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Conserved domains on  [gi|17559964|ref|NP_506407|]
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DeHydrogenases, Short chain [Caenorhabditis elegans]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143154)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  19011750|19011748|12604210|19027726|20423462
SCOP:  4000029

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 7-248 3.77e-66

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


:

Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 204.84  E-value: 3.77e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHKDIQIIiATCRDPSKAEELSNLK--DSRLHILPLDIDCDesISKLYAEVEKLVGEDGLTV 84
Cdd:cd05325   2 LITGASRGIGLELVRQLLARGNNTVI-ATCRDPSAATELAALGasHSRLHILELDVTDE--IAESAEAVAERLGDAGLDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  85 LLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNISSTAASvekIDGTF 164
Cdd:cd05325  79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGA-----------RAKIINISSRVGS---IGDNT 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964 165 NGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAM----LEIEDATKTLSDNILTLGNAHHGAYL 240
Cdd:cd05325 145 SGGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKnkgpITPEESVAGLLKVIDNLNEEDSGKFL 224


                ....*...
gi 17559964 241 NADLTVIP 248
Cdd:cd05325 225 DYDGTEIP 232
 
Name Accession Description Interval E-value
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 7-248 3.77e-66

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 204.84  E-value: 3.77e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHKDIQIIiATCRDPSKAEELSNLK--DSRLHILPLDIDCDesISKLYAEVEKLVGEDGLTV 84
Cdd:cd05325   2 LITGASRGIGLELVRQLLARGNNTVI-ATCRDPSAATELAALGasHSRLHILELDVTDE--IAESAEAVAERLGDAGLDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  85 LLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNISSTAASvekIDGTF 164
Cdd:cd05325  79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGA-----------RAKIINISSRVGS---IGDNT 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964 165 NGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAM----LEIEDATKTLSDNILTLGNAHHGAYL 240
Cdd:cd05325 145 SGGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKnkgpITPEESVAGLLKVIDNLNEEDSGKFL 224


                ....*...
gi 17559964 241 NADLTVIP 248
Cdd:cd05325 225 DYDGTEIP 232
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-214 9.30e-41

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 140.39  E-value: 9.30e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELSNL---KDSRLHILPLDIDCDESISKLYAEVEKLV 77
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGAR--VVLVARDAERLEALAAElraAGARVEVVALDVTDPDAVAALAEAVLARF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  78 GedGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISSTAasv 157
Cdd:COG0300  81 G--PIDVLVNNAGVGGGGPFE-ELDLEDLRRVFEVNVFGPVRLTRALLPLMRAR-----------GRGRIVNVSSVA--- 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17559964 158 ekidGTFNGP-LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAM 214
Cdd:COG0300 144 ----GLRGLPgMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGA 197
PRK08177 PRK08177
SDR family oxidoreductase;
3-228 1.51e-31

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 115.51  E-value: 1.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    3 PKSLLITGANRGIGLGLLKQFlkHKDIQIIIATCRDPSKAEELSNLkdSRLHILPLDIDCDESISKLyaeVEKLVGEDgL 82
Cdd:PRK08177   1 KRTALIIGASRGLGLGLVDRL--LERGWQVTATVRGPQQDTALQAL--PGVHIEKLDMNDPASLDQL---LQRLQGQR-F 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   83 TVLLNNAGILLPYDVEGEKNRKTLIRQL-ETNSVSTALITQEFLPLLKKaaakngGDGysinraAIVNISSTAASVEKID 161
Cdd:PRK08177  73 DLLFVNAGISGPAHQSAADATAAEIGQLfLTNAIAPIRLARRLLGQVRP------GQG------VLAFMSSQLGSVELPD 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559964  162 GtfnGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATKTLSDNI 228
Cdd:PRK08177 141 G---GEMPLYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMGGDNAPLDVETSVKGLVEQI 204
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-208 4.16e-27

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 103.08  E-value: 4.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964     7 LITGANRGIGLGLLKQFLKhKDIQIIIATcRDPSKAEEL-SNLKD--SRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:pfam00106   4 LVTGASSGIGRAIAKRLAK-EGAKVVLVD-RSEEKLEAVaKELGAlgGKALFIQGDVTDRAQVKALVEQAVERLG--RLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    84 VLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaKNGGDgysinraaIVNISSTAASVekidGT 163
Cdd:pfam00106  80 ILVNNAGITGLGPFS-ELSDEDWERVIDVNLTGVFNLTRAVLPAMIK---GSGGR--------IVNISSVAGLV----PY 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 17559964   164 FNGPlvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:pfam00106 144 PGGS--AYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDM 186
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 6-208 1.29e-07

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 51.07  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964     6 LLITGANRGIGLGLLKQFLKHKDIQIIIAT--CRD-----PSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVG 78
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKCLKSPGSVLVlsARNdealrQLKAEIGAERSGLRVVRVSLDLGAEAGLEQLLKALRELPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    79 EDGLT--VLLNNAGILlpYDV-EGEK---NRKTLIRQLETNSVSTALITQEFLPLLKkaaaknggDGYSINRaAIVNISS 152
Cdd:TIGR01500  83 PKGLQrlLLINNAGTL--GDVsKGFVdlsDSTQVQNYWALNLTSMLCLTSSVLKAFK--------DSPGLNR-TVVNISS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17559964   153 TAAsVEKIDGtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:TIGR01500 152 LCA-IQPFKG-----WALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDM 201
 
Name Accession Description Interval E-value
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 7-248 3.77e-66

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 204.84  E-value: 3.77e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHKDIQIIiATCRDPSKAEELSNLK--DSRLHILPLDIDCDesISKLYAEVEKLVGEDGLTV 84
Cdd:cd05325   2 LITGASRGIGLELVRQLLARGNNTVI-ATCRDPSAATELAALGasHSRLHILELDVTDE--IAESAEAVAERLGDAGLDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  85 LLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNISSTAASvekIDGTF 164
Cdd:cd05325  79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGA-----------RAKIINISSRVGS---IGDNT 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964 165 NGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAM----LEIEDATKTLSDNILTLGNAHHGAYL 240
Cdd:cd05325 145 SGGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKnkgpITPEESVAGLLKVIDNLNEEDSGKFL 224


                ....*...
gi 17559964 241 NADLTVIP 248
Cdd:cd05325 225 DYDGTEIP 232
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 4-248 1.61e-47

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: 157.01  E-value: 1.61e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIaTCRDPSKAEELSN-LKDSRLHILP--LDIDCDESISKLYAEVEKLVGed 80
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVIL-TARDVERGQAAVEkLRAEGLSVRFhqLDVTDDASIEAAADFVEEKYG-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  81 GLTVLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTAASVEki 160
Cdd:cd05324  78 GLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPA-----------GRIVNVSSGLGSLT-- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964 161 dgtfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATKTLSDNILTLGNAHHGAYL 240
Cdd:cd05324 145 --------SAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAPKTPEEGAETPVYLALLPPDGEPTGKF 216


                ....*...
gi 17559964 241 NADLTVIP 248
Cdd:cd05324 217 FSDKKVVP 224
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-214 9.30e-41

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 140.39  E-value: 9.30e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELSNL---KDSRLHILPLDIDCDESISKLYAEVEKLV 77
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGAR--VVLVARDAERLEALAAElraAGARVEVVALDVTDPDAVAALAEAVLARF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  78 GedGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISSTAasv 157
Cdd:COG0300  81 G--PIDVLVNNAGVGGGGPFE-ELDLEDLRRVFEVNVFGPVRLTRALLPLMRAR-----------GRGRIVNVSSVA--- 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17559964 158 ekidGTFNGP-LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAM 214
Cdd:COG0300 144 ----GLRGLPgMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGA 197
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 4-208 4.45e-37

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 130.81  E-value: 4.45e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYR--VIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFG--RID 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaakngGDGYsinraaIVNISSTAASVekidGT 163
Cdd:cd05374  77 VLVNNAGYGLFGPLE-ETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQ-----GSGR------IVNVSSVAGLV----PT 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17559964 164 -FNGPlvaYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05374 141 pFLGP---YCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGF 183
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-228 2.48e-34

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: 123.74  E-value: 2.48e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELSNL---KDSRLHILPLDIDCDESISKLYAEVEKLV 77
Cdd:COG1028   4 LKGKVALVTGGSSGIGRAIARALAAEGAR--VVITDRDAEALEAAAAElraAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  78 GedGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNISSTAASV 157
Cdd:COG1028  82 G--RLDILVNNAGITPPGPLE-ELTEEDWDRVLDVNLKGPFLLTRAALPHMRERG-----------GGRIVNISSIAGLR 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559964 158 ekidgtFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMggANAMLEIEDATKTLSDNI 228
Cdd:COG1028 148 ------GSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPM--TRALLGAEEVREALAARI 210
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 7-208 1.80e-33

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: 120.85  E-value: 1.80e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELSNLKDS--RLHILPLDIDCDESISKLYAEVEKLVGedGLTV 84
Cdd:cd05233   2 LVTGASSGIGRAIARRLAREGAK--VVLADRNEEALAELAAIEALggNAVAVQADVSDEEDVEALVEEALEEFG--RLDI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  85 LLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaakNGGdgysinraAIVNISSTAASVekidgtF 164
Cdd:cd05233  78 LVNNAGIARPGPLE-ELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQ---GGG--------RIVNISSVAGLR------P 139

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17559964 165 NGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05233 140 LPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPM 183
PRK08177 PRK08177
SDR family oxidoreductase;
3-228 1.51e-31

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 115.51  E-value: 1.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    3 PKSLLITGANRGIGLGLLKQFlkHKDIQIIIATCRDPSKAEELSNLkdSRLHILPLDIDCDESISKLyaeVEKLVGEDgL 82
Cdd:PRK08177   1 KRTALIIGASRGLGLGLVDRL--LERGWQVTATVRGPQQDTALQAL--PGVHIEKLDMNDPASLDQL---LQRLQGQR-F 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   83 TVLLNNAGILLPYDVEGEKNRKTLIRQL-ETNSVSTALITQEFLPLLKKaaakngGDGysinraAIVNISSTAASVEKID 161
Cdd:PRK08177  73 DLLFVNAGISGPAHQSAADATAAEIGQLfLTNAIAPIRLARRLLGQVRP------GQG------VLAFMSSQLGSVELPD 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559964  162 GtfnGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATKTLSDNI 228
Cdd:PRK08177 141 G---GEMPLYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMGGDNAPLDVETSVKGLVEQI 204
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-222 2.63e-30

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: 112.97  E-value: 2.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MS--PKSLLITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVG 78
Cdd:COG4221   1 MSdkGKVALITGASSGIGAATARALAAAGAR--VVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  79 edGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKkaaAKNGGDgysinraaIVNISSTAASVe 158
Cdd:COG4221  79 --RLDVLVNNAGVALLGPLE-ELDPEDWDRMIDVNVKGVLYVTRAALPAMR---ARGSGH--------IVNISSIAGLR- 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559964 159 kidgTFNGpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATK 222
Cdd:COG4221 144 ----PYPG-GAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAA 202
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 1-209 8.26e-30

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 111.34  E-value: 8.26e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQFLKHKDIQIIIAtCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVeklvgeD 80
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKKVYAA-VRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQA------K 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  81 GLTVLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKkaaaKNGGdgysinrAAIVNISSTAASVeki 160
Cdd:cd05354  74 DVDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLK----ANGG-------GAIVNLNSVASLK--- 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17559964 161 dgtfNGPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMG 209
Cdd:cd05354 140 ----NFPAMGtYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMA 185
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-208 4.16e-27

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 103.08  E-value: 4.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964     7 LITGANRGIGLGLLKQFLKhKDIQIIIATcRDPSKAEEL-SNLKD--SRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:pfam00106   4 LVTGASSGIGRAIAKRLAK-EGAKVVLVD-RSEEKLEAVaKELGAlgGKALFIQGDVTDRAQVKALVEQAVERLG--RLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    84 VLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaKNGGDgysinraaIVNISSTAASVekidGT 163
Cdd:pfam00106  80 ILVNNAGITGLGPFS-ELSDEDWERVIDVNLTGVFNLTRAVLPAMIK---GSGGR--------IVNISSVAGLV----PY 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 17559964   164 FNGPlvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:pfam00106 144 PGGS--AYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDM 186
PRK08264 PRK08264
SDR family oxidoreductase;
4-208 1.55e-26

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 103.05  E-value: 1.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHkDIQIIIATCRDPSKAEELsnlkDSRLHILPLDIDCDESISKLyAEVEKLVgedglT 83
Cdd:PRK08264   7 KVVLVTGANRGIGRAFVEQLLAR-GAAKVYAAARDPESVTDL----GPRVVPLQLDVTDPASVAAA-AEAASDV-----T 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKkaaaKNGGdgysinrAAIVNISSTAASVekidgt 163
Cdd:PRK08264  76 ILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLA----ANGG-------GAIVNVLSVLSWV------ 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17559964  164 fNGPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK08264 139 -NFPNLGtYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDM 183
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 4-224 1.04e-25

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: 101.59  E-value: 1.04e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFlkHKDIQIIIATCRDP--SKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEDG 81
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKL--DSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  82 LTVLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysinRAAIVNISSTAASVEKID 161
Cdd:cd09805  79 LWGLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRA------------KGRVVNVSSMGGRVPFPA 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559964 162 GTfngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGaNAMLEIEDATKTL 224
Cdd:cd09805 147 GG------AYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITG-NSELWEKQAKKLW 202
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 1-213 8.27e-25

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 98.31  E-value: 8.27e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQFLKhKDIQIIIaTCRDPSKAEELSNLKDsRLHILPLDIDCDESISKLYAEVEKLVGEd 80
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHA-RGNTVII-TGRREEKLEEAAAANP-GLHTIVLDVADPASIAALAEQVTAEFPD- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  81 gLTVLLNNAGILLPYDVEGEKNRKTLIRQ-LETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTAASVek 159
Cdd:COG3967  79 -LNVLINNAGIMRAEDLLDEAEDLADAEReITTNLLGPIRLTAAFLPHLKAQPE-----------AAIVNVSSGLAFV-- 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17559964 160 idgtfngPLVA---YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANA 213
Cdd:COG3967 145 -------PLAVtptYSATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQG 194
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 4-208 7.75e-23

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 93.83  E-value: 7.75e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDiQIIIAtCRDPSKAEE-----LSNLKDSRLHILPLDIDCDESISKLYAEVEKLVG 78
Cdd:cd05327   2 KVVVITGANSGIGKETARELAKRGA-HVIIA-CRNEEKGEEaaaeiKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  79 EdgLTVLLNNAGILLPydvegeKNRKT---LIRQLETNSVSTALITQEFLPLLKKAAAKNggdgysinraaIVNISSTAA 155
Cdd:cd05327  80 R--LDILINNAGIMAP------PRRLTkdgFELQFAVNYLGHFLLTNLLLPVLKASAPSR-----------IVNVSSIAH 140

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559964 156 SVEKIDGTFN--------GPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05327 141 RAGPIDFNDLdlennkeySPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTEL 201
PRK06953 PRK06953
SDR family oxidoreductase;
4-248 3.86e-22

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 90.90  E-value: 3.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKhkDIQIIIATCRDPSKAEELSNLKdsrLHILPLDIDCDESISKLYAeveKLVGEdGLT 83
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRA--DGWRVIATARDAAALAALQALG---AEALALDVADPASVAGLAW---KLDGE-ALD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGILLPYDVEGEK-NRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysinRAAIVNISSTAASVEKIDG 162
Cdd:PRK06953  73 AAVYVAGVYGPRTEGVEPiTREDFDAVMHTNVLGPMQLLPILLPLVEAA------------GGVLAVLSSRMGSIGDATG 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  163 TFnGPLvaYRMSKSALNSFAKSCSIDlAKYHILVTsFCPGWVKTGMGGANAMLEIEDATKTLSDNILTLGNAHHGAYLNA 242
Cdd:PRK06953 141 TT-GWL--YRASKAALNDALRAASLQ-ARHATCIA-LHPGWVRTDMGGAQAALDPAQSVAGMRRVIAQATRRDNGRFFQY 215


                 ....*.
gi 17559964  243 DLTVIP 248
Cdd:PRK06953 216 DGVELS 221
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-209 1.17e-21

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 90.29  E-value: 1.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIATCRDPSKAEELSN-LKDSRLHILPL--DIDCDESISKLYAEVEKLVGed 80
Cdd:PRK05565   6 KVAIVTGASGGIGRAIAELLAK-EGAKVVIAYDINEEAAQELLEeIKEEGGDAIAVkaDVSSEEDVENLVEQIVEKFG-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLTVLLNNAGIL---LPYDVEGEKNRKTLirqlETNSVSTALITQEFLPLLKKaaaKNGGdgysinraAIVNISSTAASV 157
Cdd:PRK05565  83 KIDILVNNAGISnfgLVTDMTDEEWDRVI----DVNLTGVMLLTRYALPYMIK---RKSG--------VIVNISSIWGLI 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17559964  158 EKIDGtfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMG 209
Cdd:PRK05565 148 GASCE------VLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMW 193
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 10-211 2.82e-20

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: 86.33  E-value: 2.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    10 GA--NRGIGLGLLKQFLKH--KdiqiIIATCRDPSKAEELSNLKDS-RLHILPLDIDCDESISKLYAEVEKLVGedGLTV 84
Cdd:pfam13561   1 GAanESGIGWAIARALAEEgaE----VVLTDLNEALAKRVEELAEElGAAVLPCDVTDEEQVEALVAAAVEKFG--RLDI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    85 LLNNAGILLPYDVEGEK-NRKTLIRQLETNSVSTALITQEFLPLLKKaaaknGGdgysinraAIVNISSTAAsvEKIDGT 163
Cdd:pfam13561  75 LVNNAGFAPKLKGPFLDtSREDFDRALDVNLYSLFLLAKAALPLMKE-----GG--------SIVNLSSIGA--ERVVPN 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 17559964   164 FNgplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGA 211
Cdd:pfam13561 140 YN----AYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLAASG 183
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-208 6.33e-20

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 85.61  E-value: 6.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIATCRDPSKAEELsnlKDSRLHILPLDIDCDESISKLYAEVEKLVGEdgLT 83
Cdd:PRK06463   8 KVALITGGTRGIGRAIAEAFLR-EGAKVAVLYNSAENEAKEL---REKGVFTIKCDVGNRDQVKKSKEVVEKEFGR--VD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGI--LLPYD-VEGEKNRktliRQLETNSVSTALITQEFLPLLKKAaaKNGgdgysinraAIVNISSTAASVEKI 160
Cdd:PRK06463  82 VLVNNAGImyLMPFEeFDEEKYN----KMIKINLNGAIYTTYEFLPLLKLS--KNG---------AIVNIASNAGIGTAA 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17559964  161 DGTfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK06463 147 EGT-----TFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDM 189
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-208 1.62e-19

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 84.44  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKH--KdiqiIIATCRDPSKAEELSN-LKDS--RLHILPLDIDCDESISKLYAEVEK 75
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADgaK----VVIYDSNEEAAEALAAeLRAAggEARVLVFDVSDEAAVRALIEAAVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   76 LVGedGLTVLLNNAGIllpydvegekNRKTLIRQL---------ETNSVSTALITQEFLPLLKKAaakngGDGysinraA 146
Cdd:PRK05653  79 AFG--ALDILVNNAGI----------TRDALLPRMseedwdrviDVNLTGTFNVVRAALPPMIKA-----RYG------R 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559964  147 IVNISSTAASVekidGtfNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK05653 136 IVNISSVSGVT----G--NPGQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDM 191
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 6-209 1.70e-19

