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Conserved domains on  [gi|1861134170|ref|WP_175979097|]
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SDR family oxidoreductase, partial [Burkholderia sp. BCC1047]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13394 super family cl32867
3-hydroxybutyrate dehydrogenase; Provisional
 1-156 5.86e-111

3-hydroxybutyrate dehydrogenase; Provisional


The actual alignment was detected with superfamily member PRK13394:

Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 315.68  E-value: 5.86e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK13394  107 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK13394  187 PGFVRTPLVDKQIPEQAKELGISEEEVVKKVMLGKTVDGVFTTVEDVAQTVLFLSSFPSAALTGQSFVVSHGWFMQ 262
 
Name Accession Description Interval E-value
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-156 5.86e-111

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 315.68  E-value: 5.86e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK13394  107 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK13394  187 PGFVRTPLVDKQIPEQAKELGISEEEVVKKVMLGKTVDGVFTTVEDVAQTVLFLSSFPSAALTGQSFVVSHGWFMQ 262
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
 1-156 1.15e-78

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 233.42  E-value: 1.15e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGgVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:TIGR01963 101 DWDRIIAVMLTSAFHTIRAALPHMKKQGWG-RIINIASAHGLVASPFKSAYVAAKHGLIGLTKVLALEVAEHGITVNAIC 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:TIGR01963 180 PGYVRTPLVEKQIADQAKTRGIPEEQVIREVMLKGQPTKRFVTVDEVAETALYLASDAAAQITGQAIVLDGGWTAQ 255
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 2-156 5.67e-41

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: 137.58  E-value: 5.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKddRG-GVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd08940   105 WDAIIALNLSAVFHTTRLALPHMKK--QGwGRIINIASVHGLVASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAIC 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:cd08940   183 PGWVLTPLVEKQISALAQKNGVPQEQAARELLLEKQPSKQFVTPEQLGDTAVFLASDAASQITGTAVSVDGGWTAQ 258
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-155 8.74e-40

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: 134.14  E-value: 8.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:COG1028   106 DWDRVLDVNLKGPFLLTRAALPHM-RERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVA 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  81 PGFVRTPLVDKQIPEQAkelgiseedvIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:COG1028   185 PGPIDTPMTRALLGAEE----------VREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLTA 249
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 1-153 3.27e-28

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: 104.05  E-value: 3.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:pfam13561  96 DFDRALDVNLYSLFLLAKAALPLM---KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAIS 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLVDkqipeqakelGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:pfam13561 173 PGPIKTLAAS----------GIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
 
Name Accession Description Interval E-value
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-156 5.86e-111

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 315.68  E-value: 5.86e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK13394  107 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK13394  187 PGFVRTPLVDKQIPEQAKELGISEEEVVKKVMLGKTVDGVFTTVEDVAQTVLFLSSFPSAALTGQSFVVSHGWFMQ 262
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 1-156 4.77e-93

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 270.22  E-value: 4.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12429  104 KWKKMIAIMLDGAFLTTKAALPIMKAQG-GGRIINMASVHGLVGSAGKAAYVSAKHGLIGLTKVVALEGATHGVTVNAIC 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK12429  183 PGYVDTPLVRKQIPDLAKERGISEEEVLEDVLLPLVPQKRFTTVEEIADYALFLASFAAKGVTGQAWVVDGGWTAQ 258
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
 1-156 1.15e-78

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 233.42  E-value: 1.15e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGgVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:TIGR01963 101 DWDRIIAVMLTSAFHTIRAALPHMKKQGWG-RIINIASAHGLVASPFKSAYVAAKHGLIGLTKVLALEVAEHGITVNAIC 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:TIGR01963 180 PGYVRTPLVEKQIADQAKTRGIPEEQVIREVMLKGQPTKRFVTVDEVAETALYLASDAAAQITGQAIVLDGGWTAQ 255
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 2-156 5.67e-41

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: 137.58  E-value: 5.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKddRG-GVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd08940   105 WDAIIALNLSAVFHTTRLALPHMKK--QGwGRIINIASVHGLVASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAIC 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:cd08940   183 PGWVLTPLVEKQISALAQKNGVPQEQAARELLLEKQPSKQFVTPEQLGDTAVFLASDAASQITGTAVSVDGGWTAQ 258
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-155 8.74e-40

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: 134.14  E-value: 8.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:COG1028   106 DWDRVLDVNLKGPFLLTRAALPHM-RERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVA 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  81 PGFVRTPLVDKQIPEQAkelgiseedvIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:COG1028   185 PGPIDTPMTRALLGAEE----------VREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLTA 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 1-149 4.04e-39

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: 132.02  E-value: 4.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05233    97 DWDRVLDVNLTGVFLLTRAALPHM-KKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVA 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861134170  81 PGFVRTPLVDKQIPEQAkelgiseedviKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVV 149
Cdd:cd05233   176 PGLVDTPMLAKLGPEEA-----------EKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPV 233
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-152 3.15e-29

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 107.45  E-value: 3.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12829  110 QWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAIL 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDV----IKKVMLGNTVdgvftTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK12829  190 PGIVRGPRMRRVIEARAQQLGIGLDEMeqeyLEKISLGRMV-----EPEDIAATALFLASPAARYITGQAISVDGN 260
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-155 2.67e-28

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 104.47  E-value: 2.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK05653  105 DWDRVIDVNLTGTFNVVRAALPPM-IKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGITVNAVA 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  81 PGFVRTPLVDKQIPEQAkelgiseEDVIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:PRK05653  184 PGFIDTDMTEGLPEEVK-------AEILKEIPLGR-----LGQPEEVANAVAFLASDAASYITGQVIPVNGGMYM 246
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 1-153 3.27e-28

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: 104.05  E-value: 3.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:pfam13561  96 DFDRALDVNLYSLFLLAKAALPLM---KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAIS 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLVDkqipeqakelGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:pfam13561 173 PGPIKTLAAS----------GIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-156 6.26e-28

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 103.73  E-value: 6.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK05557  106 DWDRVIDTNLTGVFNLTKAVARPMMKQ-RSGRIINISSVVGLMGNPGQANYAASKAGVIGFTKSLARELASRGITVNAVA 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKqIPEQAKELgiseedvikkvMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK05557  185 PGFIETDMTDA-LPEDVKEA-----------ILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHVNGGMVMG 248
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-156 6.67e-27

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 101.10  E-value: 6.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12825  107 EWDEVIDVNLSGVFHLLRAVVPPM-RKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGLVGLTKALARELAEYGITVNMVA 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKElgiseedvikkvMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK12825  186 PGDIDTDMKEATIEEAREA------------KDAETPLGRSGTPEDIARAVAFLCSDASDYITGQVIEVTGGVDVI 249
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 1-152 9.29e-27

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: 100.31  E-value: 9.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05333   100 DWDAVINVNLTGVFNVTQAVIRAMIKR-RSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAVA 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTPLVDKqIPEqakelgiseedVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05333   179 PGFIDTDMTDA-LPE-----------KVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGG 238
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-134 2.61e-26

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: 99.10  E-value: 2.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:COG4221   102 DWDRMIDVNVKGVLYVTRAALPAM-RARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIE 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  81 PGFVRTPLVDKQIPEQAKElgiSEEDVIKKVMLgntvdgvftTVQDVAQTVLFL 134
Cdd:COG4221   181 PGAVDTEFLDSVFDGDAEA---AAAVYEGLEPL---------TPEDVAEAVLFA 222
PRK12743 PRK12743
SDR family oxidoreductase;
1-156 7.09e-26

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 98.57  E-value: 7.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12743  103 EWRKIFTVDVDGAFLCSQIAARHMVKQGQGGRIINITSVHEHTPLPGASAYTAAKHALGGLTKAMALELVEHGILVNAVA 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDkQIPEQAKElgiSEEDVIKKVMLGNTvdgvfttvQDVAQTVLFLSAFPSAALTGQSFVVSHGwFMQ 156
Cdd:PRK12743  183 PGAIATPMNG-MDDSDVKP---DSRPGIPLGRPGDT--------HEIASLVAWLCSEGASYTTGQSLIVDGG-FML 245
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 1-153 9.84e-25

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: 95.50  E-value: 9.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVvIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05347   105 EWRDVIDVNLNGVFFVSQAVARHMIKQGHGKI-INICSLLSELGGPPVPAYAASKGGVAGLTKALATEWARHGIQVNAIA 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLVDKQIPEQAKelgisEEDVIKKVMLGNTVDgvfttVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:cd05347   184 PGYFATEMTEAVVADPEF-----NDDILKRIPAGRWGQ-----PEDLVGAAVFLASDASDYVNGQIIFVDGGW 246
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 1-155 1.27e-24

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 95.49  E-value: 1.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12384  104 DFDRSLQVNLVGYFLCAREFSRLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLM 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  81 PG-FVRTPLVDKQIPEQAKELGISEEDV----IKKVMLGNTVDgvfttVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:PRK12384  184 LGnLLKSPMFQSLLPQYAKKLGIKPDEVeqyyIDKVPLKRGCD-----YQDVLNMLLFYASPKASYCTGQSINVTGGQVM 258
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 1-97 1.41e-24

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 93.83  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:pfam00106 100 DWERVIDVNLTGVFNLTRAVLPAM-IKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAVA 178

                          90
                  ....*....|....*..
gi 1861134170  81 PGFVRTPLVDKQIPEQA 97
Cdd:pfam00106 179 PGGVDTDMTKELREDEG 195
PRK12826 PRK12826
SDR family oxidoreductase;
1-152 1.24e-22

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 89.98  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVH-SHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVV 79
Cdd:PRK12826  106 QWERVIDVNLTGTFLLTQAALPAL-IRAGGGRIVLTSSVAgPRVGYPGLAHYAASKAGLVGFTRALALELAARNITVNSV 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  80 CPGFVRTPLVDKQIPEQAKElgiseedvikkVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK12826  185 HPGGVDTPMAGNLGDAQWAE-----------AIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQTLPVDGG 246
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 1-152 2.24e-21

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: 86.39  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd08944   101 VWDQTMAINLRGTFLCCRHAAPRM-IARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALA 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDvikkvMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd08944   180 PGLIDTPLLLAKLAGFEGALGPGGFH-----LLIHQLQGRLGRPEDVAAAVVFLLSDDASFITGQVLCVDGG 246
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 1-152 2.55e-21

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: 86.67  E-value: 2.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05358   104 DWNKVIDVNLTGQFLCAREAIKRFRKSKIKGKIINMSSVHEKIPWPGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIA 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTPlvdkqIPEQAKELGISEEDVIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05358   184 PGAINTP-----INAEAWDDPEQRADLLSLIPMGR-----IGEPEEIAAAAAWLASDEASYVTGTTLFVDGG 245
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 1-152 2.99e-21

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: 86.28  E-value: 2.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05366   103 DLKKVYAVNVFGVLFGIQAAARQFKKLGHGGKIINASSIAGVQGFPNLGAYSASKFAVRGLTQTAAQELAPKGITVNAYA 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTPLVDkQIPEQAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05366   183 PGIVKTEMWD-YIDEEVGEIAGKPEGEGFAEFSSSIPLGRLSEPEDVAGLVSFLASEDSDYITGQTILVDGG 253
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-153 3.83e-21

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 86.05  E-value: 3.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK05565  106 EWDRVIDVNLTGVMLLTRYALPYM-IKRKSGVIVNISSIWGLIGASCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVA 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLVdkQIPEQAKELGISEEDVIkkvmlgntvdGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK05565  185 PGAIDTEMW--SSFSEEDKEGLAEEIPL----------GRLGKPEEIAKVVLFLASDDASYITGQIITVDGGW 245
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 1-155 1.28e-20

