NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17558990|ref|NP_505922|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 6-250 7.29e-72

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: 219.47  E-value: 7.29e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVKDKNiRHIIATARDVEKATDLKAI--SDPRVTALQLEVTCDksMDTFVSKVEEIVGSDGLN 83
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGN-NTVIATCRDPSAATELAALgaSHSRLHILELDVTDE--IAESAEAVAERLGDAGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLikasskvsgdqLSASRAAVVTISSGLASMTDFATG 163
Cdd:cd05325  78 VLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLL-----------LKGARAKIINISSRVGSIGDNTSG 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 164 GHapnaFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKA----LLTVEQSTAELVASFNKLNNSHNGG 239
Cdd:cd05325 147 GW----YSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAknkgPITPEESVAGLLKVIDNLNEEDSGK 222

                       250
                ....*....|.
gi 17558990 240 FFQKDLTPYPF 250
Cdd:cd05325 223 FLDYDGTEIPW 233
 
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 ...
 6-250 7.29e-72

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: 219.47  E-value: 7.29e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVKDKNiRHIIATARDVEKATDLKAI--SDPRVTALQLEVTCDksMDTFVSKVEEIVGSDGLN 83
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGN-NTVIATCRDPSAATELAALgaSHSRLHILELDVTDE--IAESAEAVAERLGDAGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLikasskvsgdqLSASRAAVVTISSGLASMTDFATG 163
Cdd:cd05325  78 VLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLL-----------LKGARAKIINISSRVGSIGDNTSG 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 164 GHapnaFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKA----LLTVEQSTAELVASFNKLNNSHNGG 239
Cdd:cd05325 147 GW----YSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAknkgPITPEESVAGLLKVIDNLNEEDSGK 222

                       250
                ....*....|.
gi 17558990 240 FFQKDLTPYPF 250
Cdd:cd05325 223 FLDYDGTEIPW 233
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-227 2.34e-37

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 131.53  E-value: 2.34e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKA---ISDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARG--ARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  78 GsdGLNLLVNNAGNAVDYPCKAKPnRALFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTISSGLASM 157
Cdd:COG0300  81 G--PIDVLVNNAGVGGGGPFEELD-LEDLRRVFEVNVFGPVRLTRALLPLMRARG-----------RGRIVNVSSVAGLR 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990 158 TdfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGG------EKALLTVEQSTAELVA 227
Cdd:COG0300 147 G-------LPGMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTAragapaGRPLLSPEEVARAILR 215
PRK08177 PRK08177
SDR family oxidoreductase;
3-230 7.17e-33

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 118.98  E-value: 7.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    3 PKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAIsdPRVTALQLEVTCDKSMDTFVSKVEEIVgsdgL 82
Cdd:PRK08177   1 KRTALIIGASRGLGLGLVDRLLERG--WQVTATVRGPQQDTALQAL--PGVHIEKLDMNDPASLDQLLQRLQGQR----F 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   83 NLLVNNAGnaVDYPCKAKPNRALFAE--QL-NVNTTSVVILTQKLMPllikasskvsgdQLSASRAAVVTISSGLASMTd 159
Cdd:PRK08177  73 DLLFVNAG--ISGPAHQSAADATAAEigQLfLTNAIAPIRLARRLLG------------QVRPGQGVLAFMSSQLGSVE- 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558990  160 FATGGHAPnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKALLTVEQSTAELVASFN 230
Cdd:PRK08177 138 LPDGGEMP---LYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMGGDNAPLDVETSVKGLVEQIE 205
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 4-213 5.53e-30

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 110.78  E-value: 5.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990     4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEK----ATDLKAISDpRVTALQLEVTCDKSMDTFVSKVEEIVGs 79
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGA--KVVLVDRSEEKleavAKELGALGG-KALFIQGDVTDRAQVKALVEQAVERLG- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    80 dGLNLLVNNAGNAVDYPcKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSglasmtd 159
Cdd:pfam00106  77 -RLDILVNNAGITGLGP-FSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSG-----------GRIVNISS------- 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990   160 faTGGHAPNAF--AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEK 213
Cdd:pfam00106 137 --VAGLVPYPGgsAYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKEL 190
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 7-235 2.07e-12

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: 64.93  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990     7 VITGANRGIGLGLVQEFVKDKNIRHIIAT--ARDVEKATDLKA-----ISDPRVTALQLEVTCDKSMDTFVSKVEEIVGS 79
Cdd:TIGR01500   4 LVTGASRGFGRTIAQELAKCLKSPGSVLVlsARNDEALRQLKAeigaeRSGLRVVRVSLDLGAEAGLEQLLKALRELPRP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    80 DGLN--LLVNNAGNAVDYPCKAKPnralFAEQLNV------NTTSVVILTQKLMPLLikasskvsgDQLSASRAAVVTIS 151
Cdd:TIGR01500  84 KGLQrlLLINNAGTLGDVSKGFVD----LSDSTQVqnywalNLTSMLCLTSSVLKAF---------KDSPGLNRTVVNIS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   152 SgLASMTDFATGGHapnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMggeKALLTVEQSTAELVASFNK 231
Cdd:TIGR01500 151 S-LCAIQPFKGWAL------YCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDM---QQQVREESVDPDMRKGLQE 220


                  ....
gi 17558990   232 LNNS 235
Cdd:TIGR01500 221 LKAK 224
 
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 ...
 6-250 7.29e-72

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: 219.47  E-value: 7.29e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVKDKNiRHIIATARDVEKATDLKAI--SDPRVTALQLEVTCDksMDTFVSKVEEIVGSDGLN 83
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGN-NTVIATCRDPSAATELAALgaSHSRLHILELDVTDE--IAESAEAVAERLGDAGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLikasskvsgdqLSASRAAVVTISSGLASMTDFATG 163
Cdd:cd05325  78 VLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLL-----------LKGARAKIINISSRVGSIGDNTSG 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 164 GHapnaFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKA----LLTVEQSTAELVASFNKLNNSHNGG 239
Cdd:cd05325 147 GW----YSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAknkgPITPEESVAGLLKVIDNLNEEDSGK 222

                       250
                ....*....|.
gi 17558990 240 FFQKDLTPYPF 250
Cdd:cd05325 223 FLDYDGTEIPW 233
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 4-250 2.02e-48

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: 159.32  E-value: 2.02e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNIrHIIATARDVEKAtdLKAIS-------DPRVtaLQLEVTCDKSMDTFVSKVEEI 76
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPG-TVILTARDVERG--QAAVEklraeglSVRF--HQLDVTDDASIEAAADFVEEK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  77 VGsdGLNLLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLAS 156
Cdd:cd05324  76 YG--GLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPA-----------GRIVNVSSGLGS 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 157 MTDfatgghapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKALLTVEQStAELVA--SFNKLNN 234
Cdd:cd05324 143 LTS-----------AYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAPKTPEEG-AETPVylALLPPDG 210

                       250
                ....*....|....*.
gi 17558990 235 SHNGGFFQKDlTPYPF 250
Cdd:cd05324 211 EPTGKFFSDK-KVVPW 225
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-227 2.34e-37

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 131.53  E-value: 2.34e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKA---ISDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARG--ARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  78 GsdGLNLLVNNAGNAVDYPCKAKPnRALFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTISSGLASM 157
Cdd:COG0300  81 G--PIDVLVNNAGVGGGGPFEELD-LEDLRRVFEVNVFGPVRLTRALLPLMRARG-----------RGRIVNVSSVAGLR 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990 158 TdfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGG------EKALLTVEQSTAELVA 227
Cdd:COG0300 147 G-------LPGMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTAragapaGRPLLSPEEVARAILR 215
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-227 2.51e-33

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: 121.05  E-value: 2.51e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKA-ISD--PRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:COG1028   4 LKGKVALVTGGSSGIGRAIARALAAEGA--RVVITDRDAEALEAAAAeLRAagGRALAVAADVTDEAAVEALVAAAVAAF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  78 GsdGLNLLVNNAGNAVDYPCKAKPnRALFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTISSGLASM 157
Cdd:COG1028  82 G--RLDILVNNAGITPPGPLEELT-EEDWDRVLDVNLKGPFLLTRAALPHMRERG-----------GGRIVNISSIAGLR 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 158 TdfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGgeKALLTVEQSTAELVA 227
Cdd:COG1028 148 G-------SPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMT--RALLGAEEVREALAA 208
PRK08177 PRK08177
SDR family oxidoreductase;
3-230 7.17e-33

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 118.98  E-value: 7.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    3 PKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAIsdPRVTALQLEVTCDKSMDTFVSKVEEIVgsdgL 82
Cdd:PRK08177   1 KRTALIIGASRGLGLGLVDRLLERG--WQVTATVRGPQQDTALQAL--PGVHIEKLDMNDPASLDQLLQRLQGQR----F 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   83 NLLVNNAGnaVDYPCKAKPNRALFAE--QL-NVNTTSVVILTQKLMPllikasskvsgdQLSASRAAVVTISSGLASMTd 159
Cdd:PRK08177  73 DLLFVNAG--ISGPAHQSAADATAAEigQLfLTNAIAPIRLARRLLG------------QVRPGQGVLAFMSSQLGSVE- 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558990  160 FATGGHAPnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKALLTVEQSTAELVASFN 230
Cdd:PRK08177 138 LPDGGEMP---LYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMGGDNAPLDVETSVKGLVEQIE 205
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 2-212 1.87e-31

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: 115.66  E-value: 1.87e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   2 SPKSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdG 81
Cdd:COG4221   4 KGKVALITGASSGIGAATARALAAAGA--RVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--R 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  82 LNLLVNNAGNAVdypckAKP----NRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsGDqlsasraaVVTISSglasm 157
Cdd:COG4221  80 LDVLVNNAGVAL-----LGPleelDPEDWDRMIDVNVKGVLYVTRAALPAMRARGS---GH--------IVNISS----- 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990 158 tdfaTGGHAPNAF--AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGE 212
Cdd:COG4221 139 ----IAGLRPYPGgaVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDS 191
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 6-209 2.26e-31

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: 115.46  E-value: 2.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAI--SDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGA--KVVLADRNEEALAELAAIeaLGGNAVAVQADVSDEEDVEALVEEALEEFG--RLD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNRAlFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSglasmtdFATG 163
Cdd:cd05233  77 ILVNNAGIARPGPLEELTDED-WDRVLDVNLTGVFLLTRAALPHMKKQGG-----------GRIVNISS-------VAGL 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17558990 164 GHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd05233 138 RPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPM 183
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 4-213 5.53e-30

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 110.78  E-value: 5.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990     4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEK----ATDLKAISDpRVTALQLEVTCDKSMDTFVSKVEEIVGs 79
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGA--KVVLVDRSEEKleavAKELGALGG-KALFIQGDVTDRAQVKALVEQAVERLG- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    80 dGLNLLVNNAGNAVDYPcKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSglasmtd 159
Cdd:pfam00106  77 -RLDILVNNAGITGLGP-FSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSG-----------GRIVNISS------- 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990   160 faTGGHAPNAF--AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEK 213
Cdd:pfam00106 137 --VAGLVPYPGgsAYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKEL 190
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 1-229 1.69e-27

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: 105.63  E-value: 1.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAiSDPRVTALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGN--TVIITGRREEKLEEAAA-ANPGLHTIVLDVADPASIAALAEQVTAEFP-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 GLNLLVNNAGNAVDYPCKAKPNRALFAEQ-LNVNTTSVVILTQKLMPLLikasskvsgdqLSASRAAVVTISSGLAsmtd 159
Cdd:COG3967  78 DLNVLINNAGIMRAEDLLDEAEDLADAEReITTNLLGPIRLTAAFLPHL-----------KAQPEAAIVNVSSGLA---- 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990 160 fatggHAPNAFA--YRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKAL----LTVEQSTAELVASF 229
Cdd:COG3967 143 -----FVPLAVTptYSATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGdpraMPLDEFADEVMAGL 213
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 4-209 2.25e-26

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: 102.69  E-value: 2.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGY--RVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFG--RID 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNRALFaEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLASMTDFATG 163
Cdd:cd05374  77 VLVNNAGYGLFGPLEETSIEEVR-ELFEVNVFGPLRVTRAFLPLMRKQGS-----------GRIVNVSSVAGLVPTPFLG 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17558990 164 ghapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd05374 145 -------PYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGF 183
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 1-203 2.46e-25

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: 100.25  E-value: 2.46e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKdKNIRHIIaTARDVE----KATDLKAISDprVTALQLEVTCDKSMDTFVSKVEEI 76
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLE-AGARVII-SARKAEacadAAEELSAYGE--CIAIPADLSSEEGIEALVARVAER 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  77 vgSDGLNLLVNNAGNAVDYPCKAKPNRAlFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlSASRAAVVTISS--GL 154
Cdd:cd08942  80 --SDRLDVLVNNAGATWGAPLEAFPESG-WDKVMDINVKSVFFLTQALLPLLRAAAT-------AENPARVINIGSiaGI 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17558990 155 ASMtdfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPG 203
Cdd:cd08942 150 VVS--------GLENYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPG 190
PRK06953 PRK06953
SDR family oxidoreductase;
4-249 8.89e-25

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 97.84  E-value: 8.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAISdprVTALQLEVTCDKSMDTFVSKVeeivgsDG-- 81
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADG--WRVIATARDAAALAALQALG---AEALALDVADPASVAGLAWKL------DGea 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAVDYPCKAKP-NRALFAEQLNVNTTSVVILTQKLMPLLikasskvsgdqlSASRAAVVTISSGLASMTDf 160
Cdd:PRK06953  71 LDAAVYVAGVYGPRTEGVEPiTREDFDAVMHTNVLGPMQLLPILLPLV------------EAAGGVLAVLSSRMGSIGD- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  161 ATGGhapNAFAYRISKAAINMFGRALANDMKddHILVASIGPGWVKTDMGGEKALLTVEQSTAELVASFNKLNNSHNGGF 240
Cdd:PRK06953 138 ATGT---TGWLYRASKAALNDALRAASLQAR--HATCIALHPGWVRTDMGGAQAALDPAQSVAGMRRVIAQATRRDNGRF 212


                 ....*....
gi 17558990  241 FQKDLTPYP 249
Cdd:PRK06953 213 FQYDGVELS 221
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 4-209 2.98e-24

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: 97.68  E-value: 2.98e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKdKNIRHIIATaRDVEKATDLKAI-----SDPRVTALQLEVTCDKSMDTFVSKVEEIVg 78
Cdd:cd05327   2 KVVVITGANSGIGKETARELAK-RGAHVIIAC-RNEEKGEEAAAEikketGNAKVEVIQLDLSSLASVRQFAEEFLARF- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  79 sDGLNLLVNNAGnavDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsaSRaaVVTISSGLASMT 158
Cdd:cd05327  79 -PRLDILINNAG---IMAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAP---------SR--IVNVSSIAHRAG 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990 159 DFAT------GGHAPNAF-AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd05327 144 PIDFndldleNNKEYSPYkAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTEL 201
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 6-235 3.12e-24