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 84.26  E-value: 1.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   6 LLITGANRGIGLGLLKQFLKHKDIQIIIATCRD--PSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdgLT 83
Cdd:cd05367   2 IILTGASRGIGRALAEELLKRGSPSVVVLLARSeePLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDGE--RD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaknggdgYSINRaAIVNISSTAASvekidGT 163
Cdd:cd05367  80 LLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKK---------RGLKK-TVVNVSSGAAV-----NP 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17559964 164 FNGpLVAYRMSKSALNSFAKSCSIDLAKYHILvtSFCPGWVKTGMG 209
Cdd:cd05367 145 FKG-WGLYCSSKAARDMFFRVLAAEEPDVRVL--SYAPGVVDTDMQ 187
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 4-208 2.59e-19

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: 83.18  E-value: 2.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELSnLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYR--VSLGLRNPEDLAALS-ASGGDVEAVPYDARDPEDARALVDALRDRFG--RID 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNISSTAAsveKIDGT 163
Cdd:cd08932  76 VLVHNAGIGRPTTLR-EGSDAELEAHFSINVIAPAELTRALLPALREAG-----------SGRVVFLNSLSG---KRVLA 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17559964 164 FNgplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd08932 141 GN---AGYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPM 182
PRK12826 PRK12826
SDR family oxidoreductase;
1-210 2.81e-19

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 83.81  E-value: 2.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLK--HKdiqiIIATCRDPSKAEELSNLKDS---RLHILPLDIDCDESISKLYAEVEK 75
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAAdgAE----VIVVDICGDDAAATAELVEAaggKARARQVDVRDRAALKAAVAAGVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   76 LVGedGLTVLLNNAGILlPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaakNGGdgysinraAIVNISSTAA 155
Cdd:PRK12826  80 DFG--RLDILVANAGIF-PLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRA---GGG--------RIVLTSSVAG 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17559964  156 SVEKIDGtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGG 210
Cdd:PRK12826 146 PRVGYPG-----LAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAG 195
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 7-208 3.50e-19

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: 83.45  E-value: 3.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHKdIQIIIATcRDPSKAEELSNL---KDSRLHILPLDIDCDESISKLYAEVEKLVGEdgLT 83
Cdd:cd05339   3 LITGGGSGIGRLLALEFAKRG-AKVVILD-INEKGAEETANNvrkAGGKVHYYKCDVSKREEVYEAAKKIKKEVGD--VT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGI---LLPYDVEGEKNRKTlirqLETNSVSTALITQEFLPLLKKaaaknggdgysINRAAIVNISSTAASVeki 160
Cdd:cd05339  79 ILINNAGVvsgKKLLELPDEEIEKT----FEVNTLAHFWTTKAFLPDMLE-----------RNHGHIVTIASVAGLI--- 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17559964 161 dgTFNGpLVAYRMSKSALNSFAKSCSIDLAKYH---ILVTSFCPGWVKTGM 208
Cdd:cd05339 141 --SPAG-LADYCASKAAAVGFHESLRLELKAYGkpgIKTTLVCPYFINTGM 188
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-208 8.18e-19

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 82.55  E-value: 8.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFlkHKD-IQIIIATCRDPSKAEELSN-LKDS--RLHILPLDIDCDESISKLYAEVEKL 76
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERL--AAQgANVVINYASSEAGAEALVAeIGALggKALAVQGDVSDAESVERAVDEAKAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   77 VGedGLTVLLNNAGILlpydvegeknRKTLIRQ---------LETNSVSTALITQEFLPLLKKaaaKNGGdgysinraAI 147
Cdd:PRK05557  81 FG--GVDILVNNAGIT----------RDNLLMRmkeedwdrvIDTNLTGVFNLTKAVARPMMK---QRSG--------RI 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559964  148 VNISSTAASVekidGTFNgpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK05557 138 INISSVVGLM----GNPG--QANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDM 192
PRK06484 PRK06484
short chain dehydrogenase; Validated
 4-222 8.77e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 84.90  E-value: 8.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdgLT 83
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQ--VVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGR--ID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGILLPY-----DVEGEKnrktLIRQLETNSVSTALITQEFLPLLkkAAAKNGgdgysinrAAIVNISSTAASVE 158
Cdd:PRK06484  82 VLVNNAGVTDPTmtatlDTTLEE----FARLQAINLTGAYLVAREALRLM--IEQGHG--------AAIVNVASGAGLVA 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559964  159 kidgtfNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMgganaMLEIEDATK 222
Cdd:PRK06484 148 ------LPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQM-----VAELERAGK 200
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
4-208 9.55e-19

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 82.42  E-value: 9.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEDGLT 83
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLE-KGTHVISISRTENKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQEDNVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 --VLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFlplLKKAAAKNGgdgysinRAAIVNISSTAAsvekid 161
Cdd:PRK06924  81 siHLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTF---MKHTKDWKV-------DKRVINISSGAA------ 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17559964  162 gtfNGPLV---AYRMSKSALNSFAKSCSIDLAK--YHILVTSFCPGWVKTGM 208
Cdd:PRK06924 145 ---KNPYFgwsAYCSSKAGLDMFTQTVATEQEEeeYPVKIVAFSPGVMDTNM 193
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 1-237 9.73e-19

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: 82.46  E-value: 9.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQFLKHKDIQIIIAtcRDPSKAEEL------SNLKDSRLHILPLDIDCDESISKLYAEVE 74
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTG--RDAERLEETrqsclqAGVSEKKILLVVADLTEEEGQDRIISTTL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  75 KLVGEdgLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysinRAAIVNISSTA 154
Cdd:cd05364  79 AKFGR--LDILVNNAGILAKGGGE-DQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT------------KGEIVNVSSVA 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964 155 ASVekidgTFNGPLvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEiEDATKTLSDNILTLGNA 234
Cdd:cd05364 144 GGR-----SFPGVL-YYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMPE-EQYIKFLSRAKETHPLG 216


                ...
gi 17559964 235 HHG 237
Cdd:cd05364 217 RPG 219
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 4-208 3.31e-18

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: 80.67  E-value: 3.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFlkHKDIQIIIATCRDPSKAEELSNLKD---SRLHILPLDIDCDESISKLYAEVEKLVGed 80
Cdd:cd05333   1 KVALVTGASRGIGRAIALRL--AAEGAKVAVTDRSEEAAAETVEEIKalgGNAAALEADVSDREAVEALVEKVEAEFG-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  81 GLTVLLNNAGIllpydvegekNRKTLIRQ---------LETNSVSTALITQEFLPLLKKAaaKNGgdgysinraAIVNIS 151
Cdd:cd05333  77 PVDILVNNAGI----------TRDNLLMRmseedwdavINVNLTGVFNVTQAVIRAMIKR--RSG---------RIINIS 135

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17559964 152 STAASVEKIdGTFNgplvaYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05333 136 SVVGLIGNP-GQAN-----YAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDM 186
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 1-202 3.83e-18

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: 80.60  E-value: 3.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQFLKHKDIQIIIA----TCRDpsKAEELSNLKDSrlHILPLDIDCDESISKLYAEVEKL 76
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISArkaeACAD--AAEELSAYGEC--IAIPADLSSEEGIEALVARVAER 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  77 vgEDGLTVLLNNAGIL--LPYDVEGEKNRKTLirqLETNSVSTALITQEFLPLLKKAAAKNggdgysiNRAAIVNISSTA 154
Cdd:cd08942  80 --SDRLDVLVNNAGATwgAPLEAFPESGWDKV---MDINVKSVFFLTQALLPLLRAAATAE-------NPARVINIGSIA 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17559964 155 ASVekIDGTFNgplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPG 202
Cdd:cd08942 148 GIV--VSGLEN---YSYGASKAAVHQLTRKLAKELAGEHITVNAIAPG 190
PRK06914 PRK06914
SDR family oxidoreductase;
1-206 5.39e-18

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 80.84  E-value: 5.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLgLLKQFLKHKDIQiIIATCRDPSKAEEL------SNLKDsRLHILPLDIDCDESISKLYAEVE 74
Cdd:PRK06914   1 MNKKIAIVTGASSGFGL-LTTLELAKKGYL-VIATMRNPEKQENLlsqatqLNLQQ-NIKVQQLDVTDQNSIHNFQLVLK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   75 KLvgeDGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISSta 154
Cdd:PRK06914  78 EI---GRIDLLVNNAGYANGGFVE-EIPVEEYRKQFETNVFGAISVTQAVLPYMRKQ-----------KSGKIINISS-- 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17559964  155 asvekIDGTFNGP-LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK06914 141 -----ISGRVGFPgLSPYVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNT 188
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 7-222 7.13e-18

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: 79.60  E-value: 7.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKhKDIQIIIATcRDPSKAEEL-------SNLKDSRLHILPLDIDCDESISKLYAEVEKLVGE 79
Cdd:cd08939   5 LITGGSSGIGKALAKELVK-EGANVIIVA-RSESKLEEAveeieaeANASGQKVSYISADLSDYEEVEQAFAQAVEKGGP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  80 dgLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAAKNggdgysinraaIVNISSTAASVEK 159
Cdd:cd08939  83 --PDLVVNCAGISIPGLFE-DLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGH-----------IVFVSSQAALVGI 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559964 160 IDGTfngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTgmgganAMLEIEDATK 222
Cdd:cd08939 149 YGYS------AYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDT------PGFEEENKTK 199
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 4-226 1.01e-17

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: 79.09  E-value: 1.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLlKQFLKHKDIQIIIaTCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:cd08929   1 KAALVTGASRGIGEAT-ARLLHAEGYRVGI-CARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaKNGGdgysinraAIVNISSTAASvekidGT 163
Cdd:cd08929  77 ALVNNAGVGVMKPVE-ELTPEEWRLVLDTNLTGAFYCIHKAAPALLR---RGGG--------TIVNVGSLAGK-----NA 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559964 164 FNGPlVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANA----MLEIEDATKTLSD 226
Cdd:cd08929 140 FKGG-AAYNASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGSPEgqawKLAPEDVAQAVLF 205
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 4-206 1.14e-17

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: 79.25  E-value: 1.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLK--HKdiqiIIATCRdpsKAEELSNLKD-------SRLHILPLDIDCDESISKLYAEVE 74
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKagAK----LILTGR---RAERLQELADelgakfpVKVLPLQLDVSDRESIEAALENLP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  75 KlvGEDGLTVLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKkaaAKNGGDgysinraaIVNISSTA 154
Cdd:cd05346  74 E--EFRDIDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMI---ARNQGH--------IINLGSIA 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17559964 155 ASvekidGTFNGPLVaYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd05346 141 GR-----YPYAGGNV-YCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVET 186
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 1-213 1.42e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 79.70  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESIsklYAEVEKLVGED 80
Cdd:PRK08263   1 MMEKVWFITGASRGFGRAWTEAALERGDR--VVATARDTATLADLAEKYGDRLLPLALDVTDRAAV---FAAVETAVEHF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 G-LTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKkaaAKNGGDgysinraaIVNISStaasvek 159
Cdd:PRK08263  76 GrLDIVVNNAGYGLFGMIE-EVTESEARAQIDTNFFGALWVTQAVLPYLR---EQRSGH--------IIQISS------- 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17559964  160 IDGTFNGPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANA 213
Cdd:PRK08263 137 IGGISAFPMSGiYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSA 191
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-202 2.01e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 79.19  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLK--HKdiqiIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVG 78
Cdd:PRK06180   2 SSMKTWLITGVSSGFGRALAQAALAagHR----VVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   79 edGLTVLLNNAGillpYDVEG---EKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISSTAA 155
Cdd:PRK06180  78 --PIDVLVNNAG----YGHEGaieESPLAEMRRQFEVNVFGAVAMTKAVLPGMRAR-----------RRGHIVNITSMGG 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17559964  156 SVekidgTFNGpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPG 202
Cdd:PRK06180 141 LI-----TMPG-IGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPG 181
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 1-211 2.50e-17

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 78.12  E-value: 2.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQFLKhKDIQIIIaTCRDPSKAEELSNlKDSRLHILPLDIDCDESISKLYAEVEKLVGEd 80
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLE-AGNTVII-TGRREERLAEAKK-ELPNIHTIVLDVGDAESVEALAEALLSEYPN- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  81 gLTVLLNNAGILLPYDVE-GEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTAASVek 159
Cdd:cd05370  79 -LDILINNAGIQRPIDLRdPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPE-----------ATIVNVSSGLAFV-- 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17559964 160 idgtfngPLVA---YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGA 211
Cdd:cd05370 145 -------PMAAnpvYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEE 192
FabG-like PRK07231
SDR family oxidoreductase;
4-228 2.59e-17

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 78.33  E-value: 2.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDiQIIIATcRDPSKAEELSNL--KDSRLHILPLDIDCDESISKLYAEVEKLVGedG 81
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGA-RVVVTD-RNEEAAERVAAEilAGGRAIAVAADVSDEADVEAAVAAALERFG--S 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGILLPY----DVEGEKNRKTLirqlETNSVSTALITQEFLPLLKKAaakNGGdgysinraAIVNISSTAAsv 157
Cdd:PRK07231  82 VDILVNNAGTTHRNgpllDVDEAEFDRIF----AVNVKSPYLWTQAAVPAMRGE---GGG--------AIVNVASTAG-- 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559964  158 ekidGTFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATKTLSDNI 228
Cdd:PRK07231 145 ----LRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTPENRAKFLATI 211
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 4-208 4.63e-17

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: 77.78  E-value: 4.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQfLKHKDIQIIIATCRDPSKAEELSNLKDS--RLHILPLDIDCDESISKLYAEVEKLVGEdg 81
Cdd:cd05347   6 KVALVTGASRGIGFGIASG-LAEAGANIVINSRNEEKAEEAQQLIEKEgvEATAFTCDVSDEEAIKAAVEAIEEDFGK-- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  82 LTVLLNNAGILLPYDVE--GEKNRKTLIrqlETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNIsstaASVEK 159
Cdd:cd05347  83 IDILVNNAGIIRRHPAEefPEAEWRDVI---DVNLNGVFFVSQAVARHMIKQ-----------GHGKIINI----CSLLS 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17559964 160 IDGTFNGPlvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05347 145 ELGGPPVP--AYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEM 191
PRK09242 PRK09242
SDR family oxidoreductase;
4-206 1.17e-16

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 76.71  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIAtcRDPSKAEELSN-LKDS----RLHILPLDIDCDESISKLYAEVEKLVg 78
Cdd:PRK09242  10 QTALITGASKGIGLAIAREFLGLGADVLIVA--RDADALAQARDeLAEEfperEVHGLAADVSDDEDRRAILDWVEDHW- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   79 eDGLTVLLNNAGILL---PYDVEGEKNRKTlirqLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTAA 155
Cdd:PRK09242  87 -DGLHILVNNAGGNIrkaAIDYTEDEWRGI----FETNLFSAFELSRYAHPLLKQHAS-----------SAIVNIGSVSG 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17559964  156 SVEKIDGtfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK09242 151 LTHVRSG------APYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRT 195
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 7-222 1.21e-16

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: 76.60  E-value: 1.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHKDIQIIIATCRDP---SKAEELSNLKDSRLHilPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:cd05350   2 LITGASSGIGRALAREFAKAGYNVALAARRTDRldeLKAELLNPNPSVEVE--ILDVTDEERNQLVIAELEAELG--GLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVEG---EKNRKTLirqlETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISSTAAsveki 160
Cdd:cd05350  78 LVIINAGVGKGTSLGDlsfKAFRETI----DTNLLGAAAILEAALPQFRAK-----------GRGHLVLISSVAA----- 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559964 161 dgtFNG--PLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMG----GANAMLEIEDATK 222
Cdd:cd05350 138 ---LRGlpGAAAYSASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTanmfTMPFLMSVEQAAK 202
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 4-228 3.11e-16

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: 75.70  E-value: 3.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIaTCRDPSK----AEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGe 79
Cdd:cd05332   4 KVVIITGASSGIGEELAYHLAR-LGARLVL-SARREERleevKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFG- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  80 dGLTVLLNNAGILLPYDVEGEK--NRKTLIrqlETNSVSTALITQEFLPLLKKaaaKNGGdgysinraAIVNISSTAasv 157
Cdd:cd05332  81 -GLDILINNAGISMRSLFHDTSidVDRKIM---EVNYFGPVALTKAALPHLIE---RSQG--------SIVVVSSIA--- 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559964 158 ekidGTFNGPL-VAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMgGANAMLEIEDATKTLSDNI 228
Cdd:cd05332 143 ----GKIGVPFrTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNI-AMNALSGDGSMSAKMDDTT 209
PRK06182 PRK06182
short chain dehydrogenase; Validated
 1-213 3.26e-16

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 75.77  E-value: 3.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQfLKHKDIQIIIATCRdpskAEELSNLKDSRLHILPLDIDCDESISklyAEVEKLVGED 80
Cdd:PRK06182   1 MQKKVALVTGASSGIGKATARR-LAAQGYTVYGAARR----VDKMEDLASLGVHPLSLDVTDEASIK---AAVDTIIAEE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 G-LTVLLNNAGillpY-------DVEGEKNRktliRQLETNSVSTALITQEFLPLLKKAAAknggdGYsinraaIVNISS 152
Cdd:PRK06182  73 GrIDVLVNNAG----YgsygaieDVPIDEAR----RQFEVNLFGAARLTQLVLPHMRAQRS-----GR------IINISS 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559964  153 taasvekIDGTFNGPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANA 213
Cdd:PRK06182 134 -------MGGKIYTPLGAwYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGDIAA 188
PRK05693 PRK05693
SDR family oxidoreductase;
4-218 4.87e-16

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 75.21  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFlKHKDIQIIiATCRdpsKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAF-KAAGYEVW-ATAR---KAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHG--GLD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGillpYDVEG---EKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaknggdgysiNRAAIVNISStaasvekI 160
Cdd:PRK05693  75 VLINNAG----YGAMGpllDGGVEAMRRQFETNVFAVVGVTRALFPLLRR------------SRGLVVNIGS-------V 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964  161 DGTFNGPLV-AYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMgGANAMLEIE 218
Cdd:PRK05693 132 SGVLVTPFAgAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQF-ASNASREAE 189
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 4-208 5.02e-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: 74.73  E-value: 5.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDIqIIIATCRDPSKAEELSNLKDsRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:cd05341   6 KVAIVTGGARGLGLAHARLLVAEGAK-VVLSDILDEEGQAAAAELGD-AARFFHLDVTDEDGWTAVVDTAREAFG--RLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVEGEKNRKtLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISSTAASVekidGT 163
Cdd:cd05341  82 VLVNNAGILTGGTVETTTLEE-WRRLLDINLTGVFLGTRAVIPPMKEA-----------GGGSIINMSSIEGLV----GD 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17559964 164 FNgpLVAYRMSKSALNSFAKSCSIDLAK--YHILVTSFCPGWVKTGM 208
Cdd:cd05341 146 PA--LAAYNASKGAVRGLTKSAALECATqgYGIRVNSVHPGYIYTPM 190
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-228 5.39e-16