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: 84.82  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05322   103 DFDRSLQVNLVGYFLCAREFSKLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLM 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  81 PG-FVRTPLVDKQIPEQAKELGISEEDV----IKKVMLGNTVDgvfttVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:cd05322   183 LGnLLKSPMFQSLLPQYAKKLGIKESEVeqyyIDKVPLKRGCD-----YQDVLNMLLFYASPKASYCTGQSINITGGQVM 257
PRK06398 PRK06398
aldose dehydrogenase; Validated
 1-152 1.63e-20

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 84.50  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKhNVRSHVVC 80
Cdd:PRK06398   95 EWDRIINVNVNGIFLMSKYTIPYMLKQ-DKGVIINIASVQSFAVTRNAAAYVTSKHAVLGLTRSIAVDYAP-TIRCVAVC 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  81 PGFVRTPLVDKQipeQAKELGISEEDVIKKVM-LGNTVD-GVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK06398  173 PGSIRTPLLEWA---AELEVGKDPEHVERKIReWGEMHPmKRVGKPEEVAYVVAFLASDLASFITGECVTVDGG 243
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
1-149 6.43e-20

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 85.28  E-value: 6.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK08324  521 DWRRSFDVNATGHFLVAREAVRIMKAQGLGGSIVFIASKNAVNPGPNFGAYGAAKAAELHLVRQLALELGPDGIRVNGVN 600

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PG--FVRTPLVDKQ-IPEQAKELGISEEDVIKKVMLGNTVdGVFTTVQDVAQTVLFLSAFPSAALTGQSFVV 149
Cdd:PRK08324  601 PDavVRGSGIWTGEwIEARAAAYGLSEEELEEFYRARNLL-KREVTPEDVAEAVVFLASGLLSKTTGAIITV 671
PRK06138 PRK06138
SDR family oxidoreductase;
1-153 8.15e-20

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 82.51  E-value: 8.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06138  104 DWDAVMRVNVGGVFLWAKYAIPIMQRQ-GGGSIVNTASQLALAGGRGRAAYVASKGAIASLTRAMALDHATDGIRVNAVA 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKVMlgntvdGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK06138  183 PGTIDTPYFRRIFARHADPEALREALRARHPM------NRFGTAEEVAQAALFLASDESSFATGTTLVVDGGW 249
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-111 1.04e-19

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 82.22  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:COG0300   105 DLRRVFEVNVFGPVRLTRALLPLM-RARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRVTAVC 183

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELgISEEDVIKKV 111
Cdd:COG0300   184 PGPVDTPFTARAGAPAGRPL-LSPEEVARAI 213
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 1-144 3.35e-19

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: 80.90  E-value: 3.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd08943   100 DWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLARCLALEGGEDGIRVNTVN 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861134170  81 P-GFVRTPLVDKQIPEQA--KELGISEEDVIKKVMLGNTVdgvftTVQDVAQTVLFLSAFPSAALTG 144
Cdd:cd08943   180 PdAVFRGSKIWEGVWRAAraKAYGLLEEEYRTRNLLKREV-----LPEDVAEAVVAMASEDFGKTTG 241
PRK06484 PRK06484
short chain dehydrogenase; Validated
 1-153 4.22e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 82.59  E-value: 4.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKddrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06484  367 DFTRVYDVNLSGAFACARAAARLMSQ---GGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVA 443

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLVdkQIPEQAKElgISEEDVIKKVMLGNTVDGvfttvQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK06484  444 PGYIETPAV--LALKASGR--ADFDSIRRRIPLGRLGDP-----EEVAEAIAFLASPAASYVNGATLTVDGGW 507
PRK07074 PRK07074
SDR family oxidoreductase;
2-144 2.07e-18

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 79.04  E-value: 2.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIyMGSVHSHEA--SPlksAYVTAKHGLLGLARVLAKEGAKHNVRSHVV 79
Cdd:PRK07074  101 WRADNALNLEAAYLCVEAVLEGMLKRSRGAVVN-IGSVNGMAAlgHP---AYSAAKAGLIHYTKLLAVEYGRFGIRANAV 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  80 CPGFVRTPL----VDK--QIPEQAKELGISEEdvikkvmlgntvdgvFTTVQDVAQTVLFLSAFPSAALTG 144
Cdd:PRK07074  177 APGTVKTQAwearVAAnpQVFEELKKWYPLQD---------------FATPDDVANAVLFLASPAARAITG 232
PRK06500 PRK06500
SDR family oxidoreductase;
1-152 2.31e-18

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 78.46  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06500  103 MFDRSFNTNVKGPYFLIQALLPLL---ANPASIVLNGSINAHIGMPNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVS 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861134170  81 PGFVRTPLVDKqipeqakeLGISEED-------VIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK06500  180 PGPVQTPLYGK--------LGLPEATldavaaqIQALVPLGR-----FGTPEEIAKAVLYLASDESAFIVGSEIIVDGG 245
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 1-152 2.79e-18

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: 78.11  E-value: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDD--RGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEG-AKHNVRSH 77
Cdd:cd05323   102 PWEKTIDVNLTGVINTTYLALHYMDKNKggKGGVIVNIGSVAGLYPAPQFPVYSASKHGVVGFTRSLADLLeYKTGVRVN 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  78 VVCPGFVRTPLVdkqipeqakelgisEEDVIKKVMLGNtvDGVFTTVQDVAQTvlFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05323   182 AICPGFTNTPLL--------------PDLVAKEAEMLP--SAPTQSPEVVAKA--IVYLIEDDEKNGAIWIVDGG 238
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 1-152 6.62e-18

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: 77.50  E-value: 6.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVViYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05326   104 EFERVLDVNVYGAFLGTKHAARVMIPAKKGSIV-SVASVAGVVGGLGPHAYTASKHAVLGLTRSAATELGEHGIRVNCVS 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLvdkqipeqAKELGISEEDVIKKVMLGN-TVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05326   183 PYGVATPL--------LTAGFGVEDEAIEEAVRGAaNLKGTALRPEDIAAAVLYLASDDSRYVSGQNLVVDGG 247
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 1-153 1.34e-17

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: 76.54  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05344   101 DWLEAFDLKLLSVIRIVRAVLPGM-KERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTVNSVL 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDViKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:cd05344   180 PGYIDTERVRRLLEARAEKEGISVEEA-EKEVASQIPLGRVGKPEELAALIAFLASEKASYITGQAILVDGGL 251
FabG-like PRK07231
SDR family oxidoreductase;
1-154 3.53e-17

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 75.25  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07231  105 EFDRIFAVNVKSPYLWTQAAVPAM-RGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVA 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  81 PGFVRTPLVDKQIPEQAKElgiSEEDVIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWF 154
Cdd:PRK07231  184 PVVVETGLLEAFMGEPTPE---NRAKFLATIPLGR-----LGTPEDIANAALFLASDEASWITGVTLVVDGGRC 249
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-152 3.70e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 75.22  E-value: 3.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12828  105 TWDRMYGVNVKTTLNASKAALPALTASG-GGRIVNIGAGAALKAGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAVL 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  81 PGFVRTPLVDKQIPeqakelgiseedvikkvmlgntvDGVFT---TVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK12828  184 PSIIDTPPNRADMP-----------------------DADFSrwvTPEQIAAVIAFLLSDEAQAITGASIPVDGG 235
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-153 4.16e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 75.14  E-value: 4.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12827  110 EWDDVIDVNLDGFFNVTQAALPPMIRARRGGRIVNIASVAGVRGNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVA 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLVDKQIPeqakelgisEEDVIKKVMLGNTVDgvfttVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK12827  190 PGAINTPMADNAAP---------TEHLLNPVPVQRLGE-----PDEVAALVAFLVSDAASYVTGQVIPVDGGF 248
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
8-152 5.21e-17

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 75.22  E-value: 5.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   8 IHVDGAFLTTKAALKHMYKDDRGGVVIyMGSVHSH-EASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 86
Cdd:PRK08226  112 INIKGVWNVTKAVLPEMIARKDGRIVM-MSSVTGDmVADPGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRT 190

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  87 PLVDKQIPEQAKElgiSEEDVIKKVMLGNTVdGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK08226  191 PMAESIARQSNPE---DPESVLTEMAKAIPL-RRLADPLEVGELAAFLASDESSYLTGTQNVIDGG 252
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-153 7.26e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 74.37  E-value: 7.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07060  100 GFDRVMAVNARGAALVARHVARAMIAAGRGGSIVNVSSQAALVGLPDHLAYCASKAALDAITRVLCVELGPHGIRVNSVN 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLVDKQIPEQAKelgiseedviKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK07060  180 PTVTLTPMAAEAWSDPQK----------SGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLPVDGGY 242
PRK06484 PRK06484
short chain dehydrogenase; Validated
 1-153 1.23e-16

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 75.66  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06484  104 EFARLQAINLTGAYLVAREALRLMIEQGHGAAIVNVASGAGLVALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVL 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGIseedVIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK06484  184 PGYVRTQMVAELERAGKLDPSA----VRSRIPLGR-----LGRPEEIAEAVFFLASDQASYITGSTLVVDGGW 247
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 1-153 1.25e-16

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: 73.96  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKH--NVRSHV 78
Cdd:cd05341   102 EWRRLLDINLTGVFLGTRAVIPPM-KEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGLTKSAALECATQgyGIRVNS 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  79 VCPGFVRTPLVDKQIPEQAKelgiseedvikKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:cd05341   181 VHPGYIYTPMTDELLIAQGE-----------MGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVTGSELVVDGGY 244
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 10-155 1.27e-16

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: 74.03  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  10 VDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLV 89
Cdd:cd05349   113 VKGALNLLQAVLPDF-KERGSGRVINIGTNLFQNPVVPYHDYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDA 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  90 DKQIPEQAKELgiseedvikkvMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:cd05349   192 SAATPKEVFDA-----------IAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQNLVVDGGLVM 246
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 1-153 1.54e-16

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: 73.66  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSH-EASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVV 79
Cdd:cd05368    93 DWDFAMNLNVRSMYLMIKAVLPKMLAR-KDGSIINMSSVASSiKGVPNRFVYSTTKAAVIGLTKSVAADFAQQGIRCNAI 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861134170  80 CPGFVRTPLVDKQI-----PEQAKelgiseEDVIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:cd05368   172 CPGTVDTPSLEERIqaqpdPEEAL------KAFAARQPLGR-----LATPEEVAALAVYLASDESAYVTGTAVVIDGGW 239
PRK07063 PRK07063
SDR family oxidoreductase;
1-89 1.78e-16

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 73.55  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07063  109 DWRRCFAVDLDGAWNGCRAVLPGMV-ERGRGSIVNIASTHAFKIIPGCFPYPVAKHGLLGLTRALGIEYAARNVRVNAIA 187


                  ....*....
gi 1861134170  81 PGFVRTPLV 89
Cdd:PRK07063  188 PGYIETQLT 196
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 1-155 3.30e-16

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 72.73  E-value: 3.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12935  107 DWERVIDVNLSSVFNTTSAVLPYITEAE-EGRIISISSIIGQAGGFGQTNYSAAKAGMLGFTKSLALELAKTNVTVNAIC 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  81 PGFVRTPLVdKQIPEQAKELGISEedvIKKVMLGNTvdgvfttvQDVAQTVLFLsAFPSAALTGQSFVVSHGWFM 155
Cdd:PRK12935  186 PGFIDTEMV-AEVPEEVRQKIVAK---IPKKRFGQA--------DEIAKGVVYL-CRDGAYITGQQLNINGGLYM 247
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 1-88 2.71e-15