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: 96.97  E-value: 3.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVKDKNIRHIIATARDVEKATDLKAISDPRVTALQleVTCDKSMDTFVSKVEEIVGSDG--LN 83
Cdd:cd05367   2 IILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEELRPGLRVTT--VKADLSDAAGVEQLLEAIRKLDgeRD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSKVSgdqlsasraaVVTISSGLASMTDFATG 163
Cdd:cd05367  80 LLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKKT----------VVNVSSGAAVNPFKGWG 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558990 164 ghapnafAYRISKAAINMFGRALANDMKDDHILvaSIGPGWVKTDMgGEKALLTVEQStaELVASFNKLNNS 235
Cdd:cd05367 150 -------LYCSSKAARDMFFRVLAAEEPDVRVL--SYAPGVVDTDM-QREIRETSADP--ETRSRFRSLKEK 209
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 4-211 9.12e-23

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: 93.88  E-value: 9.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFvkDKNIRHIIATA--RDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSDG 81
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKL--DSLGFTVLAGCltKNGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  82 LNLLVNNAG-NAVDYPCKAKPnRALFAEQLNVNTTSVVILTQKLMPLLIKAsskvsgdqlsasRAAVVTISSGLASMTDF 160
Cdd:cd09805  79 LWGLVNNAGiLGFGGDEELLP-MDDYRKCMEVNLFGTVEVTKAFLPLLRRA------------KGRVVNVSSMGGRVPFP 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17558990 161 ATGghapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGG 211
Cdd:cd09805 146 AGG-------AYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITG 189
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 1-214 2.12e-22

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: 92.08  E-value: 2.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKNIRhIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIvgsd 80
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKK-VYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKDV---- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 glNLLVNNAGnaVDYPCKAKPNRALFA--EQLNVNTTSVVILTQKLMPLLIKasskvsgdqlsASRAAVVTISSgLASMT 158
Cdd:cd05354  76 --DVVINNAG--VLKPATLLEEGALEAlkQEMDVNVFGLLRLAQAFAPVLKA-----------NGGGAIVNLNS-VASLK 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 159 DFatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM----GGEKA 214
Cdd:cd05354 140 NF------PAMGTYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMaagaGGPKE 193
PRK08264 PRK08264
SDR family oxidoreductase;
4-227 7.07e-22

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 90.72  E-value: 7.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKdKNIRHIIATARDVEKATDLkaisDPRVTALQLEVTCDKSMDTFVSKVeeivgSDgLN 83
Cdd:PRK08264   7 KVVLVTGANRGIGRAFVEQLLA-RGAAKVYAAARDPESVTDL----GPRVVPLQLDVTDPASVAAAAEAA-----SD-VT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSgLASMTDFATG 163
Cdd:PRK08264  76 ILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGG-----------GAIVNVLS-VLSWVNFPNL 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558990  164 GhapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGgekALLTVEQSTAELVA 227
Cdd:PRK08264 144 G------TYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMA---AGLDAPKASPADVA 198
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 4-209 1.35e-21

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 89.34  E-value: 1.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAiSDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGY--RVSLGLRNPEDLAALSA-SGGDVEAVPYDARDPEDARALVDALRDRFG--RID 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKpNRALFAEQLNVNTTSVVILTQKLMPLLIkasskvsgdqlSASRAAVVTISSGLASMTdfatg 163
Cdd:cd08932  76 VLVHNAGIGRPTTLREG-SDAELEAHFSINVIAPAELTRALLPALR-----------EAGSGRVVFLNSLSGKRV----- 138

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17558990 164 gHAPNAfAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd08932 139 -LAGNA-GYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPM 182
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-210 5.40e-21

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 88.36  E-value: 5.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDkNIRHIIATARDVEKATDL-KAISDPRVTAL--QLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:PRK05565   6 KVAIVTGASGGIGRAIAELLAKE-GAKVVIAYDINEEAAQELlEEIKEEGGDAIavKADVSSEEDVENLVEQIVEKFG-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAGnavdypckaKPNRALFAEQ--------LNVNTTSVVILTQKLMPLLIKASSKVsgdqlsasraaVVTISS 152
Cdd:PRK05565  83 KIDILVNNAG---------ISNFGLVTDMtdeewdrvIDVNLTGVMLLTRYALPYMIKRKSGV-----------IVNISS 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  153 --GLASmtdfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMG 210
Cdd:PRK05565 143 iwGLIG---------ASCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMW 193
PRK08219 PRK08219
SDR family oxidoreductase;
1-209 9.48e-20

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 84.60  E-value: 9.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDkniRHIIATARDVEKATDLkAISDPRVTALQLEVTCDKSMDTFVSKVEEivgsd 80
Cdd:PRK08219   1 MERPTALITGASRGIGAAIARELAPT---HTLLLGGRPAERLDEL-AAELPGATPFPVDLTDPEAIAAAVEQLGR----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 gLNLLVNNAGNAVDYPCkAKPNRALFAEQLNVNTTSVVILTQKLMPllikasskvsgdQLSASRAAVVTISSGlasmtdf 160
Cdd:PRK08219  72 -LDVLVHNAGVADLGPV-AESTVDEWRATLEVNVVAPAELTRLLLP------------ALRAAHGHVVFINSG------- 130

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17558990  161 atGGHAPNA--FAYRISKAAInmfgRALANDMKDD---HILVASIGPGWVKTDM 209
Cdd:PRK08219 131 --AGLRANPgwGSYAASKFAL----RALADALREEepgNVRVTSVHPGRTDTDM 178
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 10-210 3.78e-19

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: 83.25  E-value: 3.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    10 GA--NRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAISDP-RVTALQLEVTCDKSMDTFVSKVEEIVGsdGLNLLV 86
Cdd:pfam13561   1 GAanESGIGWAIARALAEEG--AEVVLTDLNEALAKRVEELAEElGAAVLPCDVTDEEQVEALVAAAVEKFG--RLDILV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    87 NNAGNAVDypcKAKP----NRALFAEQLNVNTTSVVILTQKLMPLLikasskvsgdqlsASRAAVVTISSGLASMTdfat 162
Cdd:pfam13561  77 NNAGFAPK---LKGPfldtSREDFDRALDVNLYSLFLLAKAALPLM-------------KEGGSIVNLSSIGAERV---- 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 17558990   163 gghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMG 210
Cdd:pfam13561 137 ---VPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLAA 181
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 1-211 4.48e-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: 83.23  E-value: 4.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLK------AISDPRVTALQLEVTCDKSMDTFVSKVE 74
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLG--ARLALTGRDAERLEETRqsclqaGVSEKKILLVVADLTEEEGQDRIISTTL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  75 EIVGSdgLNLLVNNAGNAVDYPCKAKpNRALFAEQLNVNTTSVVILTQKLMPLLIKasskvsgdqlsaSRAAVVTISSgl 154
Cdd:cd05364  79 AKFGR--LDILVNNAGILAKGGGEDQ-DIEEYDKVMNLNLRAVIYLTKLAVPHLIK------------TKGEIVNVSS-- 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990 155 asmtdFATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGG 211
Cdd:cd05364 142 -----VAGGRSFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHR 193
PRK09242 PRK09242
SDR family oxidoreductase;
4-207 1.29e-18

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 82.10  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVE----KATDLKAISDPR-VTALQLEVTCDKSMDTFVSKVEEivG 78
Cdd:PRK09242  10 QTALITGASKGIGLAIAREFLGLG--ADVLIVARDADalaqARDELAEEFPEReVHGLAADVSDDEDRRAILDWVED--H 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 SDGLNLLVNNAG-----NAVDYpckakpNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSg 153
Cdd:PRK09242  86 WDGLHILVNNAGgnirkAAIDY------TEDEWRGIFETNLFSAFELSRYAHPLLKQHAS-----------SAIVNIGS- 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17558990  154 LASMTDFATGghAPnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK09242 148 VSGLTHVRSG--AP----YGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRT 195
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-209 1.87e-17

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 78.66  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKA---ISDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGA--KVVIYDSNEEAAEALAAelrAAGGEARVLVFDVSDEAAVRALIEAAVEAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   78 GsdGLNLLVNNAGNAVDypckaKPNRALFAEQ----LNVNTTSVVILTQKLMPLLIKasskvsgdqlsASRAAVVTISS- 152
Cdd:PRK05653  81 G--ALDILVNNAGITRD-----ALLPRMSEEDwdrvIDVNLTGTFNVVRAALPPMIK-----------ARYGRIVNISSv 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990  153 -GLASMtdfatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK05653 143 sGVTGN---------PGQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDM 191
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 4-207 2.31e-17

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: 78.64  E-value: 2.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAISDPR---VTALQLEVTCDKSMDTFVSKVEEIVGSD 80
Cdd:cd05329   7 KTALVTGGTKGIGYAIVEELAGLG--AEVYTCARNQKELDECLTEWREKgfkVEGSVCDVSSRSERQELMDTVASHFGGK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 gLNLLVNNAG-----NAVDYPCKAkpnralFAEQLNVNTTSVVILTQKLMPLLiKASSKvsgdqlsasrAAVVTISSgLA 155
Cdd:cd05329  85 -LNILVNNAGtnirkEAKDYTEED------YSLIMSTNFEAAYHLSRLAHPLL-KASGN----------GNIVFISS-VA 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17558990 156 SMTDFATGghAPnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:cd05329 146 GVIAVPSG--AP----YGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIAT 191
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 6-231 2.75e-17

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: 78.14  E-value: 2.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVKdkNIRHIIATARDVEKATDLKA---ISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGL 82
Cdd:cd05350   1 VLITGASSGIGRALAREFAK--AGYNVALAARRTDRLDELKAellNPNPSVEVEILDVTDEERNQLVIAELEAELG--GL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  83 NLLVNNAGNAVDYPCKA---KPNRALFaeqlNVNTTSVVILTQKLMPLLikasskvsgdqLSASRAAVVTISS--GLASM 157
Cdd:cd05350  77 DLVIINAGVGKGTSLGDlsfKAFRETI----DTNLLGAAAILEAALPQF-----------RAKGRGHLVLISSvaALRGL 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990 158 tdfatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMG----GEKALLTVEQSTAELVASFNK 231
Cdd:cd05350 142 ---------PGAAAYSASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTanmfTMPFLMSVEQAAKRIYKAIKK 210
PRK12826 PRK12826
SDR family oxidoreductase;
1-212 3.80e-17

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 78.03  E-value: 3.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKNirHIIATAR---DVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGA--EVIVVDIcgdDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   78 GsdGLNLLVNNAGNAvdypckakpNRALFAEQ--------LNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVT 149
Cdd:PRK12826  82 G--RLDILVANAGIF---------PLTPFAEMddeqwervIDVNLTGTFLLTQAALPALIRAG-----------GGRIVL 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  150 ISSglasmtdfATGGHAPNAF--AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGE 212
Cdd:PRK12826 140 TSS--------VAGPRVGYPGlaHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGN 196
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 4-209 4.01e-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: 4.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAISDP---RVTALQLEVTCDKSMDTFVSKVEEIVGSd 80
Cdd:cd05347   6 KVALVTGASRGIGFGIASGLAEAGA--NIVINSRNEEKAEEAQQLIEKegvEATAFTCDVSDEEAIKAAVEAIEEDFGK- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 gLNLLVNNAG-----NAVDYPckakpnRALFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTIssglA 155
Cdd:cd05347  83 -IDILVNNAGiirrhPAEEFP------EAEWRDVIDVNLNGVFFVSQAVARHMIKQG-----------HGKIINI----C 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17558990 156 SMTDFATGghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd05347 141 SLLSELGG---PPVPAYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEM 191
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-209 1.42e-16

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 76.54  E-value: 1.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    3 PKSVVITGANRGIGLGLVQEFVKDKNIRHIIATARDVEKATDLKAISD--PRVTALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:PRK12745   2 RPVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQELRAlgVEVIFFPADVADLSAHEAMLDAAQAAWG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAGNAV----DYpCKAKPNRalFAEQLNVNTTSVVILTQKLMPLLIKASskvsGDQLSASRAaVVTISSGLAS 156
Cdd:PRK12745  80 RIDCLVNNAGVGVkvrgDL-LDLTPES--FDRVLAINLRGPFFLTQAVAKRMLAQP----EPEELPHRS-IVFVSSVNAI 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17558990  157 MTdfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK12745 152 MV-------SPNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 6-236 2.26e-16

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: 75.72  E-value: 2.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVKdKNIRhIIATARDVEKATDLKA-ISD---PRVTALQLEVTCDksmDTFVSKVEE-IVGSD 80
Cdd:cd05356   4 AVVTGATDGIGKAYAEELAK-RGFN-VILISRTQEKLDAVAKeIEEkygVETKTIAADFSAG---DDIYERIEKeLEGLD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 gLNLLVNNAGNAVDYPCK-AKPNRALFAEQLNVNTTSVVILTQKLMPLLikasskvsgdqLSASRAAVVTISSGLASMTd 159
Cdd:cd05356  79 -IGILVNNVGISHSIPEYfLETPEDELQDIINVNVMATLKMTRLILPGM-----------VKRKKGAIVNISSFAGLIP- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 160 fatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM--GGEKALLTVeqSTAELVAS-FNKLNNSH 236
Cdd:cd05356 146 ------TPLLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMskIRKSSLFVP--SPEQFVRSaLNTLGLSK 217
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 1-229 4.78e-16

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: 74.65  E-value: 4.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAiSDPRVTALQLEVTCDKSMDTFVSKVeeIVGSD 80
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLEAGN--TVIITGRREERLAEAKK-ELPNIHTIVLDVGDAESVEALAEAL--LSEYP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 GLNLLVNNAGNAVDYPC-KAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTISSGLAsmtd 159
Cdd:cd05370  78 NLDILINNAGIQRPIDLrDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQP-----------EATIVNVSSGLA---- 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990 160 FATGGHAPNafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEK--------ALLTVEQSTAELVASF 229
Cdd:cd05370 143 FVPMAANPV---YCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERrnpdggtpRKMPLDEFVDEVVAGL 217
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 4-204 5.06e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 75.05  E-value: 5.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:PRK08265   7 KVAIVTGGATLIGAAVARALVAAGA--RVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFG--RVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGNAVDYPCKAkpNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasraAVVTISSGLASmtdFATG 163
Cdd:PRK08265  83 ILVNLACTYLDDGLAS--SRADWLAALDVNLVSAAMLAQAAHPHLARGGG------------AIVNFTSISAK---FAQT 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17558990  164 GHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPGW 204
Cdd:PRK08265 146 GRW----LYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGW 182
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-209 9.33e-16