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 74.91  E-value: 5.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKhKDIQIIIATCRDPSKAEELSNL---KDSRLHILPLDIDCDESISKLYAEVEKLV 77
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLAR-AGADVVVHYRSDEEAAEELVEAveaLGRRAQAVQADVTDKAALEAAVAAAVERF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   78 GedGLTVLLNNAGILlpydvegekNRKTL--------IRQLETNSVSTALITQEFLPLLKKAaakNGGdgysinraAIVN 149
Cdd:PRK12825  83 G--RIDILVNNAGIF---------EDKPLadmsddewDEVIDVNLSGVFHLLRAVVPPMRKQ---RGG--------RIVN 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964  150 ISSTAASVekidGTFNGplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGAnamlEIEDATKTLSDNI 228
Cdd:PRK12825 141 ISSVAGLP----GWPGR--SNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEA----TIEEAREAKDAET 209
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 4-206 8.50e-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: 74.42  E-value: 8.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdgLT 83
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAR-EGARVVVNYYRSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGP--VD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVEGEKNRKTL-----IRQLETnSVSTAL-ITQEFLPLLKKAAAknggdgysinrAAIVNISSTaasv 157
Cdd:cd05349  78 TIVNNALIDFPFDPDQRKTFDTIdwedyQQQLEG-AVKGALnLLQAVLPDFKERGS-----------GRVINIGTN---- 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17559964 158 ekidgTFNGPLVA---YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd05349 142 -----LFQNPVVPyhdYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-211 1.79e-15

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 73.07  E-value: 1.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIATCRDPSKAEElsnlkdsRLHILPLDIDCDesISKLYAEVEKLvgedglT 83
Cdd:PRK06550   6 KTVLITGAASGIGLAQARAFLA-QGAQVYGVDKQDKPDLSG-------NFHFLQLDLSDD--LEPLFDWVPSV------D 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdGYSInraaIVNISSTAASVEkidgt 163
Cdd:PRK06550  70 ILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLER-------KSGI----IINMCSIASFVA----- 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17559964  164 fNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGA 211
Cdd:PRK06550 134 -GGGGAAYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAA 180
PRK07326 PRK07326
SDR family oxidoreductase;
4-210 1.97e-15

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 73.12  E-value: 1.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIaTCRDPSKAEELSN--LKDSRLHILPLDIDCDESISKLYAEVEKLVGedG 81
Cdd:PRK07326   7 KVALITGGSKGIGFAIAEALLA-EGYKVAI-TARDQKELEEAAAelNNKGNVLGLAADVRDEADVQRAVDAIVAAFG--G 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaakngGDGYsinraaIVNISSTAasvekid 161
Cdd:PRK07326  83 LDVLIANAGVGHFAPVE-ELTPEEWRLVIDTNLTGAFYTIKAAVPALKR------GGGY------IINISSLA------- 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17559964  162 GT--FNGPlVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGG 210
Cdd:PRK07326 143 GTnfFAGG-AAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNG 192
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 4-208 2.84e-15

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: 72.72  E-value: 2.84e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDPSKAEELSNLKDS-RLHILPLDIDCDESISKLYAEVEKLVGedGL 82
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINPKvKATFVQCDVTSWEQLAAAFKKAIEKFG--RV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  83 TVLLNNAGILLP----YDVEGEKNRKTLIrqlETNSVSTALITQEFLPLLKKaaaKNGGDGysinrAAIVNISStAASVE 158
Cdd:cd05323  79 DILINNAGILDEksylFAGKLPPPWEKTI---DVNLTGVINTTYLALHYMDK---NKGGKG-----GVIVNIGS-VAGLY 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17559964 159 KIDGTfngplVAYRMSKSALNSFAKS-CSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05323 147 PAPQF-----PVYSASKHGVVGFTRSlADLLEYKTGVRVNAICPGFTNTPL 192
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 4-227 5.35e-15

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: 72.02  E-value: 5.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFlkHKD-IQIIIATC---RDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGe 79
Cdd:cd05366   3 KVAIITGAAQGIGRAIAERL--AADgFNIVLADLnleEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFG- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  80 dGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknGGDGYSINraaivnisstAASVEK 159
Cdd:cd05366  80 -SFDVMVNNAGIAPITPLL-TITEEDLKKVYAVNVFGVLFGIQAAARQFKKL----GHGGKIIN----------ASSIAG 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559964 160 IDGTFNgpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATKTLSDN 227
Cdd:cd05366 144 VQGFPN--LGAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEIAGKPEGEG 209
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 4-206 3.04e-14

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 70.18  E-value: 3.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQfLKHKDIQ--IIIATCRDPSKAEELSNLKDSR----LHILPLDIDCDESIsklyAEVEKLV 77
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVR-LASDPSKrfKVYATMRDLKKKGRLWEAAGALaggtLETLQLDVCDSKSV----AAAVERV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  78 GEDGLTVLLNNAGILL--PYDVEGEKNRKTLirqLETNSVSTALITQEFLPLLKKaaaknggdgysiNRAAIVNISStaa 155
Cdd:cd09806  76 TERHVDVLVCNAGVGLlgPLEALSEDAMASV---FDVNVFGTVRMLQAFLPDMKR------------RGSGRILVTS--- 137

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17559964 156 SVEKIDGT-FNGplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd09806 138 SVGGLQGLpFND---VYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHT 186
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 7-228 4.53e-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: 69.30  E-value: 4.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHkDIQIIIATCRDPSKAEELSNL---KDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:cd05359   2 LVTGGSRGIGKAIALRLAER-GADVVINYRKSKDAAAEVAAEieeLGGKAVVVRADVSQPQDVEEMFAAVKERFG--RLD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNA--GILLPYDvegEKNRKTLIRQLETNSVSTALITQEFLPLLkkaAAKNGGdgysinraAIVNISSTAAsvekid 161
Cdd:cd05359  79 VLVSNAaaGAFRPLS---ELTPAHWDAKMNTNLKALVHCAQQAAKLM---RERGGG--------RIVAISSLGS------ 138

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559964 162 GTFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMggANAMLEIEDATKTLSDNI 228
Cdd:cd05359 139 IRALPNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDA--LAHFPNREDLLEAAAANT 203
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 4-203 4.77e-14

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 69.65  E-value: 4.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQfLKHKDIQIIIATcRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:PRK08265   7 KVAIVTGGATLIGAAVARA-LVAAGARVAIVD-IDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFG--RVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGIllpYDVEGEK-NRKTLIRQLETNSVSTALITQEFLPLLKKaaakNGGdgysinraAIVNISSTAASVekidG 162
Cdd:PRK08265  83 ILVNLACT---YLDDGLAsSRADWLAALDVNLVSAAMLAQAAHPHLAR----GGG--------AIVNFTSISAKF----A 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17559964  163 TFNGPLvaYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGW 203
Cdd:PRK08265 144 QTGRWL--YPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGW 182
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
4-208 6.05e-14

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 69.29  E-value: 6.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIATcRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:PRK07067   7 KVALLTGAASGIGEAVAERYLA-EGARVVIAD-IKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGIllpYDVEG--EKNRKTLIRQLETNSVSTALITQeflpllkkAAAK---NGGDGysinrAAIVNISSTAasve 158
Cdd:PRK07067  83 ILFNNAAL---FDMAPilDISRDSYDRLFAVNVKGLFFLMQ--------AVARhmvEQGRG-----GKIINMASQA---- 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17559964  159 kidGTFNGPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK07067 143 ---GRRGEALVShYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPM 190
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 8-208 9.03e-14

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: 68.40  E-value: 9.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   8 ITGANRGIGLGLLKQFLKHKDIQIIIAtcRDPSK----AEELSNLKDSRLHILPLDIDCDESI-SKLYAEVEKL-VGedg 81
Cdd:cd05356   6 VTGATDGIGKAYAEELAKRGFNVILIS--RTQEKldavAKEIEEKYGVETKTIAADFSAGDDIyERIEKELEGLdIG--- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  82 ltVLLNNAGILLPYDVE-GEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNISSTAASVeki 160
Cdd:cd05356  81 --ILVNNVGISHSIPEYfLETPEDELQDIINVNVMATLKMTRLILPGMVKRK-----------KGAIVNISSFAGLI--- 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17559964 161 dgtfngP---LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05356 145 ------PtplLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKM 189
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
3-211 9.70e-14

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 68.64  E-value: 9.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    3 PKSLLITGANRGIGLGLLKQFLKhkDIQIIIATCRDPSKA----EELSNLKDSRLHILPLDI----DCDESISKLYAEve 74
Cdd:PRK12824   2 KKIALVTGAKRGIGSAIARELLN--DGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVtdteECAEALAEIEEE-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   75 klvgEDGLTVLLNNAGIllpydvegekNRKTLIRQ---------LETNSVSTALITQEFLPllkkaAAKNGGDGysinra 145
Cdd:PRK12824  78 ----EGPVDILVNNAGI----------TRDSVFKRmshqewndvINTNLNSVFNVTQPLFA-----AMCEQGYG------ 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559964  146 AIVNISSTAAsvekIDGTFNGPlvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGA 211
Cdd:PRK12824 133 RIINISSVNG----LKGQFGQT--NYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQ 192
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-208 1.33e-13

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 68.45  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIGLGLLKQFLKHK-DIQiIIATCRDPSKAEELSNLKD--SRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGfDLA-INDRPDDEELAATQQELRAlgVEVIFFPADVADLSAHEAMLDAAQAAWG--RID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGIllpydveGEKNRKTLI--------RQLETNSVSTALITQEFLpllkKAAAKNGGDGYSINRaAIVNISS--- 152
Cdd:PRK12745  83 CLVNNAGV-------GVKVRGDLLdltpesfdRVLAINLRGPFFLTQAVA----KRMLAQPEPEELPHR-SIVFVSSvna 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17559964  153 TAASVEKIDgtfngplvaYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK12745 151 IMVSPNRGE---------YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
PRK08219 PRK08219
SDR family oxidoreductase;
1-208 1.37e-13

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 67.65  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKHKDiqiIIATCRDPSKAEELSNLKDSrLHILPLDIDCDESISklyAEVEKLvgeD 80
Cdd:PRK08219   1 MERPTALITGASRGIGAAIARELAPTHT---LLLGGRPAERLDELAAELPG-ATPFPVDLTDPEAIA---AAVEQL---G 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLTVLLNNAGILLPYDVeGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysinRAAIVNISSTAasveki 160
Cdd:PRK08219  71 RLDVLVHNAGVADLGPV-AESTVDEWRATLEVNVVAPAELTRLLLPALRAA------------HGHVVFINSGA------ 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17559964  161 dGTFNGP-LVAYRMSKSALNSFAKSCSIDLAKyHILVTSFCPGWVKTGM 208
Cdd:PRK08219 132 -GLRANPgWGSYAASKFALRALADALREEEPG-NVRVTSVHPGRTDTDM 178
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 4-226 2.21e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 67.51  E-value: 2.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFL-KHKDIQIIIATCRDPSKAeeLSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGL 82
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAaRGARVALIGRGAAPLSQT--LPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG--RL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   83 TVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTAASvekIDG 162
Cdd:PRK12828  84 DALVNIAGAFVWGTIA-DGDADTWDRMYGVNVKTTLNASKAALPALTASGG-----------GRIVNIGAGAAL---KAG 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559964  163 TFNGplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATKTLSD 226
Cdd:PRK12828 149 PGMG---AYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMPDADFSRWVTPEQ 209
PRK09009 PRK09009
SDR family oxidoreductase;
4-206 5.36e-13

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 66.24  E-value: 5.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFL-KHKDIQIIIATCRDPSkaeelsNLKDSRLHILPLDIDCDESISKLYAEVEKLvgedgl 82
Cdd:PRK09009   1 MNILIVGGSGGIGKAMVKQLLeRYPDATVHATYRHHKP------DFQHDNVQWHALDVTDEAEIKQLSEQFTQL------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   83 TVLLNNAGILLPYDVEGEKNRKTL-----IRQLETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISstaASV 157
Cdd:PRK09009  69 DWLINCVGMLHTQDKGPEKSLQALdadffLQNITLNTLPSLLLAKHFTPKLKQS-----------ESAKFAVIS---AKV 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17559964  158 EKIDGTFNGPLVAYRMSKSALNSFAKSCSIDLAKY--HILVTSFCPGWVKT 206
Cdd:PRK09009 135 GSISDNRLGGWYSYRASKAALNMFLKTLSIEWQRSlkHGVVLALHPGTTDT 185
PRK09730 PRK09730
SDR family oxidoreductase;
7-208 8.95e-13

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 66.03  E-value: 8.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIG--LGLLkqfLKHKDIQIIIATCRDPSKAEELSNL---KDSRLHILPLDIDCDESISKLYAEVEKLVGEdg 81
Cdd:PRK09730   5 LVTGGSRGIGraTALL---LAQEGYTVAVNYQQNLHAAQEVVNLitqAGGKAFVLQADISDENQVVAMFTAIDQHDEP-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGILLpydvegeknRKTLIRQLET---NSVSTALITQEFL---PLLKKAAAKNGGDGysinrAAIVNISSTAA 155
Cdd:PRK09730  80 LAALVNNAGILF---------TQCTVENLTAeriNRVLSTNVTGYFLccrEAVKRMALKHGGSG-----GAIVNVSSAAS 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17559964  156 SVEKidgtfNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK09730 146 RLGA-----PGEYVDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
PRK08017 PRK08017
SDR family oxidoreductase;
4-206 1.18e-12

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 65.49  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLgLLKQFLKHKDIQiIIATCRdpsKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGeDGLT 83
Cdd:PRK08017   3 KSVLITGCSSGIGL-EAALELKRRGYR-VLAACR---KPDDVARMNSLGFTGILLDLDDPESVERAADEVIALTD-NRLY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGillpYDVEGEKN---RKTLIRQLETNSVSTALITQEFLPllkkaAAKNGGDGYSINRAAIVNISSTAAsveki 160
Cdd:PRK08017  77 GLFNNAG----FGVYGPLStisRQQMEQQFSTNFFGTHQLTMLLLP-----AMLPHGEGRIVMTSSVMGLISTPG----- 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17559964  161 dgtfNGplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK08017 143 ----RG---AYAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRT 181
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 4-208 1.23e-12

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: 65.57  E-value: 1.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKdiQIIIATCRDPSKAEELSnlKDSRLHILPLDIDCDESISKLYAEveklvgEDGLT 83
Cdd:cd05368   3 KVALITAAAQGIGRAIALAFAREG--ANVIATDINEEKLKELE--RGPGITTRVLDVTDKEQVAALAKE------EGRID 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILlPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPllKKAAAKNGgdgysinraAIVNISSTAASVEKIDGT 163
Cdd:cd05368  73 VLFNCAGFV-HHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLP--KMLARKDG---------SIINMSSVASSIKGVPNR 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17559964 164 FngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05368 141 F-----VYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPS 180
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 4-206 1.42e-12

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: 65.16  E-value: 1.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKdiQIIIATCRDPSKAEE-LSNLKDSRLHILPL--DIDCDESISKLYAEVEKLVGED 80
Cdd:cd05329   7 KTALVTGGTKGIGYAIVEELAGLG--AEVYTCARNQKELDEcLTEWREKGFKVEGSvcDVSSRSERQELMDTVASHFGGK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  81 gLTVLLNNAGILLP---YDVEGEKNRktLIrqLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNISSTAASV 157
Cdd:cd05329  85 -LNILVNNAGTNIRkeaKDYTEEDYS--LI--MSTNFEAAYHLSRLAHPLLKASG-----------NGNIVFISSVAGVI 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17559964 158 EKidgtfngPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd05329 149 AV-------PSGApYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIAT 191
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 4-208 1.60e-12

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: 65.25  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDPSKA--EELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdg 81
Cdd:cd08933  10 KVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQAleSELNRAGPGSCKFVPCDVTKEEDIKTLISVTVERFGR-- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  82 LTVLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysinRAAIVNISSTAASVEKID 161
Cdd:cd08933  88 IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKS------------QGNIINLSSLVGSIGQKQ 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17559964 162 GtfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd08933 156 A------APYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPL 196
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 4-206 1.62e-12

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 64.99  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQfLKHKDIQIIIATCRDPSKAEELSNLKDS--RLHILPLDIDCDESISKLYAEVEKLVGedG 81
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEA-LAEAGATVAFNDGLAAEARELAAALEAAggRAHAIAADLADPASVQRFFDAAAAALG--G 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGI-----LLPYDVEgeknrkTLIRQLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNISSTAA- 155
Cdd:PRK12939  85 LDGLVNNAGItnsksATELDID------TWDAVMNVNVRGTFLMLRAALPHLRDSG-----------RGRIVNLASDTAl 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17559964  156 -SVEKidgtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK12939 148 wGAPK--------LGAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTAT 191
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 4-209 1.70e-12

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 65.57  E-value: 1.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIAtCRDPSKAEELS-----NLKDSRLHILPLDIDCDESISKLYAEVekLVG 78
Cdd:cd09807   2 KTVIITGANTGIGKETARELAR-RGARVIMA-CRDMAKCEEAAaeirrDTLNHEVIVRHLDLASLKSIRAFAAEF--LAE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  79 EDGLTVLLNNAGILL-PYDVEgEKNRKTlirQLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTAASV 157
Cdd:cd09807  78 EDRLDVLINNAGVMRcPYSKT-EDGFEM---QFGVNHLGHFLLTNLLLDLLKKSAP-----------SRIVNVSSLAHKA 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17559964 158 EKI---DGTFNGP---LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMG 209
Cdd:cd09807 143 GKInfdDLNSEKSyntGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELG 200
PRK09072 PRK09072
SDR family oxidoreductase;
4-226 1.87e-12

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 64.96  E-value: 1.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQfLKHKDIQIIIATcRDPSKAEELSN--LKDSRLHILPLDIDCDESISKLYAEVEKLvgeDG 81
Cdd:PRK09072   6 KRVLLTGASGGIGQALAEA-LAAAGARLLLVG-RNAEKLEALAArlPYPGRHRWVVADLTSEAGREAVLARAREM---GG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGI----LL----PYDVEgeknrktliRQLETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISST 153
Cdd:PRK09072  81 INVLINNAGVnhfaLLedqdPEAIE---------RLLALNLTAPMQLTRALLPLLRAQ-----------PSAMVVNVGST 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559964  154 AASVekidgTFNGpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM--GGANAMleiEDATKTLSD 226
Cdd:PRK09072 141 FGSI-----GYPG-YASYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAMnsEAVQAL---NRALGNAMD 206
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 7-208 2.21e-12

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: 64.80  E-value: 2.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKhKDIQIIIATCrdpskAEELSNLKDSRLHILPLDI----DCDESISKLYAEVEklvgedGL 82
Cdd:cd05331   2 IVTGAAQGIGRAVARHLLQ-AGATVIALDL-----PFVLLLEYGDPLRLTPLDVadaaAVREVCSRLLAEHG------PI 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  83 TVLLNNAGILLPydvegeknrkTLIRQLETNSVSTALITQEFLPL-LKKAAAKNGGDGYSinrAAIVNISSTAASVEKID 161
Cdd:cd05331  70 DALVNCAGVLRP----------GATDPLSTEDWEQTFAVNVTGVFnLLQAVAPHMKDRRT---GAIVTVASNAAHVPRIS 136

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17559964 162 gtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05331 137 ------MAAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAM 177
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 2-208 2.33e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 64.74  E-value: 2.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    2 SPKSLLITGANRGIGLGLLKQfLKHKDIQiIIATCRDPSKAEELSNlkDSRLHILPLDIDCDESISKLYAEVEKLvgeDG 81
Cdd:PRK07060   8 SGKSVLVTGASSGIGRACAVA-LAQRGAR-VVAAARNAAALDRLAG--ETGCEPLRLDVGDDAAIRAALAAAGAF---DG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 ltvLLNNAGILL---PYDVEGEKNRktliRQLETNSVSTALITQEFLPllKKAAAKNGGdgysinraAIVNISSTAASVE 158
Cdd:PRK07060  81 ---LVNCAGIASlesALDMTAEGFD----RVMAVNARGAALVARHVAR--AMIAAGRGG--------SIVNVSSQAALVG 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17559964  159 KIDgtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK07060 144 LPD------HLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 1-209 2.49e-12