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: 70.08  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVViYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd08932    96 ELEAHFSINVIAPAELTRALLPALREAGSGRVV-FLNSLSGKRVLAGNAGYSASKFALRALAHALRQEGWDHGVRVSAVC 174


                  ....*...
gi 1861134170  81 PGFVRTPL 88
Cdd:cd08932   175 PGFVDTPM 182
PRK06172 PRK06172
SDR family oxidoreductase;
1-156 5.98e-15

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 69.39  E-value: 5.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06172  108 EFDAIMGVNVKGVWLCMKYQIPLMLAQG-GGAIVNTASVAGLGAAPKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVC 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVdkqipEQAKElgiSEEDVIKKVMLGNTVdGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK06172  187 PAVIDTDMF-----RRAYE---ADPRKAEFAAAMHPV-GRIGKVEEVASAVLYLCSDGASFTTGHALMVDGGATAQ 253
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
3-152 9.30e-15

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 68.98  E-value: 9.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   3 KKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPG 82
Cdd:PRK08643  104 DKVYNINVGGVIWGIQAAQEAFKKLGHGGKIINATSQAGVVGNPELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPG 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  83 FVRTPL---VDKQIPEQA-KELGISEEDVIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK08643  184 IVKTPMmfdIAHQVGENAgKPDEWGMEQFAKDITLGR-----LSEPEDVANCVSFLAGPDSDYITGQTIIVDGG 252
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 2-152 1.03e-14

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: 69.11  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIyMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:cd08936   112 WDKILDVNVKATALMTKAVVPEMEKRGGGSVVI-VSSVAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAP 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  82 GFVRTPLVDKQIPEQAKELGISEEDVIKKvmLGNTvdgvfttvQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd08936   191 GLIKTSFSSALWMDKAVEESMKETLRIRR--LGQP--------EDCAGIVSFLCSEDASYITGETVVVGGG 251
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-156 1.11e-14

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 68.96  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  10 VDGAFLTTKAALKHMyKDDRGGVVIYMGS-------VHSHEasplksaYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPG 82
Cdd:PRK08642  119 VKGALNTIQAALPGM-REQGFGRIINIGTnlfqnpvVPYHD-------YTTAKAALLGLTRNLAAELGPYGITVNMVSGG 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  83 FVRTPLVDKQIPEQAKELgISEEDVIKKVmlgntvdgvfTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK08642  191 LLRTTDASAATPDEVFDL-IAATTPLRKV----------TTPQEFADAVLFFASPWARAVTGQNLVVDGGLVMN 253
PRK07774 PRK07774
SDR family oxidoreductase;
1-156 1.49e-14

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 68.23  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKddRGGVVIYMGSvhSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07774  109 YYKKFMSVNLDGALVCTRAVYKHMAK--RGGGAIVNQS--STAAWLYSNFYGLAKVGLNGLTQQLARELGGMNIRVNAIA 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKelgiseEDVIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK07774  185 PGPIDTEATRTVTPKEFV------ADMVKGIPLSR-----MGTPEDLVGMCLFLLSDEASWITGQIFNVDGGQIIR 249
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 1-155 1.61e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 68.45  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKddRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07890  106 HWRAVIELNVLGTLRLTQAFTPALAE--SGGSIVMINSMVLRHSQPKYGAYKMAKGALLAASQSLATELGPQGIRVNSVA 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKVMlGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:PRK07890  184 PGYIWGDPLKGYFRHQAGKYGVTVEQIYAETA-ANSDLKRLPTDDEVASAVLFLASDLARAITGQTLDVNCGEYH 257
PRK07069 PRK07069
short chain dehydrogenase; Validated
 1-152 1.74e-14

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 68.20  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKH--NVRSHV 78
Cdd:PRK07069  102 EWRRVMAINVESIFLGCKHALPYL-RASQPASIVNISSVAAFKAEPDYTAYNASKAAVASLTKSIALDCARRglDVRCNS 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  79 VCPGFVRTPLVDKqipeQAKELGisEEDVIKKVMLGNTVdGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK07069  181 IHPTFIRTGIVDP----IFQRLG--EEEATRKLARGVPL-GRLGEPDDVAHAVLYLASDESRFVTGAELVIDGG 247
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 2-152 2.49e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 68.05  E-value: 2.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKS----AYVTAKHGLLGLARVLAKEGAKHNVRSH 77
Cdd:PRK08213  113 WDKVMNLNVRGLFLLSQAVAKRSMIPRGYGRIINVASVAGLGGNPPEVmdtiAYNTSKGAVINFTRALAAEWGPHGIRVN 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  78 VVCPGFVRTPLVDKQIPEqakelgiSEEDVIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK08213  193 AIAPGFFPTKMTRGTLER-------LGEDLLAHTPLGR-----LGDDEDLKGAALLLASDASKHITGQILAVDGG 255
PRK08589 PRK08589
SDR family oxidoreductase;
2-152 2.63e-14

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 67.88  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKddRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:PRK08589  107 FDKIMAVDMRGTFLMTKMLLPLMME--QGGSIINTSSFSGQAADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAP 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  82 GFVRTPLVDKQIPEQAKELGISEEDVIKKVmlgnTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK08589  185 GTIETPLVDKLTGTSEDEAGKTFRENQKWM----TPLGRLGKPEEVAKLVVFLASDDSSFITGETIRIDGG 251
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 17-132 2.89e-14

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 67.64  E-value: 2.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  17 TKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEQ 96
Cdd:cd05374   113 TRAFLPLMRKQ-GSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSA 191

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1861134170  97 AKELGISE-EDVIKKVML-GNTVDGVFTTVQDVAQTVL 132
Cdd:cd05374   192 LEDPEISPyAPERKEIKEnAAGVGSNPGDPEKVADVIV 229
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 1-152 3.18e-14

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: 67.44  E-value: 3.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05364   106 EYDKVMNLNLRAVIYLTKLAVPHLIKTK--GEIVNVSSVAGGRSFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVS 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  81 PGFVRTPLvdkqipeqAKELGISEEDVIK--KVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05364   184 PGVIVTGF--------HRRMGMPEEQYIKflSRAKETHPLGRPGTVDEVAEAIAFLASDASSFITGQLLPVDGG 249
PLN02253 PLN02253
xanthoxin dehydrogenase
 1-153 5.50e-14

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 67.16  E-value: 5.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVViYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PLN02253  119 EFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIV-SLCSVASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVS 197

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861134170  81 PGFVRTPLVDKQIPEQAKelgisEEDVIK--KVMLGNTVD--GVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PLN02253  198 PYAVPTALALAHLPEDER-----TEDALAgfRAFAGKNANlkGVELTVDDVANAVLFLASDEARYISGLNLMIDGGF 269
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 2-149 6.22e-14

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: 66.84  E-value: 6.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:cd05369   105 FKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNISATYAYTGSPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAP 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  82 G-FVRTPLVDKQIPEQAKELGIseedvIKKVMLGNtvdgvFTTVQDVAQTVLFLSAfPSAA-LTGQSFVV 149
Cdd:cd05369   185 GpIPTTEGMERLAPSGKSEKKM-----IERVPLGR-----LGTPEEIANLALFLLS-DAASyINGTTLVV 243
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 1-153 8.11e-14

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: 66.22  E-value: 8.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05359    99 HWDAKMNTNLKALVHCAQQAAKLM-RERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVS 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPlVDKQIPEQAKELgiseEDVIKKVMLGNTVdgvftTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:cd05359   178 PGVIDTD-ALAHFPNREDLL----EAAAANTPAGRVG-----TPQDVADAVGFLCSDAARMITGQTLVVDGGL 240
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 1-152 9.02e-14

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: 66.32  E-value: 9.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAF-LTTKAalkH-MYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHV 78
Cdd:cd05329   107 DYSLIMSTNFEAAYhLSRLA---HpLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGALNQLTRSLACEWAKDNIRVNA 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  79 VCPGFVRTPLVdkqipeqakELGISEEDVIKKVmLGNTVDGVFTTVQDVAQTVLFLsAFPSAA-LTGQSFVVSHG 152
Cdd:cd05329   184 VAPWVIATPLV---------EPVIQQKENLDKV-IERTPLKRFGEPEEVAALVAFL-CMPAASyITGQIIAVDGG 247
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 1-156 9.07e-14

(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: 66.19  E-value: 9.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05353   111 DWDLVMRVHLKGSFKVTRAAWPYM-RKQKFGRIINTSSAAGLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIA 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGfVRTPLVDKQIPEQAKELGISEEdvikkvmlgntvdgvfttvqdVAQTVLFLSAfPSAALTGQSFVVSHGWFMQ 156
Cdd:cd05353   190 PA-AGSRMTETVMPEDLFDALKPEY---------------------VAPLVLYLCH-ESCEVTGGLFEVGAGWIGK 242
PRK05867 PRK05867
SDR family oxidoreductase;
1-153 1.00e-13

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 66.21  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEAS-PLK-SAYVTAKHGLLGLARVLAKEGAKHNVRSHV 78
Cdd:PRK05867  109 EFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGVIINTASMSGHIINvPQQvSHYCASKAAVIHLTKAMAVELAPHKIRVNS 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  79 VCPGFVRTPLVdkqipEQAKELGISEEDVIKKVMLGNTvdgvfttvQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK05867  189 VSPGYILTELV-----EPYTEYQPLWEPKIPLGRLGRP--------EELAGLYLYLASEASSYMTGSDIVIDGGY 250
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 1-152 1.67e-13

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: 65.43  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSV---------HSHEASPLKSA-YVTAKHGLLGLARVLAKEGA 70
Cdd:cd08930   106 QWNEVLNVNLGGAFLCSQAFIKLF-KKQGKGSIINIASIygviapdfrIYENTQMYSPVeYSVIKAGIIHLTKYLAKYYA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  71 KHNVRSHVVCPGfvrtPLVDKQIPEQAKELgiseedvIKKVMLGNTVDgvfttVQDVAQTVLFLSAFPSAALTGQSFVVS 150
Cdd:cd08930   185 DTGIRVNAISPG----GILNNQPSEFLEKY-------TKKCPLKRMLN-----PEDLRGAIIFLLSDASSYVTGQNLVID 248


                  ..
gi 1861134170 151 HG 152
Cdd:cd08930   249 GG 250
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 1-152 3.88e-13

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: 64.41  E-value: 3.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05331    91 DWEQTFAVNVTGVFNLLQAVAPHM-KDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELAPYGVRCNVVS 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  81 PGFVRTPL-------------VDKQIPEQAKeLGISeedvIKKVmlgntvdgvfTTVQDVAQTVLFLSAFPSAALTGQSF 147
Cdd:cd05331   170 PGSTDTAMqrtlwhdedgaaqVIAGVPEQFR-LGIP----LGKI----------AQPADIANAVLFLASDQAGHITMHDL 234


                  ....*
gi 1861134170 148 VVSHG 152
Cdd:cd05331   235 VVDGG 239
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 1-99 4.40e-13

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 64.36  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK08936  108 DWNKVINTNLTGAFLGSREAIKYFVEHDIKGNIINMSSVHEQIPWPLFVHYAASKGGVKLMTETLAMEYAPKGIRVNNIG 187

                          90       100
                  ....*....|....*....|.
gi 1861134170  81 PGFVRTPLVDKQI--PEQAKE 99
Cdd:PRK08936  188 PGAINTPINAEKFadPKQRAD 208
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-154 4.69e-13