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 74.07  E-value: 9.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDkNIRHIIATARDVEKATDLKA-ISDP--RVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQ-GANVVINYASSEAGAEALVAeIGALggKALAVQGDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   78 GsdGLNLLVNNAGNAVDYPCkAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSgLASM 157
Cdd:PRK05557  82 G--GVDILVNNAGITRDNLL-MRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRS-----------GRIINISS-VVGL 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17558990  158 TDFATGGHapnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK05557 147 MGNPGQAN------YAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDM 192
PRK05693 PRK05693
SDR family oxidoreductase;
4-210 1.37e-15

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 74.06  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFvKDKNiRHIIATARdveKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAF-KAAG-YEVWATAR---KAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHG--GLD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGNAVDYPCKAKPNRALfAEQLNVNTTSVVILTQKLMPLLIKasskvsgdqlsaSRAAVVTISSGLASMTdfatg 163
Cdd:PRK05693  75 VLINNAGYGAMGPLLDGGVEAM-RRQFETNVFAVVGVTRALFPLLRR------------SRGLVVNIGSVSGVLV----- 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17558990  164 ghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMG 210
Cdd:PRK05693 137 --TPFAGAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQFA 181
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 4-209 1.40e-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: 73.49  E-value: 1.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFV-KDKNIrHIIATARDVEKATDLKAI-SDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdG 81
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLkKGAKV-AILDRNENPGAAAELQAInPKVKATFVQCDVTSWEQLAAAFKKAIEKFG--R 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  82 LNLLVNNAG----NAVDYPCKAKPNRALfaeQLNVNTTSVVILTQKLMPLLIKASSKVSGdqlsasraAVVTISSglasm 157
Cdd:cd05323  78 VDILINNAGildeKSYLFAGKLPPPWEK---TIDVNLTGVINTTYLALHYMDKNKGGKGG--------VIVNIGS----- 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17558990 158 tdfaTGGHAPNAFA--YRISKAAINMFGRALANDMKDDH-ILVASIGPGWVKTDM 209
Cdd:cd05323 142 ----VAGLYPAPQFpvYSASKHGVVGFTRSLADLLEYKTgVRVNAICPGFTNTPL 192
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 4-233 2.12e-15

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 73.08  E-value: 2.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKD--KNIRHIIATARDVEKATDLKAiSDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdG 81
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAEAgaTVAFNDGLAAEARELAAALEA-AGGRAHAIAADLADPASVQRFFDAAAAALG--G 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAG-----NAVDYpckakpNRALFAEQLNVNTTSVVILTQKLMPLLIkasskvsgdqlSASRAAVVTISSGLAS 156
Cdd:PRK12939  85 LDGLVNNAGitnskSATEL------DIDTWDAVMNVNVRGTFLMLRAALPHLR-----------DSGRGRIVNLASDTAL 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990  157 MTdfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDmggekalLTVEQSTAELVASFNKLN 233
Cdd:PRK12939 148 WG-------APKLGAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATE-------ATAYVPADERHAYYLKGR 210
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-209 7.38e-15

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 71.74  E-value: 7.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDkNIRHIIATARDVEKATDLKAISdprvtalQLEVTCDKSMDTFVSKVEEIVGSD--G 81
Cdd:PRK06463   8 KVALITGGTRGIGRAIAEAFLRE-GAKVAVLYNSAENEAKELREKG-------VFTIKCDVGNRDQVKKSKEVVEKEfgR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAVDYPC----KAKPNRalfaeQLNVNTTSVVILTQKLMPLLiKASSkvsgdqlsasRAAVVTISSglasm 157
Cdd:PRK06463  80 VDVLVNNAGIMYLMPFeefdEEKYNK-----MIKINLNGAIYTTYEFLPLL-KLSK----------NGAIVNIAS----- 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17558990  158 tDFATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK06463 139 -NAGIGTAAEGTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDM 189
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
3-229 9.77e-15

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 71.34  E-value: 9.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    3 PKSVVITGANRGIGLGLVQEFVKDKniRHIIATAR-DVEKATDL---KAISDPRVTALQLEVTCDKSMDTFVSKVEEIVG 78
Cdd:PRK12824   2 KKIALVTGAKRGIGSAIARELLNDG--YRVIATYFsGNDCAKDWfeeYGFTEDQVRLKELDVTDTEECAEALAEIEEEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 sdGLNLLVNNAGNAVDYPCKAKPNRALFaEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISS--GLAS 156
Cdd:PRK12824  80 --PVDILVNNAGITRDSVFKRMSHQEWN-DVINTNLNSVFNVTQPLFAAMCEQGY-----------GRIINISSvnGLKG 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558990  157 MtdFAtgghAPNafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMggekalltVEQSTAELVASF 229
Cdd:PRK12824 146 Q--FG----QTN---YSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPM--------VEQMGPEVLQSI 201
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
4-212 9.93e-15

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 71.25  E-value: 9.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKdKNIrHIIATAR-DVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSDGL 82
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLE-KGT-HVISISRtENKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQEDNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   83 N--LLVNNAGnAVDyPckAKPNRALFAEQLN----VNTTSVVILTQKLMplliKASSKVSGDQLsasraaVVTISSGLAS 156
Cdd:PRK06924  80 SsiHLINNAG-MVA-P--IKPIEKAESEELItnvhLNLLAPMILTSTFM----KHTKDWKVDKR------VINISSGAAK 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990  157 MTDFATGghapnafAYRISKAAINMFGRALANDMKDDH--ILVASIGPGWVKTDMGGE 212
Cdd:PRK06924 146 NPYFGWS-------AYCSSKAGLDMFTQTVATEQEEEEypVKIVAFSPGVMDTNMQAQ 196
FabG-like PRK07231
SDR family oxidoreductase;
4-228 1.12e-14

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 71.01  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAI--SDPRVTALQLEVTCDKSMDTFVSKVEEIVGSdg 81
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGA--RVVVTDRNEEAAERVAAEilAGGRAIAVAADVSDEADVEAAVAAALERFGS-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTISSglasmtdfa 161
Cdd:PRK07231  82 VDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEG-----------GGAIVNVAS--------- 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558990  162 TGGHAPNAF--AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKALLTVEQSTAELVAS 228
Cdd:PRK07231 142 TAGLRPRPGlgWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTPENRAKFLAT 210
PRK07326 PRK07326
SDR family oxidoreductase;
4-212 1.60e-14

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 70.42  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKdKNIRHIIaTARDVEKATDLKAI--SDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdG 81
Cdd:PRK07326   7 KVALITGGSKGIGFAIAEALLA-EGYKVAI-TARDQKELEEAAAElnNKGNVLGLAADVRDEADVQRAVDAIVAAFG--G 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAVdypckAKPNRALFAEQ----LNVNTTSVVIltqklmpllikaSSKVSGDQLSASRAAVVTISSgLASm 157
Cdd:PRK07326  83 LDVLIANAGVGH-----FAPVEELTPEEwrlvIDTNLTGAFY------------TIKAAVPALKRGGGYIINISS-LAG- 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  158 TDFATGGHAPNAfayriSKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGE 212
Cdd:PRK07326 144 TNFFAGGAAYNA-----SKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGH 193
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 4-224 2.58e-14

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: 70.31  E-value: 2.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVkdKNIRHIIATARDVEK----ATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGs 79
Cdd:cd05332   4 KVVIITGASSGIGEELAYHLA--RLGARLVLSARREERleevKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFG- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  80 dGLNLLVNNAGnavdypckaKPNRALFAEQ--------LNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTIS 151
Cdd:cd05332  81 -GLDILINNAG---------ISMRSLFHDTsidvdrkiMEVNYFGPVALTKAALPHLIERSQ-----------GSIVVVS 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558990 152 SGLASMTdfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMgGEKALLTVEQSTAE 224
Cdd:cd05332 140 SIAGKIG-------VPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNI-AMNALSGDGSMSAK 204
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 4-209 3.53e-14

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: 69.50  E-value: 3.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAISDP---RVTALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGA--KVAVTDRSEEAAAETVEEIKAlggNAAALEADVSDREAVEALVEKVEAEFG-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 GLNLLVNNAGNAVDypckakpnrALFA----EQ----LNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISS 152
Cdd:cd05333  77 PVDILVNNAGITRD---------NLLMrmseEDwdavINVNLTGVFNVTQAVIRAMIKRRS-----------GRIINISS 136

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990 153 GLASMTDFatgGHApNafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd05333 137 VVGLIGNP---GQA-N---YAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDM 186
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 4-209 3.71e-14

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: 69.67  E-value: 3.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVK---DKNIRHIIaTARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSd 80
Cdd:cd05352   9 KVAIVTGGSRGIGLAIARALAEagaDVAIIYNS-APRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGK- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 gLNLLVNNAGNAVDYPCKAKPNRAlFAEQLNVNTTSVVILTQKLMPLLIKasskvsgdQLSASraAVVTissglASMTdf 160
Cdd:cd05352  87 -IDILIANAGITVHKPALDYTYEQ-WNKVIDVNLNGVFNCAQAAAKIFKK--------QGKGS--LIIT-----ASMS-- 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17558990 161 atgGHAPNA----FAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd05352 148 ---GTIVNRpqpqAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDL 197
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 4-233 6.31e-14

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: 68.84  E-value: 6.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDkNIRHIIATARDVEKATDLKAI---SDPRVTALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:cd05362   4 KVALVTGASRGIGRAIAKRLARD-GASVVVNYASSKAAAEEVVAEieaAGGKAIAVQADVSDPSQVARLFDAAEKAFG-- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 GLNLLVNNAGNAVDYPCkAKPNRALFAEQLNVNTTSVVILTQKlmpllikASSKVSGDqlsasrAAVVTISSGLASMTdf 160
Cdd:cd05362  81 GVDILVNNAGVMLKKPI-AETSEEEFDRMFTVNTKGAFFVLQE-------AAKRLRDG------GRIINISSSLTAAY-- 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558990 161 atgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMggekallTVEQSTAELVASFNKLN 233
Cdd:cd05362 145 -----TPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM-------FYAGKTEEAVEGYAKMS 205
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 4-208 7.96e-14

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


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 68.85  E-value: 7.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEK----ATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEivGS 79
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGA--KLILTGRRAERlqelADELGAKFPVKVLPLQLDVSDRESIEAALENLPE--EF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  80 DGLNLLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsGDqlsasraaVVTISSglasmtd 159
Cdd:cd05346  77 RDIDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQ---GH--------IINLGS------- 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17558990 160 faTGGHAP--NAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTD 208
Cdd:cd05346 139 --IAGRYPyaGGNVYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETE 187
PRK06914 PRK06914
SDR family oxidoreductase;
1-208 8.39e-14

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 69.28  E-value: 8.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKA------ISDpRVTALQLEVTCDKSMDTFVSKVE 74
Cdd:PRK06914   1 MNKKIAIVTGASSGFGLLTTLELAKKG--YLVIATMRNPEKQENLLSqatqlnLQQ-NIKVQQLDVTDQNSIHNFQLVLK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   75 EIvgsDGLNLLVNNAGNAVdypckakpnrALFAE---------QLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrA 145
Cdd:PRK06914  78 EI---GRIDLLVNNAGYAN----------GGFVEeipveeyrkQFETNVFGAISVTQAVLPYMRKQKS-----------G 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558990  146 AVVTISSgLASMTDFatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTD 208
Cdd:PRK06914 134 KIINISS-ISGRVGF------PGLSPYVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNTN 189
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 4-212 1.33e-13

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 67.92  E-value: 1.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKdKNIRHIIaTARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHA-EGYRVGI-CARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKasskvsgdqlsaSRAAVVTISSgLASMTDFaTG 163
Cdd:cd08929  77 ALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRR------------GGGTIVNVGS-LAGKNAF-KG 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17558990 164 GHAPNAfayriSKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGE 212
Cdd:cd08929 143 GAAYNA-----SKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGS 186
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 4-214 4.54e-13

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: 66.72  E-value: 4.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAIsdPRVTALQLEVTCDKSMDTFVSKVEEIvgsdglN 83
Cdd:cd05368   3 KVALITAAAQGIGRAIALAFAREG--ANVIATDINEEKLKELERG--PGITTRVLDVTDKEQVAALAKEEGRI------D 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAG-----NAVDypCKAKPnralFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLASMT 158
Cdd:cd05368  73 VLFNCAGfvhhgSILD--CEDDD----WDFAMNLNVRSMYLMIKAVLPKMLARKD-----------GSIINMSSVASSIK 135

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990 159 DfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKA 214
Cdd:cd05368 136 G------VPNRFVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERI 185
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 1-214 4.99e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 66.99  E-value: 4.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGlglvQEFVK------DKnirhIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVE 74
Cdd:PRK08263   1 MMEKVWFITGASRGFG----RAWTEaalergDR----VVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   75 EIVGSdgLNLLVNNAGNAVDYPCKAKPNRALFAeQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSgl 154
Cdd:PRK08263  73 EHFGR--LDIVVNNAGYGLFGMIEEVTESEARA-QIDTNFFGALWVTQAVLPYLREQRS-----------GHIIQISS-- 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  155 asmtdFATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKA 214
Cdd:PRK08263 137 -----IGGISAFPMSGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSA 191
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
4-209 5.58e-13

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 66.75  E-value: 5.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSdgLN 83
Cdd:PRK08226   7 KTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGR--ID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAG-----NAVDYPckaKPNRALfaeQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTISSGLASMT 158
Cdd:PRK08226  85 ILVNNAGvcrlgSFLDMS---DEDRDF---HIDINIKGVWNVTKAVLPEMIARK-----------DGRIVMMSSVTGDMV 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17558990  159 dfATGGHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK08226 148 --ADPGET----AYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPM 192
PRK06182 PRK06182
short chain dehydrogenase; Validated
 1-223 1.09e-12

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 65.75  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKNIrhIIATARDVEKATDLKAISdprVTALQLEVTCDKSMdtfVSKVEEIVGSD 80
Cdd:PRK06182   1 MQKKVALVTGASSGIGKATARRLAAQGYT--VYGAARRVDKMEDLASLG---VHPLSLDVTDEASI---KAAVDTIIAEE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 G-LNLLVNNAG----NAV-DYPC-KAKpnralfaEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSg 153
Cdd:PRK06182  73 GrIDVLVNNAGygsyGAIeDVPIdEAR-------RQFEVNLFGAARLTQLVLPHMRAQRS-----------GRIINISS- 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558990  154 lasmtdfaTGG--HAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKA--LLTVEQSTA 223
Cdd:PRK06182 134 --------MGGkiYTPLGAWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGDIAAdhLLKTSGNGA 199
PRK06484 PRK06484
short chain dehydrogenase; Validated
 4-209 1.22e-12