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 64.65  E-value: 2.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKHKdiqiIIATCRDPSKAEelsnLKDSRLHILPLDIDCDESISKLYAEVEKLVGE- 79
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANG----ANVVNADIHGGD----GQHENYQFVPTDVSSAEEVNHTVAEIIEKFGRi 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   80 DGLtvlLNNAGILLP------YDVEG--EKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaKNGGdgysinraAIVNIS 151
Cdd:PRK06171  79 DGL---VNNAGINIPrllvdeKDPAGkyELNEAAFDKMFNINQKGVFLMSQAVARQMVK---QHDG--------VIVNMS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964  152 STAASvEKIDGTfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWV-KTGMG 209
Cdd:PRK06171 145 SEAGL-EGSEGQ-----SCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILeATGLR 197
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 4-206 2.71e-12

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: 64.78  E-value: 2.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIATCRDPSKAEELSNLKDSRLHI----LPLDIDCDESISKLYAEVEKLVGe 79
Cdd:cd08940   3 KVALVTGSTSGIGLGIARALAA-AGANIVLNGFGDAAEIEAVRAGLAAKHGVkvlyHGADLSKPAAIEDMVAYAQRQFG- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  80 dGLTVLLNNAGILLPYDVEG---EKNRKTLIRQLETNSVSTALItqefLPLLKKaaaKNGGdgysinraAIVNISST--- 153
Cdd:cd08940  81 -GVDILVNNAGIQHVAPIEDfptEKWDAIIALNLSAVFHTTRLA----LPHMKK---QGWG--------RIINIASVhgl 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17559964 154 AASVEKidgtfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd08940 145 VASANK---------SAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLT 188
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 4-206 3.13e-12

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: 64.15  E-value: 3.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHkDIQIIIATcRDPSK----AEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGE 79
Cdd:cd05369   4 KVAFITGGGTGIGKAIAKAFAEL-GASVAIAG-RKPEVleaaAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFGK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  80 dgLTVLLNNAGILLPYDVEG--EKNRKTLIrqlETNSVSTALITQEFLPLLKKaaAKNGGdgysinraAIVNISSTAASv 157
Cdd:cd05369  82 --IDILINNAAGNFLAPAESlsPNGFKTVI---DIDLNGTFNTTKAVGKRLIE--AKHGG--------SILNISATYAY- 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17559964 158 ekiDGtfnGPLVAYR-MSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd05369 146 ---TG---SPFQVHSaAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPT 189
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 4-212 3.17e-12

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: 64.41  E-value: 3.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFlkHKDIQIIIATCRdpsKAEELSNLKDSRLHILPLDIDcdesISKLYAEVEKLVGEDGLT 83
Cdd:cd05351   8 KRALVTGAGKGIGRATVKAL--AKAGARVVAVSR---TQADLDSLVRECPGIEPVCVD----LSDWDATEEALGSVGPVD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAG--ILLPYdveGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAAKnggdgysinrAAIVNISSTAASVEKID 161
Cdd:cd05351  79 LLVNNAAvaILQPF---LEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVP----------GSIVNVSSQASQRALTN 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17559964 162 GTfngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGAN 212
Cdd:cd05351 146 HT------VYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDN 190
PRK06484 PRK06484
short chain dehydrogenase; Validated
 2-206 4.04e-12

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 65.26  E-value: 4.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    2 SPKSLLITGANRGIGLGLLKQFLKHKDIQIIIAtcRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdg 81
Cdd:PRK06484 268 SPRVVAITGGARGIGRAVADRFAAAGDRLLIID--RDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGR-- 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGILLPYDVEGEKNRKTLIRQLETNsVSTALITQeflpllkKAAAKNGGDGysinrAAIVNISSTAASvekid 161
Cdd:PRK06484 344 LDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVN-LSGAFACA-------RAAARLMSQG-----GVIVNLGSIASL----- 405

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17559964  162 gtfnGPLV---AYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK06484 406 ----LALPprnAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 7-207 4.30e-12

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: 63.83  E-value: 4.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHKDIQIIIAtcRDPSKAEE-LSNLKDSRLHILPldIDCDESISKLYAEVEKLVGED--GLT 83
Cdd:cd05344   5 LVTAASSGIGLAIARALAREGARVAICA--RNRENLERaASELRAGGAGVLA--VVADLTDPEDIDRLVEKAGDAfgRVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVEGEKNRKTLiRQLETNSVSTALITQEFLPLLKKAaakngGDGysinraAIVNISSTAAsVEKIDgt 163
Cdd:cd05344  81 ILVNNAGGPPPGPFAELTDEDWL-EAFDLKLLSVIRIVRAVLPGMKER-----GWG------RIVNISSLTV-KEPEP-- 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17559964 164 fngPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTG 207
Cdd:cd05344 146 ---NLVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 7-225 4.37e-12

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: 63.83  E-value: 4.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHkDIQIIIATCRDPSKAEELS---NLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:cd05362   7 LVTGASRGIGRAIAKRLARD-GASVVVNYASSKAAAEEVVaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG--GVD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEflpllkkaAAKNGGDGysinrAAIVNISSTAAsvekidGT 163
Cdd:cd05362  84 ILVNNAGVMLKKPIA-ETSEEEFDRMFTVNTKGAFFVLQE--------AAKRLRDG-----GRIINISSSLT------AA 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559964 164 FNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATKTLS 225
Cdd:cd05362 144 YTPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYAKMS 205
PRK08267 PRK08267
SDR family oxidoreductase;
3-224 8.53e-12

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 63.03  E-value: 8.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    3 PKSLLITGANRGIGLGLLKQFLKHK------DIqiiiatcrDPSKAEELSN-LKDSRLHILPLDIDCDESISKLYAEVEK 75
Cdd:PRK08267   1 MKSIFITGAASGIGRATALLFAAEGwrvgayDI--------NEAGLAALAAeLGAGNAWTGALDVTDRAAWDAALADFAA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   76 LVGeDGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTAA 155
Cdd:PRK08267  73 ATG-GRLDVLFNNAGILRGGPFE-DIPLEAHDRVIDINVKGVLNGAHAALPYLKATPG-----------ARVINTSSASA 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  156 svekidgTFNGP-LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATKTL 224
Cdd:PRK08267 140 -------IYGQPgLAVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGSTKRL 202
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 7-208 1.16e-11

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: 62.87  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQF-LKHKDIQIIiaTCRDPSKAEELSNL---KDSRLHILPLDIDCDESISKLYAEVEKLVGedGL 82
Cdd:cd05337   5 IVTGASRGIGRAIATELaARGFDIAIN--DLPDDDQATEVVAEvlaAGRRAIYFQADIGELSDHEALLDQAWEDFG--RL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  83 TVLLNNAGILLP-----YDVEGEknrkTLIRQLETNSVSTALITQEF-LPLLKKAAAKNGGDGYSINraaIVNISSTAAS 156
Cdd:cd05337  81 DCLVNNAGIAVRprgdlLDLTED----SFDRLIAINLRGPFFLTQAVaRRMVEQPDRFDGPHRSIIF---VTSINAYLVS 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17559964 157 VEKIDgtfngplvaYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05337 154 PNRGE---------YCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDM 196
PRK07577 PRK07577
SDR family oxidoreductase;
1-208 1.54e-11

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 62.05  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDPSKAEELsnlkdsrlhilpldIDCDESISKLYAEV-EKLVGE 79
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIARSAIDDFPGEL--------------FACDLADIEQTAATlAQINEI 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   80 DGLTVLLNNAGILLPYDVeGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTAasvek 159
Cdd:PRK07577  67 HPVDAIVNNVGIALPQPL-GKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQ-----------GRIVNICSRA----- 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17559964  160 IDGTFNgpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK07577 130 IFGALD--RTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 4-243 1.70e-11

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: 62.09  E-value: 1.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHkDIQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdgLT 83
Cdd:cd05326   5 KVAIITGGASGIGEATARLFAKH-GARVVIADIDDDAGQAVAAELGDPDISFVHCDVTVEADVRAAVDTAVARFGR--LD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGIL--LPYDVEgEKNRKTLIRQLETNSVSTALITqeflpllKKAAAKNGGDGysinRAAIVNISSTAASVEKId 161
Cdd:cd05326  82 IMFNNAGVLgaPCYSIL-ETSLEEFERVLDVNVYGAFLGT-------KHAARVMIPAK----KGSIVSVASVAGVVGGL- 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964 162 gtfnGPLvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLE---IEDATKTLSDNILTLGN----A 234
Cdd:cd05326 149 ----GPH-AYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEdeaIEEAVRGAANLKGTALRpediA 223


                ....*....
gi 17559964 235 HHGAYLNAD 243
Cdd:cd05326 224 AAVLYLASD 232
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 4-208 1.86e-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: 62.35  E-value: 1.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKH-KDIQII-IATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdg 81
Cdd:cd05352   9 KVAIVTGGSRGIGLAIARALAEAgADVAIIyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGK-- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  82 LTVLLNNAGI-----LLPYDVEGEKNrktlIRQLETNSV-STAlitQEFLPLLKkaaaKNGgdgysinRAAIVNISSTAA 155
Cdd:cd05352  87 IDILIANAGItvhkpALDYTYEQWNK----VIDVNLNGVfNCA---QAAAKIFK----KQG-------KGSLIITASMSG 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17559964 156 SVEKIDgtfnGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05352 149 TIVNRP----QPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDL 197
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 7-207 1.89e-11

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: 62.02  E-value: 1.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKhKDIQIIIATCrDPSKAEELSNLKDSRLHILPLDID--CDESISKLYAEVEKLVGedGLTV 84
Cdd:cd08943   5 LVTGGASGIGLAIAKRLAA-EGAAVVVADI-DPEIAEKVAEAAQGGPRALGVQCDvtSEAQVQSAFEQAVLEFG--GLDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  85 LLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaAKNGGDgysinraAIVNISSTAasvekidgTF 164
Cdd:cd08943  81 VVSNAGIATSSPIA-ETSLEDWNRSMDINLTGHFLVSREAFRIMKS--QGIGGN-------IVFNASKNA--------VA 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17559964 165 NGP-LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTG 207
Cdd:cd08943 143 PGPnAAAYSAAKAAEAHLARCLALEGGEDGIRVNTVNPDAVFRG 186
PRK06482 PRK06482
SDR family oxidoreductase;
3-220 2.00e-11

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 62.44  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    3 PKSLLITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLyaeVEKLVGEDG- 81
Cdd:PRK06482   2 SKTWFITGASSGFGRGMTERLLARGDR--VAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAV---VDRAFAALGr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGILLPYDVEGEKNRKtLIRQLETNSVSTALITQEFLPLLKkaaAKNGGdgysinraAIVNISSTAASVekid 161
Cdd:PRK06482  77 IDVVVSNAGYGLFGAAEELSDAQ-IRRQIDTNLIGSIQVIRAALPHLR---RQGGG--------RIVQVSSEGGQI---- 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964  162 gTFNGpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDA 220
Cdd:PRK06482 141 -AYPG-FSLYHATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFGAGLDRGAPLDA 197
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 4-208 3.48e-11

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: 61.25  E-value: 3.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLkHKDIQIIIATcRDPSKAEELSNLKDSRLHILPLDIDCDESISklyAEVEKLVGEDG-L 82
Cdd:cd05345   6 KVAIVTGAGSGFGEGIARRFA-QEGARVVIAD-INADGAERVAADIGEAAIAIQADVTKRADVE---AMVEAALSKFGrL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  83 TVLLNNAGIllpydveGEKNRKTLI-------RQLETNSVSTALITQEFLPLLKKaaaknGGDGysinraAIVNISSTAA 155
Cdd:cd05345  81 DILVNNAGI-------THRNKPMLEvdeeefdRVFAVNVKSIYLSAQALVPHMEE-----QGGG------VIINIASTAG 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17559964 156 SVEKidgtfngP-LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05345 143 LRPR-------PgLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPL 189
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
4-208 5.19e-11

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 60.97  E-value: 5.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDPSK-AEELSNlKDSRLHILPLDIDCDESISKLYAEVEKLVGEdgL 82
Cdd:PRK08226   7 KTALITGALQGIGEGIARVFARHGANLILLDISPEIEKlADELCG-RGHRCTAVVADVRDPASVAAAIKRAKEKEGR--I 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   83 TVLLNNAGI--LLPYDVEGEKNRKTlirQLETNSVSTALITQEFLPLLkkaAAKNGGdgysinraAIVNISSTAASVEKI 160
Cdd:PRK08226  84 DILVNNAGVcrLGSFLDMSDEDRDF---HIDINIKGVWNVTKAVLPEM---IARKDG--------RIVMMSSVTGDMVAD 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17559964  161 DGTfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK08226 150 PGE-----TAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPM 192
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 4-227 6.23e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 60.54  E-value: 6.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLgLLKQFLKHKDIQIIIATCRDPSKAEELSNLKDS--RLHILPLDIDCDESISKLYAEVEKLVGedG 81
Cdd:PRK08085  10 KNILITGSAQGIGF-LLATGLAEYGAEIIINDITAERAELAVAKLRQEgiKAHAAPFNVTHKQEVEAAIEHIEKDIG--P 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGILL--PYDVEGEKNRKTLIrqlETNSVSTALITQeflpllkkAAAKnggdgYSINRAA--IVNISSTAASV 157
Cdd:PRK08085  87 IDVLINNAGIQRrhPFTEFPEQEWNDVI---AVNQTAVFLVSQ--------AVAR-----YMVKRQAgkIINICSMQSEL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  158 EKidgtfnGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMgganamleiedaTKTLSDN 227
Cdd:PRK08085 151 GR------DTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEM------------TKALVED 202
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-208 1.35e-10

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 59.70  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHK-DIQIIIATCRDPSK-AEELSNLkDSRLHILPLDIDCDESISklyAEVEKLVGEDG 81
Cdd:PRK07666   8 KNALITGAGRGIGRAVAIALAKEGvNVGLLARTEENLKAvAEEVEAY-GVKVVIATADVSDYEEVT---AAIEQLKNELG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 -LTVLLNNAGI-----LLPYDVEGEKnrktliRQLETNSVSTALITQEFLPLLKKaaaKNGGDgysinraaIVNISSTAa 155
Cdd:PRK07666  84 sIDILINNAGIskfgkFLELDPAEWE------KIIQVNLMGVYYATRAVLPSMIE---RQSGD--------IINISSTA- 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17559964  156 svekidGTFNGPLV-AYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK07666 146 ------GQKGAAVTsAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDM 193
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 4-219 1.46e-10

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: 59.66  E-value: 1.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDIQII--IATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGE-D 80
Cdd:cd08930   3 KIILITGAAGLIGKAFCKALLSAGARLILadINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGRiD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  81 GltvLLNNAGIllpyDVEGEKNR------KTLIRQLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNISSTA 154
Cdd:cd08930  83 I---LINNAYP----SPKVWGSRfeefpyEQWNEVLNVNLGGAFLCSQAFIKLFKKQG-----------KGSIINIASIY 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964 155 ASV-----EKIDGTFNGPLVaYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWV--------------KTGMGGanaML 215
Cdd:cd08930 145 GVIapdfrIYENTQMYSPVE-YSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIlnnqpseflekytkKCPLKR---ML 220


                ....
gi 17559964 216 EIED 219
Cdd:cd08930 221 NPED 224
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 4-206 2.37e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 59.28  E-value: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKH-KDIQII-IATCRDPSKAEELSNLKDSRLHILPLDIdCDESISKlyAEVEKLVGEDG 81
Cdd:PRK06701  47 KVALITGGDSGIGRAVAVLFAKEgADIAIVyLDEHEDANETKQRVEKEGVKCLLIPGDV-SDEAFCK--DAVEETVRELG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 -LTVLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysinrAAIVNisstAASVEKI 160
Cdd:PRK06701 124 rLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG-------------SAIIN----TGSITGY 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17559964  161 DGtfNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK06701 187 EG--NETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWT 230
PRK05993 PRK05993
SDR family oxidoreductase;
4-240 2.48e-10

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 59.27  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFlkHKDIQIIIATCRdpsKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGeDGLT 83
Cdd:PRK05993   5 RSILITGCSSGIGAYCARAL--QSDGWRVFATCR---KEEDVAALEAEGLEAFQLDYAEPESIAALVAQVLELSG-GRLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaakngGDGysinraAIVNISSTAASVE-KIDG 162
Cdd:PRK05993  79 ALFNNGAYGQPGAVE-DLPTEALRAQFEANFFGWHDLTRRVIPVMRKQ-----GQG------RIVQCSSILGLVPmKYRG 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559964  163 tfngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMgGANAMLEIEdatktlsDNILTLGNAHHGAYL 240
Cdd:PRK05993 147 -------AYNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRF-RANALAAFK-------RWIDIENSVHRAAYQ 209
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 7-220 3.01e-10

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: 58.73  E-value: 3.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHKDIQIIIATCRDPSK--AEELSNLkDSRLHILPLDIDCDESISKLYAEVEKLVGedGLTV 84
Cdd:cd05365   3 IVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEavAAAIQQA-GGQAIGLECNVTSEQDLEAVVKATVSQFG--GITI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  85 LLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknGGdgysinrAAIVNISSTAASVEKIDgtf 164
Cdd:cd05365  80 LVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKA----GG-------GAILNISSMSSENKNVR--- 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17559964 165 ngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDA 220
Cdd:cd05365 146 ---IAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLTPEIERA 198
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 4-208 3.17e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 58.80  E-value: 3.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLlKQFLKHKDIQIIIaTCRdpsKAEELsnlKDSRLHILPLDID-----CD----ESISKLYAEVE 74
Cdd:PRK08213  13 KTALVTGGSRGLGLQI-AEALGEAGARVVL-SAR---KAEEL---EEAAAHLEALGIDalwiaADvadeADIERLAEETL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   75 KLVGedGLTVLLNNAGILLPYDVEG---EKNRKTLirqlETNSVSTALITQEflpLLKKAAAKNGGdgysinrAAIVNIs 151
Cdd:PRK08213  85 ERFG--HVDILVNNAGATWGAPAEDhpvEAWDKVM----NLNVRGLFLLSQA---VAKRSMIPRGY-------GRIINV- 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964  152 staASVEKIDGTFNGPL--VAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK08213 148 ---ASVAGLGGNPPEVMdtIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKM 203
PRK07069 PRK07069
short chain dehydrogenase; Validated
 81-228 3.77e-10

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 58.57  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLTVLLNNAGILLPYDVEGEKnRKTLIRQLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTAASVEki 160
Cdd:PRK07069  79 GLSVLVNNAGVGSFGAIEQIE-LDEWRRVMAINVESIFLGCKHALPYLRASQP-----------ASIVNISSVAAFKA-- 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559964  161 dgtfNGPLVAYRMSKSALNSFAKSCSIDLAK--YHILVTSFCPGWVKTGM-GGANAMLEIEDATKTLSDNI 228
Cdd:PRK07069 145 ----EPDYTAYNASKAAVASLTKSIALDCARrgLDVRCNSIHPTFIRTGIvDPIFQRLGEEEATRKLARGV 211
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 7-211 3.90e-10