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 64.51  E-value: 4.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK08993  108 DWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIA 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  81 PGFVRTplvdkqipEQAKELGISEEDviKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWF 154
Cdd:PRK08993  188 PGYMAT--------NNTQQLRADEQR--SAEILDRIPAGRWGLPSDLMGPVVFLASSASDYINGYTIAVDGGWL 251
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 2-152 5.23e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 64.37  E-value: 5.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRGGV------VIYMGSVHSheasplKSAYVTAKHGLLGLARVLAKEGAKHNVR 75
Cdd:PRK06057  105 WQRVQDVNLTSVYLCCKAALPHMVRQGKGSIintasfVAVMGSATS------QISYTASKGGVLAMSRELGVQFARQGIR 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  76 SHVVCPGFVRTPLVDK---QIPEQAKElgiseedvikkvMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK06057  179 VNALCPGPVNTPLLQElfaKDPERAAR------------RLVHVPMGRFAEPEEIAAAVAFLASDDASFITASTFLVDGG 246
PRK07856 PRK07856
SDR family oxidoreductase;
12-152 1.11e-12

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 63.41  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  12 GAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKhNVRSHVVCPGFVRTplvdk 91
Cdd:PRK07856  109 APLLVAQAANAVMQQQPGGGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNLTRSLAVEWAP-KVRVNAVVVGLVRT----- 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  92 qipEQAkELGISEEDVIKKVmlGNTVD-GVFTTVQDVAQTVLFLSAFPSAALTGQSFVVsHG 152
Cdd:PRK07856  183 ---EQS-ELHYGDAEGIAAV--AATVPlGRLATPADIAWACLFLASDLASYVSGANLEV-HG 237
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-155 1.25e-12

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 63.25  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12824  103 EWNDVINTNLNSVFNVTQPLFAAM-CEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGFTKALASEGARYGITVNCIA 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  81 PGFVRTPLVDkQIPEQAKElGISEEdvIKKVMLGntvdgvftTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:PRK12824  182 PGYIATPMVE-QMGPEVLQ-SIVNQ--IPMKRLG--------TPEEIAAAVAFLVSEAAGFITGETISINGGLYM 244
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 2-152 1.35e-12

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: 63.33  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKH--MYKDDRGGVvIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVV 79
Cdd:cd08945   104 WLDVVETNLTGVFRVTKEVLKAggMLERGTGRI-INIASTGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNAV 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861134170  80 CPGFVRTPLVDKQIPEQAKELGISEEDVIK----KVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd08945   183 CPGFVETPMAASVREHYADIWEVSTEEAFDritaRVPLGR-----YVTPEEVAGMVAYLIGDGAAAVTAQALNVCGG 254
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-156 1.55e-12

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 63.07  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12939  107 TWDAVMNVNVRGTFLMLRAALPHL-RDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIGMTRSLARELGGRGITVNAIA 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVdkqipEQAKelgisEEDVIKKVMLGNTVDGVfTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK12939  186 PGLTATEAT-----AYVP-----ADERHAYYLKGRALERL-QVPDDVAGAVLFLLSDAARFVTGQLLPVNGGFVMN 250
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 1-152 1.94e-12

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: 62.59  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05365   100 DFEWAFKLNLFSAFRLSQLCAPHMQKA-GGGAILNISSMSSENKNVRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVA 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTplvdkqipEQAKELGISEedvIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05365   179 PGAVKT--------DALASVLTPE---IERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSGG 239
PRK07831 PRK07831
SDR family oxidoreductase;
2-150 2.31e-12

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 62.74  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:PRK07831  121 WSRVLDVTLTGTFRATRAALRYMRARGHGGVIVNNASVLGWRAQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAP 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861134170  82 GFVRTPLVDKqipeqakelgISEEDVIKKvMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVS 150
Cdd:PRK07831  201 SIAMHPFLAK----------VTSAELLDE-LAAREAFGRAAEPWEVANVIAFLASDYSSYLTGEVVSVS 258
PRK07454 PRK07454
SDR family oxidoreductase;
1-142 2.41e-12

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 62.28  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07454  106 DWQWVIQLNLTSVFQCCSAVLPGM-RARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFTKCLAEEERSHGIRVCTIT 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  81 PGFVRTPLVDkqipeqakelgiSEE---DVIKKVMLgntvdgvftTVQDVAQTVLFLSAFPSAAL 142
Cdd:PRK07454  185 LGAVNTPLWD------------TETvqaDFDRSAML---------SPEQVAQTILHLAQLPPSAV 228
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 17-153 2.94e-12

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 62.05  E-value: 2.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  17 TKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKhNVRSHVVCPGFVRTPLVDKQIpeq 96
Cdd:PRK06077  123 SQELAKEM---REGGAIVNIASVAGIRPAYGLSIYGAMKAAVINLTKYLALELAP-KIRVNAIAPGFVKTKLGESLF--- 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1861134170  97 aKELGISEEDVIKKVmlgnTVDGVFTTVQDVAQTVLFLSAFPSaaLTGQSFVVSHGW 153
Cdd:PRK06077  196 -KVLGMSEKEFAEKF----TLMGKILDPEEVAEFVAAILKIES--ITGQVFVLDSGE 245
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 1-156 6.66e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 61.21  E-value: 6.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06841  112 DWDKTIDINLKGSFLMAQAVGRHMIAA-GGGKIVNLASQAGVVALERHVAYCASKAGVVGMTKVLALEWGPYGITVNAIS 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQipeQAKELGiseEDVIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFMQ 156
Cdd:PRK06841  191 PTVVLTELGKKA---WAGEKG---ERAKKLIPAGR-----FAYPEEIAAAALFLASDAAAMITGENLVIDGGYTIQ 255
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 1-105 1.07e-11

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: 60.81  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIyMGSVHSHEAS-PLKSA-YVTAKHGLLGLARVLAKEGAKHNVRSHV 78
Cdd:cd05352   109 QWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLII-TASMSGTIVNrPQPQAaYNASKAAVIHLAKSLAVEWAKYFIRVNS 187

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1861134170  79 VCPGFVRTPL---VDKQIPEQ------AKELGISEE 105
Cdd:cd05352   188 ISPGYIDTDLtdfVDKELRKKwesyipLKRIALPEE 223
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-95 1.26e-11

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 60.36  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVhSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:PRK08217  115 FQSVIDVNLTGVFLCGREAAAKMIESGSKGVIINISSI-ARAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAP 193

                          90
                  ....*....|....
gi 1861134170  82 GFVRTPLVDKQIPE 95
Cdd:PRK08217  194 GVIETEMTAAMKPE 207
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 1-152 1.35e-11

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: 60.37  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05362   104 EFDRMFTVNTKGAFFVLQEAAKRL---RDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVA 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELgiseedvIKKVMLGNTVdgvfTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05362   181 PGPVDTDMFYAGKTEEAVEG-------YAKMSPLGRL----GEPEDIAPVVAFLASPDGRWVNGQVIRANGG 241
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 1-87 2.28e-11

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 60.03  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06171  109 AFDKMFNINQKGVFLMSQAVARQMVKQ-HDGVIVNMSSEAGLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVA 187

                          90
                  ....*....|..
gi 1861134170  81 PGF-----VRTP 87
Cdd:PRK06171  188 PGIleatgLRTP 199
PRK07832 PRK07832
SDR family oxidoreductase;
1-90 2.28e-11

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 60.06  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07832  101 QWRRMVDVNLMGPIHVIETFVPPMVAAGRGGHLVNVSSAAGLVALPWHAAYSASKFGLRGLSEVLRFDLARHGIGVSVVV 180

                          90
                  ....*....|
gi 1861134170  81 PGFVRTPLVD 90
Cdd:PRK07832  181 PGAVKTPLVN 190
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-153 2.31e-11

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 59.59  E-value: 2.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06550   91 EWQHIFDTNLTSTFLLTRAYLPQM-LERKSGIIINMCSIASFVAGGGGAAYTASKHALAGFTKQLALDYAKDGIQVFGIA 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  81 PGFVRTPL--VDKQIPEQAKElgISEEDVIKKvmlgntvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK06550  170 PGAVKTPMtaADFEPGGLADW--VARETPIKR----------WAEPEEVAELTLFLASGKADYMQGTIVPIDGGW 232
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-152 4.41e-11

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 59.03  E-value: 4.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGS-VHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06463  103 YNKMIKINLNGAIYTTYEFLPLL-KLSKNGAIVNIASnAGIGTAAEGTTFYAITKAGIIILTRRLAFELGKYGIRVNAVA 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTPL-VDKQIPEQAKELgisEEDVIKKvmlgnTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK06463  182 PGWVETDMtLSGKSQEEAEKL---RELFRNK-----TVLKTTGKPEDIANIVLFLASDDARYITGQVIVADGG 246
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 1-152 6.44e-11

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 58.60  E-value: 6.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12937  106 DFDRTIATNLRGAFVVLREAARHL---GQGGRIINLSTSVIALPLPGYGPYAASKAAVEGLVHVLANELRGRGITVNAVA 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861134170  81 PGFVRTPL-VDKQIPEQAkelgiseeDVIKKVM----LGntvdgvftTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK12937  183 PGPVATELfFNGKSAEQI--------DQLAGLAplerLG--------TPEEIAAAVAFLAGPDGAWVNGQVLRVNGG 243
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 17-132 1.01e-10

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: 57.98  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  17 TKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQipeq 96
Cdd:cd05332   120 TKAALPHL-IERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNA---- 194

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1861134170  97 akelgISEEDVIKKVMLGNTVDGVftTVQDVAQTVL 132
Cdd:cd05332   195 -----LSGDGSMSAKMDDTTANGM--SPEECALEIL 223
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 2-101 1.36e-10

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: 57.69  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKddrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:cd05355   130 LEKTFRTNIFSMFYLTKAALPHLKK---GSSIINTTSVTAYKGSPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAP 206

                          90       100
                  ....*....|....*....|.
gi 1861134170  82 GFVRTPLVDKQIP-EQAKELG 101
Cdd:cd05355   207 GPIWTPLIPSSFPeEKVSEFG 227
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 12-95 2.39e-10

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: 56.62  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  12 GAFLTTKAALKHMYKDDRGgVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVR-SHVVCPGFVRTPLVD 90
Cdd:cd05373   111 GGFLAAREAAKRMLARGRG-TIIFTGATASLRGRAGFAAFAGAKFALRALAQSMARELGPKGIHvAHVIIDGGIDTDFIR 189


                  ....*
gi 1861134170  91 KQIPE 95
Cdd:cd05373   190 ERFPK 194
PRK08628 PRK08628
SDR family oxidoreductase;
49-153 2.52e-10

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 56.89  E-value: 2.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  49 SAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQI---PEQAKELgiseEDVIKKVMLGNTvdgvFTTVQ 125
Cdd:PRK08628  151 SGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWIatfDDPEAKL----AAITAKIPLGHR----MTTAE 222

                          90       100
                  ....*....|....*....|....*...
gi 1861134170 126 DVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK08628  223 EIADTAVFLLSERSSHTTGQWLFVDGGY 250
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-112 2.64e-10

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 56.62  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07666  107 EWEKIIQVNLMGVYYATRAVLPSM-IERQSGDIINISSTAGQKGAAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALT 185

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTPLvdkqipeqAKELGISEEDViKKVM 112
Cdd:PRK07666  186 PSTVATDM--------AVDLGLTDGNP-DKVM 208
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 5-152 2.79e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 56.84  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   5 MQAIHVDGAFLttkaalKHMYkDDRGGVVIYMGSVHSheASPLKS---AYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:PRK06523  112 LAAVRLDRALL------PGMI-ARGSGVIIHVTSIQR--RLPLPEsttAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSP 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  82 GFVRTPLVDKQIPEQAKELGISEEDVIKKVM--LGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK06523  183 GWIETEAAVALAERLAEAAGTDYEGAKQIIMdsLGGIPLGRPAEPEEVAELIAFLASDRAASITGTEYVIDGG 255
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 1-122 4.91e-10