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 66.80  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNIrhIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSdgLN 83
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQ--VVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGR--ID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGnAVDYPCKAKPNRAL--FAEQLNVNTTSVVILTQKLMPLLIKASSKvsgdqlsasrAAVVTISSGLASMTDfa 161
Cdd:PRK06484  82 VLVNNAG-VTDPTMTATLDTTLeeFARLQAINLTGAYLVAREALRLMIEQGHG----------AAIVNVASGAGLVAL-- 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17558990  162 tgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK06484 149 -----PKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 7-235 2.07e-12

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: 64.93  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990     7 VITGANRGIGLGLVQEFVKDKNIRHIIAT--ARDVEKATDLKA-----ISDPRVTALQLEVTCDKSMDTFVSKVEEIVGS 79
Cdd:TIGR01500   4 LVTGASRGFGRTIAQELAKCLKSPGSVLVlsARNDEALRQLKAeigaeRSGLRVVRVSLDLGAEAGLEQLLKALRELPRP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    80 DGLN--LLVNNAGNAVDYPCKAKPnralFAEQLNV------NTTSVVILTQKLMPLLikasskvsgDQLSASRAAVVTIS 151
Cdd:TIGR01500  84 KGLQrlLLINNAGTLGDVSKGFVD----LSDSTQVqnywalNLTSMLCLTSSVLKAF---------KDSPGLNRTVVNIS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   152 SgLASMTDFATGGHapnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMggeKALLTVEQSTAELVASFNK 231
Cdd:TIGR01500 151 S-LCAIQPFKGWAL------YCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDM---QQQVREESVDPDMRKGLQE 220


                  ....
gi 17558990   232 LNNS 235
Cdd:TIGR01500 221 LKAK 224
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 6-225 2.77e-12

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 64.51  E-value: 2.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVkDKNIRHIIA--TARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLA-KAGASVVIAdlKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFG--GIT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSglasmtdFATG 163
Cdd:cd05365  79 ILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGG-----------GAILNISS-------MSSE 140

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558990 164 GHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDmgGEKALLTVEQSTAEL 225
Cdd:cd05365 141 NKNVRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTD--ALASVLTPEIERAML 200
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 4-217 2.83e-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: 64.48  E-value: 2.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMD----TFVSKVEEIVGS 79
Cdd:cd08933  10 KVVIVTGGSRGIGRGIVRAFVENGA--KVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTKEedikTLISVTVERFGR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  80 dgLNLLVNNAGNavdYPCKAKPNRAL---FAEQLNVNTTSVVILTQKLMPLLIKasskvsgdqlsaSRAAVVTISSGLAS 156
Cdd:cd08933  88 --IDCLVNNAGW---HPPHQTTDETSaqeFRDLLNLNLISYFLASKYALPHLRK------------SQGNIINLSSLVGS 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558990 157 MtdfatgGHApNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKALLT 217
Cdd:cd08933 151 I------GQK-QAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQT 204
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 4-228 7.39e-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: 63.45  E-value: 7.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNIRHIIATARD-VEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGL 82
Cdd:cd05344   2 KVALVTAASSGIGLAIARALAREGARVAICARNREnLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFG--RV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  83 NLLVNNAGNAvdyPCK--AKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLAS--MT 158
Cdd:cd05344  80 DILVNNAGGP---PPGpfAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGW-----------GRIVNISSLTVKepEP 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990 159 DFATGGhapnafayrISKAAINMFGRALANDMKDDHILVASIGPGWVKTD-------MGGEKALLTVEQSTAELVAS 228
Cdd:cd05344 146 NLVLSN---------VARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTErvrrlleARAEKEGISVEEAEKEVASQ 213
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 4-210 8.01e-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: 63.26  E-value: 8.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARdveKATDLKAI--SDPRVTALQLEVTCDksmdtfvSKVEEIVGSDG 81
Cdd:cd05351   8 KRALVTGAGKGIGRATVKALAKAGA--RVVAVSR---TQADLDSLvrECPGIEPVCVDLSDW-------DATEEALGSVG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  82 -LNLLVNNAGNAVDYPCKAKPNRAlFAEQLNVNTTSVVILTQKLMPLLIKASSKvsgdqlsasrAAVVTISSGLASMtdf 160
Cdd:cd05351  76 pVDLLVNNAAVAILQPFLEVTKEA-FDRSFDVNVRAVIHVSQIVARGMIARGVP----------GSIVNVSSQASQR--- 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17558990 161 ATGGHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMG 210
Cdd:cd05351 142 ALTNHT----VYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMG 187
PRK09072 PRK09072
SDR family oxidoreductase;
4-209 8.38e-12

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 63.42  E-value: 8.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKA-ISDP-RVTALQLEVTCDKSMDTFVSKVEEIvgsDG 81
Cdd:PRK09072   6 KRVLLTGASGGIGQALAEALAAAG--ARLLLVGRNAEKLEALAArLPYPgRHRWVVADLTSEAGREAVLARAREM---GG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAVDYPCKAKPNRALfAEQLNVNTTSVVILTQKLMPLLIKasskvsgdqlsASRAAVVTISSGLASMtdfa 161
Cdd:PRK09072  81 INVLINNAGVNHFALLEDQDPEAI-ERLLALNLTAPMQLTRALLPLLRA-----------QPSAMVVNVGSTFGSI---- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17558990  162 tgGHAPNAfAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK09072 145 --GYPGYA-SYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAM 189
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 7-209 8.95e-12

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: 63.25  E-value: 8.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   7 VITGANRGIGLGLVQEFVKDKNIRHIIATaRDVEKATDLKAISDP---RVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd05337   5 IVTGASRGIGRAIATELAARGFDIAINDL-PDDDQATEVVAEVLAagrRAIYFQADIGELSDHEALLDQAWEDFG--RLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVdypckaKPNRAL-------FAEQLNVNTTSVVILTQKLMPLLIKASSKVSGdqLSASRAAVVTISSGLAS 156
Cdd:cd05337  82 CLVNNAGIAV------RPRGDLldltedsFDRLIAINLRGPFFLTQAVARRMVEQPDRFDG--PHRSIIFVTSINAYLVS 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17558990 157 mtdfatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd05337 154 ----------PNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDM 196
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-209 9.08e-12

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 62.67  E-value: 9.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKdkNIRHIIATarDVEKATDLKaisdPRVTALQLEVTCDksmdtfVSKVEEIVGSdgLN 83
Cdd:PRK06550   6 KTVLITGAASGIGLAQARAFLA--QGAQVYGV--DKQDKPDLS----GNFHFLQLDLSDD------LEPLFDWVPS--VD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSKVsgdqlsasraaVVTISSgLASMTdfATG 163
Cdd:PRK06550  70 ILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGI-----------IINMCS-IASFV--AGG 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17558990  164 GHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK06550 136 GGA----AYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPM 177
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 4-210 1.22e-11

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: 62.87  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKdKNIRHIIAtARDVEKATdlKAISDPRVTALQLEVTCDK----SMDTFVSKVEEIVGS 79
Cdd:cd09807   2 KTVIITGANTGIGKETARELAR-RGARVIMA-CRDMAKCE--EAAAEIRRDTLNHEVIVRHldlaSLKSIRAFAAEFLAE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  80 -DGLNLLVNNAGNavdYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLiKASSKvsgdqlsaSRaaVVTISS-----G 153
Cdd:cd09807  78 eDRLDVLINNAGV---MRCPYSKTEDGFEMQFGVNHLGHFLLTNLLLDLL-KKSAP--------SR--IVNVSSlahkaG 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990 154 LASMTDFATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMG 210
Cdd:cd09807 144 KINFDDLNSEKSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELG 200
PRK09009 PRK09009
SDR family oxidoreductase;
4-244 1.28e-11

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 62.39  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNIRHIIATARdvEKATDLKaisDPRVTALQLEVTCDKSMDTFVSKVEEIvgsdglN 83
Cdd:PRK09009   1 MNILIVGGSGGIGKAMVKQLLERYPDATVHATYR--HHKPDFQ---HDNVQWHALDVTDEAEIKQLSEQFTQL------D 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGnAVDYPCKAkPNRAL-------FAEQLNVNTTSVVILTQKLMPLLiKASSkvsgdqlsasRAAVVTISSGLAS 156
Cdd:PRK09009  70 WLINCVG-MLHTQDKG-PEKSLqaldadfFLQNITLNTLPSLLLAKHFTPKL-KQSE----------SAKFAVISAKVGS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  157 MTDFATGGHapnaFAYRISKAAINMFGRALA----NDMKddHILVASIGPGWVKTDMGG-------EKALLTVEQSTAEL 225
Cdd:PRK09009 137 ISDNRLGGW----YSYRASKAALNMFLKTLSiewqRSLK--HGVVLALHPGTTDTALSKpfqqnvpKGKLFTPEYVAQCL 210

                        250
                 ....*....|....*....
gi 17558990  226 VASFNKLNNSHNGGFFQKD 244
Cdd:PRK09009 211 LGIIANATPAQSGSFLAYD 229
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 1-209 1.50e-11

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: 62.46  E-value: 1.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKNIRHIiaTARDVEKATdlkaisdpRVTALQLE--------VTCDKSMDTFVSK 72
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYI--TGRTILPQL--------PGTAEEIEarggkcipVRCDHSDDDEVEA 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  73 VEEIVGS--DG-LNLLVNNAGNAVDyPCKAKPNRALFAEQL----NVNTTSV---VILTQKLMPLLIKASSKVsgdqlsa 142
Cdd:cd09763  71 LFERVAReqQGrLDILVNNAYAAVQ-LILVGVAKPFWEEPPtiwdDINNVGLrahYACSVYAAPLMVKAGKGL------- 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990 143 sraaVVTISSGLASMTDFAtgghapnaFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd09763 143 ----IVIISSTGGLEYLFN--------VAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTEL 197
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-207 2.70e-11

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 61.67  E-value: 2.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVK---DknirhIIATARDVEKATDLKAISDP--RVTALQLEVTCDKSMDTFVSKVEEIVG 78
Cdd:PRK06935  16 KVAIVTGGNTGLGQGYAVALAKagaD-----IIITTHGTNWDETRRLIEKEgrKVTFVQVDLTKPESAEKVVKEALEEFG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 SdgLNLLVNNAGNAvdypckaKPNRAL-FAEQ-----LNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTIss 152
Cdd:PRK06935  91 K--IDILVNNAGTI-------RRAPLLeYKDEdwnavMDINLNSVYHLSQAVAKVMAKQGS-----------GKIINI-- 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  153 glASMTDFATGGHAPnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK06935 149 --ASMLSFQGGKFVP---AYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 4-209 7.91e-11

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 60.27  E-value: 7.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVkdkniRH---IIATARDVEKatdLKAISD---------PRVTALQLEVTCDKSMDTFVS 71
Cdd:PRK08945  13 RIILVTGAGDGIGREAALTYA-----RHgatVILLGRTEEK---LEAVYDeieaaggpqPAIIPLDLLTATPQNYQQLAD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   72 KVEEIVGS-DGLnllVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTI 150
Cdd:PRK08945  85 TIEEQFGRlDGV---LHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPA-----------ASLVFT 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558990  151 SSGLasmtdfatgGHAPNAF--AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK08945 151 SSSV---------GRQGRANwgAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 4-209 8.12e-11

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 60.46  E-value: 8.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFvKDKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:PRK12829  12 LRVLVTGGASGIGRAIAEAF-AEAGARVHVCDVSEAALAATAARLPGAKVTATVADVADPAQVERVFDTAVERFG--GLD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLiKASskvsgdqlsaSRAAVVTISSGLASMTDFATG 163
Cdd:PRK12829  89 VLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLL-KAS----------GHGGVIIALSSVAGRLGYPGR 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17558990  164 GHapnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK12829 158 TP------YAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPR 197
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 4-209 8.87e-11

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: 60.20  E-value: 8.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd08944   4 KVAIVTGAGAGIGAACAARLAREGA--RVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFG--GLD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIkasskvsgdqlSASRAAVVTISSGLAsmtdfaTG 163
Cdd:cd08944  80 LLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMI-----------ARGGGSIVNLSSIAG------QS 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17558990 164 GhAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd08944 143 G-DPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPL 187
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-209 1.05e-10

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 59.88  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDkNIRHIIATARDVEKATDLKAI---SDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLARA-GADVVVHYRSDEEAAEELVEAveaLGRRAQAVQADVTDKAALEAAVAAAVERF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   78 GsdGLNLLVNNAGNAVDYPCkAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLASM 157
Cdd:PRK12825  83 G--RIDILVNNAGIFEDKPL-ADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRG-----------GRIVNISSVAGLP 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17558990  158 tdfATGGHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK12825 149 ---GWPGRS----NYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDM 193
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 6-209 1.12e-10

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: 59.67  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFV-KDKNIrhIIATARDVEKATDLKAI---SDPRVTALQLEVTCDKSMDTFVSKVEEIVGSdg 81
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAeRGADV--VINYRKSKDAAAEVAAEieeLGGKAVVVRADVSQPQDVEEMFAAVKERFGR-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  82 LNLLVNNAGNAVDYPCkAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLAsmtdfa 161
Cdd:cd05359  77 LDVLVSNAAAGAFRPL-SELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGG-----------GRIVAISSLGS------ 138

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17558990 162 tGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd05359 139 -IRALPNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDA 185
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 6-209 1.23e-10

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: 59.56  E-value: 1.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVK--------DKNIRHIIATARDVEKATdlkaisdPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:cd05339   2 VLITGGGSGIGRLLALEFAKrgakvvilDINEKGAEETANNVRKAG-------GKVHYYKCDVSKREEVYEAAKKIKKEV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  78 GSdgLNLLVNNAGNAVDYPCKAKPNRaLFAEQLNVNTTSVVILTQKLMPLLIKasskvsgdqlsASRAAVVTISS----- 152
Cdd:cd05339  75 GD--VTILINNAGVVSGKKLLELPDE-EIEKTFEVNTLAHFWTTKAFLPDMLE-----------RNHGHIVTIASvagli 140

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 153 GLASMTDFATgghapnafayriSKAAINMFGRALANDMK---DDHILVASIGPGWVKTDM 209
Cdd:cd05339 141 SPAGLADYCA------------SKAAAVGFHESLRLELKaygKPGIKTTLVCPYFINTGM 188
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 4-209 2.05e-10