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: 58.32  E-value: 3.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQfLKHKDIQIIIATCRDPSKAEELSNLKDSRLHI--LPLDIDCDESISKLYAEVEKLVGEdgLTV 84
Cdd:cd08945   7 LVTGATSGIGLAIARR-LGKEGLRVFVCARGEEGLATTVKELREAGVEAdgRTCDVRSVPEIEALVAAAVARYGP--IDV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  85 LLNNAGIL-----------LPYDVegeknrktlirqLETNSVSTALITQEFLpllkkaaaKNGGDGySINRAAIVNISST 153
Cdd:cd08945  84 LVNNAGRSgggataeladeLWLDV------------VETNLTGVFRVTKEVL--------KAGGML-ERGTGRIINIAST 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17559964 154 AASVEKIDGTfngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGA 211
Cdd:cd08945 143 GGKQGVVHAA------PYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAAS 194
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 4-208 4.02e-10

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 58.55  E-value: 4.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDPSKAEELSNLKDSRLHILPL--DIDCDESISKLYA----EVEKLV 77
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIgaNLESLHGVEALYSsldnELQNRT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   78 GEDGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKkaaaknggdgysiNRAAIVNISSTAASV 157
Cdd:PRK12747  85 GSTKFDILINNAGIGPGAFIE-ETTEQFFDRMVSVNAKAPFFIIQQALSRLR-------------DNSRIINISSAATRI 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17559964  158 EKIDgtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK12747 151 SLPD------FIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM 195
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 1-206 4.06e-10

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: 58.61  E-value: 4.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQFLKHKDIQIIiaTCRDPSK-----AEELSNlKDSRLHILPLDIDCDESISKLYAEVEK 75
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYI--TGRTILPqlpgtAEEIEA-RGGKCIPVRCDHSDDDEVEALFERVAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  76 lvGEDG-LTVLLNNA-----GILLPYDVEGEKNRKTLIRQLETNSVSTALITQEF-LPLLKKAAAKnggdgysinraAIV 148
Cdd:cd09763  78 --EQQGrLDILVNNAyaavqLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYaAPLMVKAGKG-----------LIV 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17559964 149 NISSTAAsvekIDGTFNgplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd09763 145 IISSTGG----LEYLFN---VAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRT 195
PRK08628 PRK08628
SDR family oxidoreductase;
4-206 4.19e-10

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 58.43  E-value: 4.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIatCRDPSKAEELSNL--KDSRLHILPLDIDCDESISKLYAEVEKLVGE-D 80
Cdd:PRK08628   8 KVVIVTGGASGIGAAISLRLAEEGAIPVIF--GRSAPDDEFAEELraLQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRiD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLtvlLNNAGIllpYDVEG-EKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysinRAAIVNISSTAASvek 159
Cdd:PRK08628  86 GL---VNNAGV---NDGVGlEAGREAFVASLERNLIHYYVMAHYCLPHLKAS------------RGAIVNISSKTAL--- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17559964  160 idgTFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK08628 145 ---TGQGGTSGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMT 188
PRK09291 PRK09291
SDR family oxidoreductase;
3-207 4.29e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 58.47  E-value: 4.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    3 PKSLLITGAN----RGIGLGLLKQflKHKdiqiIIATCRDPSKAEELSN---LKDSRLHILPLDIDCDesisklyAEVEK 75
Cdd:PRK09291   2 SKTILITGAGsgfgREVALRLARK--GHN----VIAGVQIAPQVTALRAeaaRRGLALRVEKLDLTDA-------IDRAQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   76 LVGEDgLTVLLNNAGIL-------LPYDVegeknrktLIRQLETNSVSTALITQEFLPllKKAAAKNGgdgysinraAIV 148
Cdd:PRK09291  69 AAEWD-VDVLLNNAGIGeagavvdIPVEL--------VRELFETNVFGPLELTQGFVR--KMVARGKG---------KVV 128

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  149 NISSTAasvekidGTFNGPLV-AYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTG 207
Cdd:PRK09291 129 FTSSMA-------GLITGPFTgAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTG 181
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 1-206 4.44e-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: 58.32  E-value: 4.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQfLKHKDIQIIIATCRdpskAEELSNLKD------SRLHILPLDIdCDESisKLYAEVE 74
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARA-LAAEGAAVAIAARR----VDRLEALADeleaegGKALVLELDV-TDEQ--QVDAAVE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  75 KLVGEDG-LTVLLNNAGILLPYDVEGeKNRKTLIRQLETNSVSTALITQEFLPLLKkaaAKNGGDgysinraaIVNISSt 153
Cdd:cd08934  73 RTVEALGrLDILVNNAGIMLLGPVED-ADTTDWTRMIDTNLLGLMYTTHAALPHHL---LRNKGT--------IVNISS- 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17559964 154 aasvekIDGTFNGPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd08934 140 ------VAGRVAVRNSAvYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDT 187
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-208 5.14e-10

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 57.97  E-value: 5.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKhKDIQIIIATCrdpskaeELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEd 80
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVE-AGAKVIGFDQ-------AFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGP- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 gLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKkaaAKNGGdgysinraAIVNISSTAASVEKI 160
Cdd:PRK08220  77 -LDVLVNAAGILRMGATD-SLSDEDWQQTFAVNAGGAFNLFRAVMPQFR---RQRSG--------AIVTVGSNAAHVPRI 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17559964  161 DgtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK08220 144 G------MAAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDM 185
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 4-208 5.32e-10

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 58.15  E-value: 5.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDiQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:PRK12829  12 LRVLVTGGASGIGRAIAEAFAEAGA-RVHVCDVSEAALAATAARLPGAKVTATVADVADPAQVERVFDTAVERFG--GLD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGILLPY----DVEGEKNRKTlirqLETNSVSTALITQEFLPLLKkaAAKNGGdgysinraAIVNISSTAasvek 159
Cdd:PRK12829  89 VLVNNAGIAGPTggidEITPEQWEQT----LAVNLNGQFYFARAAVPLLK--ASGHGG--------VIIALSSVA----- 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17559964  160 idGTFNGPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK12829 150 --GRLGYPGRTpYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPR 197
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 7-208 5.43e-10

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 58.34  E-value: 5.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIGLGLLKQfLKHKDIQIIIATcRDPSKAEELSNL---KDSRLHILPLDID----CDESISKLYAEVEKL-VG 78
Cdd:PLN02780  57 LVTGPTDGIGKGFAFQ-LARKGLNLVLVA-RNPDKLKDVSDSiqsKYSKTQIKTVVVDfsgdIDEGVKRIKETIEGLdVG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   79 edgltVLLNNAGILLPYDVEGEKNRKTLIRQL-ETNSVSTALITQEFLP-LLKKaaaknggdgysiNRAAIVNISSTAAS 156
Cdd:PLN02780 135 -----VLINNVGVSYPYARFFHEVDEELLKNLiKVNVEGTTKVTQAVLPgMLKR------------KKGAIINIGSGAAI 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17559964  157 VEKIDgtfngPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PLN02780 198 VIPSD-----PLYAvYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKM 245
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-206 7.29e-10

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 57.42  E-value: 7.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKH-KDIQIIIATCRDPSK--AEELSNLkDSRLHILPLDIDCDESISKLYAEVEKLV 77
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEgYDIAVNYARSRKAAEetAEEIEAL-GRKALAVKANVGDVEKIKEMFAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   78 GedGLTVLLNNA--GILLP-YDVEGEKNRKTlirqLETNSVSTALITQEFLPLLKKaaaKNGGdgysinraAIVNISSTA 154
Cdd:PRK08063  81 G--RLDVFVNNAasGVLRPaMELEESHWDWT----MNINAKALLFCAQEAAKLMEK---VGGG--------KIISLSSLG 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17559964  155 ASVEKIDGTFNGplvayrMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK08063 144 SIRYLENYTTVG------VSKAALEALTRYLAVELAPKGIAVNAVSGGAVDT 189
PRK06398 PRK06398
aldose dehydrogenase; Validated
 4-235 7.56e-10

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 57.53  E-value: 7.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFlKHKDIQIIIATCRDPSKAeelsnlkDSRLhilpldIDCDES-ISKLYAEVEKLVGEDG- 81
Cdd:PRK06398   7 KVAIVTGGSQGIGKAVVNRL-KEEGSNVINFDIKEPSYN-------DVDY------FKVDVSnKEQVIKGIDYVISKYGr 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGILLpYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaakngGDGysinraAIVNISSTAASVekid 161
Cdd:PRK06398  73 IDILVNNAGIES-YGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQ-----DKG------VIINIASVQSFA---- 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559964  162 GTFNGplVAYRMSKSALNSFAKSCSIDLAKYhILVTSFCPGWVKTGMGGANAMLEIEDATKTLSDNILTLGNAH 235
Cdd:PRK06398 137 VTRNA--AAYVTSKHAVLGLTRSIAVDYAPT-IRCVAVCPGSIRTPLLEWAAELEVGKDPEHVERKIREWGEMH 207
PRK06123 PRK06123
SDR family oxidoreductase;
4-208 1.50e-09

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 56.71  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLK-----------QFLKHKDI-QIIIATCRDpskaeelsnlKDSRLHILPLDIDCDESISKLYA 71
Cdd:PRK06123   3 KVMIITGASRGIGAATALlaaergyavclNYLRNRDAaEAVVQAIRR----------QGGEALAVAADVADEADVLRLFE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   72 EVEKLVGEdgLTVLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEflpLLKKAAAKNGGDGysinrAAIVNIS 151
Cdd:PRK06123  73 AVDRELGR--LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCARE---AVKRMSTRHGGRG-----GAIVNVS 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17559964  152 STAASVEKidgtfNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK06123 143 SMAARLGS-----PGEYIDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK08251 PRK08251
SDR family oxidoreductase;
4-221 1.75e-09

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 56.48  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFL-KHKDiqiiIATCR------DPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKL 76
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAaKGRD----LALCArrtdrlEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   77 VGedGLTVLLNNAGILLPYDVEG---EKNRKTlirqLETNSVStALITQEF-LPLLKKAaaknggdgysiNRAAIVNISS 152
Cdd:PRK08251  79 LG--GLDRVIVNAGIGKGARLGTgkfWANKAT----AETNFVA-ALAQCEAaMEIFREQ-----------GSGHLVLISS 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559964  153 TAASVekidgTFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM--GGANAMLEIEDAT 221
Cdd:PRK08251 141 VSAVR-----GLPGVKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMnaKAKSTPFMVDTET 206
PRK07063 PRK07063
SDR family oxidoreductase;
4-206 2.04e-09

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 56.21  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHkDIQIIIATCRDPSKAEELSNLKDS----RLHILPLDIDCDESISKLYAEVEKLVGe 79
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFARE-GAAVALADLDAALAERAAAAIARDvagaRVLAVPADVTDAASVAAAVAAAEEAFG- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   80 dGLTVLLNNAGILL---PYDVEGEKNRKTLIRQLET--NSVSTAlitqefLPLLkkaAAKNGGdgysinraAIVNISSTA 154
Cdd:PRK07063  86 -PLDVLVNNAGINVfadPLAMTDEDWRRCFAVDLDGawNGCRAV------LPGM---VERGRG--------SIVNIASTH 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17559964  155 ASvEKIDGTFngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK07063 148 AF-KIIPGCF-----PYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIET 193
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 4-206 2.41e-09

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: 56.24  E-value: 2.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKdIQIIIATCRDPSKAEEL-SNLKDSRLHILPL--DIDCDESISKLYAEVEKLVGed 80
Cdd:cd05358   4 KVALVTGASSGIGKAIAIRLATAG-ANVVVNYRSKEDAAEEVvEEIKAVGGKAIAVqaDVSKEEDVVALFQSAIKEFG-- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  81 GLTVLLNNAGI---LLPYDVEGEKNRKTLirqlETNSVSTALITQEFLPLLKKAAAKnggdgysinrAAIVNISSTAasv 157
Cdd:cd05358  81 TLDILVNNAGLqgdASSHEMTLEDWNKVI----DVNLTGQFLCAREAIKRFRKSKIK----------GKIINMSSVH--- 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17559964 158 EKIDGTFNgplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd05358 144 EKIPWPGH---VNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINT 189
PRK07454 PRK07454
SDR family oxidoreductase;
2-249 2.86e-09

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 55.74  E-value: 2.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    2 SPKSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDP--SKAEELSNLKdSRLHILPLDIDCDESISklyAEVEKLVGE 79
Cdd:PRK07454   5 SMPRALITGASSGIGKATALAFAKAGWDLALVARSQDAleALAAELRSTG-VKAAAYSIDLSNPEAIA---PGIAELLEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   80 DGL-TVLLNNAGI-----LLPYDVEGEKnrktliRQLETNSVSTALITQEFLPLLKKaaaKNGGdgysinraAIVNISST 153
Cdd:PRK07454  81 FGCpDVLINNAGMaytgpLLEMPLSDWQ------WVIQLNLTSVFQCCSAVLPGMRA---RGGG--------LIINVSSI 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  154 AAsvekiDGTFNGpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT-----GMGGAN----AMLEIEdatkTL 224
Cdd:PRK07454 144 AA-----RNAFPQ-WGAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTplwdtETVQADfdrsAMLSPE----QV 213

                        250       260
                 ....*....|....*....|....*
gi 17559964  225 SDNILTLGNAHHGAYLNaDLTVIPN 249
Cdd:PRK07454 214 AQTILHLAQLPPSAVIE-DLTLMPS 237
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 1-231 2.87e-09

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 55.86  E-value: 2.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQfLKHKDIQIIIA----TCRDPSKAEELS----------NLKDSRLHILPLDIDCDESI 66
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALR-LAKAGATVVVAaktaSEGDNGSAKSLPgtieetaeeiEAAGGQALPIVVDVRDEDQV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  67 SKLYAEVEKLVGedGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaakngGDGYsinraa 146
Cdd:cd05338  80 RALVEATVDQFG--RLDILVNNAGAIWLSLVE-DTPAKRFDLMQRVNLRGTYLLSQAALPHMVKA-----GQGH------ 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964 147 IVNISSTAASvekidgTFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATKT--- 223
Cdd:cd05338 146 ILNISPPLSL------RPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPAATELSGGSDPARARspe 219


                ....*....
gi 17559964 224 -LSDNILTL 231
Cdd:cd05338 220 iLSDAVLAI 228
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 6-204 3.18e-09

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 55.92  E-value: 3.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    6 LLITGANRGIGLGLLKQFLKHKdiQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdgLTVL 85
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQG--HKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRN--IDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   86 LNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISSTAASVEKIDGTfn 165
Cdd:PRK10538  79 VNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVER-----------NHGHIINIGSTAGSWPYAGGN-- 145

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 17559964  166 gplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWV 204
Cdd:PRK10538 146 ----VYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLV 180
PRK06947 PRK06947
SDR family oxidoreductase;
4-206 4.22e-09

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 55.20  E-value: 4.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGlLKQFLKHKDIQIIIATCRDPSKAEELSNL-KDSRLHILPL--DIDCDESISKLYAEVEKLVGed 80
Cdd:PRK06947   3 KVVLITGASRGIGRA-TAVLAAARGWSVGINYARDAAAAEETADAvRAAGGRACVVagDVANEADVIAMFDAVQSAFG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLTVLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEflpLLKKAAAKNGGDGysinrAAIVNISSTAASVeki 160
Cdd:PRK06947  80 RLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCARE---AARRLSTDRGGRG-----GAIVNVSSIASRL--- 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17559964  161 dGTFNgPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK06947 149 -GSPN-EYVDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIET 192
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 4-224 4.29e-09

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: 55.15  E-value: 4.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHK------DIQiiiatcrDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLV 77
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGwfvglyDID-------EDGLAALAAELGAENVVAGALDVTDRAAWAAALADFAAAT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  78 GEdGLTVLLNNAGILL--PY-DVEGEKNRktliRQLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTA 154
Cdd:cd08931  74 GG-RLDALFNNAGVGRggPFeDVPLAAHD----RMVDINVKGVLNGAYAALPYLKATPG-----------ARVINTASSS 137

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559964 155 asvekidGTFNGP-LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMggANAMLEIEDATKTL 224
Cdd:cd08931 138 -------AIYGQPdLAVYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPI--LTKGETGAAPKKGL 199
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
3-196 5.06e-09

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 56.01  E-value: 5.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    3 PKSL-----LITGANRGIGLGLLKQFLK---HkdiqiIIATCRDPSK----AEELSNLKDSRlhILPLDIDCDESISKLY 70
Cdd:PRK08324 417 PKPLagkvaLVTGAAGGIGKATAKRLAAegaC-----VVLADLDEEAaeaaAAELGGPDRAL--GVACDVTDEAAVQAAF 489

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   71 AEVEKLVGedGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKkaAAKNGGDgysinraaIVNI 150
Cdd:PRK08324 490 EEAALAFG--GVDIVVSNAGIAISGPIE-ETSDEDWRRSFDVNATGHFLVAREAVRIMK--AQGLGGS--------IVFI 556

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17559964  151 SSTAAsvekidgTFNGPL-VAYRMSKSALNSFAKSCSIDLAKYHILV 196
Cdd:PRK08324 557 ASKNA-------VNPGPNfGAYGAAKAAELHLVRQLALELGPDGIRV 596
PRK06181 PRK06181
SDR family oxidoreductase;
4-206 8.28e-09

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 54.60  E-value: 8.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHkDIQIIIATcRDPSK----AEELSNLKDSRLhILPLDIDCDESISKLYAEVEKLVGe 79
Cdd:PRK06181   2 KVVIITGASEGIGRALAVRLARA-GAQLVLAA-RNETRlaslAQELADHGGEAL-VVPTDVSDAEACERLIEAAVARFG- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   80 dGLTVLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaknggdgysiNRAAIVNISSTAAsvek 159
Cdd:PRK06181  78 -GIDILVNNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKA------------SRGQIVVVSSLAG---- 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17559964  160 idgtFNGPL--VAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK06181 141 ----LTGVPtrSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVAT 185
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 57-204 1.12e-08

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 54.19  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   57 PLDIDCDESISKLYAEVEKLVGedGLTVLLNNAgILLPYDVEGEKNRKTLIRQ-LETNSVSTALITQEFLPLLKKAaakn 135
Cdd:PRK07890  60 PTDITDEDQCANLVALALERFG--RVDALVNNA-FRVPSMKPLADADFAHWRAvIELNVLGTLRLTQAFTPALAES---- 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964  136 ggdgysinRAAIVNISStaASVEKIDGTFNgplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWV 204
Cdd:PRK07890 133 --------GGSIVMINS--MVLRHSQPKYG----AYKMAKGALLAASQSLATELGPQGIRVNSVAPGYI 187
PRK07074 PRK07074
SDR family oxidoreductase;
3-206 1.14e-08

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 54.39  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    3 PKSL-LITGANRGIGLGLLKQFLKHKDIqiIIATCRDPSKAEELS-NLKDSRLHILPLDIDCDESISklyAEVEKLVGED 80
Cdd:PRK07074   1 TKRTaLVTGAAGGIGQALARRFLAAGDR--VLALDIDAAALAAFAdALGDARFVPVACDLTDAASLA---AALANAAAER 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLT-VLLNNAGILLP---YDVEGEKNRKTLIRQLEtnsvSTALITQEFLPLLKKAAaknggdgysinRAAIVNIsstaAS 156
Cdd:PRK07074  76 GPVdVLVANAGAARAaslHDTTPASWRADNALNLE----AAYLCVEAVLEGMLKRS-----------RGAVVNI----GS 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17559964  157 VEKIdGTFNGPlvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK07074 137 VNGM-AALGHP--AYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKT 183
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 4-214 1.18e-08