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: 55.72  E-value: 4.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd08939   105 EFERGMDVNYFGSLNVAHAVLPLM-KEQRPGHIVFVSSQAALVGIYGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVY 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTPLVD---KQIPEQAKELG-----ISEEDVIKKVM--LGNTVDGVFT 122
Cdd:cd08939   184 PPDTDTPGFEeenKTKPEETKAIEgssgpITPEEAARIIVkgLDRGYDDVFT 235
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-153 6.27e-10

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 55.90  E-value: 6.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06935  114 DWNAVMDINLNSVYHLSQAVAKVMAKQ-GSGKIINIASMLSFQGGKFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIA 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861134170  81 PGFVRTplvdkqipeqAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK06935  193 PGYIKT----------ANTAPIRADKNRNDEILKRIPAGRWGEPDDLMGAAVFLASRASDYVNGHILAVDGGW 255
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 1-88 7.78e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 55.32  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDrGGVVIYMGSVHSHEAS-PLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVV 79
Cdd:PRK07478  107 GWRETLATNLTSAFLGAKHQIPAMLARG-GGSLIFTSTFVGHTAGfPGMAAYAASKAGLIGLTQVLAAEYGAQGIRVNAL 185


                  ....*....
gi 1861134170  80 CPGFVRTPL 88
Cdd:PRK07478  186 LPGGTDTPM 194
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 8-143 8.53e-10

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: 54.44  E-value: 8.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   8 IHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTP 87
Cdd:cd02266    61 ANVVGTRRLLEAARELM-KAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASEGWGNGLPATAVACGTWAGS 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1861134170  88 LVdkqipeqAKELGISEEdvikkvMLGNTVDGVFT-TVQDVAQTVLFLSAFPSAALT 143
Cdd:cd02266   140 GM-------AKGPVAPEE------ILGNRRHGVRTmPPEEVARALLNALDRPKAGVC 183
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 1-104 8.53e-10

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: 55.24  E-value: 8.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd08934   103 DWTRMIDTNLLGLMYTTHAALPHH-LLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIE 181

                          90       100
                  ....*....|....*....|....*..
gi 1861134170  81 PGFVRTPLVD---KQIPEQAKELGISE 104
Cdd:cd08934   182 PGTVDTELRDhitHTITKEAYEERIST 208
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-155 1.06e-09

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 55.03  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07067  103 SYDRLFAVNVKGLFFLMQAVARHMVEQGRGGKIINMASQAGRRGEALVSHYCATKAAVISYTQSAALALIRHGINVNAIA 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDviKKVMLGNTVD-GVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:PRK07067  183 PGVVDTPMWDQVDALFARYENRPPGE--KKRLVGEAVPlGRMGVPDDLTGMALFLASADADYIVAQTYNVDGGNWM 256
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-154 1.07e-09

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 55.30  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK12481  106 DWDDVININQKTVFFLSQAVAKQFVKQGNGGKIINIASMLSFQGGIRVPSYTASKSAVMGLTRALATELSQYNINVNAIA 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKKvmlgntvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWF 154
Cdd:PRK12481  186 PGYMATDNTAALRADTARNEAILERIPASR----------WGTPDDLAGPAIFLSSSASDYVTGYTLAVDGGWL 249
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-134 1.20e-09

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 54.89  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK08220   99 DWQQTFAVNAGGAFNLFRAVMPQF-RRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSLAKCVGLELAPYGVRCNVVS 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861134170  81 PGFVRTPL-------------VDKQIPEQAKeLGISeedvIKKVmlgntvdgvfTTVQDVAQTVLFL 134
Cdd:PRK08220  178 PGSTDTDMqrtlwvdedgeqqVIAGFPEQFK-LGIP----LGKI----------ARPQEIANAVLFL 229
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 1-101 1.74e-09

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: 54.45  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05330   106 EFDKVVSINLRGVFYGLEKVLKVM-REQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVVGLTRNSAVEYGQYGIRINAIA 184

                          90       100
                  ....*....|....*....|....*
gi 1861134170  81 PGFVRTPLVD---KQI-PEQAKELG 101
Cdd:cd05330   185 PGAILTPMVEgslKQLgPENPEEAG 209
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 1-147 2.31e-09

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: 54.12  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVViYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05340   108 VWQDV*QVNVNATFMLTQALLPLLLKSDAGSLV-FTSSSVGRQGRANWGAYAVSKFATEGL*QVLADEYQQRNLRVNCIN 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861134170  81 PGFVRTPLVDKQIPeqakelgiSEEDVIKKvmlgntvdgvftTVQDVAQTVLFLSAFPSAALTGQSF 147
Cdd:cd05340   187 PGGTRTAMRASAFP--------TEDPQKLK------------TPADIMPLYLWLMGDDSRRKTGMTF 233
PRK09135 PRK09135
pteridine reductase; Provisional
 1-152 2.82e-09

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 53.78  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKddRGGVVIYMGSVHSHEasPLK--SAYVTAKHGLLGLARVLAKEGAKHnVRSHV 78
Cdd:PRK09135  108 QWDDLFASNLKAPFFLSQAAAPQLRK--QRGAIVNITDIHAER--PLKgyPVYCAAKAALEMLTRSLALELAPE-VRVNA 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  79 VCPGFVRTPLVDKQIPEQAKelgiseEDVIKKVMLGNTvdgvfTTVQDVAQTVLFLsAFPSAALTGQSFVVSHG 152
Cdd:PRK09135  183 VAPGAILWPEDGNSFDEEAR------QAILARTPLKRI-----GTPEDIAEAVRFL-LADASFITGQILAVDGG 244
PRK06114 PRK06114
SDR family oxidoreductase;
2-153 4.00e-09

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 53.63  E-value: 4.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRG---------GVVIYMGSVHSHeasplksaYVTAKHGLLGLARVLAKEGAKH 72
Cdd:PRK06114  110 WQTVMDINLTGVFLSCQAEARAMLENGGGsivniasmsGIIVNRGLLQAH--------YNASKAGVIHLSKSLAMEWVGR 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  73 NVRSHVVCPGFVRTPLVDKqiPEQAKELGISEEdvikkvmlgNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK06114  182 GIRVNSISPGYTATPMNTR--PEMVHQTKLFEE---------QTPMQRMAKVDEMVGPAVFLLSDAASFCTGVDLLVDGG 250


                  .
gi 1861134170 153 W 153
Cdd:PRK06114  251 F 251
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 12-152 8.84e-09

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: 52.54  E-value: 8.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  12 GAFLTTKAALKHMYKddRGGVVIYM----GSVHSHEASPlksaYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTP 87
Cdd:cd08933   122 SYFLASKYALPHLRK--SQGNIINLsslvGSIGQKQAAP----YVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTP 195

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861134170  88 LVDkqipeqakELGISEED---VIKKVMLGNTVdGVFTTVQDVAQTVLFLSAfPSAALTGQSFVVSHG 152
Cdd:cd08933   196 LWE--------ELAAQTPDtlaTIKEGELAQLL-GRMGTEAESGLAALFLAA-EATFCTGIDLLLSGG 253
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 1-152 9.44e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 52.37  E-value: 9.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07097  110 DFRQVIDIDLNAPFIVSKAVIPSMIKK-GHGKIINICSMMSELGRETVSAYAAAKGGLKMLTKNIASEYGEANIQCNGIG 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPlvdkqipeQAKELGISEEDV----IKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK07097  189 PGYIATP--------QTAPLRELQADGsrhpFDQFIIAKTPAARWGDPEDLAGPAVFLASDASNFVNGHILYVDGG 256
PRK05717 PRK05717
SDR family oxidoreductase;
2-152 9.81e-09

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 52.58  E-value: 9.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKhmYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKhNVRSHVVCP 81
Cdd:PRK05717  110 WNRVLAVNLTGPMLLAKHCAP--YLRAHNGAIVNLASTRARQSEPDTEAYAASKGGLLALTHALAISLGP-EIRVNAVSP 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  82 GFvrtplVDKQIPEQAKELGISEEDVIKKVMlgntvdGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK05717  187 GW-----IDARDPSQRRAEPLSEADHAQHPA------GRVGTVEDVAAMVAWLLSRQAGFVTGQEFVVDGG 246
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 1-87 1.01e-08

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: 52.39  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHV-- 78
Cdd:cd05360   100 EFRRVFDVNYLGHVYGTLAALPHLRRRG-GGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESLRAELAHDGAPISVtl 178


                  ....*....
gi 1861134170  79 VCPGFVRTP 87
Cdd:cd05360   179 VQPTAMNTP 187
PRK07326 PRK07326
SDR family oxidoreductase;
1-107 1.21e-08

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 51.94  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKddRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07326  105 EWRLVIDTNLTGAFYTIKAAVPALKR--GGGYIINISSLAGTNFFAGGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIM 182

                          90       100
                  ....*....|....*....|....*..
gi 1861134170  81 PGFVRTPLVDKQiPEQAKELGISEEDV 107
Cdd:PRK07326  183 PGSVATHFNGHT-PSEKDAWKIQPEDI 208
PRK06128 PRK06128
SDR family oxidoreductase;
14-101 1.69e-08

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 51.78  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  14 FLTTKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDK-- 91
Cdd:PRK06128  171 FWLCKAAIPHL---PPGASIINTGSIQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSgg 247

                          90
                  ....*....|
gi 1861134170  92 QIPEQAKELG 101
Cdd:PRK06128  248 QPPEKIPDFG 257
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-152 1.78e-08

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: 51.62  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05345   103 EFDRVFAVNVKSIYLSAQALVPHM-EEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVTATKAMAVELAPRNIRVNCLC 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTPLVdkqipeqaKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05345   182 PVAGETPLL--------SMFMGEDTPENRAKFRATIPLGRLSTPDDIANAALYLASDEASFITGVALEVDGG 245
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 3-112 1.90e-08

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: 51.47  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   3 KKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIyMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKE---GAKHNVRSHVV 79
Cdd:cd05339   101 EKTFEVNTLAHFWTTKAFLPDMLERNHGHIVT-IASVAGLISPAGLADYCASKAAAVGFHESLRLElkaYGKPGIKTTLV 179

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1861134170  80 CPGFVRTPLVDKqIPEQAKELG--ISEEDVIKKVM 112
Cdd:cd05339   180 CPYFINTGMFQG-VKTPRPLLApiLEPEYVAEKIV 213
PRK07985 PRK07985
SDR family oxidoreductase;
2-88 2.55e-08

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 51.53  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKddrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:PRK07985  153 FQKTFAINVFALFWLTQEAIPLLPK---GASIITTSSIQAYQPSPHLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAP 229


                  ....*..
gi 1861134170  82 GFVRTPL 88
Cdd:PRK07985  230 GPIWTAL 236
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 13-152 2.87e-08

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: 50.99  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  13 AFLTTKAALKHMYKDDRGgVVIYMGSVHSHEAspLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLvdKQ 92
Cdd:cd08937   116 TLWCCRAVLPHMLERQQG-VIVNVSSIATRGI--YRIPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPP--RK 190

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  93 IPEQAKELGISEEDVIKKVmLGNTVD----GVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd08937   191 IPRNAAPMSEQEKVWYQRI-VDQTLDsslmGRYGTIDEQVRAILFLASDEASYITGTVLPVGGG 253
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 14-155 2.95e-08

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 51.04  E-value: 2.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  14 FLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVdkqI 93
Cdd:cd05361   109 FALLQAAIAQM-KKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSPTY---F 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  94 PEQAKELGISEEDVIKKvmlgNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:cd05361   185 PTSDWENNPELRERVKR----DVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFAGGYLP 242
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
1-155 3.50e-08