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: 59.31  E-value: 2.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKnirHIIATARDVEKATDLKAIS-----DPRVTALQLEVTCDKSMDTFVSKVEEIVG 78
Cdd:cd05366   3 KVAIITGAAQGIGRAIAERLAADG---FNIVLADLNLEEAAKSTIQeiseaGYNAVAVGADVTDKDDVEALIDQAVEKFG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  79 SdgLNLLVNNAGNAVDYPCKAKPnRALFAEQLNVNTTSVVILTQKLMPLLIKAssKVSGDQLSASRAAvvtissGLASMt 158
Cdd:cd05366  80 S--FDVMVNNAGIAPITPLLTIT-EEDLKKVYAVNVFGVLFGIQAAARQFKKL--GHGGKIINASSIA------GVQGF- 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17558990 159 dfatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd05366 148 --------PNLGAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM 190
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 4-220 2.16e-10

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: 59.13  E-value: 2.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVkdKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd09761   2 KVAIVTGGGHGIGKQICLDFL--EAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLG--RID 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNRAlFAEQLNVNTTSVVILtqklmpllikasSKVSGDQLSASRAAVVTISSGLASMTDfatg 163
Cdd:cd09761  78 VLVNNAARGSKGILSSLLLEE-WDRILSVNLTGPYEL------------SRYCRDELIKNKGRIINIASTRAFQSE---- 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990 164 ghaPNAFAYRISKAAINMFGRALANDMKDDhILVASIGPGWVKTDMGGEKALLTVEQ 220
Cdd:cd09761 141 ---PDSEAYAASKGGLVALTHALAMSLGPD-IRVNCISPGWINTTEQQEFTAAPLTQ 193
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 1-203 2.41e-10

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: 58.94  E-value: 2.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKniRHIIATAR-----DVEKATDLKAISDPRVTALQ------LEVTCDKSMDTF 69
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAG--ATVVVAAKtasegDNGSAKSLPGTIEETAEEIEaaggqaLPIVVDVRDEDQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  70 V-SKVEEIVGSDG-LNLLVNNAG-----NAVDYPCKakpnraLFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsa 142
Cdd:cd05338  79 VrALVEATVDQFGrLDILVNNAGaiwlsLVEDTPAK------RFDLMQRVNLRGTYLLSQAALPHMVKAGQ--------- 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558990 143 srAAVVTISSGLASmtdfatgGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPG 203
Cdd:cd05338 144 --GHILNISPPLSL-------RPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPS 195
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 4-209 2.94e-10

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: 58.55  E-value: 2.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNIrhIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd05341   6 KVAIVTGGARGLGLAHARLLVAEGAK--VVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFG--RLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAVDYPCKAKPNrALFAEQLNVNTTSVVILTQKLMPLLIKasskvsgdqlsASRAAVVTISSGLASMTDfatg 163
Cdd:cd05341  82 VLVNNAGILTGGTVETTTL-EEWRRLLDINLTGVFLGTRAVIPPMKE-----------AGGGSIINMSSIEGLVGD---- 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17558990 164 ghaPNAFAYRISKAAINMFGRALANDM--KDDHILVASIGPGWVKTDM 209
Cdd:cd05341 146 ---PALAAYNASKGAVRGLTKSAALECatQGYGIRVNSVHPGYIYTPM 190
PRK06101 PRK06101
SDR family oxidoreductase;
5-236 3.21e-10

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 58.73  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    5 SVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAISDpRVTALQLEVTCDKSMDTFVSKVEEIVgsdglNL 84
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQG--WQVIACGRNQSVLDELHTQSA-NIFTLAFDVTDHPGTKAALSQLPFIP-----EL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   85 LVNNAGNAvDYPCKAKPNRALFAEQLNVNTTSVViltqklmpllikasSKVSGDQLSASRAAVVTISSGLASmtDFATgg 164
Cdd:PRK06101  75 WIFNAGDC-EYMDDGKVDATLMARVFNVNVLGVA--------------NCIEGIQPHLSCGHRVVIVGSIAS--ELAL-- 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990  165 haPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKA-----LLTVEQSTAELVASFNKlNNSH 236
Cdd:PRK06101 136 --PRAEAYGASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTfampmIITVEQASQEIRAQLAR-GKSH 209
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 4-209 4.40e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 58.42  E-value: 4.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFvKDKNIRhIIATARDV----EKATDLKAISdprVTALQLEVTCDKSMDT--FVSKVEEIV 77
Cdd:PRK08213  13 KTALVTGGSRGLGLQIAEAL-GEAGAR-VVLSARKAeeleEAAAHLEALG---IDALWIAADVADEADIerLAEETLERF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   78 GsdGLNLLVNNAGN-----AVDYPCKAkpnralFAEQLNVNTTSVVILTQKLMPLLIKASSKvsgdqlsasrAAVVTISS 152
Cdd:PRK08213  88 G--HVDILVNNAGAtwgapAEDHPVEA------WDKVMNLNVRGLFLLSQAVAKRSMIPRGY----------GRIINVAS 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558990  153 --GLasmtdfatGGHAP---NAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK08213 150 vaGL--------GGNPPevmDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKM 203
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-211 4.76e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 58.39  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEfVKDKNIRhIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:PRK06180   2 SSMKTWLITGVSSGFGRALAQA-ALAAGHR-VVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAGnavdYPCKAKPNRALFAE---QLNVNTTSVVILTQKLMPllikasskvsgdQLSASRAA-VVTISS--GL 154
Cdd:PRK06180  78 PIDVLVNNAG----YGHEGAIEESPLAEmrrQFEVNVFGAVAMTKAVLP------------GMRARRRGhIVNITSmgGL 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990  155 ASMtdfatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGG 211
Cdd:PRK06180 142 ITM---------PGIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPGSFRTDWAG 189
PRK06484 PRK06484
short chain dehydrogenase; Validated
 2-207 4.93e-10

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 59.09  E-value: 4.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    2 SPKSVVITGANRGIGLGLVQEFVKDKNIRHIIAtaRDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSdg 81
Cdd:PRK06484 268 SPRVVAITGGARGIGRAVADRFAAAGDRLLIID--RDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGR-- 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGnavdypckakpnralFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqLSASRAAVVTISSG--LASMTD 159
Cdd:PRK06484 344 LDVLVNNAG---------------IAEVFKPSLEQSAEDFTRVYDVNLSGA-------FACARAAARLMSQGgvIVNLGS 401

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17558990  160 FATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK06484 402 IASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-234 1.12e-09

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 57.01  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDK-NIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSdgL 82
Cdd:PRK07666   8 KNALITGAGRGIGRAVAIALAKEGvNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGS--I 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   83 NLLVNNAGNAvDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIkasSKVSGDqlsasraaVVTISSglasmtdfaT 162
Cdd:PRK07666  86 DILINNAGIS-KFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMI---ERQSGD--------IINISS---------T 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  163 GGH--APNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM--------GGEKALLTVEqSTAELVASFNKL 232
Cdd:PRK07666 145 AGQkgAAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMavdlgltdGNPDKVMQPE-DLAEFIVAQLKL 223


                 ..
gi 17558990  233 NN 234
Cdd:PRK07666 224 NK 225
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
4-209 1.29e-09

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 56.96  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVkDKNIRHIIATaRDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:PRK07067   7 KVALLTGAASGIGEAVAERYL-AEGARVVIAD-IKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGnAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKAsskvsgdqlsASRAAVVTISSglasmtdfATG 163
Cdd:PRK07067  83 ILFNNAA-LFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQ----------GRGGKIINMAS--------QAG 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17558990  164 --GHAPNAfAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK07067 144 rrGEALVS-HYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPM 190
PRK06181 PRK06181
SDR family oxidoreductase;
4-208 1.74e-09

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 56.53  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDL-KAISDPRVTALQleVTCDKSMDTFVSKVEEIVGSD-- 80
Cdd:PRK06181   2 KVVIITGASEGIGRALAVRLARAGA--QLVLAARNETRLASLaQELADHGGEALV--VPTDVSDAEACERLIEAAVARfg 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPllikasskvsgdQLSASRAAVVTISSgLASMTDf 160
Cdd:PRK06181  78 GIDILVNNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALP------------HLKASRGQIVVVSS-LAGLTG- 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17558990  161 atgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTD 208
Cdd:PRK06181 144 -----VPTRSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATD 186
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 4-206 4.81e-09

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: 55.42  E-value: 4.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNIrhIIATARDVEKATDLKA--ISDP--RVTALQLEVTCDKSMDTFVSKVEEIVGS 79
Cdd:cd08930   3 KIILITGAAGLIGKAFCKALLSAGAR--LILADINAPALEQLKEelTNLYknRVIALELDITSKESIKELIESYLEKFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  80 dgLNLLVNNAGNAVDYPCKAKPNR--ALFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTISSGLASM 157
Cdd:cd08930  81 --IDILINNAYPSPKVWGSRFEEFpyEQWNEVLNVNLGGAFLCSQAFIKLFKKQG-----------KGSIINIASIYGVI 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17558990 158 T-DFA--TGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVK 206
Cdd:cd08930 148 ApDFRiyENTQMYSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIL 199
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 4-225 5.82e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 55.15  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLgLVQEFVKDKNIRHII--ATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdG 81
Cdd:PRK08085  10 KNILITGSAQGIGF-LLATGLAEYGAEIIIndITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIG--P 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAVDYPCKAKPNRAlFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTISS-----GLAS 156
Cdd:PRK08085  87 IDVLINNAGIQRRHPFTEFPEQE-WNDVIAVNQTAVFLVSQAVARYMVKRQ-----------AGKIINICSmqselGRDT 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558990  157 MTDFATgghapnafayriSKAAINMFGRALANDMKDDHILVASIGPGWVKTDMggEKALLTVEQSTAEL 225
Cdd:PRK08085 155 ITPYAA------------SKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEM--TKALVEDEAFTAWL 209
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 1-232 6.48e-09

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: 54.85  E-value: 6.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKA---ISDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEG--AAVAIAARRVDRLEALADeleAEGGKALVLELDVTDEQQVDAAVERTVEAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  78 GsdGLNLLVNNAGNAVDYPCKAKPNrALFAEQLNVNTTSVVILTQKLMPLLikasskvsgdqLSASRAAVVTISSglasm 157
Cdd:cd08934  79 G--RLDILVNNAGIMLLGPVEDADT-TDWTRMIDTNLLGLMYTTHAALPHH-----------LLRNKGTIVNISS----- 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558990 158 tdFATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKALLTVEQSTAELVASFNKL 232
Cdd:cd08934 140 --VAGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAYEERISTIRKL 212
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 4-209 6.56e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 55.36  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVqefvkdkniRHIIAT-AR----DVEKATdLKAIS-----DPRVTALQLEVTCDKSMDTFVSKV 73
Cdd:PRK05872  10 KVVVVTGAARGIGAELA---------RRLHARgAKlalvDLEEAE-LAALAaelggDDRVLTVVADVTDLAAMQAAAEEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   74 EEIVGsdGLNLLVNNAGNAVDYPCkAKPNRALFAEQLNVNTTSVVILTQKLMPLLIkasskvsgdqlsASRAAVVTISSg 153
Cdd:PRK05872  80 VERFG--GIDVVVANAGIASGGSV-AQVDPDAFRRVIDVNLLGVFHTVRATLPALI------------ERRGYVLQVSS- 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990  154 LASmtdFATgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK05872 144 LAA---FAA---APGMAAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDL 193
PRK07454 PRK07454
SDR family oxidoreductase;
2-207 6.93e-09

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 54.58  E-value: 6.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    2 SPKSVVITGANRGIGLGLVQEFVKdKNIrHIIATARDVEKATDLKA-ISDPRVTALQleVTCDKS-MDTFVSKVEEIVGS 79
Cdd:PRK07454   5 SMPRALITGASSGIGKATALAFAK-AGW-DLALVARSQDALEALAAeLRSTGVKAAA--YSIDLSnPEAIAPGIAELLEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   80 DGL-NLLVNNAGNAVDYPCKAKPnRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSglasmt 158
Cdd:PRK07454  81 FGCpDVLINNAGMAYTGPLLEMP-LSDWQWVIQLNLTSVFQCCSAVLPGMRARGG-----------GLIINVSS------ 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17558990  159 dfatggHAP-NAF----AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK07454 143 ------IAArNAFpqwgAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNT 190
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 1-219 9.59e-09

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 54.56  E-value: 9.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLglvqefvkdknirhiiATARDVEKATDLKAISD-------------PRVTALQLEVTCDKSMD 67
Cdd:PRK07825   3 LRGKVVAITGGARGIGL----------------ATARALAALGARVAIGDldealaketaaelGLVVGGPLDVTDPASFA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   68 TFVSKVEEIVGSdgLNLLVNNAG-----NAVDypckaKPNRALFAeQLNVNTTSVVILTQKLMPllikasskvsgDQLSA 142
Cdd:PRK07825  67 AFLDAVEADLGP--IDVLVNNAGvmpvgPFLD-----EPDAVTRR-ILDVNVYGVILGSKLAAP-----------RMVPR 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  143 SRAAVVTISSgLASMTdfATGGHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM----GGEKALLTV 218
Cdd:PRK07825 128 GRGHVVNVAS-LAGKI--PVPGMA----TYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELiagtGGAKGFKNV 200


                 .
gi 17558990  219 E 219
Cdd:PRK07825 201 E 201
PRK06138 PRK06138
SDR family oxidoreductase;
4-209 1.02e-08

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 54.39  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKA--ISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdG 81
Cdd:PRK06138   6 RVAIVTGAGSGIGRATAKLFAREG--ARVVVADRDAEAAERVAAaiAAGGRAFARQGDVGSAEAVEALVDFVAARWG--R 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAG-----NAVDYPckakPN--RALFaeqlNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGL 154
Cdd:PRK06138  82 LDVLVNNAGfgcggTVVTTD----EAdwDAVM----RVNVGGVFLWAKYAIPIMQRQGG-----------GSIVNTASQL 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  155 AsmtdfaTGGHAPNAfAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK06138 143 A------LAGGRGRA-AYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPY 190
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 4-203 1.02e-08

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: 54.18  E-value: 1.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATdlKAISDPRVTALQLEVTCD-KSMDtfVSK-------VEE 75
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELVKEG--ANVIIVARSESKLE--EAVEEIEAEANASGQKVSyISAD--LSDyeeveqaFAQ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  76 IVGSDGL-NLLVNNAGNAVdypckAKPNRALFAEQL----NVNTTSVVILTQKLMPLLikasskvsgdqLSASRAAVVTI 150
Cdd:cd08939  76 AVEKGGPpDLVVNCAGISI-----PGLFEDLTAEEFergmDVNYFGSLNVAHAVLPLM-----------KEQRPGHIVFV 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17558990 151 SSGLASmtdFATGGHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPG 203
Cdd:cd08939 140 SSQAAL---VGIYGYS----AYCPSKFALRGLAESLRQELKPYNIRVSVVYPP 185
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 4-126 1.16e-08