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 54.14  E-value: 1.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIG----LGLLKqflKHKDIQIIiatCRDPSKAEEL-------SNLKDSRLHIlpLDIDCDESISKLYAE 72
Cdd:cd09808   2 RSFLITGANSGIGkaaaLAIAK---RGGTVHMV---CRNQTRAEEArkeieteSGNQNIFLHI--VDMSDPKQVWEFVEE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  73 VEKLVGEdgLTVLLNNAGILLPydvEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISS 152
Cdd:cd09808  74 FKEEGKK--LHVLINNAGCMVN---KRELTEDGLEKNFATNTLGTYILTTHLIPVLEKE-----------EDPRVITVSS 137

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559964 153 TAASVEKID--------GTFNGPLVaYRMSKSA----LNSFAKSC-SIDLAKYHilvtsfcPGWVKTGmGGANAM 214
Cdd:cd09808 138 GGMLVQKLNtnnlqserTAFDGTMV-YAQNKRQqvimTEQWAKKHpEIHFSVMH-------PGWADTP-AVRNSM 203
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 1-206 1.98e-08

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 53.35  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKHkDIQIIIATCRDPSKAEELSNLKDSRLHIL--PLDIDCDESISKLYAEVEKLVG 78
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKE-GAKVVIADLNDEAAAAAAEALQKAGGKAIgvAMDVTDEEAINAGIDYAVETFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   79 edGLTVLLNNAGILLPYDVEG---EKNRKTlirqLETNSVSTALITQEFLPLLKkaaAKNGGdgysinraAIVNISST-- 153
Cdd:PRK12429  81 --GVDILVNNAGIQHVAPIEDfptEKWKKM----IAIMLDGAFLTTKAALPIMK---AQGGG--------RIINMASVhg 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17559964  154 -AASVEKidgtfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK12429 144 lVGSAGK---------AAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDT 188
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-206 2.37e-08

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 53.17  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKhKDIQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEd 80
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAR-EGARVVVNYHQSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGK- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLTVLLNNAGILLPYDVEGEKNRKTLI-----RQLEtNSVSTAL-ITQEFLPLLKkaAAKNGgdgysinraAIVNISSTa 154
Cdd:PRK08642  81 PITTVVNNALADFSFDGDARKKADDITwedfqQQLE-GSVKGALnTIQAALPGMR--EQGFG---------RIINIGTN- 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17559964  155 asvekidgTFNGPLVAYR---MSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK08642 148 --------LFQNPVVPYHdytTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK05866 PRK05866
SDR family oxidoreductase;
4-208 2.52e-08

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 53.59  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIAtcrdpSKAEELSNLKD------SRLHILPLDIDCDESISKLYAEVEKLV 77
Cdd:PRK05866  41 KRILLTGASSGIGEAAAEQFARRGATVVAVA-----RREDLLDAVADritragGDAMAVPCDLSDLDAVDALVADVEKRI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   78 GedGLTVLLNNAG--ILLP--------YDVEgeknrktliRQLETNSVSTALITQEFLPLLKKAaakngGDGYsinraaI 147
Cdd:PRK05866 116 G--GVDILINNAGrsIRRPlaesldrwHDVE---------RTMVLNYYAPLRLIRGLAPGMLER-----GDGH------I 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559964  148 VNISSTAASVEKIdgtfngPLV-AYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK05866 174 INVATWGVLSEAS------PLFsVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-206 2.58e-08

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 53.20  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIATCRDP-SKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdgL 82
Cdd:PRK06935  16 KVAIVTGGNTGLGQGYAVALAK-AGADIIITTHGTNwDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGK--I 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   83 TVLLNNAGI-----LLPYDvegEKNRKTLIrqlETNSVSTALITQEflplLKKAAAKNGgdgysinRAAIVNIsstaASV 157
Cdd:PRK06935  93 DILVNNAGTirrapLLEYK---DEDWNAVM---DINLNSVYHLSQA----VAKVMAKQG-------SGKIINI----ASM 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17559964  158 EKIDGtfnGPLV-AYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK06935 152 LSFQG---GKFVpAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 7-207 2.92e-08

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: 52.90  E-value: 2.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHKDIQIIIAtcRDPSKAEELSNLKDSRLHILPLDIDCD----ESISKLYAEVEKLVGedGL 82
Cdd:cd05343  10 LVTGASVGIGAAVARALVQHGMKVVGCA--RRVDKIEALAAECQSAGYPTLFPYQCDlsneEQILSMFSAIRTQHQ--GV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  83 TVLLNNAGILLPYDVEGEKNR--KTLirqLETNSVSTALITQEflpLLKKAAAKNGGDGYsinraaIVNISSTAASVeki 160
Cdd:cd05343  86 DVCINNAGLARPEPLLSGKTEgwKEM---FDVNVLALSICTRE---AYQSMKERNVDDGH------IININSMSGHR--- 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17559964 161 dgTFNGPLVA-YRMSKSALNSFAKSCSIDL--AKYHILVTSFCPGWVKTG 207
Cdd:cd05343 151 --VPPVSVFHfYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETE 198
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 7-208 3.62e-08

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 52.80  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIGLGLLKQfLKHKDIQIIIATCRDPSKAEELSNL------KDSRLHILPLDIdcdESISKLYAEVEKLVGED 80
Cdd:PRK12827  10 LITGGSGGLGRAIAVR-LAADGADVIVLDIHPMRGRAEADAVaagieaAGGKALGLAFDV---RDFAATRAALDAGVEEF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 G-LTVLLNNAGIL--LPYDvegEKNRKTLIRQLETNSVSTALITQEFLPLLkkAAAKNGGdgysinraAIVNISSTAAsv 157
Cdd:PRK12827  86 GrLDILVNNAGIAtdAAFA---ELSIEEWDDVIDVNLDGFFNVTQAALPPM--IRARRGG--------RIVNIASVAG-- 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17559964  158 ekidGTFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK12827 151 ----VRGNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPM 197
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 4-245 4.40e-08

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: 52.58  E-value: 4.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGA--NRGIGLGLLKQFLKHKdIQIIIaTCRDPS---KAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVG 78
Cdd:cd05372   2 KRILITGIanDRSIAWGIAKALHEAG-AELAF-TYQPEAlrkRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  79 E-DGLTVLLNNA---GILLPYDvegEKNRKTLIRQLETNSVSTALITQEFLPLLkkaaaKNGGdgysinraAIVNISSTA 154
Cdd:cd05372  80 KlDGLVHSIAFApkvQLKGPFL---DTSRKGFLKALDISAYSLVSLAKAALPIM-----NPGG--------SIVTLSYLG 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964 155 AsvEKIDGTFNGPLVAyrmsKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT----GMGGANAMLEIEDATKTLSDNILT 230
Cdd:cd05372 144 S--ERVVPGYNVMGVA----KAALESSVRYLAYELGRKGIRVNAISAGPIKTlaasGITGFDKMLEYSEQRAPLGRNVTA 217

                       250
                ....*....|....*..
gi 17559964 231 --LGNAhhGAYLNADLT 245
Cdd:cd05372 218 eeVGNT--AAFLLSDLS 232
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 4-206 5.07e-08

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: 52.29  E-value: 5.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKH-KDIQIIIATCRDPsKAEELSNL---KDSRLHILPLDIDCDESISKLYAEVEKLVGe 79
Cdd:cd05355  27 KKALITGGDSGIGRAVAIAFAREgADVAINYLPEEED-DAEETKKLieeEGRKCLLIPGDLGDESFCRDLVKEVVKEFG- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  80 dGLTVLLNNAGILLPY----DVEGEKNRKTLirqlETNSVSTALITQEFLPLLKKAAAknggdgysinraaIVNISStaa 155
Cdd:cd05355 105 -KLDILVNNAAYQHPQesieDITTEQLEKTF----RTNIFSMFYLTKAALPHLKKGSS-------------IINTTS--- 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17559964 156 sVEKIDGtfNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd05355 164 -VTAYKG--SPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWT 211
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 1-228 5.32e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 52.21  E-value: 5.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLK--HKdiqiIIATCRDPSKAEELSNLKdsrlhILPLDIDCDESISKLYAEVEKLVG 78
Cdd:PRK06179   2 SNSKVALVTGASSGIGRATAEKLARagYR----VFGTSRNPARAAPIPGVE-----LLELDVTDDASVQAAVDEVIARAG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   79 EdgLTVLLNNAGILLPYDVEgeknrKTLIRQ----LETNSVSTALITQEFLPLLKKAaakngGDGysinRaaIVNISSta 154
Cdd:PRK06179  73 R--IDVLVNNAGVGLAGAAE-----ESSIAQaqalFDTNVFGILRMTRAVLPHMRAQ-----GSG----R--IINISS-- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  155 asvekIDGTFNGPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMgGANAM----------LEIEDATKT 223
Cdd:PRK06179 133 -----VLGFLPAPYMAlYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF-DANAPepdsplaeydRERAVVSKA 206


                 ....*
gi 17559964  224 LSDNI 228
Cdd:PRK06179 207 VAKAV 211
PRK06949 PRK06949
SDR family oxidoreductase;
1-208 5.50e-08

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 52.07  E-value: 5.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGlgllKQF---LKHKDIQIIIATCRdpskaeeLSNLKDSRL---------HILPLDIDCDESISK 68
Cdd:PRK06949   7 LEGKVALVTGASSGLG----ARFaqvLAQAGAKVVLASRR-------VERLKELRAeieaeggaaHVVSLDVTDYQSIKA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   69 LYAEVEKLVGEdgLTVLLNNAGI--------LLPYDVEgeknrktliRQLETNSVSTALITQEflpLLKKAAAKNGGDGY 140
Cdd:PRK06949  76 AVAHAETEAGT--IDILVNNSGVsttqklvdVTPADFD---------FVFDTNTRGAFFVAQE---VAKRMIARAKGAGN 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  141 SINRAAIVNISSTAA--SVEKIDgtfngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK06949 142 TKPGGRIINIASVAGlrVLPQIG--------LYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
PRK07832 PRK07832
SDR family oxidoreductase;
4-208 8.40e-08

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 51.58  E-value: 8.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIG----LGLLKQ----FLKHKDIQIIIATcrdpskAEELSNLKDSRLHILPLDIDCDESISKLYAEVEK 75
Cdd:PRK07832   1 KRCFVTGAASGIGrataLRLAAQgaelFLTDRDADGLAQT------VADARALGGTVPEHRALDISDYDAVAAFAADIHA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   76 LVGedGLTVLLNNAGILLPYDVEGEKNR--KTLIrqlETNSVSTALITQEFLPllKKAAAKNGGDgysinraaIVNISST 153
Cdd:PRK07832  75 AHG--SMDVVMNIAGISAWGTVDRLTHEqwRRMV---DVNLMGPIHVIETFVP--PMVAAGRGGH--------LVNVSSA 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17559964  154 AasvekidGTFNGPL-VAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK07832 140 A-------GLVALPWhAAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPL 188
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-202 8.92e-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: 51.51  E-value: 8.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKHKdIQIIIATCRDPSKAEELS---NLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdgLT 83
Cdd:cd05357   4 LVTGAAKRIGRAIAEALAAEG-YRVVVHYNRSEAEAQRLKdelNALRNSAVLVQADLSDFAACADLVAAAFRAFGR--CD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVeGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNIsstaasvekIDGT 163
Cdd:cd05357  81 VLVNNASAFYPTPL-GQGSEDAWAELFGINLKAPYLLIQAFARRLAGSR-----------NGSIINI---------IDAM 139

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17559964 164 FNGPL---VAYRMSKSALNSFAKSCSIDLAKYhILVTSFCPG 202
Cdd:cd05357 140 TDRPLtgyFAYCMSKAALEGLTRSAALELAPN-IRVNGIAPG 180
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 4-208 9.07e-08

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: 51.34  E-value: 9.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFlKHKDIQIIIATcRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:cd08944   4 KVAIVTGAGAGIGAACAARL-AREGARVVVAD-IDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFG--GLD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGI--LLPY--DVEGEKNRKTLirqlETNSVSTALITQEFLPLLkkaAAKNGGdgysinraAIVNISStaasvek 159
Cdd:cd08944  80 LLVNNAGAmhLTPAiiDTDLAVWDQTM----AINLRGTFLCCRHAAPRM---IARGGG--------SIVNLSS------- 137

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17559964 160 IDGTFNGPLV-AYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd08944 138 IAGQSGDPGYgAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPL 187
PRK06172 PRK06172
SDR family oxidoreductase;
2-208 1.24e-07

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 51.29  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    2 SPKSLLITGANRGIGLGLLKQFLKhKDIQIIIATcRDPSKAEELSNL-KD--SRLHILPLDIDCDESISKLyaeVEKLVG 78
Cdd:PRK06172   6 SGKVALVTGGAAGIGRATALAFAR-EGAKVVVAD-RDAAGGEETVALiREagGEALFVACDVTRDAEVKAL---VEQTIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   79 EDG-LTVLLNNAGIllpydvEGEKNRktLIRQLE--------TNSVSTALITQEFLPLLkkaaAKNGGdgysinrAAIVN 149
Cdd:PRK06172  81 AYGrLDYAFNNAGI------EIEQGR--LAEGSEaefdaimgVNVKGVWLCMKYQIPLM----LAQGG-------GAIVN 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964  150 ISSTAASVekidGTFNGPLvaYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK06172 142 TASVAGLG----AAPKMSI--YAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM 194
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 6-208 1.29e-07

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 51.07  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964     6 LLITGANRGIGLGLLKQFLKHKDIQIIIAT--CRD-----PSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVG 78
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKCLKSPGSVLVlsARNdealrQLKAEIGAERSGLRVVRVSLDLGAEAGLEQLLKALRELPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    79 EDGLT--VLLNNAGILlpYDV-EGEK---NRKTLIRQLETNSVSTALITQEFLPLLKkaaaknggDGYSINRaAIVNISS 152
Cdd:TIGR01500  83 PKGLQrlLLINNAGTL--GDVsKGFVdlsDSTQVQNYWALNLTSMLCLTSSVLKAFK--------DSPGLNR-TVVNISS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17559964   153 TAAsVEKIDGtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:TIGR01500 152 LCA-IQPFKG-----WALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDM 201
PRK05854 PRK05854
SDR family oxidoreductase;
1-182 1.51e-07

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 51.22  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQfLKHKDIQIIIATcRDPSKAEE-LSNLK----DSRLHILPLDIDCDESISKLYAEVEk 75
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARR-LAAAGAEVILPV-RNRAKGEAaVAAIRtavpDAKLSLRALDLSSLASVAALGEQLR- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   76 lvgEDGLTV--LLNNAGILLPydvegeKNRKTLIR----QLETNSVSTALITQEFLPLLKKAaaknggdgysinRAAIVN 149
Cdd:PRK05854  89 ---AEGRPIhlLINNAGVMTP------PERQTTADgfelQFGTNHLGHFALTAHLLPLLRAG------------RARVTS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 17559964  150 ISSTAASVEKI-------DGTFNGpLVAYRMSKSALNSFA 182
Cdd:PRK05854 148 QSSIAARRGAInwddlnwERSYAG-MRAYSQSKIAVGLFA 186
PRK06138 PRK06138
SDR family oxidoreductase;
4-208 1.53e-07

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 50.92  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKdiQIIIATCRDPSKAEELSNL--KDSRLHILPLDIDCDESISKLYAEVEKLVGedG 81
Cdd:PRK06138   6 RVAIVTGAGSGIGRATAKLFAREG--ARVVVADRDAEAAERVAAAiaAGGRAFARQGDVGSAEAVEALVDFVAARWG--R 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGillpYDVEG------EKNRKTLIRqleTNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISSTAA 155
Cdd:PRK06138  82 LDVLVNNAG----FGCGGtvvttdEADWDAVMR---VNVGGVFLWAKYAIPIMQRQGG-----------GSIVNTASQLA 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17559964  156 SVEKIDGTfngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK06138 144 LAGGRGRA------AYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPY 190
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-206 1.96e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 50.67  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQfLKHKDIQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEd 80
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIG-LAKAGADIVGVGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGH- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 gLTVLLNNAGILlpydvegekNRKTLIRQLETNSVSTALITQEFLPLLKKAAAK------NGGDgysinraaIVNIssta 154
Cdd:PRK12481  84 -IDILINNAGII---------RRQDLLEFGNKDWDDVININQKTVFFLSQAVAKqfvkqgNGGK--------IINI---- 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17559964  155 ASVEKIDGTFNGPlvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK12481 142 ASMLSFQGGIRVP--SYTASKSAVMGLTRALATELSQYNINVNAIAPGYMAT 191
PRK06124 PRK06124
SDR family oxidoreductase;
7-206 2.39e-07

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 50.48  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIGLGLLKQFLK---HkdiqiIIATCRDPSKAEE-LSNLKDSRL--HILPLDIDCDESISKLYAEVEKLVGed 80
Cdd:PRK06124  15 LVTGSARGLGFEIARALAGagaH-----VLVNGRNAATLEAaVAALRAAGGaaEALAFDIADEEAVAAAFARIDAEHG-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLTVLLNNAGillpydvegEKNRKTL-------IRQL-ETNSVSTALitqeflpLLKKAAAKNGGDGYsinrAAIVNISS 152
Cdd:PRK06124  88 RLDILVNNVG---------ARDRRPLaelddaaIRALlETDLVAPIL-------LSRLAAQRMKRQGY----GRIIAITS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17559964  153 TAASVEKIDGtfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK06124 148 IAGQVARAGD------AVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 4-215 2.73e-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: 50.31  E-value: 2.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKhKDIQIIIATCRdPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:cd05363   4 KTALITGSARGIGRAFAQAYVR-EGARVAIADIN-LEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SID 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGIllpYDVEG--EKNRKTLIRQLETNSVSTALITQeflpllkkAAAKN---GGDGysinrAAIVNISSTAasve 158
Cdd:cd05363  80 ILVNNAAL---FDLAPivDITRESYDRLFAINVSGTLFMMQ--------AVARAmiaQGRG-----GKIINMASQA---- 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964 159 kidGTFNGPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM-GGANAML 215
Cdd:cd05363 140 ---GRRGEALVGvYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHwDGVDAKF 195
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 4-223 2.90e-07

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: 50.15  E-value: 2.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDP--SKAEELSNLKDSRLHILP--LDIdcdESISKLYAEVEKLVGE 79
Cdd:cd08935   6 KVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKgdKVAKEITALGGRAIALAAdvLDR---ASLERAREEIVAQFGT 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  80 dgLTVLLNNAGILLP--------YDVEGEKN-----RKTLIRQLETNSVSTALITQEFL-PLLKKaaaknggdgysiNRA 145
Cdd:cd08935  83 --VDILINGAGGNHPdattdpehYEPETEQNffdldEEGWEFVFDLNLNGSFLPSQVFGkDMLEQ------------KGG 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964 146 AIVNISSTAA--SVEKIdgtfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGgaNAMLEIEDATKT 223
Cdd:cd08935 149 SIINISSMNAfsPLTKV--------PAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQN--RKLLINPDGSYT 218
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 1-219 3.12e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 49.94  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKHkDIQIIIATcRDPSKAEElSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEd 80
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAAL-GARVAIGD-LDEALAKE-TAAELGLVVGGPLDVTDPASFAAFLDAVEADLGP- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 gLTVLLNNAGI--LLPYDVEGEknrKTLIRQLETNSVSTALITQEFLPllkkAAAKNGgdgysinRAAIVNISStAASVE 158
Cdd:PRK07825  79 -IDVLVNNAGVmpVGPFLDEPD---AVTRRILDVNVYGVILGSKLAAP----RMVPRG-------RGHVVNVAS-LAGKI 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559964  159 KIDGtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT------GMGGANAMLEIED 219
Cdd:PRK07825 143 PVPG-----MATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTeliagtGGAKGFKNVEPED 204
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-211 3.21e-07