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 50.78  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYkdDRG-GVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVV 79
Cdd:PRK12938  104 DWTAVIDTNLTSLFNVTKQVIDGMV--ERGwGRIINISSVNGQKGQFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTV 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  80 CPGFVRTPLVdKQIpeqakelgisEEDVIKKVmLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:PRK12938  182 SPGYIGTDMV-KAI----------RPDVLEKI-VATIPVRRLGSPDEIGSIVAWLASEESGFSTGADFSLNGGLHM 245
PRK06181 PRK06181
SDR family oxidoreductase;
12-133 3.57e-08

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 50.75  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  12 GAFLTTKAALKHMyKDDRGGVVIyMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDK 91
Cdd:PRK06181  113 GAVYCTHAALPHL-KASRGQIVV-VSSLAGLTGVPTRSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATDIRKR 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1861134170  92 QIPEQAKELGISEEDvIKKVMlgntvdgvftTVQDVAQTVLF 133
Cdd:PRK06181  191 ALDGDGKPLGKSPMQ-ESKIM----------SAEECAEAILP 221
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 12-155 4.42e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 50.80  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  12 GAFLTTKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLvdk 91
Cdd:PRK06701  159 SYFHMTKAALPHL---KQGSAIINTGSITGYEGNETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPL--- 232

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  92 qIPEQAkelgiSEEDVIKkvmLGNTvdgvfTTVQDVAQTV------LFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:PRK06701  233 -IPSDF-----DEEKVSQ---FGSN-----TPMQRPGQPEelapayVFLASPDSSYITGQMLHVNGGVIV 288
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 16-129 4.99e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 50.29  E-value: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  16 TTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPL------V 89
Cdd:PRK06179  111 MTRAVLPHMRAQ-GSGRIINISSVLGFLPAPYMALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFdanapeP 189

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1861134170  90 DKQIPEQAKELGISEEDVIKKVMLGNTVDGVFTTVQDVAQ 129
Cdd:PRK06179  190 DSPLAEYDRERAVVSKAVAKAVKKADAPEVVADTVVKAAL 229
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 17-90 5.64e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 50.69  E-value: 5.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861134170  17 TKAALKHMYKDDRGgVVIYMGSVHSHEASPLKSAYVTAKHGLLGL---ARV-LAKEGAkhNVRSHVVCPGFVRTPLVD 90
Cdd:PRK07109  124 TLAALRHMRPRDRG-AIIQVGSALAYRSIPLQSAYCAAKHAIRGFtdsLRCeLLHDGS--PVSVTMVQPPAVNTPQFD 198
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 1-152 8.66e-08

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 49.58  E-value: 8.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAaLKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKhNVRSHVVC 80
Cdd:cd05357   101 AWAELFGINLKAPYLLIQA-FARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLTRSAALELAP-NIRVNGIA 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTPlVDKQIPEQakelgiseEDVIKKVMLGNTVDgvfttVQDVAQTVLFLSAFPSaaLTGQSFVVSHG 152
Cdd:cd05357   179 PGLILLP-EDMDAEYR--------ENALRKVPLKRRPS-----AEEIADAVIFLLDSNY--ITGQIIKVDGG 234
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 2-91 1.04e-07

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: 49.25  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVD--GAFLTTKAALKHMYKDDRGGVVIyMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVV 79
Cdd:cd05350    97 KAFRETIDTNllGAAAILEAALPQFRAKGRGHLVL-ISSVAALRGLPGAAAYSASKAALSSLAESLRYDVKKRGIRVTVI 175

                          90
                  ....*....|..
gi 1861134170  80 CPGFVRTPLVDK 91
Cdd:cd05350   176 NPGFIDTPLTAN 187
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 2-144 1.15e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 49.23  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:PRK06198  108 FDRHFAVNVRAPFFLMQEAIKLMRRRKAEGTIVNIGSMSAHGGQPFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNI 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  82 GFVRTPLVDKQipeQAKELGISE---EDVIKKVMLGNTVDgvfttVQDVAQTVLFLSAFPSAALTG 144
Cdd:PRK06198  188 GWMATEGEDRI---QREFHGAPDdwlEKAAATQPFGRLLD-----PDEVARAVAFLLSDESGLMTG 245
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 2-155 1.35e-07

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 49.15  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:cd05363   101 YDRLFAINVSGTLFMMQAVARAMIAQGRGGKIINMASQAGRRGEALVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAP 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  82 GFVRTPLVDKQIPEQAKELGISEEDviKKVMLGNTVD-GVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:cd05363   181 GVVDGEHWDGVDAKFARYENRPRGE--KKRLVGEAVPfGRMGRAEDLTGMAIFLASTDADYIVAQTYNVDGGNWM 253
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 7-153 1.66e-07

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: 49.01  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   7 AIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 86
Cdd:cd05351   105 DVNVRAVIHVSQIVARGMIARGVPGSIVNVSSQASQRALTNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMT 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861134170  87 PLVDKQIPEQAKelgiseedviKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:cd05351   185 DMGRDNWSDPEK----------AKKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDGGF 241
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 5-88 1.69e-07

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 48.80  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   5 MQAIHVDGAFLTTKAALKHMYKDdrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHnVRSHVVCPGFV 84
Cdd:PRK06200  112 IFNVNVKGYLLGAKAALPALKAS--GGSMIFTLSNSSFYPGGGGPLYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGT 188


                  ....
gi 1861134170  85 RTPL 88
Cdd:PRK06200  189 VTDL 192
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 1-152 2.10e-07

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: 48.73  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKhNVRSHVVC 80
Cdd:cd09761    98 EWDRILSVNLTGPYELSRYCRDELIKN--KGRIINIASTRAFQSEPDSEAYAASKGGLVALTHALAMSLGP-DIRVNCIS 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVikkvmlgntvdGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd09761   175 PGWINTTEQQEFTAAPLTQEDHAQHPA-----------GRVGTPKDIANLVLFLCQQDAGFITGETFIVDGG 235
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 1-116 2.67e-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: 47.90  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALkhmYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKhnVRSHVVC 80
Cdd:cd11730    89 AWRRILDANLTGAALVLKHAL---ALLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVARKEVRG--LRLTLVR 163

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1861134170  81 PGFVRTPLVdkQIPEQAKELGISEEDVIKKVMLGNT 116
Cdd:cd11730   164 PPAVDTGLW--APPGRLPKGALSPEDVAAAILEAHQ 197
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 12-142 3.20e-07

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: 47.89  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  12 GAFLTTKAALKHMYKDdrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDK 91
Cdd:cd08929   109 AFYCIHKAAPALLRRG--GGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGS 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  92 QIPEQAKelgISEEdvikkvmlgntvdgvfttvqDVAQTVLFLSAFPSAAL 142
Cdd:cd08929   187 PEGQAWK---LAPE--------------------DVAQAVLFALEMPARAL 214
PRK06947 PRK06947
SDR family oxidoreductase;
3-152 3.22e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 48.26  E-value: 3.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   3 KKMQAIHVDGAFLTTKAALKHMYKD--DRGGVVIYMGSVHSHEASPLKSA-YVTAKHGLLGLARVLAKEGAKHNVRSHVV 79
Cdd:PRK06947  106 RRMFDTNVLGAYLCAREAARRLSTDrgGRGGAIVNVSSIASRLGSPNEYVdYAGSKGAVDTLTLGLAKELGPHGVRVNAV 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861134170  80 CPGfvrtpLVDKQI------PEQAKELGiseedvikkvmlGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK06947  186 RPG-----LIETEIhasggqPGRAARLG------------AQTPLGRAGEADEVAETIVWLLSDAASYVTGALLDVGGG 247
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 1-120 4.51e-07

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: 47.51  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMykDDRG---GVVIYMGSVHSHEASPLKSA--YVTAKHGLLGLARVLAKE--GAKHN 73
Cdd:cd05343   107 GWKEMFDVNVLALSICTREAYQSM--KERNvddGHIININSMSGHRVPPVSVFhfYAATKHAVTALTEGLRQElrEAKTH 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  74 VRSHVVCPGFVRTPLVDK---QIPEQAKELGIS-----EEDVIKKV-MLGNTVDGV 120
Cdd:cd05343   185 IRATSISPGLVETEFAFKlhdNDPEKAAATYESipclkPEDVANAVlYVLSTPPHV 240
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 2-86 5.91e-07

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: 47.23  E-value: 5.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKhMYKDDRGGVVIYMGSVhsheASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:cd05324   103 ARETMKTNFFGTVDVTQALLP-LLKKSPAGRIVNVSSG----LGSLTSAYGVSKAALNALTRILAKELKETGIKVNACCP 177


                  ....*
gi 1861134170  82 GFVRT 86
Cdd:cd05324   178 GWVKT 182
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 2-145 7.80e-07

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: 47.09  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYK---DDRGGVVIYMGSVHSHEASPLKS-AYVTAKHGLLGLARVLAKEGAKHNVRSH 77
Cdd:cd08942   106 WDKVMDINVKSVFFLTQALLPLLRAaatAENPARVINIGSIAGIVVSGLENySYGASKAAVHQLTRKLAKELAGEHITVN 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861134170  78 VVCPGFVRTPLVDKQIPEQAkelgiSEEDVIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQ 145
Cdd:cd08942   186 AIAPGRFPSKMTAFLLNDPA-----ALEAEEKSIPLGR-----WGRPEDMAGLAIMLASRAGAYLTGA 243
PRK08340 PRK08340
SDR family oxidoreductase;
1-116 8.61e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 47.11  E-value: 8.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIH-VDGAFLTTkAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVV 79
Cdd:PRK08340  101 DWLEAALLHlVAPGYLTT-LLIQAWLEKKMKGVLVYLSSVSVKEPMPPLVLADVTRAGLVQLAKGVSRTYGGKGIRAYTV 179

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1861134170  80 CPGFVRTPLVDKQIPEQAKELGISEEDVIKKVMLGNT 116
Cdd:PRK08340  180 LLGSFDTPGARENLARIAEERGVSFEETWEREVLERT 216
PRK08267 PRK08267
SDR family oxidoreductase;
3-111 1.16e-06

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 46.47  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   3 KKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPG 82
Cdd:PRK08267  102 DRVIDINVKGVLNGAHAALPYL-KATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEALDLEWRRHGIRVADVMPL 180

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1861134170  83 FVRTPLVDKQIPE----QAKELG--ISEEDVIKKV 111
Cdd:PRK08267  181 FVDTAMLDGTSNEvdagSTKRLGvrLTPEDVAEAV 215
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 7-89 1.39e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 46.47  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   7 AIHVDGAFLTTKAALKHMYKDDRGGVViYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 86
Cdd:PRK07825  107 DVNVYGVILGSKLAAPRMVPRGRGHVV-NVASLAGKIPVPGMATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNT 185


                  ...
gi 1861134170  87 PLV 89
Cdd:PRK07825  186 ELI 188
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 1-152 1.77e-06

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: 45.91  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDrGGVVIYMGSVHSHeaSPLKS--AYVTAKHGLLGLARVLAKEGAKHNVRSHV 78
Cdd:cd08935   119 GWEFVFDLNLNGSFLPSQVFGKDMLEQK-GGSIINISSMNAF--SPLTKvpAYSAAKAAVSNFTQWLAVEFATTGVRVNA 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861134170  79 VCPGFVRTPlvdkqipeQAKELGISEE----DVIKKVmLGNTVDGVFTTVQDVAQTVLFL-SAFPSAALTGQSFVVSHG 152
Cdd:cd08935   196 IAPGFFVTP--------QNRKLLINPDgsytDRSNKI-LGRTPMGRFGKPEELLGALLFLaSEKASSFVTGVVIPVDGG 265
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 1-104 2.07e-06

