTPLV 220
Cdd:cd05328 132 tearavalaehagqpGYLAYAGSKEALTVWTRRRAaTWLYGAGVRVNTVAPGP----VETPILQAFLqDPRGGESVDAFV 207


                ...
gi 17568967 221 TYM 223
Cdd:cd05328 208 TPM 210
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 8-132 4.26e-05

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 44.93  E-value: 4.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGKTYALELAKRGCKVVV--NDLGGDRHGTssssSMADkvvqeiksaGGQAVanydsVEFGDKIVKTAI 85
Cdd:cd05271   1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVpyRCEAYARRLL----VMGD---------LGQVL-----FVEFDLRDDESI 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17568967  86 DN-FGRIDIVINNAGILRD---VSFlkmteldWDlifkVHVKGAYAVTKAA 132
Cdd:cd05271  63 RKaLEGSDVVINLVGRLYEtknFSF-------ED----VHVEGPERLAKAA 102
PRK08340 PRK08340
SDR family oxidoreductase;
11-102 9.99e-05

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 43.64  E-value: 9.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   11 IVTGAGGGLGKTYALELAKRGCKVVVndlggdrhgTSSSSSMADKVVQEIKSAGG-QAV-ANYDSVEFGDKIVKTAIDNF 88
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVI---------SSRNEENLEKALKELKEYGEvYAVkADLSDKDDLKNLVKEAWELL 74

                         90
                 ....*....|....
gi 17568967   89 GRIDIVINNAGILR 102
Cdd:PRK08340  75 GGIDALVWNAGNVR 88
PRK07023 PRK07023
SDR family oxidoreductase;
10-181 1.11e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 43.46  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   10 AIVTGAGGGLGKTYALELAKRGCKVvvndLGGDRHGTSSSSSMADKVVQEIKS--AGGQAVANYdsvefgdkIVKTAIDN 87
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAV----LGVARSRHPSLAAAAGERLAEVELdlSDAAAAAAW--------LAGDLLAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   88 FGR---IDIVINNAGILRDVSFLkmTELDWDLI---FKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQAN 161
Cdd:PRK07023  72 FVDgasRVLLINNAGTVEPIGPL--ATLDAAAIaraVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSV 149

                        170       180
                 ....*....|....*....|
gi 17568967  162 YAAAKSALIGLSNSLAQEGA 181
Cdd:PRK07023 150 YCATKAALDHHARAVALDAN 169
PRK09186 PRK09186
flagellin modification protein A; Provisional
 6-192 1.73e-04

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 43.05  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    6 DGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRhGTSSSSSMADKVVQEIKSAGGQAVANYDSVEfgdKIVKTAI 85
Cdd:PRK09186   3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEA-LNELLESLGKEFKSKKLSLVELDITDQESLE---EFLSKSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   86 DNFGRIDIVINNA-------GilrdVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHG-NF 157
Cdd:PRK09186  79 EKYGKIDGAVNCAyprnkdyG----KKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVApKF 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 17568967  158 GQAN---------YAAAKSALIGLSNSLAQEGAKYNILANTLVP 192
Cdd:PRK09186 155 EIYEgtsmtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSP 198
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 12-132 4.76e-04

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 41.84  E-value: 4.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  12 VTGAGGGLGKTYALELAKRGCKVvvndlggdrHGTSSSSSMADKVvqeiksaggqAVANYDSVEFgdkivktAIDNFgRI 91
Cdd:cd05254   4 ITGATGMLGRALVRLLKERGYEV---------IGTGRSRASLFKL----------DLTDPDAVEE-------AIRDY-KP 56

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17568967  92 DIVINNAGILR-DVsflkmTELDWDLIFKVHVKGAYAVTKAA 132
Cdd:cd05254  57 DVIINCAAYTRvDK-----CESDPELAYRVNVLAPENLARAA 93
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-193 4.92e-04

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 41.67  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    3 LRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNdlggdrhgtSSSSSMADKVVQEIKSAGG--QAVANYDSVEFGDKI 80
Cdd:PRK05786   1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCIN---------SRNENKLKRMKKTLSKYGNihYVVGDVSSTESARNV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   81 VKTAIDNFGRIDIVINNAGILRDVSFLKMTELDwDLIFKvHVKGAYAVTKAAWPYMRdqKYGRIVVTSSNAGVHGNF-GQ 159
Cdd:PRK05786  72 IEKAAKVLNAIDGLVVTVGGYVEDTVEEFSGLE-EMLTN-HIKIPLYAVNASLRFLK--EGSSIVLVSSMSGIYKASpDQ 147

                        170       180       190
                 ....*....|....*....|....*....|....
gi 17568967  160 ANYAAAKSALIGLSNSLAQEGAKYNILANTLVPT 193
Cdd:PRK05786 148 LSYAVAKAGLAKAVEILASELLGRGIRVNGIAPT 181
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
8-179 1.55e-03

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 40.05  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    8 KVAIVTGAGGGLGKTYALELAKRGCKVV---------VNDLGGDRHG--TSSSSSMADkvvqeiksaggqaVANYDSvEF 76
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVIsisrtenkeLTKLAEQYNSnlTFHSLDLQD-------------VHELET-NF 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   77 GDKIVKTAIDNFGRIDIvINNAGILRDVSFLKMTELDwDLIFKVHVKGAYAV------TKAAWPYMRDQkygRIVVTSSN 150
Cdd:PRK06924  68 NEILSSIQEDNVSSIHL-INNAGMVAPIKPIEKAESE-ELITNVHLNLLAPMiltstfMKHTKDWKVDK---RVINISSG 142