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 49.96  E-value: 3.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHK-DIQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGedGL 82
Cdd:PRK08217   6 KVIVITGGAQGLGRAMAEYLAQKGaKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFG--QL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   83 TVLLNNAGIL----LPYDVEGEKNRKTLIRQLetNSVSTALITQEFLpLLKKAAAK--NGGDGysinrAAIVNISST--A 154
Cdd:PRK08217  84 NGLINNAGILrdglLVKAKDGKVTSKMSLEQF--QSVIDVNLTGVFL-CGREAAAKmiESGSK-----GVIINISSIarA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17559964  155 ASVekidGTFNgplvaYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGA 211
Cdd:PRK08217 156 GNM----GQTN-----YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAA 203
PRK07201 PRK07201
SDR family oxidoreductase;
4-208 3.34e-07

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 50.72  E-value: 3.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIAtcRDPSKAEELSNL---KDSRLHILPLDIDCDESISKLyaeVEKLVGE- 79
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGATVFLVA--RNGEALDELVAEiraKGGTAHAYTCDLTDSAAVDHT---VKDILAEh 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   80 DGLTVLLNNAG------ILLPY----DVEgeknrktliRQLETNSVSTALITQEFLPLLkkaAAKNGGDgysinraaIVN 149
Cdd:PRK07201 447 GHVDYLVNNAGrsirrsVENSTdrfhDYE---------RTMAVNYFGAVRLILGLLPHM---RERRFGH--------VVN 506

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  150 ISSTAASVekidgtfNGP-LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK07201 507 VSSIGVQT-------NAPrFSAYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPM 559
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 4-208 4.65e-07

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 49.23  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQfLKHKDIQIIIATCRDPSKAEELSN-LKDSRLHILPLDIDCD--ESISKLYAEVEKLVGEd 80
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVA-LAQEGAKVVINYNSSKEAAENLVNeLGKEGHDVYAVQADVSkvEDANRLVEEAVNHFGK- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 gLTVLLNNAGIllPYDVEGEK-NRKTLIRQLETNSVSTALITQEFLPLLKKAaakNGGdgysinraAIVNISSTAASVek 159
Cdd:PRK12935  85 -VDILVNNAGI--TRDRTFKKlNREDWERVIDVNLSSVFNTTSAVLPYITEA---EEG--------RIISISSIIGQA-- 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17559964  160 idGTFNGplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK12935 149 --GGFGQ--TNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEM 193
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 6-208 5.07e-07

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: 49.11  E-value: 5.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   6 LLITGANRGIGLGLLKQFLKHKDIQIIIAtcRDPSKAEELSNLKDSRLH----ILPLDID------CDESISKLYAEVEK 75
Cdd:cd05340   7 ILVTGASDGIGREAALTYARYGATVILLG--RNEEKLRQVADHINEEGGrqpqWFILDLLtctsenCQQLAQRIAVNYPR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  76 LvgeDGltvLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISStaa 155
Cdd:cd05340  85 L---DG---VLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDA-----------GSLVFTSS--- 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17559964 156 SVEKIDGTFNGplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05340 145 SVGRQGRANWG---AYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAM 194
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-207 5.34e-07

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 49.40  E-value: 5.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANR--GIGLGLLKQFLKH-KDIQIIIATCRDPSK------------AEELSNLkDSRLHILPLDIDCDESISK 68
Cdd:PRK12859   7 KVAVVTGVSRldGIGAAICKELAEAgADIFFTYWTAYDKEMpwgvdqdeqiqlQEELLKN-GVKVSSMELDLTQNDAPKE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   69 LYAEVEKLVGEDglTVLLNNAGillpYDVEGEKNRKT---LIRQLETNSVSTALITQEFLPLLKKaaaKNGGdgysinra 145
Cdd:PRK12859  86 LLNKVTEQLGYP--HILVNNAA----YSTNNDFSNLTaeeLDKHYMVNVRATTLLSSQFARGFDK---KSGG-------- 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559964  146 AIVNISStaasvekidGTFNGPLV---AYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTG 207
Cdd:PRK12859 149 RIINMTS---------GQFQGPMVgelAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTG 204
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 7-209 5.68e-07

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: 49.21  E-value: 5.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   7 LITGANRGIGLGLLKQFLKhKDIQIIIATcRDPSKAEELSNLKDsRLHILPLDIdCDESISKlyAEVEKLVGEDG-LTVL 85
Cdd:cd05371   6 VVTGGASGLGLATVERLLA-QGAKVVILD-LPNSPGETVAKLGD-NCRFVPVDV-TSEKDVK--AALALAKAKFGrLDIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  86 LNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALI-TQEFLPLLKKAAAKNGGDGYSiNRAAIVNISSTAAsvekidgtF 164
Cdd:cd05371  80 VNCAGIAVAAKTYNKKGQQPHSLELFQRVINVNLIgTFNVIRLAAGAMGKNEPDQGG-ERGVIINTASVAA--------F 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17559964 165 NGPL--VAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMG 209
Cdd:cd05371 151 EGQIgqAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLL 197
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 4-206 6.24e-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: 49.11  E-value: 6.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDiQIIIATCRDPSKAEElsnLKDSRLHILPLDIDCDESISKLYAEVEKLVGEDGLT 83
Cdd:cd09761   2 KVAIVTGGGHGIGKQICLDFLEAGD-KVVFADIDEERGADF---AEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRID 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  84 VLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaknggdgysiNRAAIVNISSTAASVEKIDGT 163
Cdd:cd09761  78 VLVNNAARGSKGILS-SLLLEEWDRILSVNLTGPYELSRYCRDELIK------------NKGRIINIASTRAFQSEPDSE 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17559964 164 fngplvAYRMSKSALNSFAKSCSIDLAKYhILVTSFCPGWVKT 206
Cdd:cd09761 145 ------AYAASKGGLVALTHALAMSLGPD-IRVNCISPGWINT 180
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 7-220 6.25e-07

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 49.07  E-value: 6.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIGLGLLKQFLKHKDIQIIIATCRDPSK--AEELSNLKDSRLHIlPLDIDCDESISKLY-AEVEKLvgeDGLT 83
Cdd:PRK06113  15 IITGAGAGIGKEIAITFATAGASVVVSDINADAANhvVDEIQQLGGQAFAC-RCDITSEQELSALAdFALSKL---GKVD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGI--LLPYDVEGEknrkTLIRQLETNSVSTALITQEFLPLLKKAAaknGGdgysinraAIVNISSTAASVEKID 161
Cdd:PRK06113  91 ILVNNAGGggPKPFDMPMA----DFRRAYELNVFSFFHLSQLVAPEMEKNG---GG--------VILTITSMAAENKNIN 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964  162 gtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDA 220
Cdd:PRK06113 156 ------MTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQK 208
PRK12743 PRK12743
SDR family oxidoreductase;
2-210 6.82e-07

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 48.88  E-value: 6.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    2 SPKSLLITGANRGIG----LGLLKQFLkhkDIQIIIAtcRDPSKAEELSNLKDS---RLHILPLDIDCDESISKLyaeVE 74
Cdd:PRK12743   1 MAQVAIVTASDSGIGkacaLLLAQQGF---DIGITWH--SDEEGAKETAEEVRShgvRAEIRQLDLSDLPEGAQA---LD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   75 KLVGE-DGLTVLLNNAG-------ILLPYDvegeknrktLIRQLETNSVSTAlitqeFLpLLKKAAAK--NGGDGysinr 144
Cdd:PRK12743  73 KLIQRlGRIDVLVNNAGamtkapfLDMDFD---------EWRKIFTVDVDGA-----FL-CSQIAARHmvKQGQG----- 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559964  145 AAIVNISSTAASVEKIDGTfngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGG 210
Cdd:PRK12743 133 GRIINITSVHEHTPLPGAS------AYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNG 192
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 4-91 7.56e-07

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 48.92  E-value: 7.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLG----LLKQFLKHKDIQIIIaTCRDPSKAEE-LSNLKDS------RLHILPLDIDCDESISKLYAE 72
Cdd:cd08941   2 KVVLVTGANSGLGLAicerLLAEDDENPELTLIL-ACRNLQRAEAaCRALLAShpdarvVFDYVLVDLSNMVSVFAAAKE 80

                        90
                ....*....|....*....
gi 17559964  73 VEKLVgeDGLTVLLNNAGI 91
Cdd:cd08941  81 LKKRY--PRLDYLYLNAGI 97
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-209 8.80e-07

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 48.56  E-value: 8.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDPSKAEELSNLKD---SRLHILPlDIDCDESISKLYAEVEKLV 77
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKEnggEGIGVLA-DVSTREGCETLAKATIDRY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   78 GedGLTVLLNNAGILLpYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaknGGdgysinraAIVNISSTAASV 157
Cdd:PRK06077  83 G--VADILVNNAGLGL-FSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMRE-----GG--------AIVNIASVAGIR 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17559964  158 ekidgTFNGpLVAYRMSKSALNSFAKSCSIDLAKyHILVTSFCPGWVKTGMG 209
Cdd:PRK06077 147 -----PAYG-LSIYGAMKAAVINLTKYLALELAP-KIRVNAIAPGFVKTKLG 191
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 1-209 1.03e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 48.50  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFLKhKDIQIIIATcRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGed 80
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAA-KGARVALLD-RSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFG-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLTVLLNNAGI--LLP-YDVEGEKNRKTLirqlETNSVSTALITQEFLPLLKKAAaknGGdgysinraAIVNISSTAASV 157
Cdd:PRK06841  89 RIDILVNSAGValLAPaEDVSEEDWDKTI----DINLKGSFLMAQAVGRHMIAAG---GG--------KIVNLASQAGVV 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17559964  158 eKIDGTfngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMG 209
Cdd:PRK06841 154 -ALERH-----VAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELG 199
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 4-208 1.13e-06

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 48.33  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIAtcRDPSKAE----ELSNLKDSRLHILPLDI------DCDEsiskLYAEV 73
Cdd:PRK08945  13 RIILVTGAGDGIGREAALTYARHGATVILLG--RTEEKLEavydEIEAAGGPQPAIIPLDLltatpqNYQQ----LADTI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   74 EKLVGE-DGLtvlLNNAGIL---LPYDvegEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVN 149
Cdd:PRK08945  87 EEQFGRlDGV---LHNAGLLgelGPME---QQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPA-----------ASLVF 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964  150 ISStaaSVEKIDGTFNGplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK08945 150 TSS---SVGRQGRANWG---AYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 7-211 1.53e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 47.84  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIGLGLLKQFLKHKdiQIIIATCRDPSKAEELSN-LKDSRL--HILPLDIDCDESISKLYAEVEKLVGEdgLT 83
Cdd:PRK07523  14 LVTGSSQGIGYALAEGLAQAG--AEVILNGRDPAKLAAAAEsLKGQGLsaHALAFDVTDHDAVRAAIDAFEAEIGP--ID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQeflpllkkAAAKnggdgYSINRAA--IVNISSTAASVEKid 161
Cdd:PRK07523  90 ILVNNAGMQFRTPLE-DFPADAFERLLRTNISSVFYVGQ--------AVAR-----HMIARGAgkIINIASVQSALAR-- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17559964  162 gtfngPLVA-YRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGA 211
Cdd:PRK07523 154 -----PGIApYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAA 199
PRK08589 PRK08589
SDR family oxidoreductase;
4-227 1.62e-06

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 47.85  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEdgLT 83
Cdd:PRK08589   7 KVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGR--VD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGIllpyDVEGEKNRKTLI----RQLETNSVSTALITQEFLPLLkkaaAKNGGdgysinraAIVNISSTAASVEK 159
Cdd:PRK08589  85 VLFNNAGV----DNAAGRIHEYPVdvfdKIMAVDMRGTFLMTKMLLPLM----MEQGG--------SIINTSSFSGQAAD 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559964  160 IDGTfngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGANAMLEIEDATKTLSDN 227
Cdd:PRK08589 149 LYRS------GYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSEDEAGKTFREN 210
PRK07024 PRK07024
SDR family oxidoreductase;
1-208 1.63e-06

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 48.00  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKsLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDPSKAEELSNLKDSRLHILPLDIdCDesISKLYAEVEKLVGED 80
Cdd:PRK07024   1 MPLK-VFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARVSVYAADV-RD--ADALAAAAADFIAAH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLT-VLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLpllkkAAAKNGGdgysinRAAIVNISSTAAsVEK 159
Cdd:PRK07024  77 GLPdVVIANAGISVGTLTEEREDLAVFREVMDTNYFGMVATFQPFI-----APMRAAR------RGTLVGIASVAG-VRG 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17559964  160 IDGTfnGplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK07024 145 LPGA--G---AYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPM 188
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
4-232 2.15e-06

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 47.41  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFlkHKD-IQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESiSKLYAEVEKLVGEDG- 81
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRL--VEDgFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDR-DQVFAAVRQVVDTFGd 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGIllpydvegekNRKTLIrqlETnsvstalITQEflpLLKKAAAKN-GGDGYSINRA-----------AIVN 149
Cdd:PRK08643  80 LNVVVNNAGV----------APTTPI---ET-------ITEE---QFDKVYNINvGGVIWGIQAAqeafkklghggKIIN 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  150 ISSTAASVEkidgtfNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMG-------GANAMLEIEDATK 222
Cdd:PRK08643 137 ATSQAGVVG------NPELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMfdiahqvGENAGKPDEWGME 210

                        250
                 ....*....|
gi 17559964  223 TLSDNIlTLG 232
Cdd:PRK08643 211 QFAKDI-TLG 219
PRK07023 PRK07023
SDR family oxidoreductase;
7-208 3.06e-06

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 46.93  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIGLGLLKQFLKhKDIQII-IATCRDPskaeELSNLKDSRLHILPLDI-DCDESISKLYAEVEKLVGEDGLTV 84
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLLQ-PGIAVLgVARSRHP----SLAAAAGERLAEVELDLsDAAAAAAWLAGDLLAAFVDGASRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   85 LL-NNAGILLPYDVEGEKNRKTLIRQLETNsVSTalitqeflPLLKKAAAKNGGDGYSINRaaIVNISSTAA-------S 156
Cdd:PRK07023  80 LLiNNAGTVEPIGPLATLDAAAIARAVGLN-VAA--------PLMLTAALAQAASDAAERR--ILHISSGAArnayagwS 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17559964  157 VekidgtfngplvaYRMSKSALNSFAKSCSIDlAKYHILVTSFCPGWVKTGM 208
Cdd:PRK07023 149 V-------------YCATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGM 186
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 2-208 3.17e-06

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 47.04  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    2 SPKSLLITGANRGIGLGLLKQfLKHKDIQIIIATCRDPSKAEELS---NLKDSRLHILPLDIDCDESISKLYAEVEKLVG 78
Cdd:PRK12937   4 SNKVAIVTGASRGIGAAIARR-LAADGFAVAVNYAGSAAAADELVaeiEAAGGRAIAVQADVADAAAVTRLFDAAETAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   79 edGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTalitqeFLPLlkKAAAKNGGDGysinrAAIVNISStaaSVE 158
Cdd:PRK12937  83 --RIDVLVNNAGVMPLGTIA-DFDLEDFDRTIATNLRGA------FVVL--REAARHLGQG-----GRIINLST---SVI 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17559964  159 KIDGTFNGPlvaYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK12937 144 ALPLPGYGP---YAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
PRK05717 PRK05717
SDR family oxidoreductase;
7-206 3.67e-06

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 46.81  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIGLGlLKQFLKHKDIQIIIATCRDPSKAEELSNLKDSRLHIlPLDIDCDESISKLYAEVEKLVGEdgLTVLL 86
Cdd:PRK05717  14 LVTGAARGIGLG-IAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFI-AMDVADEAQVAAGVAEVLGQFGR--LDALV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   87 NNAGILLPYDVEGEK-NRKTLIRQLETNSVSTALITQEFLPLLKkaaAKNGgdgysinraAIVNISSTAASVEKIDGTfn 165
Cdd:PRK05717  90 CNAAIADPHNTTLESlSLAHWNRVLAVNLTGPMLLAKHCAPYLR---AHNG---------AIVNLASTRARQSEPDTE-- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17559964  166 gplvAYRMSKSALNSFAKSCSIDLAKyHILVTSFCPGWVKT 206
Cdd:PRK05717 156 ----AYAASKGGLLALTHALAISLGP-EIRVNAVSPGWIDA 191
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 4-224 3.68e-06

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 46.72  E-value: 3.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLK--HKdiqiIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEDg 81
Cdd:cd08951   8 KRIFITGSSDGLGLAAARTLLHqgHE----VVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNAIGRFD- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  82 ltVLLNNAGILLpydvegEKNRKTLI----RQLETNSVS----TALITQEFLPLLKKAAAKNGGDgysinraaivnisst 153
Cdd:cd08951  83 --AVIHNAGILS------GPNRKTPDtgipAMVAVNVLApyvlTALIRRPKRLIYLSSGMHRGGN--------------- 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559964 154 aASVEKID--GTFNGPLVAYRMSKSALNSFAKSCSIDLAKyhILVTSFCPGWVKTGMGGANAMLEIEDATKTL 224
Cdd:cd08951 140 -ASLDDIDwfNRGENDSPAYSDSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPTKMGGAGAPDDLEQGHLTQ 209
PRK12746 PRK12746
SDR family oxidoreductase;
4-206 3.94e-06

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 46.57  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIqIIIATCRDPSKAEELSNLKDS---RLHILPLDIDCDESISKLYA----EVEKL 76
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGAL-VAIHYGRNKQAADETIREIESnggKAFLIEADLNSIDGVKKLVEqlknELQIR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   77 VGEDGLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaknggdgysinRAAIVNISSTAAS 156
Cdd:PRK12746  86 VGTSEIDILVNNAGIGTQGTIE-NTTEEIFDEIMAVNIKAPFFLIQQTLPLLRA-------------EGRVINISSAEVR 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17559964  157 VekidgTFNGPlVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK12746 152 L-----GFTGS-IAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKT 195
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 4-90 7.45e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 45.81  E-value: 7.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLK---HkdiqiIIATCRDPSK----AEELSNLKDSRLHILPLDIDCDESISKLYAEVekl 76
Cdd:PRK06125   8 KRVLITGASKGIGAAAAEAFAAegcH-----LHLVARDADAlealAADLRAAHGVDVAVHALDLSSPEAREQLAAEA--- 79

                         90
                 ....*....|....
gi 17559964   77 vgeDGLTVLLNNAG 90
Cdd:PRK06125  80 ---GDIDILVNNAG 90
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 1-210 8.93e-06

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 45.68  E-value: 8.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKqfLKHKDIQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGed 80
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIAR--LLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLE-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLTVLLNNAGIllpydvegeKNRKTLIRQ--------LETNSVSTALITQEFL-PLLKKAAAKnggdgysinraaIVNIS 151
Cdd:PRK12936  80 GVDILVNNAGI---------TKDGLFVRMsdedwdsvLEVNLTATFRLTRELThPMMRRRYGR------------IINIT 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964  152 STAASvekidgTFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGG 210
Cdd:PRK12936 139 SVVGV------TGNPGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTG 191
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-207 9.24e-06