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 45.74  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYK-----DDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVR 75
Cdd:cd05371   104 LFQRVINVNLIGTFNVIRLAAGAMGKnepdqGGERGVIINTASVAAFEGQIGQAAYSASKGGIVGMTLPIARDLAPQGIR 183

                          90       100
                  ....*....|....*....|....*....
gi 1861134170  76 SHVVCPGFVRTPLVdKQIPEQAKELGISE 104
Cdd:cd05371   184 VVTIAPGLFDTPLL-AGLPEKVRDFLAKQ 211
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 1-153 2.17e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 45.77  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKddRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK08265  102 DWLAALDVNLVSAAMLAQAAHPHLAR--GGGAIVNFTSISAKFAQTGRWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVS 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861134170  81 PGFVRTPLVDkqipeqakELGISEEDVIKKV-----MLGNTVDGvfttvQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK08265  180 PGWTWSRVMD--------ELSGGDRAKADRVaapfhLLGRVGDP-----EEVAQVVAFLCSDAASFVTGADYAVDGGY 244
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 5-82 2.22e-06

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: 45.81  E-value: 2.22e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861134170   5 MQAIHVDGAFLTTKAALKHMYKDdrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHnVRSHVVCPG 82
Cdd:cd05348   110 LFHINVKGYILGAKAALPALYAT--EGSVIFTVSNAGFYPGGGGPLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPG 184
PRK05650 PRK05650
SDR family oxidoreductase;
1-107 2.40e-06

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 45.80  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKhMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK05650  100 DWDWQIAINLMGVVKGCKAFLP-LFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETLLVELADDEIGVHVVC 178

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1861134170  81 PGFVRTPLVDK---QIPEQAKELG-------ISEEDV 107
Cdd:PRK05650  179 PSFFQTNLLDSfrgPNPAMKAQVGkllekspITAADI 215
PRK06101 PRK06101
SDR family oxidoreductase;
28-91 2.63e-06

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 45.63  E-value: 2.63e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  28 DRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDK 91
Cdd:PRK06101  118 SCGHRVVIVGSIASELALPRAEAYGASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDK 181
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 4-86 2.68e-06

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: 45.29  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   4 KMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGF 83
Cdd:cd05356   106 DIINVNVMATLKMTRLILPGM-VKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYL 184


                  ...
gi 1861134170  84 VRT 86
Cdd:cd05356   185 VAT 187
PRK07775 PRK07775
SDR family oxidoreductase;
8-141 2.85e-06

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 45.52  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   8 IHVDGAFLTTKAALKHMYKDDRGGVViYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTP 87
Cdd:PRK07775  117 IHLVGANRLATAVLPGMIERRRGDLI-FVGSDVALRQRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTG 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  88 LVDKQIPEQakeLGISEEDVIKkvmLGNTVDGVFTTVQDVAQTVLFLSAFPSAA 141
Cdd:PRK07775  196 MGWSLPAEV---IGPMLEDWAK---WGQARHDYFLRASDLARAITFVAETPRGA 243
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 1-89 2.98e-06

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 45.33  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK05876  106 DWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAETLAREVTADGIGVSVLC 185


                  ....*....
gi 1861134170  81 PGFVRTPLV 89
Cdd:PRK05876  186 PMVVETNLV 194
PRK09186 PRK09186
flagellin modification protein A; Provisional
 8-153 3.25e-06

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 45.37  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   8 IHVDGAFLTTKAALKHmYKDDRGGVVIYMGSV--------HSHEASPLKSA--YVTAKHGLLGLARVLAKEGAKHNVRSH 77
Cdd:PRK09186  116 LHLGSSFLFSQQFAKY-FKKQGGGNLVNISSIygvvapkfEIYEGTSMTSPveYAAIKAGIIHLTKYLAKYFKDSNIRVN 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  78 VVCPGFVrtplVDKQiPEQAkeLGISEEDVIKKVMLgntvdgvftTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK09186  195 CVSPGGI----LDNQ-PEAF--LNAYKKCCNGKGML---------DPDDICGTLVFLLSDQSKYITGQNIIVDDGF 254
PRK07035 PRK07035
SDR family oxidoreductase;
2-152 3.27e-06

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 45.39  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:PRK07035  110 FQKTVDVNIRGYFFMSVEAGKLM-KEQGGGSIVNVASVNGVSPGDFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLP 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  82 GFVRTPLVDkqipeqakelGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK07035  189 GLTDTKFAS----------ALFKNDAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTGECLNVDGG 249
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 1-138 4.68e-06

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: 44.58  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGgVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd05346   102 DWETMIDTNVKGLLNVTRLILPIMIARNQG-HIINLGSIAGRYPYAGGNVYCATKAAVRQFSLNLRKDLIGTGIRVTNIE 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  81 PGFVRT--PLV----DKqipEQAKelgiseedvikkvmlgNTVDGV-FTTVQDVAQTVLFLSAFP 138
Cdd:cd05346   181 PGLVETefSLVrfhgDK---EKAD----------------KVYEGVePLTPEDIAETILWVASRP 226
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 2-134 4.98e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 44.67  E-value: 4.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASP--LKSAyvTAKHGLLGLARVLAKE-GAKHNVRSHV 78
Cdd:PRK07677  102 WNSVIDIVLNGTFYCSQAVGKYWIEKGIKGNIINMVATYAWDAGPgvIHSA--AAKAGVLAMTRTLAVEwGRKYGIRVNA 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  79 VCPGFV-RTPLVDKqipeqakeLGISEE---DVIKKVMLGNtvdgvFTTVQDVAQTVLFL 134
Cdd:PRK07677  180 IAPGPIeRTGGADK--------LWESEEaakRTIQSVPLGR-----LGTPEEIAGLAYFL 226
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 2-88 5.31e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 44.76  E-value: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKddRG-GVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK07523  111 FERLLRTNISSVFYVGQAVARHMIA--RGaGKIINIASVQSALARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIA 188


                  ....*...
gi 1861134170  81 PGFVRTPL 88
Cdd:PRK07523  189 PGYFDTPL 196
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 2-155 1.21e-05

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: 43.61  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHM-----YKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRS 76
Cdd:cd05337   105 FDRLIAINLRGPFFLTQAVARRMveqpdRFDGPHRSIIFVTSINAYLVSPNRGEYCISKAGLSMATRLLAYRLADEGIAV 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861134170  77 HVVCPGFVRTplvDKQIPEQAKelgisEEDVIKKvmlGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGWFM 155
Cdd:cd05337   185 HEIRPGLIHT---DMTAPVKEK-----YDELIAA---GLVPIRRWGQPEDIAKAVRTLASGLLPYSTGQPINIDGGLSM 252
PRK07814 PRK07814
SDR family oxidoreductase;
7-152 1.22e-05

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 43.61  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   7 AIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHnVRSHVVCPGFVRT 86
Cdd:PRK07814  116 TFNVATAHALTVAAVPLMLEHSGGGSVINISSTMGRLAGRGFAAYGTAKAALAHYTRLAALDLCPR-IRVNAIAPGSILT 194

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  87 PLVDkqipeqakelGISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK07814  195 SALE----------VVAANDELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKTLEVDGG 250
PRK06124 PRK06124
SDR family oxidoreductase;
13-152 2.19e-05

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 42.78  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  13 AFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTplvdkq 92
Cdd:PRK06124  123 PILLSRLAAQRM-KRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFAT------ 195

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  93 ipeQAKELGISEEDVIKKVMLGNTVdGVFTTVQDVAQTVLFLsAFPSAA-LTGQSFVVSHG 152
Cdd:PRK06124  196 ---ETNAAMAADPAVGPWLAQRTPL-GRWGRPEEIAGAAVFL-ASPAASyVNGHVLAVDGG 251
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 8-111 2.24e-05

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: 42.82  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   8 IHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTP 87
Cdd:cd08931   106 INVKGVLNGAYAALPYL-KATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTP 184

                          90       100
                  ....*....|....*....|....*...
gi 1861134170  88 LVD--KQIPEQAKELGI--SEEDVIKKV 111
Cdd:cd08931   185 ILTkgETGAAPKKGLGRvlPVSDVAKVV 212
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 2-87 2.60e-05

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: 42.31  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKddrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKE--GAKHNVRSHVV 79
Cdd:cd05334    93 WDLMWKQNLWTSFIASHLATKHLLS---GGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAEnsGLPAGSTANAI 169


                  ....*...
gi 1861134170  80 CPGFVRTP 87
Cdd:cd05334   170 LPVTLDTP 177
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 3-86 2.68e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 42.59  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   3 KKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPG 82
Cdd:PRK06180  103 RRQFEVNVFGAVAMTKAVLPGMRAR-RRGHIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPG 181


                  ....
gi 1861134170  83 FVRT 86
Cdd:PRK06180  182 SFRT 185
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-152 2.94e-05

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 42.46  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMY-KDDRGGVVIYMGSVH-SHEASPLKSA----YVTAKHGLLGLARVLAKEGAKHNV 74
Cdd:PRK07792  112 EWDAVIAVHLRGHFLLTRNAAAYWRaKAKAAGGPVYGRIVNtSSEAGLVGPVgqanYGAAKAGITALTLSAARALGRYGV 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  75 RSHVVCPGfVRTPL---VDKQIPEQAKElgiseedvikkvmlgnTVDGVftTVQDVAQTVLFLSAFPSAALTGQSFVVsH 151
Cdd:PRK07792  192 RANAICPR-ARTAMtadVFGDAPDVEAG----------------GIDPL--SPEHVVPLVQFLASPAAAEVNGQVFIV-Y 251


                  .
gi 1861134170 152 G 152
Cdd:PRK07792  252 G 252
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 1-92 3.76e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 42.05  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVvIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK08085  109 EWNDVIAVNQTAVFLVSQAVARYMVKRQAGKI-INICSMQSELGRDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIA 187

                          90
                  ....*....|....*.
gi 1861134170  81 PGFVRT----PLVDKQ 92
Cdd:PRK08085  188 PGYFKTemtkALVEDE 203
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 8-153 3.94e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 42.25  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   8 IHVDGAFLTTKAALKHMYKDdrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGfvrtP 87
Cdd:PRK07576  116 IDLLGTFNVLKAAYPLLRRP--GASIIQISAPQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPG----P 189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861134170  88 LVDKqipEQAKELGISEED---VIKKVMLGNtvdgvFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK07576  190 IAGT---EGMARLAPSPELqaaVAQSVPLKR-----NGTKQDIANAALFLASDMASYITGVVLPVDGGW 250
PRK07577 PRK07577
SDR family oxidoreductase;
8-152 5.14e-05

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 41.64  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   8 IHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHeASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTP 87
Cdd:PRK07577   98 LNVRAAVQVTQAFLEGM-KLREQGRIVNICSRAIF-GALDRTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETE 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  88 LVDKQIPeqakeLGISEEdvikKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK07577  176 LFRQTRP-----VGSEEE----KRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDGG 231
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
20-152 6.83e-05

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 41.24  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  20 ALKHMYKDDrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVdKQIPEQAKE 99
Cdd:PRK08063  124 AAKLMEKVG-GGKIISLSSLGSIRYLENYTTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDAL-KHFPNREEL 201

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1861134170 100 LgiseEDVIKKVMLGNTVdgvftTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK08063  202 L----EDARAKTPAGRMV-----EPEDVANAVLFLCSPEADMIRGQTIIVDGG 245
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 14-152 8.12e-05