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: 54.39  E-value: 1.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNIR-HIIATARDVEKATDLKAISDPR----VTALQLEVTCDKSMDTFVSKVEEivg 78
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLASDPSKRfKVYATMRDLKKKGRLWEAAGALaggtLETLQLDVCDSKSVAAAVERVTE--- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 17558990  79 sDGLNLLVNNAGNAVDYPCKAKPNRALfAEQLNVNTTSVVILTQKLMP 126
Cdd:cd09806  78 -RHVDVLVCNAGVGLLGPLEALSEDAM-ASVFDVNVFGTVRMLQAFLP 123
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 4-230 1.47e-08

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 53.93  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd05345   6 KVAIVTGAGSGFGEGIARRFAQEG--ARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFG--RLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGnavdYPCKAKP----NRALFAEQLNVNTTSVVILTQKLMPLLIKASSKVsgdqlsasraaVVTISSglasmtd 159
Cdd:cd05345  82 ILVNNAG----ITHRNKPmlevDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGV-----------IINIAS------- 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17558990 160 fATGGHA-PNAFAYRISKAAINMFGRALANDMKDDHILVASIGPgwvktdMGGEKALLT--VEQSTAELVASFN 230
Cdd:cd05345 140 -TAGLRPrPGLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCP------VAGETPLLSmfMGEDTPENRAKFR 206
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 1-203 2.05e-08

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 53.48  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKnirhiiATARDVekatDLK--AISDPRVTALQLEVTCDKSMDTFVSKVEEIVG 78
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANG------ANVVNA----DIHggDGQHENYQFVPTDVSSAEEVNHTVAEIIEKFG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 sdGLNLLVNNAGnaVDYP----------CKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSKVsgdqlsasraaVV 148
Cdd:PRK06171  77 --RIDGLVNNAG--INIPrllvdekdpaGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGV-----------IV 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990  149 TISS--GLAsmtdfATGGHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPG 203
Cdd:PRK06171 142 NMSSeaGLE-----GSEGQS----CYAATKAALNSFTRSWAKELGKHNIRVVGVAPG 189
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 7-225 2.30e-08

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 53.31  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    7 VITGANRGIGLGLVQEFvkdknirhiiATARDVEKATDLK---------AISDP--RVTALQLEVTCDKSMDTFVSKVEE 75
Cdd:PRK06113  15 IITGAGAGIGKEIAITF----------ATAGASVVVSDINadaanhvvdEIQQLggQAFACRCDITSEQELSALADFALS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   76 IVGsdGLNLLVNNAGNAVDYPCKAKPNRALFAEQLNVntTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLA 155
Cdd:PRK06113  85 KLG--KVDILVNNAGGGGPKPFDMPMADFRRAYELNV--FSFFHLSQLVAPEMEKNGG-----------GVILTITSMAA 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  156 SMTDFatgghapNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDmgGEKALLTVEQSTAEL 225
Cdd:PRK06113 150 ENKNI-------NMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTD--ALKSVITPEIEQKML 210
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 6-229 3.95e-08

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: 52.47  E-value: 3.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVKdkNIRHIIATARdveKATDLKAISDPrVTALQLEVTCDKSMDTFVSKVEEIVGsdGLNLL 85
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQ--AGATVIALDL---PFVLLLEYGDP-LRLTPLDVADAAAVREVCSRLLAEHG--PIDAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  86 VNNAGNavdypCKAKPNRALFAEQ----LNVNTTSVVILTQKLMPllikasskvsgdQLSASRA-AVVTISSGLAsmtdf 160
Cdd:cd05331  73 VNCAGV-----LRPGATDPLSTEDweqtFAVNVTGVFNLLQAVAP------------HMKDRRTgAIVTVASNAA----- 130

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558990 161 atggHAP--NAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMggEKALLTVEQSTAELVASF 229
Cdd:cd05331 131 ----HVPriSMAAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAM--QRTLWHDEDGAAQVIAGV 195
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 6-205 4.45e-08

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 52.45  E-value: 4.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    6 VVITGANRGIGLGLVQEFVKdkNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSdgLNLL 85
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQ--QGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRN--IDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   86 VNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTISSglasmtdfaTGGH 165
Cdd:PRK10538  79 VNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERN-----------HGHIINIGS---------TAGS 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 17558990  166 APNAFA--YRISKAAINMFGRALANDMKDDHILVASIGPGWV 205
Cdd:PRK10538 139 WPYAGGnvYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLV 180
PRK07063 PRK07063
SDR family oxidoreductase;
4-90 5.58e-08

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 52.36  E-value: 5.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDkNIRHIIAtARDVEK----ATDLKA-ISDPRVTALQLEVTCDKSMDTFVSKVEEIVG 78
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFARE-GAAVALA-DLDAALaeraAAAIARdVAGARVLAVPADVTDAASVAAAVAAAEEAFG 85

                         90
                 ....*....|..
gi 17558990   79 sdGLNLLVNNAG 90
Cdd:PRK07063  86 --PLDVLVNNAG 95
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 4-232 5.83e-08

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 52.00  E-value: 5.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDK---------SMDTfvsKVE 74
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESlhgvealysSLDN---ELQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   75 EIVGSDGLNLLVNNAGNAVDYPCKaKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasraaVVTISSGl 154
Cdd:PRK12747  82 NRTGSTKFDILINNAGIGPGAFIE-ETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSR-------------IINISSA- 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990  155 asmtdfATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKALLTVEQSTAELVASFNKL 232
Cdd:PRK12747 147 ------ATRISLPDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYATTISAFNRL 218
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 4-208 6.98e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 51.83  E-value: 6.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDlkaisdPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:PRK06523  10 KRALVTGGTKGIGAATVARLLEAG--ARVVTTARSRPDDLP------EGVEFVAADLTTAEGCAAVARAVLERLG--GVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGNAVDYPCK-AKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLASMTdfat 162
Cdd:PRK06523  80 ILVHVLGGSSAPAGGfAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGS-----------GVIIHVTSIQRRLP---- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17558990  163 gghAPNAF-AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTD 208
Cdd:PRK06523 145 ---LPESTtAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
PRK07985 PRK07985
SDR family oxidoreductase;
1-212 7.03e-08

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 52.30  E-value: 7.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVK---DKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYARegaDVAISYLPVEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   78 GsdGLNLLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasraaVVTISSGLASM 157
Cdd:PRK07985 127 G--GLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGAS-------------IITTSSIQAYQ 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990  158 TdfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM---GGE 212
Cdd:PRK07985 192 P-------SPHLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALqisGGQ 242
PRK07074 PRK07074
SDR family oxidoreductase;
3-207 7.29e-08

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 51.69  E-value: 7.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    3 PKSVVI-TGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDL-KAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSd 80
Cdd:PRK07074   1 TKRTALvTGAAGGIGQALARRFLAAGD--RVLALDIDAAALAAFaDALGDARFVPVACDLTDAASLAAALANAAAERGP- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 gLNLLVNNAGNAVDYPCkAKPNRALFAEQLNVNTTSVViltqklmpLLIKAsskVSGDQLSASRAAVVTIssglASMTDF 160
Cdd:PRK07074  78 -VDVLVANAGAARAASL-HDTTPASWRADNALNLEAAY--------LCVEA---VLEGMLKRSRGAVVNI----GSVNGM 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17558990  161 ATGGHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK07074 141 AALGHP----AYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKT 183
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 4-90 8.67e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 51.58  E-value: 8.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEK----ATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIvgs 79
Cdd:PRK06125   8 KRVLITGASKGIGAAAAEAFAAEGC--HLHLVARDADAlealAADLRAAHGVDVAVHALDLSSPEAREQLAAEAGDI--- 82

                         90
                 ....*....|.
gi 17558990   80 dglNLLVNNAG 90
Cdd:PRK06125  83 ---DILVNNAG 90
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 4-207 9.03e-08

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: 51.30  E-value: 9.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKdKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTcdkSMDTFVSKVEEIVGSDG-L 82
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAR-EGARVVVNYYRSTESAEAVAAEAGERAIAIQADVR---DRDQVQAMIEEAKNHFGpV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  83 NLLVNNAgnAVDYPCKAKPNRAL-------FAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLA 155
Cdd:cd05349  77 DTIVNNA--LIDFPFDPDQRKTFdtidwedYQQQLEGAVKGALNLLQAVLPDFKERGS-----------GRVINIGTNLF 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17558990 156 smtdfatggHAPNAF--AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:cd05349 144 ---------QNPVVPyhDYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 4-243 1.04e-07

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: 51.34  E-value: 1.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAISDPRVTALqlevTCDKSMDTFVSKVEEIVGSDG-L 82
Cdd:cd08951   8 KRIFITGSSDGLGLAAARTLLHQGH--EVVLHARSQKRAADAKAACPGAAGVL----IGDLSSLAETRKLADQVNAIGrF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  83 NLLVNNAGNAVDYPCKAKPNRAlfAEQLNVNTTSVVILTQKLMP--LLIKASSKVSgdqlsasraavvtiSSGLASMTDF 160
Cdd:cd08951  82 DAVIHNAGILSGPNRKTPDTGI--PAMVAVNVLAPYVLTALIRRpkRLIYLSSGMH--------------RGGNASLDDI 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 161 ATGGHAPNAF-AYRISKAAINMFGRALANDMKDdhILVASIGPGWVKTDMGGEKALLTVEQS--TAELVASFNKLNNSHN 237
Cdd:cd08951 146 DWFNRGENDSpAYSDSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPTKMGGAGAPDDLEQGhlTQVWLAESDDPQALTS 223


                ....*.
gi 17558990 238 GGFFQK 243
Cdd:cd08951 224 GGYFYH 229
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 1-90 1.12e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 51.44  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKdKNIRhIIATARDVEKATdlkaiSDPRVTALQLEVTCDKSMDTFVSKVEEIVGSd 80
Cdd:PRK06179   2 SNSKVALVTGASSGIGRATAEKLAR-AGYR-VFGTSRNPARAA-----PIPGVELLELDVTDDASVQAAVDEVIARAGR- 73

                         90
                 ....*....|
gi 17558990   81 gLNLLVNNAG 90
Cdd:PRK06179  74 -IDVLVNNAG 82
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-212 1.21e-07

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 51.23  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    3 PKSVVITGANR--GIGLGLVQEFVKDKNirHIIAT---ARDVEKATDL---------KAISDP--RVTALQLEVTCDKSM 66
Cdd:PRK12748   5 KKIALVTGASRlnGIGAAVCRRLAAKGI--DIFFTywsPYDKTMPWGMhdkepvllkEEIESYgvRCEHMEIDLSQPYAP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   67 DTFVSKVEEIVGSdgLNLLVNNAGNAVDYPCKAkpnraLFAEQLN----VNTTSVVILTQklmpLLIKASSKVSGDQlsa 142
Cdd:PRK12748  83 NRVFYAVSERLGD--PSILINNAAYSTHTRLEE-----LTAEQLDkhyaVNVRATMLLSS----AFAKQYDGKAGGR--- 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558990  143 sraaVVTISSG--LASMtdfatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTD-MGGE 212
Cdd:PRK12748 149 ----IINLTSGqsLGPM---------PDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGwITEE 208
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 3-215 1.62e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 50.77  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    3 PKSVVITGANRGIGLGLVQEFVkDKNIRHIIATARDVEKATDLKA-ISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSDG 81
Cdd:PRK06198   6 GKVALVTGGTQGLGAAIARAFA-ERGAAGLVICGRNAEKGEAQAAeLEALGAKAVFVQADLSDVEDCRRVVAAADEAFGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNA-----VDypckAKPnrALFAEQLNVNTTSVVILTQKLMPLLIKasSKVSGdqlsasraAVVTISsglaS 156
Cdd:PRK06198  85 LDALVNAAGLTdrgtiLD----TSP--ELFDRHFAVNVRAPFFLMQEAIKLMRR--RKAEG--------TIVNIG----S 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17558990  157 MTdfATGGHaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDmgGEKAL 215
Cdd:PRK06198 145 MS--AHGGQ-PFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE--GEDRI 198
PRK12746 PRK12746
SDR family oxidoreductase;
4-212 1.89e-07

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 50.80  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDkSMDTFVSKVEEI------- 76
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFLIEADLN-SIDGVKKLVEQLknelqir 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   77 VGSDGLNLLVNNAGNAVDYPCKaKPNRALFAEQLNVNTTSVVILTQKLMPLLikassKVSGDQLSASRAAVVTISSGlas 156
Cdd:PRK12746  86 VGTSEIDILVNNAGIGTQGTIE-NTTEEIFDEIMAVNIKAPFFLIQQTLPLL-----RAEGRVINISSAEVRLGFTG--- 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990  157 mtdfatgghapnAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGE 212
Cdd:PRK12746 157 ------------SIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAK 200
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 4-208 2.22e-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: 50.53  E-value: 2.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNIrhIIATARDVEKATD-LKAISDPRVTALQLEVTC-DKsmDTFVSKVEEIVGSDG 81
Cdd:cd08935   6 KVAVITGGTGVLGGAMARALAQAGAK--VAALGRNQEKGDKvAKEITALGGRAIALAADVlDR--ASLERAREEIVAQFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  82 -LNLLVNNAGNAvdypckaKPNRALFAEQLNVNTTSVVI--------------LTQKLMPllikaSSKVSGDQLSASRAA 146
Cdd:cd08935  82 tVDILINGAGGN-------HPDATTDPEHYEPETEQNFFdldeegwefvfdlnLNGSFLP-----SQVFGKDMLEQKGGS 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558990 147 VVTISSglasMTDFATGGHAPnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTD 208
Cdd:cd08935 150 IINISS----MNAFSPLTKVP---AYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
PRK07023 PRK07023
SDR family oxidoreductase;
7-212 2.38e-07