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 45.45  E-value: 9.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    3 PKSLLITGANRGIGLG------LLKQ----FLKH--KDIQIIIATCRDPSK---AEELSNlKDSRLHILPLDIDCDESIS 67
Cdd:PRK12748   5 KKIALVTGASRLNGIGaavcrrLAAKgidiFFTYwsPYDKTMPWGMHDKEPvllKEEIES-YGVRCEHMEIDLSQPYAPN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   68 KLYAEVEKLVGEdgLTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFlpllkkAAAKNGGDGYSInraai 147
Cdd:PRK12748  84 RVFYAVSERLGD--PSILINNAAYSTHTRLE-ELTAEQLDKHYAVNVRATMLLSSAF------AKQYDGKAGGRI----- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559964  148 VNISStaasvekidGTFNGPL---VAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTG 207
Cdd:PRK12748 150 INLTS---------GQSLGPMpdeLAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTG 203
PRK09186 PRK09186
flagellin modification protein A; Provisional
 4-205 1.04e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 45.37  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIQII--IATCRDPSKAEEL-SNLKDSRLHILPLDIDCDESISKLYAEVEKLVGEd 80
Cdd:PRK09186   5 KTILITGAGGLIGSALVKAILEAGGIVIAadIDKEALNELLESLgKEFKSKKLSLVELDITDQESLEEFLSKSAEKYGK- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 gLTVLLNNA-------GILLpYDVEGEKNRKTLIRQLEtnsvSTALITQEFLPLLKkaaaKNGGdgysinrAAIVNISS- 152
Cdd:PRK09186  84 -IDGAVNCAyprnkdyGKKF-FDVSLDDFNENLSLHLG----SSFLFSQQFAKYFK----KQGG-------GNLVNISSi 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  153 ---TAASVEKIDGTFNGPLVAYRMSKSALNSFAKScsidLAKY----HILVTSFCPGWVK 205
Cdd:PRK09186 147 ygvVAPKFEIYEGTSMTSPVEYAAIKAGIIHLTKY----LAKYfkdsNIRVNCVSPGGIL 202
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 4-206 1.24e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 45.11  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFlKHKDIQIIIATCRDPS---KAEELSNLkdsrlhILPLDIDCDESISKLYAEVEKLVGed 80
Cdd:PRK06057   8 RVAVITGGGSGIGLATARRL-AAEGATVVVGDIDPEAgkaAADEVGGL------FVPTDVTDEDAVNALFDTAAETYG-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 GLTVLLNNAGILLPYD--VEgEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaakngGDGYSINRAAIVNISSTAASve 158
Cdd:PRK06057  79 SVDIAFNNAGISPPEDdsIL-NTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQ-----GKGSIINTASFVAVMGSATS-- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17559964  159 kidgtfngpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK06057 151 ---------QISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNT 189
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 2-202 1.83e-05

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 44.54  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    2 SPKSLLITGANRGIGLGLLKQFLKHKdiQIIIATCRdpSKAEELSNLKDSRLHILPLDIDCDESISKLYAEVEKLVgeDG 81
Cdd:PRK06483   1 MPAPILITGAGQRIGLALAWHLLAQG--QPVIVSYR--THYPAIDGLRQAGAQCIQADFSTNAGIMAFIDELKQHT--DG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   82 LTVLLNNAGILLPyDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKkaaaknggdGYSINRAAIVNIssTAASVEKid 161
Cdd:PRK06483  75 LRAIIHNASDWLA-EKPGAPLADVLARMMQIHVNAPYLLNLALEDLLR---------GHGHAASDIIHI--TDYVVEK-- 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17559964  162 GTFNGplVAYRMSKSALNSFAKSCSidlAKY--HILVTSFCPG 202
Cdd:PRK06483 141 GSDKH--IAYAASKAALDNMTLSFA---AKLapEVKVNSIAPA 178
PRK08278 PRK08278
SDR family oxidoreductase;
4-201 2.43e-05

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 44.51  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDP---------SKAEELSNLKDSRLHILpLDIDCDESISklyAEVE 74
Cdd:PRK08278   7 KTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPhpklpgtihTAAEEIEAAGGQALPLV-GDVRDEDQVA---AAVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   75 KLVGE-DGLTVLLNNAG-ILLPYDVEGEKNRKTLIRQLetNSVSTALITQEFLPLLKKAAAknggdgysinrAAIVNISS 152
Cdd:PRK08278  83 KAVERfGGIDICVNNASaINLTGTEDTPMKRFDLMQQI--NVRGTFLVSQACLPHLKKSEN-----------PHILTLSP 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17559964  153 TAasveKIDGTFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCP 201
Cdd:PRK08278 150 PL----NLDPKWFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 4-206 3.14e-05

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 44.12  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQfLKHKDIQIIIATCRDP---SKAEELSNLKDSRLHiLPLDIDCDESISKLYAEVEKLVGEd 80
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALE-LARAGAAVAIADLNQDganAVADEINKAGGKAIG-VAMDVTNEDAVNAGIDKVAERFGS- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 gLTVLLNNAGILLPYDVEGEKNRKTliRQLETNSVSTA-LITQEFLPLLKKAaaKNGGdgysinraAIVNIsstaASVEK 159
Cdd:PRK13394  85 -VDILVSNAGIQIVNPIENYSFADW--KKMQAIHVDGAfLTTKAALKHMYKD--DRGG--------VVIYM----GSVHS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17559964  160 IDGTfngPL-VAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK13394 148 HEAS---PLkSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 4-208 3.87e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 43.81  E-value: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLgLLKQFLKHKDIQIIIaTCRDPSK----AEELSNlkDSRLHILPLDIDCDESISKLYAEVEKLVGe 79
Cdd:PRK05872  10 KVVVVTGAARGIGA-ELARRLHARGAKLAL-VDLEEAElaalAAELGG--DDRVLTVVADVTDLAAMQAAAEEAVERFG- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   80 dGLTVLLNNAGI-----LLPYDVEgeknrkTLIRQLETNSVSTALITQEFLPLLKKAAaknggdGYsinraaIVNISSTA 154
Cdd:PRK05872  85 -GIDVVVANAGIasggsVAQVDPD------AFRRVIDVNLLGVFHTVRATLPALIERR------GY------VLQVSSLA 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17559964  155 AsvekidgTFNGP-LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:PRK05872 146 A-------FAAAPgMAAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDL 193
PLN00015 PLN00015
protochlorophyllide reductase
 7-98 4.75e-05

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 43.54  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIGLGLLKQFLKHKDIQIIIAtCRDPSKAEELSN---LKDSRLHILPLDIDCDESISKLYAEVEKLvgEDGLT 83
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKWHVVMA-CRDFLKAERAAKsagMPKDSYTVMHLDLASLDSVRQFVDNFRRS--GRPLD 77

                         90
                 ....*....|....*
gi 17559964   84 VLLNNAGILLPYDVE 98
Cdd:PLN00015  78 VLVCNAAVYLPTAKE 92
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 84-202 5.86e-05

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: 43.38  E-value: 5.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    84 VLLNNAGILLPY------DVEGEKNRKTLIRQLE----TNSVSTALITQEFLPLLKKAAAKNGGDGYSInraaiVNIsst 153
Cdd:TIGR02685  87 VLVNNASAFYPTpllrgdAGEGVGDKKSLEVQVAelfgSNAIAPYFLIKAFAQRQAGTRAEQRSTNLSI-----VNL--- 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17559964   154 aasvekIDGTFNGPLVA---YRMSKSALNSFAKSCSIDLAKYHILVTSFCPG 202
Cdd:TIGR02685 159 ------CDAMTDQPLLGftmYTMAKHALEGLTRSAALELAPLQIRVNGVAPG 204
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 4-206 6.56e-05

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: 42.90  E-value: 6.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKdiQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDEsisklYAEVEKL----VGE 79
Cdd:cd08937   5 KVVVVTGAAQGIGRGVAERLAGEG--ARVLLVDRSELVHEVLAEILAAGDAAHVHTADLET-----YAGAQGVvraaVER 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  80 DG-LTVLLNNAG---ILLPYDVEGEKNRKTLIRQletnSVSTALIT-QEFLPLLkkAAAKNGgdgysinraAIVNISSTA 154
Cdd:cd08937  78 FGrVDVLINNVGgtiWAKPYEHYEEEQIEAEIRR----SLFPTLWCcRAVLPHM--LERQQG---------VIVNVSSIA 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17559964 155 asvekidgTFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd08937 143 --------TRGIYRIPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEA 186
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 4-98 8.81e-05

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 42.89  E-value: 8.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIAtCRDPSKAEELSN---LKDSRLHILPLDIDCDESISKLYAEVEKLVGEd 80
Cdd:cd09810   2 GTVVITGASSGLGLAAAKALARRGEWHVVMA-CRDFLKAEQAAQevgMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRP- 79

                        90
                ....*....|....*...
gi 17559964  81 gLTVLLNNAGILLPYDVE 98
Cdd:cd09810  80 -LDALVCNAAVYLPTAKE 96
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 4-201 9.32e-05

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 42.43  E-value: 9.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRDP---------SKAEElsnLKDSRLHILPL--DI-DCDESISKLYA 71
Cdd:cd09762   4 KTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPhpklpgtiyTAAEE---IEAAGGKALPCivDIrDEDQVRAAVEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  72 EVEKLVGEDgltVLLNNA-GILLPYDVEGEKNRKTLIRQLetNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNI 150
Cdd:cd09762  81 AVEKFGGID---ILVNNAsAISLTGTLDTPMKRYDLMMGV--NTRGTYLCSKACLPYLKKS-----------KNPHILNL 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17559964 151 SStAASVEKIdgtFNGPLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCP 201
Cdd:cd09762 145 SP-PLNLNPK---WFKNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK05855 PRK05855
SDR family oxidoreductase;
147-207 1.20e-04

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 42.66  E-value: 1.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559964  147 IVNISSTAASvekidgtfnGP---LVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTG 207
Cdd:PRK05855 447 IVNVASAAAY---------APsrsLPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTN 501
PRK07856 PRK07856
SDR family oxidoreductase;
4-206 1.39e-04

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 41.84  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHkDIQIIIATCRDPSKAEelsnlkDSRLHILPLDIDCDESISKLYAEVEKLVGedGLT 83
Cdd:PRK07856   7 RVVLVTGGTRGIGAGIARAFLAA-GATVVVCGRRAPETVD------GRPAEFHAADVRDPDQVAALVDAIVERHG--RLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGiLLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAAknGGdgysinraAIVNISSTAASvEKIDGT 163
Cdd:PRK07856  78 VLVNNAG-GSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPG--GG--------SIVNIGSVSGR-RPSPGT 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17559964  164 fngplVAYRMSKSALNSFAKSCSIDLAKyHILVTSFCPGWVKT 206
Cdd:PRK07856 146 -----AAYGAAKAGLLNLTRSLAVEWAP-KVRVNAVVVGLVRT 182
PRK06101 PRK06101
SDR family oxidoreductase;
5-212 1.76e-04

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 41.78  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    5 SLLITGANRGIGLGLLKQFLKhKDIQIIiATCRDPSKAEELSNlKDSRLHILPLDI-DCDESISKLyaEVEKLVGEdglt 83
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAK-QGWQVI-ACGRNQSVLDELHT-QSANIFTLAFDVtDHPGTKAAL--SQLPFIPE---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   84 VLLNNAGILlPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAaaknggdgysiNRAAIVNISSTAASVEKIDgt 163
Cdd:PRK06101  74 LWIFNAGDC-EYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCG-----------HRVVIVGSIASELALPRAE-- 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17559964  164 fngplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGAN 212
Cdd:PRK06101 140 ------AYGASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKN 182
PRK07814 PRK07814
SDR family oxidoreductase;
7-206 1.82e-04

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 41.69  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    7 LITGANRGIGLGLLKQFLKH-KDIQIIIATCRDPSKAEELSNLKDSRLHILPLDIDCDESISKLyaeVEKLVGEDG-LTV 84
Cdd:PRK07814  14 VVTGAGRGLGAAIALAFAEAgADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGL---AGQAVEAFGrLDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   85 LLNNAGILLPYDVEGEKNrKTLIRQLETNSVSTALITQEFLPLLKKAAaknGGdgysinrAAIVNISSTAasvekidGTF 164
Cdd:PRK07814  91 VVNNVGGTMPNPLLSTST-KDLADAFTFNVATAHALTVAAVPLMLEHS---GG-------GSVINISSTM-------GRL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17559964  165 NGP-LVAYRMSKSALNSFAKSCSIDLAKyHILVTSFCPGWVKT 206
Cdd:PRK07814 153 AGRgFAAYGTAKAALAHYTRLAALDLCP-RIRVNAIAPGSILT 194
PRK07035 PRK07035
SDR family oxidoreductase;
4-211 2.07e-04

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 41.54  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLG---LLKQFLKHkdiqiIIATCRdpsKAEELSNLKDS------RLHILPLDIDCDESISKLYAEVE 74
Cdd:PRK07035   9 KIALVTGASRGIGEAiakLLAQQGAH-----VIVSSR---KLDGCQAVADAivaaggKAEALACHIGEMEQIDALFAHIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   75 KLVGEdgLTVLLNNAGIlLPY-----DVEGEKNRKTlirqLETNSVSTALITQEFLPLLKkaaaKNGGdgysinrAAIVN 149
Cdd:PRK07035  81 ERHGR--LDILVNNAAA-NPYfghilDTDLGAFQKT----VDVNIRGYFFMSVEAGKLMK----EQGG-------GSIVN 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559964  150 ISSTAASvekIDGTFNGplvAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGMGGA 211
Cdd:PRK07035 143 VASVNGV---SPGDFQG---IYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASA 198
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 4-95 2.11e-04

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 41.81  E-value: 2.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   4 KSLLITGANRGIGLGLLKQFLKHkDIQIIIAtCRDPSKAEE-----LSNLKDSRLHILPLDIDCDESISKLYAEVEKLVG 78
Cdd:cd09809   2 KVIIITGANSGIGFETARSFALH-GAHVILA-CRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNS 79

                        90
                ....*....|....*...
gi 17559964  79 EdgLTVLLNNAGIL-LPY 95
Cdd:cd09809  80 P--LHVLVCNAAVFaLPW 95
PRK09134 PRK09134
SDR family oxidoreductase;
2-178 2.81e-04

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 41.07  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    2 SPKSLLITGANRGIGLGLLKQFLKHK-DIQIIIATCRDpsKAEELS---NLKDSRLHILPLDIDCDESISKLYAEVEKLV 77
Cdd:PRK09134   8 APRAALVTGAARRIGRAIALDLAAHGfDVAVHYNRSRD--EAEALAaeiRALGRRAVALQADLADEAEVRALVARASAAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   78 GEdgLTVLLNNAGILLpYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKAAaknggdgysinRAAIVNIsstaasv 157
Cdd:PRK09134  86 GP--ITLLVNNASLFE-YDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADA-----------RGLVVNM------- 144

                        170       180
                 ....*....|....*....|....
gi 17559964  158 ekIDGTFNGP---LVAYRMSKSAL 178
Cdd:PRK09134 145 --IDQRVWNLnpdFLSYTLSKAAL 166
PRK09135 PRK09135
pteridine reductase; Provisional
 1-202 5.11e-04

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 40.30  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    1 MSPKSLLITGANRGIGLGLLKQFlkHKDIQIIIATCRDpSKAE------ELSNLKDSRLHILPLDIDCDESISKLYAEVE 74
Cdd:PRK09135   4 DSAKVALITGGARRIGAAIARTL--HAAGYRVAIHYHR-SAAEadalaaELNALRPGSAAALQADLLDPDALPELVAACV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   75 KLVGedGLTVLLNNAGILLPYDVeGEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaknggdgysiNRAAIVNISSTA 154
Cdd:PRK09135  81 AAFG--RLDALVNNASSFYPTPL-GSITEAQWDDLFASNLKAPFFLSQAAAPQLRK------------QRGAIVNITDIH 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17559964  155 AsvEKidgtfngPL---VAYRMSKSALNSFAKSCSIDLAKyHILVTSFCPG 202
Cdd:PRK09135 146 A--ER-------PLkgyPVYCAAKAALEMLTRSLALELAP-EVRVNAVAPG 186
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 1-208 7.22e-04

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: 39.81  E-value: 7.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQFLKHKDIQIIIATCRD---PSKAEELSNLKDSRLHILPLDIdCDESISKLY--AEVEK 75
Cdd:cd05330   1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEgleAAKAALLEIAPDAEVLLIKADV-SDEAQVEAYvdATVEQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  76 LVGEDGltvLLNNAGIllpydvEGEKN------RKTLIRQLETNSVSTALITQEFLPLLKKAaakngGDGysinraAIVN 149
Cdd:cd05330  80 FGRIDG---FFNNAGI------EGKQNltedfgADEFDKVVSINLRGVFYGLEKVLKVMREQ-----GSG------MIVN 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559964 150 IsstaASVEKIDGTFNGplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKTGM 208
Cdd:cd05330 140 T----ASVGGIRGVGNQ--SGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPM 192
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 4-206 1.89e-03

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 38.55  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964    4 KSLLITGANRGIGLGLLKQFLKHKdIQIIIATCRDPSKAEE-LSNLKDS--RLHILPLDIDCDESISKLyaeVEKLVGED 80
Cdd:PRK08936   8 KVVVITGGSTGLGRAMAVRFGKEK-AKVVINYRSDEEEANDvAEEIKKAggEAIAVKGDVTVESDVVNL---IQTAVKEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   81 G-LTVLLNNAGILLPYDVEgEKNRKTLIRQLETNSVSTALITQEFLpllkKAAAKNGGDGysinraAIVNISSTAasvEK 159
Cdd:PRK08936  84 GtLDVMINNAGIENAVPSH-EMSLEDWNKVINTNLTGAFLGSREAI----KYFVEHDIKG------NIINMSSVH---EQ 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17559964  160 ID-GTFngplVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:PRK08936 150 IPwPLF----VHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
45-219 3.53e-03

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 37.79  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   45 LSNLKDSRLHILPLDIDCDESISKLYAEVEKLVGE-DGLTVLLNNAGIllpYDVEGE---KNRKTLIRQLETNSVSTALI 120
Cdd:PRK08594  53 ADTLEGQESLLLPCDVTSDEEITACFETIKEEVGViHGVAHCIAFANK---EDLRGEfleTSRDGFLLAQNISAYSLTAV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  121 TQEFLPLLKkaaaknggDGYSInraaivnISSTAASVEKIDGTFNGPLVAyrmsKSALNSFAKSCSIDLAKYHILVTSFC 200
Cdd:PRK08594 130 AREAKKLMT--------EGGSI-------VTLTYLGGERVVQNYNVMGVA----KASLEASVKYLANDLGKDGIRVNAIS 190

                        170       180
                 ....*....|....*....|....
gi 17559964  201 PGWVKT----GMGGANAML-EIED 219
Cdd:PRK08594 191 AGPIRTlsakGVGGFNSILkEIEE 214
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 1-206 3.78e-03

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: 37.91  E-value: 3.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964   1 MSPKSLLITGANRGIGLGLLKQfLKHKDIQIIIATCRDPSKAEELSNLKDSRLHILPL--DIDCDESISKLYAEVEKLVG 78
Cdd:cd08936   8 LANKVALVTASTDGIGLAIARR-LAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTvcHVGKAEDRERLVATAVNLHG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559964  79 edGLTVLLNNAGILLPYDVEGEKNRKTLIRQLETNSVSTALITQEFLPLLKKaaaKNGGdgysinraAIVNISSTAASVe 158
Cdd:cd08936  87 --GVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEK---RGGG--------SVVIVSSVAAFH- 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17559964 159 kidgTFNGpLVAYRMSKSALNSFAKSCSIDLAKYHILVTSFCPGWVKT 206
Cdd:cd08936 153 ----PFPG-LGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKT 195
 
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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