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 41.37  E-value: 8.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  14 FLTTKAALKHMYKDDrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT-PLVDKQ 92
Cdd:PRK06113  123 FHLSQLVAPEMEKNG-GGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTdALKSVI 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  93 IPEqakelgiseedvIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK06113  202 TPE------------IEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGG 249
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 19-152 8.53e-05

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 41.08  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  19 AALKHMYKDDRGGVV----IYMGSVHsheasplKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPlvDKQIP 94
Cdd:PRK12823  126 AVLPHMLAQGGGAIVnvssIATRGIN-------RVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAP--PRRVP 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  95 EQAKELGISEEDVIKKVM---LGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK12823  197 RNAAPQSEQEKAWYQQIVdqtLDSSLMKRYGTIDEQVAAILFLASDEASYITGTVLPVGGG 257
PRK06123 PRK06123
SDR family oxidoreductase;
2-152 1.25e-04

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 40.53  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYK--DDRGGVVIYMGSVHSHEASPLKSA-YVTAKHGLLGLARVLAKEGAKHNVRSHV 78
Cdd:PRK06123  105 LTRIFATNVVGSFLCAREAVKRMSTrhGGRGGAIVNVSSMAARLGSPGEYIdYAASKGAIDTMTIGLAKEVAAEGIRVNA 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861134170  79 VCPGfvrtpLVDKQIPEQAKELGISEEdvikkvMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK06123  185 VRPG-----VIYTEIHASGGEPGRVDR------VKAGIPMGRGGTAEEVARAILWLLSDEASYTTGTFIDVSGG 247
PRK06914 PRK06914
SDR family oxidoreductase;
1-138 1.70e-04

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 40.39  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK06914  104 EYRKQFETNVFGAISVTQAVLPYMRKQ-KSGKIINISSISGRVGFPGLSPYVSSKYALEGFSESLRLELKPFGIDVALIE 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  81 PGFVRTPL--VDKQIPEQAKELGISEEDVIKKVM-LGNTVDGVFTTVQDVAQTVLFLSAFP 138
Cdd:PRK06914  183 PGSYNTNIweVGKQLAENQSETTSPYKEYMKKIQkHINSGSDTFGNPIDVANLIVEIAESK 243
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 1-89 1.97e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 40.34  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYkdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK05872  108 AFRRVIDVNLLGVFHTVRATLPALI--ERRGYVLQVSSLAAFAAAPGMAAYCASKAGVEAFANALRLEVAHHGVTVGSAY 185


                  ....*....
gi 1861134170  81 PGFVRTPLV 89
Cdd:PRK05872  186 LSWIDTDLV 194
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 17-152 2.55e-04

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 39.87  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  17 TKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTpLVDKQIPEQ 96
Cdd:cd05372   123 AKAALPIM---NPGGSIVTLSYLGSERVVPGYNVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKT-LAASGITGF 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1861134170  97 AKELGISEedviKKVMLGNTVdgvftTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05372   199 DKMLEYSE----QRAPLGRNV-----TAEEVGNTAAFLLSDLSSGITGEIIYVDGG 245
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 2-152 2.56e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 39.79  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDrGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:PRK05875  111 WRRTVDLNVNGTMYVLKHAARELVRGG-GGSFVGISSIAASNTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRP 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  82 GFVRTPLVDKqipeqakelgISEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK05875  190 GLIRTDLVAP----------ITESPELSADYRACTPLPRVGEVEDVANLAMFLLSDAASWITGQVINVDGG 250
PRK06139 PRK06139
SDR family oxidoreductase;
6-87 2.94e-04

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 39.70  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   6 QAIHVD--GAFLTTKAALKhMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKH-NVrsHV--VC 80
Cdd:PRK06139  110 QVIQTNliGYMRDAHAALP-IFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLRGFSEALRGELADHpDI--HVcdVY 186


                  ....*..
gi 1861134170  81 PGFVRTP 87
Cdd:PRK06139  187 PAFMDTP 193
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 1-110 3.34e-04

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 39.45  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDdRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK08339  108 DWEGAVKLLLYPAVYLTRALVPAMERK-GFGRIIYSTSVAIKEPIPNIALSNVVRISMAGLVRTLAKELGPKGITVNGIM 186

                          90       100       110
                  ....*....|....*....|....*....|
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDVIKK 110
Cdd:PRK08339  187 PGIIRTDRVIQLAQDRAKREGKSVEEALQE 216
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 49-152 4.25e-04

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


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 39.14  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  49 SAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPlvdKQIPEQAKelgiseEDVIKKVMLGNTVdgvfTTVQDVA 128
Cdd:TIGR02685 171 TMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLP---DAMPFEVQ------EDYRRKVPLGQRE----ASAEQIA 237

                          90       100
                  ....*....|....*....|....
gi 1861134170 129 QTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:TIGR02685 238 DVVIFLVSPKAKYITGTCIKVDGG 261
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 2-107 1.40e-03

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: 37.81  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRG-GVVIYMGSVHSHEASPlksAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd09763   113 WDDINNVGLRAHYACSVYAAPLMVKAGKGlIVIISSTGGLEYLFNV---AYGVGKAAIDRMAADMAHELKPHGVAVVSLW 189

                          90       100
                  ....*....|....*....|....*..
gi 1861134170  81 PGFVRTPLVDKQIPEQAKELGISEEDV 107
Cdd:cd09763   190 PGFVRTELVLEMPEDDEGSWHAKERDA 216
PRK08703 PRK08703
SDR family oxidoreductase;
1-98 1.63e-03

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 37.22  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKhMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKH-NVRSHVV 79
Cdd:PRK08703  111 EWVNQYRINTVAPMGLTRALFP-LLKQSPDASVIFVGESHGETPKAYWGGFGASKAALNYLCKVAADEWERFgNLRANVL 189

                          90
                  ....*....|....*....
gi 1861134170  80 CPGFVRTPLVDKQIPEQAK 98
Cdd:PRK08703  190 VPGPINSPQRIKSHPGEAK 208
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 42-152 1.73e-03

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: 37.47  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  42 HEASPLKSAYVTAKHGLLGLARVLAKE-GAKHNVRSHVVCPGFVRTPLvdkqipeqakeLGISEEDVIKKVMLGNTVD-- 118
Cdd:cd05328   142 HAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPI-----------LQAFLQDPRGGESVDAFVTpm 210

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1861134170 119 GVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:cd05328   211 GRRAEPDEIAPVIAFLASDAASWINGANLFVDGG 244
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
35-152 1.78e-03

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 37.39  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  35 YMGSVhshEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDkqipeqakelGISEEDVIKKVMLG 114
Cdd:PRK06079  144 YFGSE---RAIPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAVT----------GIKGHKDLLKESDS 210

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1861134170 115 NTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK06079  211 RTVDGVGVTIEEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-88 2.36e-03

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 36.86  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   7 AIHVDGAFLTTKAALKHMYKDDRG-----GVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:PRK12745  111 AINLRGPFFLTQAVAKRMLAQPEPeelphRSIVFVSSVNAIMVSPNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRP 190


                  ....*..
gi 1861134170  82 GFVRTPL 88
Cdd:PRK12745  191 GLIKTDM 197
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 1-86 2.41e-03

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 36.77  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVhSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK08945  116 VWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSV-GRQGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCIN 194


                  ....*.
gi 1861134170  81 PGFVRT 86
Cdd:PRK08945  195 PGGTRT 200
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 1-100 2.42e-03

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: 36.87  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKhMYKDDRGGVViYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:cd09805   102 DYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVV-NVSSMGGRVPFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIE 179

                          90       100
                  ....*....|....*....|..
gi 1861134170  81 PGFVRTPLVDKQIPE--QAKEL 100
Cdd:cd09805   180 PGNFKTGITGNSELWekQAKKL 201
PRK05855 PRK05855
SDR family oxidoreductase;
1-90 3.04e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 36.88  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   1 DWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK05855  415 DWDRVLDVNLWGVIHGCRLFGRQMVERGTGGHIVNVASAAAYAPSRSLPAYATSKAAVLMLSECLRAELAAAGIGVTAIC 494

                          90
                  ....*....|
gi 1861134170  81 PGFVRTPLVD 90
Cdd:PRK05855  495 PGFVDTNIVA 504
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 2-152 3.81e-03

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 36.21  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   2 WKKMQAIHVDGAFLTTKAALKHMYKDDRggvVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCP 81
Cdd:PRK12747  112 FDRMVSVNAKAPFFIIQQALSRLRDNSR---IINISSAATRISLPDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILP 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861134170  82 GFVRTPLvdkqipeQAKELgisEEDVIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQSFVVSHG 152
Cdd:PRK12747  189 GFIKTDM-------NAELL---SDPMMKQYATTISAFNRLGEVEDIADTAAFLASPDSRWVTGQLIDVSGG 249
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-155 3.92e-03

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 36.30  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   7 AIHVDGAFLTTkAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 86
Cdd:PRK12859  125 MVNVRATTLLS-SQFARGFDKKSGGRIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDT 203

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861134170  87 PLvdkqipeqakelgISEEdvIKKVMLGNTVDGVFTTVQDVAQTVLFLSAFPSAALTGQsFVVSHGWFM 155
Cdd:PRK12859  204 GW-------------MTEE--IKQGLLPMFPFGRIGEPKDAARLIKFLASEEAEWITGQ-IIHSEGGFK 256
PRK09730 PRK09730
SDR family oxidoreductase;
4-86 4.28e-03

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 36.37  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170   4 KMQAIHVDGAFLTTKAALKHMYKDD--RGGVVIYMGSVHSHEASPLKSA-YVTAKHGLLGLARVLAKEGAKHNVRSHVVC 80
Cdd:PRK09730  106 RVLSTNVTGYFLCCREAVKRMALKHggSGGAIVNVSSAASRLGAPGEYVdYAASKGAIDTLTTGLSLEVAAQGIRVNCVR 185


                  ....*.
gi 1861134170  81 PGFVRT 86
Cdd:PRK09730  186 PGFIYT 191
PRK09291 PRK09291
SDR family oxidoreductase;
8-86 5.61e-03

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 35.74  E-value: 5.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861134170   8 IHVDGAFLTTKAALKHMYKDDRGGVViYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 86
Cdd:PRK09291  103 TNVFGPLELTQGFVRKMVARGKGKVV-FTSSMAGLITGPFTGAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK07041 PRK07041
SDR family oxidoreductase;
12-152 5.77e-03

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 35.78  E-value: 5.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  12 GAFLTTKAAlkhmyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKhnVRSHVVCPGFVRTPLVDK 91
Cdd:PRK07041  103 GAYRVARAA-----RIAPGGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLALELAP--VRVNTVSPGLVDTPLWSK 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861134170  92 QIPEQakelgiseedviKKVMLGNTVD----GVFTTVQDVAQTVLFLSAFPSAalTGQSFVVSHG 152
Cdd:PRK07041  176 LAGDA------------REAMFAAAAErlpaRRVGQPEDVANAILFLAANGFT--TGSTVLVDGG 226
PRK12746 PRK12746
SDR family oxidoreductase;
50-153 7.41e-03

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 35.39  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861134170  50 AYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLvdkqipeQAKELGISEedvIKKVMLGNTVDGVFTTVQDVAQ 129
Cdd:PRK12746  159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI-------NAKLLDDPE---IRNFATNSSVFGRIGQVEDIAD 228

                          90       100
                  ....*....|....*....|....
gi 1861134170 130 TVLFLSAFPSAALTGQSFVVSHGW 153
Cdd:PRK12746  229 AVAFLASSDSRWVTGQIIDVSGGF 252
 
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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