                        170       180
                 ....*....|....*....|....*....
gi 17568967  151 AGVHGNFGQANYAAAKSALIGLSNSLAQE 179
Cdd:PRK06924 143 AAKNPYFGWSAYCSSKAGLDMFTQTVATE 171
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 7-132 1.64e-03

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 40.29  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGKTYALELAKRGCKVVvndlggdrHGTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIVKTAID 86
Cdd:cd05237   2 GKTILVTGGAGSIGSELVRQILKFGPKKL--------IVFDRDENKLHELVRELRSRFPHDKLRFIIGDVRDKERLRRAF 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17568967  87 NFGRIDIVInNAGILRDVSflkMTELDWDLIFKVHVKGAYAVTKAA 132
Cdd:cd05237  74 KERGPDIVF-HAAALKHVP---SMEDNPEEAIKTNVLGTKNVIDAA 115
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 9-167 1.71e-03

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 39.74  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967    9 VAIVTGAGGGLGKTYALELAKRGCKVVVNdlgGDRHgtsssssmadKVVQEIKSAGGQA-------VANYDSVEfgdKIV 81
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHKVIAT---GRRQ----------ERLQELKDELGDNlyiaqldVRNRAAIE---EML 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   82 KTAIDNFGRIDIVINNAGI-LRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQA 160
Cdd:PRK10538  66 ASLPAEWRNIDVLVNNAGLaLGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGN 145


                 ....*..
gi 17568967  161 NYAAAKS 167
Cdd:PRK10538 146 VYGATKA 152
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 8-144 1.83e-03

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: 40.06  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   8 KVAIVTGAGGGLGktyaLELAKRgckVVVNDLGGDRHG---TSSSSSMADKVVQEIKSAGGQAVANYD--SVEFGD---- 78
Cdd:cd08941   2 KVVLVTGANSGLG----LAICER---LLAEDDENPELTlilACRNLQRAEAACRALLASHPDARVVFDyvLVDLSNmvsv 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17568967  79 -KIVKTAIDNFGRIDIVINNAGILRDVSflkmteLDW-DLIFKVHVKGAYAVTkaaWPYMRDQKYGRI 144
Cdd:cd08941  75 fAAAKELKKRYPRLDYLYLNAGIMPNPG------IDWiGAIKEVLTNPLFAVT---NPTYKIQAEGLL 133
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
54-182 3.19e-03

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 38.92  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   54 DKVVQEIKSAGGQAVA--NYDSVEFGD--KIVKTAIDNfGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVT 129
Cdd:PRK07904  48 DAAVAQMKAAGASSVEviDFDALDTDShpKVIDAAFAG-GDVDVAIVAFGLLGDAEELWQNQRKAVQIAEINYTAAVSVG 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  130 KAAWPYMRDQKYGRIVVTSSNAGV---HGNFgqaNYAAAKSAL----IGLSNSLAQEGAK 182
Cdd:PRK07904 127 VLLGEKMRAQGFGQIIAMSSVAGErvrRSNF---VYGSTKAGLdgfyLGLGEALREYGVR 183
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 7-95 4.00e-03

Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176203 [Multi-domain]  Cd Length: 323  Bit Score: 39.02  E-value: 4.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967   7 GKVAIVTGAGGGLGkTYALELAKR-GCKVVvndlggdrhGTSSSSSMADKVvqeiKSAGGQAVANYDSVEFGDKiVKTAI 85
Cdd:cd08241 140 GETVLVLGAAGGVG-LAAVQLAKAlGARVI---------AAASSEEKLALA----RALGADHVIDYRDPDLRER-VKALT 204

                        90
                ....*....|
gi 17568967  86 DNFGrIDIVI 95
Cdd:cd08241 205 GGRG-VDVVY 213
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 9-105 4.71e-03

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 38.74  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967     9 VAIVTGAGGGLGKTYALELAKR----GCKVVV---NDLGGDRHGTSSSSSMADKVVQEIKSaggqAVANYDSVEFGDKIV 81
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLsarNDEALRQLKAEIGAERSGLRVVRVSL----DLGAEAGLEQLLKAL 77

                          90       100
                  ....*....|....*....|....*.
gi 17568967    82 KTAI--DNFGRIdIVINNAGILRDVS 105
Cdd:TIGR01500  78 RELPrpKGLQRL-LLINNAGTLGDVS 102
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
 145-172 5.18e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 39.17  E-value: 5.18e-03
                        10        20
                ....*....|....*....|....*...
gi 17568967 145 VVTSSNAGVHGNFGQANYAAAKSALIGL 172
Cdd:cd08956 325 VLFSSAAGVLGSPGQANYAAANAFLDAL 352
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
 11-153 6.05e-03

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 38.40  E-value: 6.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568967  11 IVTGAGGGLGKTYALELAKRGCKVvvndlggdrHGTSSSSSMADKVVQEIKSAGgqavaNYDSVEF--GDKIVKT-AIDN 87
Cdd:cd05227   3 LVTGATGFIASHIVEQLLKAGYKV---------RGTVRSLSKSAKLKALLKAAG-----YNDRLEFviVDDLTAPnAWDE 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17568967  88 FGR-IDIVINNAgilrdvSFLKMTELDW--DLIfKVHVKGAYAVTKAAwpymrdQKYG---RIVVTSSNAGV 153
Cdd:cd05227  69 ALKgVDYVIHVA------SPFPFTGPDAedDVI-DPAVEGTLNVLEAA------KAAGsvkRVVLTSSVAAV 127
 
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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