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 50.40  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    7 VITGANRGIGLGLVQEFVkDKNIRhIIATARdvEKATDLKAISDPRVTALQLEVTcdksmDTfvSKVEEIVGSDGLN--- 83
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLL-QPGIA-VLGVAR--SRHPSLAAAAGERLAEVELDLS-----DA--AAAAAWLAGDLLAafv 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 ------LLVNNAGnAVD--YPCKAKPNRALfAEQLNVNTTSVVILTQKLmpllIKASSKvsgdqlsASRAAVVTISSGLA 155
Cdd:PRK07023  74 dgasrvLLINNAG-TVEpiGPLATLDAAAI-ARAVGLNVAAPLMLTAAL----AQAASD-------AAERRILHISSGAA 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558990  156 SmtdfatgghapNAFA----YRISKAAINMFGRALANDmKDDHILVASIGPGWVKTDMGGE 212
Cdd:PRK07023 141 R-----------NAYAgwsvYCATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGMQAT 189
PRK08628 PRK08628
SDR family oxidoreductase;
4-207 4.30e-07

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 49.57  E-value: 4.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNIRHIIA-TARDVEKATDLKAISdPRVTALQLEVT----CDKSMDTFVSKVEEIvg 78
Cdd:PRK08628   8 KVVIVTGGASGIGAAISLRLAEEGAIPVIFGrSAPDDEFAEELRALQ-PRAEFVQVDLTddaqCRDAVEQTVAKFGRI-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 sDGlnlLVNNAGnaVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLlikasskvsgdqLSASRAAVVTISSGLAsmt 158
Cdd:PRK08628  85 -DG---LVNNAG--VNDGVGLEAGREAFVASLERNLIHYYVMAHYCLPH------------LKASRGAIVNISSKTA--- 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17558990  159 dfATG-GhapNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK08628 144 --LTGqG---GTSGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMT 188
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
4-202 4.33e-07

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 50.23  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKA--ISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdG 81
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEG--ACVVLADLDEEAAEAAAAelGGPDRALGVACDVTDEAAVQAAFEEAALAFG--G 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAVdypckAKPN----RALFAEQLNVNTTSVVILTQKLMPLLIKAssKVSGDqlsasraaVVTISSGLAsm 157
Cdd:PRK08324 499 VDIVVSNAGIAI-----SGPIeetsDEDWRRSFDVNATGHFLVAREAVRIMKAQ--GLGGS--------IVFIASKNA-- 561

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 17558990  158 tdFATGghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGP 202
Cdd:PRK08324 562 --VNPG---PNFGAYGAAKAAELHLVRQLALELGPDGIRVNGVNP 601
PRK07775 PRK07775
SDR family oxidoreductase;
6-210 4.65e-07

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 49.75  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    6 VVITGANRGIGLGLVQEFVKDKnirHIIAT-ARDVEKATDL--KAISDP-RVTALQLEVTCDKSMDTFVSKVEEIVGSdg 81
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAG---FPVALgARRVEKCEELvdKIRADGgEAVAFPLDVTDPDSVKSFVAQAEEALGE-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAvdYPCKA-KPNRALFAEQLNVNttsvVILTQKLmpllikaSSKVSGDQLSASRAAVVTISSGLASMtdf 160
Cdd:PRK07775  88 IEVLVSGAGDT--YFGKLhEISTEQFESQVQIH----LVGANRL-------ATAVLPGMIERRRGDLIFVGSDVALR--- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17558990  161 atggHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMG 210
Cdd:PRK07775 152 ----QRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMG 197
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 4-202 5.03e-07

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: 49.31  E-value: 5.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDL--KAISDPRVTALQLEVTCDksmDTFVSKVEEIVGS-D 80
Cdd:cd08943   2 KVALVTGGASGIGLAIAKRLAAEGA--AVVVADIDPEIAEKVaeAAQGGPRALGVQCDVTSE---AQVQSAFEQAVLEfG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 GLNLLVNNAGNAVDYPCkAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKAssKVSGDQL-SASRAAVvtissglasmtd 159
Cdd:cd08943  77 GLDIVVSNAGIATSSPI-AETSLEDWNRSMDINLTGHFLVSREAFRIMKSQ--GIGGNIVfNASKNAV------------ 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17558990 160 fATGghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGP 202
Cdd:cd08943 142 -APG---PNAAAYSAAKAAEAHLARCLALEGGEDGIRVNTVNP 180
PRK08589 PRK08589
SDR family oxidoreductase;
4-207 5.66e-07

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 49.39  E-value: 5.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAISDP--RVTALQLEVTCDKSMDTFVSKVEEIVGSdg 81
Cdd:PRK08589   7 KVAVITGASTGIGQASAIALAQEG--AYVLAVDIAEAVSETVDKIKSNggKAKAYHVDISDEQQVKDFASEIKEQFGR-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGnaVD--------YPCKakpnraLFAEQLNVNTTSVVILTQKLMPLLIKASSKVsgdqlsasraaVVTIS-S 152
Cdd:PRK08589  83 VDVLFNNAG--VDnaagriheYPVD------VFDKIMAVDMRGTFLMTKMLLPLMMEQGGSI-----------INTSSfS 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  153 GLASmtDFATGGhapnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK08589 144 GQAA--DLYRSG-------YNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIET 189
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 2-227 5.67e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 48.94  E-value: 5.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    2 SPKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAISDPRVtaLQLEVTCDKSMDtfvskvEEIVGSDG 81
Cdd:PRK07060   8 SGKSVLVTGASSGIGRACAVALAQRG--ARVVAAARNAAALDRLAGETGCEP--LRLDVGDDAAIR------AALAAAGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAVdypckAKPNRALFAEQ----LNVNTTSVVILTQKLMPLLIKAsskvsgdqlsASRAAVVTISSgLASM 157
Cdd:PRK07060  78 FDGLVNCAGIAS-----LESALDMTAEGfdrvMAVNARGAALVARHVARAMIAA----------GRGGSIVNVSS-QAAL 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  158 TDFatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMgGEKALLTVEQSTAELVA 227
Cdd:PRK07060 142 VGL------PDHLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPM-AAEAWSDPQKSGPMLAA 204
PRK08267 PRK08267
SDR family oxidoreductase;
3-209 7.31e-07

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 48.78  E-value: 7.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    3 PKSVVITGANRGIGLGLVQEFVK--------DKNIRHIIATARDvekatdlkaISDPRVTALQLEVT----CDKSMDTFV 70
Cdd:PRK08267   1 MKSIFITGAASGIGRATALLFAAegwrvgayDINEAGLAALAAE---------LGAGNAWTGALDVTdraaWDAALADFA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   71 SkveeivGSDG-LNLLVNNAGNAVDYPCKAKPNRALFAeQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVT 149
Cdd:PRK08267  72 A------ATGGrLDVLFNNAGILRGGPFEDIPLEAHDR-VIDINVKGVLNGAHAALPYLKATPG-----------ARVIN 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  150 ISSglASmtdfATGGhAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK08267 134 TSS--AS----AIYG-QPGLAVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAM 186
PRK07201 PRK07201
SDR family oxidoreductase;
4-209 7.42e-07

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 49.56  E-value: 7.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNIrhIIATARDVEKATDLKA-ISDP--RVTALQLEVTCDKSMDTFvskVEEIVGS- 79
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGAT--VFLVARNGEALDELVAeIRAKggTAHAYTCDLTDSAAVDHT---VKDILAEh 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   80 DGLNLLVNNAGNAVDYPCKAKPNRAL-FAEQLNVNTTSVVILTQKLMPLLIKassKVSGDqlsasraaVVTISSglasmt 158
Cdd:PRK07201 447 GHVDYLVNNAGRSIRRSVENSTDRFHdYERTMAVNYFGAVRLILGLLPHMRE---RRFGH--------VVNVSS------ 509

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17558990  159 dFATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK07201 510 -IGVQTNAPRFSAYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPM 559
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 4-203 8.01e-07

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: 48.43  E-value: 8.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKnIRHIIATARDVEKATDLKA---ISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSd 80
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEG-YRVVVHYNRSEAEAQRLKDelnALRNSAVLVQADLSDFAACADLVAAAFRAFGR- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 gLNLLVNNAGNAVDYPCKAKPNRALfAEQLNVNTTSVVILTQKLMPLLikasskvsgdqLSASRAAVVTISSglaSMTDF 160
Cdd:cd05357  79 -CDVLVNNASAFYPTPLGQGSEDAW-AELFGINLKAPYLLIQAFARRL-----------AGSRNGSIINIID---AMTDR 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17558990 161 ATGGHapnaFAYRISKAAINMFGRALANDMKDDhILVASIGPG 203
Cdd:cd05357 143 PLTGY----FAYCMSKAALEGLTRSAALELAPN-IRVNGIAPG 180
PRK05993 PRK05993
SDR family oxidoreductase;
4-207 8.97e-07

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 48.87  E-value: 8.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARdveKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsDGLN 83
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDG--WRVFATCR---KEEDVAALEAEGLEAFQLDYAEPESIAALVAQVLELSG-GRLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNN-----AGNAVDYPCKAkpnralFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLasmt 158
Cdd:PRK05993  79 ALFNNgaygqPGAVEDLPTEA------LRAQFEANFFGWHDLTRRVIPVMRKQGQ-----------GRIVQCSSIL---- 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17558990  159 dfatgGHAPNAF--AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK05993 138 -----GLVPMKYrgAYNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIET 183
PRK12742 PRK12742
SDR family oxidoreductase;
4-209 9.18e-07

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 48.60  E-value: 9.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKD-KNIRHIIATARDveKATDLKAisDPRVTALQLEVTcdkSMDTFVSKVEEivgSDGL 82
Cdd:PRK12742   7 KKVLVLGGSRGIGAAIVRRFVTDgANVRFTYAGSKD--AAERLAQ--ETGATAVQTDSA---DRDAVIDVVRK---SGAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   83 NLLVNNAGNavdypckakpnrALFAEQLNVNTTSVviltQKLMPLLIKASSKVSgdqLSASR-----AAVVTISSGLASM 157
Cdd:PRK12742  77 DILVVNAGI------------AVFGDALELDADDI----DRLFKINIHAPYHAS---VEAARqmpegGRIIIIGSVNGDR 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17558990  158 TDFATGGhapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK12742 138 MPVAGMA------AYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDA 183
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 4-209 9.75e-07

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 48.46  E-value: 9.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDkNIRHIIATARDVEKATDL-KAISDP--RVTALQLEVTcdkSMDTFVSKVEEIVGSD 80
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQE-GAKVVINYNSSKEAAENLvNELGKEghDVYAVQADVS---KVEDANRLVEEAVNHF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 G-LNLLVNNAGNAVDYPCKaKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLASMTD 159
Cdd:PRK12935  83 GkVDILVNNAGITRDRTFK-KLNREDWERVIDVNLSSVFNTTSAVLPYITEAEE-----------GRIISISSIIGQAGG 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17558990  160 FATGGhapnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK12935 151 FGQTN-------YSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEM 193
PRK06172 PRK06172
SDR family oxidoreductase;
2-209 9.79e-07

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 48.59  E-value: 9.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    2 SPKSVVITGANRGIGLGLVQEFVKdKNIRHIIATARDVEKATDLKAISDPRVTAL--QLEVTCDKSMDTFVSKVEEIVGS 79
Cdd:PRK06172   6 SGKVALVTGGAAGIGRATALAFAR-EGAKVVVADRDAAGGEETVALIREAGGEALfvACDVTRDAEVKALVEQTIAAYGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   80 dgLNLLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGlasmtd 159
Cdd:PRK06172  85 --LDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGG-----------GAIVNTASV------ 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17558990  160 fATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK06172 146 -AGLGAAPKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM 194
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 7-209 1.10e-06

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: 48.30  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   7 VITGANRGIGLGLVQEFVKdKNIRhIIATARDVEK-ATDLKAISDP--RVTALQLEVTCDKSMDTFVSKVEEIVGSdgLN 83
Cdd:cd08945   7 LVTGATSGIGLAIARRLGK-EGLR-VFVCARGEEGlATTVKELREAgvEADGRTCDVRSVPEIEALVAAAVARYGP--ID 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAvDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLlikasskvsGDQLSASRAAVVTISSglasmtdfaTG 163
Cdd:cd08945  83 VLVNNAGRS-GGGATAELADELWLDVVETNLTGVFRVTKEVLKA---------GGMLERGTGRIINIAS---------TG 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17558990 164 GHAPNAFA--YRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd08945 144 GKQGVVHAapYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPM 191
PRK08017 PRK08017
SDR family oxidoreductase;
4-207 1.14e-06

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 48.16  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARdveKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSDgLN 83
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRG--YRVLAACR---KPDDVARMNSLGFTGILLDLDDPESVERAADEVIALTDNR-LY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGNAVDYPCKAKpNRALFAEQLNVNTTSVVILTQKLMPLLikasskvsgdqLSASRAAVVTISS--GLASmtdfa 161
Cdd:PRK08017  77 GLFNNAGFGVYGPLSTI-SRQQMEQQFSTNFFGTHQLTMLLLPAM-----------LPHGEGRIVMTSSvmGLIS----- 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17558990  162 tgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK08017 140 ----TPGRGAYAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRT 181
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-209 1.54e-06

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 48.29  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATarDVEKA-TDLKAISDpRV--TALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:PRK08261 211 KVALVTGAARGIGAAIAEVLARDG--AHVVCL--DVPAAgEALAAVAN-RVggTALALDITAPDAPARIAEHLAERHG-- 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAGNAVDypcK--AKPNRALFAEQLNVNTTSVVILTQKLMpllikaSSKVSGDQlsasrAAVVTISS--GLA- 155
Cdd:PRK08261 284 GLDIVVHNAGITRD---KtlANMDEARWDSVLAVNLLAPLRITEALL------AAGALGDG-----GRIVGVSSisGIAg 349

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990  156 --SMTDFATgghapnafayriSKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK08261 350 nrGQTNYAA------------SKAGVIGLVQALAPLLAERGITINAVAPGFIETQM 393
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 1-214 1.83e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 47.73  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKdKNIRhIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAA-KGAR-VALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFG-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAG-----NAVDYPckakpnRALFAEQLNVNTTSVVILTQKLMPLLIKASskvSGDQLS-ASRAAVVTISsgl 154
Cdd:PRK06841  89 RIDILVNSAGvallaPAEDVS------EEDWDKTIDINLKGSFLMAQAVGRHMIAAG---GGKIVNlASQAGVVALE--- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  155 asmtdfatgGHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMG-----GEKA 214
Cdd:PRK06841 157 ---------RHV----AYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGkkawaGEKG 208
PRK05867 PRK05867
SDR family oxidoreductase;
1-209 1.97e-06

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 47.72  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKatdLKAISDpRVTAL---QLEVTCDKSM-DTFVSKVEEI 76
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAG--AQVAIAARHLDA---LEKLAD-EIGTSggkVVPVCCDVSQhQQVTSMLDQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   77 VGS-DGLNLLVNNAGNAVDYPCKAKPnRALFAEQLNVNTTSVVILTQklmpllikasskvsgdqlSASRAaVVTISSGLA 155
Cdd:PRK05867  81 TAElGGIDIAVCNAGIITVTPMLDMP-LEEFQRLQNTNVTGVFLTAQ------------------AAAKA-MVKQGQGGV 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990  156 SMTDFATGGHAPN----AFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK05867 141 IINTASMSGHIINvpqqVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 4-209 2.08e-06

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 47.48  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKdkniRH--IIATARDVEKATD-LKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAA----RGarVALIGRGAAPLSQtLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAGnAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLASMTDF 160
Cdd:PRK12828  82 RLDALVNIAG-AFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGG-----------GRIVNIGAGAALKAGP 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17558990  161 ATGghapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK12828 150 GMG-------AYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPP 191
PRK06128 PRK06128
SDR family oxidoreductase;
1-207 2.47e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 47.55  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVK---DKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFARegaDIALNYLPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKEL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   78 GsdGLNLLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSKVSGDQLSASRAAvvtissglASM 157
Cdd:PRK06128 133 G--GLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGASIINTGSIQSYQPS--------PTL 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17558990  158 TDFATgghapnafayriSKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK06128 203 LDYAS------------TKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWT 240
PRK06500 PRK06500
SDR family oxidoreductase;
4-211 2.73e-06

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 47.26  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:PRK06500   7 KTALITGGTSGIGLETARQFLAEG--ARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFG--RLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGNAVDYPCKAKpNRALFAEQLNVNTTSVVILTQKLMPLLIKASSKVsgdqLSASRAAVVtissGLasmtdfatg 163
Cdd:PRK06500  83 AVFINAGVAKFAPLEDW-DEAMFDRSFNTNVKGPYFLIQALLPLLANPASIV----LNGSINAHI----GM--------- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 17558990  164 ghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGG 211
Cdd:PRK06500 145 ---PNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYG 189
PRK05854 PRK05854
SDR family oxidoreductase;
1-186 2.85e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 47.37  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVqefvkdkniRHIIATARDV----------EKATDL--KAISDPRVTALQLEVTCDKSmdt 68
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLA---------RRLAAAGAEVilpvrnrakgEAAVAAirTAVPDAKLSLRALDLSSLAS--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   69 fVSKVEEIVGSDG--LNLLVNNAGnaVDYPckakPNRAL----FAEQLNVNTTSVVILTQKLMPLLIKASSKV-SGDQLS 141
Cdd:PRK05854  80 -VAALGEQLRAEGrpIHLLINNAG--VMTP----PERQTtadgFELQFGTNHLGHFALTAHLLPLLRAGRARVtSQSSIA 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17558990  142 ASRAAV----VTISSGLASMTdfatgghapnafAYRISKAAINMFGRAL 186
Cdd:PRK05854 153 ARRGAInwddLNWERSYAGMR------------AYSQSKIAVGLFALEL 189
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 4-207 2.95e-06

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: 47.51  E-value: 2.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKdKNIRHIIATARDVEKATDLKA---ISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSd 80
Cdd:cd09810   2 GTVVITGASSGLGLAAAKALAR-RGEWHVVMACRDFLKAEQAAQevgMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRP- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 gLNLLVNNAGnaVDYPCKAKPNRAL--FAEQLNVNTTSVVILTQKLMPLLIKASSK-------VSGDQLSASRAAVVTIS 151
Cdd:cd09810  80 -LDALVCNAA--VYLPTAKEPRFTAdgFELTVGVNHLGHFLLTNLLLEDLQRSENAsprivivGSITHNPNTLAGNVPPR 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990 152 SGLASMTDFATGGHAPN----------AFAYRISKAAINMFGRALANDMKDDH-ILVASIGPGWVKT 207
Cdd:cd09810 157 ATLGDLEGLAGGLKGFNsmidggefegAKAYKDSKVCNMLTTYELHRRLHEETgITFNSLYPGCIAE 223
PRK07577 PRK07577
SDR family oxidoreductase;
1-209 3.51e-06

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 46.64  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEK-------ATDLkaiSDPRVTALQLevtcdksmdtfvskv 73
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGH--QVIGIARSAIDdfpgelfACDL---ADIEQTAATL--------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   74 EEIVGSDGLNLLVNNAGNAVDYPCKAKPNRALFAeQLNVNTTSVVILTQKLMPllikaSSKVSGdqlsASRaaVVTISSg 153
Cdd:PRK07577  61 AQINEIHPVDAIVNNVGIALPQPLGKIDLAALQD-VYDLNVRAAVQVTQAFLE-----GMKLRE----QGR--IVNICS- 127

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990  154 lasmtdFATGGhAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK07577 128 ------RAIFG-ALDRTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-208 4.10e-06

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 46.64  E-value: 4.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKD-KNIRHIIATARDV--EKATDLKAISdPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEgYDIAVNYARSRKAaeETAEEIEALG-RKALAVKANVGDVEKIKEMFAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   78 GsdGLNLLVNNAGNAVDYPckakpnrALFAEQ------LNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTIS 151
Cdd:PRK08063  81 G--RLDVFVNNAASGVLRP-------AMELEEshwdwtMNINAKALLFCAQEAAKLMEKVGG-----------GKIISLS 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990  152 SglasmtdFATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTD 208
Cdd:PRK08063 141 S-------LGSIRYLENYTTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 7-209 4.23e-06

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 46.78  E-value: 4.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    7 VITGANRGIGLGLVQEFVKdKNIrHIIATARDVEKATDLKAISDPRVTALQLE-VTCDKS--MDTFVSKVEEIVGSDGLN 83
Cdd:PLN02780  57 LVTGPTDGIGKGFAFQLAR-KGL-NLVLVARNPDKLKDVSDSIQSKYSKTQIKtVVVDFSgdIDEGVKRIKETIEGLDVG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   84 LLVNNAGnaVDYPCKA---KPNRALFAEQLNVNTTSVVILTQKLMPLLIKASskvsgdqlsasRAAVVTISSGLASMTDf 160
Cdd:PLN02780 135 VLINNVG--VSYPYARffhEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRK-----------KGAIINIGSGAAIVIP- 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17558990  161 atggHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PLN02780 201 ----SDPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKM 245
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-208 4.25e-06

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 46.44  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKNIRHIIATARDVEKATDLKAISDpRVTALQLEVTCDKSMDTFVSKVEEIVGSd 80
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQVEALGR-KFHFITADLIQQKDIDSIVSQAVEVMGH- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 gLNLLVNNAGnavdypCKAKPNRALFAEQ-----LNVNTTSVVILTQKLMPLLIKasskvsgdqlSASRAAVVTIssglA 155
Cdd:PRK12481  84 -IDILINNAG------IIRRQDLLEFGNKdwddvININQKTVFFLSQAVAKQFVK----------QGNGGKIINI----A 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17558990  156 SMTDFATGGHAPnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTD 208
Cdd:PRK12481 143 SMLSFQGGIRVP---SYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 6-209 4.60e-06

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: 46.42  E-value: 4.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRGIGLGLVQEFVkdkniRH---IIATARDVEKatdLKAISD---------PRVTALQLEVTCDKSMDTFVSKV 73
Cdd:cd05340   7 ILVTGASDGIGREAALTYA-----RYgatVILLGRNEEK---LRQVADhineeggrqPQWFILDLLTCTSENCQQLAQRI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  74 EEIVGSdgLNLLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSg 153
Cdd:cd05340  79 AVNYPR--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDA-----------GSLVFTSS- 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990 154 lasmtdfaTGGHAPNAF--AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd05340 145 --------SVGRQGRANwgAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAM 194
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 2-208 4.74e-06

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: 46.35  E-value: 4.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   2 SPKSVVITGANRGIGLGLVQEFVKdKNIRhIIATARDVEK----ATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:cd05343   5 RGRVALVTGASVGIGAAVARALVQ-HGMK-VVGCARRVDKiealAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  78 GsdGLNLLVNNAGNAVDYPCKAKPNRAlFAEQLNVNTTSVVILTQklmpLLIKASSKVSGDqlsasRAAVVTISSglasm 157
Cdd:cd05343  83 Q--GVDVCINNAGLARPEPLLSGKTEG-WKEMFDVNVLALSICTR----EAYQSMKERNVD-----DGHIININS----- 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990 158 tdfaTGGH----APNAFAYRISKAAINMFGRALANDM--KDDHILVASIGPGWVKTD 208
Cdd:cd05343 146 ----MSGHrvppVSVFHFYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETE 198
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 4-209 5.34e-06

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: 46.29  E-value: 5.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVkdKNIRHIIATARDVEKATDLKAISDP-RVTALQLEVTcDK-----SMDTFVSKVeeiv 77
Cdd:cd08931   1 KAIFITGAASGIGRETALLFA--RNGWFVGLYDIDEDGLAALAAELGAeNVVAGALDVT-DRaawaaALADFAAAT---- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  78 gSDGLNLLVNNAGNAVDYPCKAKPNRALFAeQLNVNTTSVVILTQKLMPLLIKAsskvsgdqlSASRAAVVTISSGLASM 157
Cdd:cd08931  74 -GGRLDALFNNAGVGRGGPFEDVPLAAHDR-MVDINVKGVLNGAYAALPYLKAT---------PGARVINTASSSAIYGQ 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17558990 158 TDFATgghapnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd08931 143 PDLAV---------YSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPI 185
PRK05855 PRK05855
SDR family oxidoreductase;
1-208 5.60e-06

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 46.90  E-value: 5.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVkdkniRH---IIATARD---VEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVE 74
Cdd:PRK05855 313 FSGKLVVVTGAGSGIGRETALAFA-----REgaeVVASDIDeaaAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVR 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   75 EIVGsdGLNLLVNNAG-----NAVDYPckakpnralfAEQ----LNVNTTSVViltqklmpllikasskvSGDQLSASRa 145
Cdd:PRK05855 388 AEHG--VPDIVVNNAGigmagGFLDTS----------AEDwdrvLDVNLWGVI-----------------HGCRLFGRQ- 437

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  146 avvtissglasMTDFATGGHAPN-----AF-------AYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTD 208
Cdd:PRK05855 438 -----------MVERGTGGHIVNvasaaAYapsrslpAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTN 501
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 4-153 5.79e-06

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 46.05  E-value: 5.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNIRHIIatARDVEKATDLKA-----ISDPRVTALQLEVTCDKSMDTFVSKVEEivG 78
Cdd:cd09808   2 RSFLITGANSGIGKAAALAIAKRGGTVHMV--CRNQTRAEEARKeieteSGNQNIFLHIVDMSDPKQVWEFVEEFKE--E 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  79 SDGLNLLVNNAGNAVDypcKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsaSRaaVVTISSG 153
Cdd:cd09808  78 GKKLHVLINNAGCMVN---KRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEED---------PR--VITVSSG 138
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 4-221 6.02e-06

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 46.19  E-value: 6.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKAISDPRVTALQLEVTCdksMDTFVSKVEEIVGSDG-L 82
Cdd:cd05348   5 EVALITGGGSGLGRALVERFVAEG--AKVAVLDRSAEKVAELRADFGDAVVGVEGDVRS---LADNERAVARCVERFGkL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  83 NLLVNNAG------NAVDYPckAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSKVsgdqlsasraaVVTISSglas 156
Cdd:cd05348  80 DCFIGNAGiwdystSLVDIP--EEKLDEAFDELFHINVKGYILGAKAALPALYATEGSV-----------IFTVSN---- 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558990 157 mTDFATGGHAPnafAYRISKAAINMFGRALANDMKdDHILVASIGPGWVKTDMGGEKALLTVEQS 221
Cdd:cd05348 143 -AGFYPGGGGP---LYTASKHAVVGLVKQLAYELA-PHIRVNGVAPGGMVTDLRGPASLGQGETS 202
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 4-213 7.77e-06

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: 45.84  E-value: 7.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDK-----NIR-HIIATARDVEKATDLKAisdpRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:cd05358   4 KVALVTGASSGIGKAIAIRLATAGanvvvNYRsKEDAAEEVVEEIKAVGG----KAIAVQADVSKEEDVVALFQSAIKEF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  78 GSdgLNLLVNNAGnaVDYPCkakPNRALFAEQ----LNVNTTSVVILTQKLMPLLIKasSKVSGdqlsasraAVVTISSg 153
Cdd:cd05358  80 GT--LDILVNNAG--LQGDA---SSHEMTLEDwnkvIDVNLTGQFLCAREAIKRFRK--SKIKG--------KIINMSS- 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 154 laSMTDFATGGHApnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEK 213
Cdd:cd05358 142 --VHEKIPWPGHV----NYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEA 195
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-210 8.03e-06

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 45.93  E-value: 8.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANR--GIGLGLVQEFVK-------------DKNIRHIIATARDVEKATDLKAiSDPRVTALQLEVTCDKSMDT 68
Cdd:PRK12859   7 KVAVVTGVSRldGIGAAICKELAEagadifftywtayDKEMPWGVDQDEQIQLQEELLK-NGVKVSSMELDLTQNDAPKE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   69 FVSKVEEIVGSDglNLLVNNAGNAVDypckaKPNRALFAEQL----NVNTTSVVILTQKLMPLLikasskvsgDQLSASR 144
Cdd:PRK12859  86 LLNKVTEQLGYP--HILVNNAAYSTN-----NDFSNLTAEELdkhyMVNVRATTLLSSQFARGF---------DKKSGGR 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990  145 aaVVTISSGLASmtdfatgGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGwvKTDMG 210
Cdd:PRK12859 150 --IINMTSGQFQ-------GPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPG--PTDTG 204
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-209 8.13e-06

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 45.65  E-value: 8.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKdkniRHIIATARDVEKATDlkaiSDPRVTALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVE----AGAKVIGFDQAFLTQ----EDYPFATFVLDVSDAAAVAQVCQRLLAETG-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAG----NAVDypckakpnrALFAEQ----LNVNTTSVVILTQKLMPllikasskvsgdQLSASRA-AVVTIS 151
Cdd:PRK08220  76 PLDVLVNAAGilrmGATD---------SLSDEDwqqtFAVNAGGAFNLFRAVMP------------QFRRQRSgAIVTVG 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  152 SGLAsmtdfatggHAP--NAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK08220 135 SNAA---------HVPriGMAAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDM 185
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 4-232 9.23e-06

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: 45.52  E-value: 9.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKdKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDksmDTFVSKVEEIVGSDG-L 82
Cdd:cd05326   5 KVAIITGGASGIGEATARLFAK-HGARVVIADIDDDAGQAVAAELGDPDISFVHCDVTVE---ADVRAAVDTAVARFGrL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  83 NLLVNNAGnAVDYPCKAKPNRAL--FAEQLNVNTTSVViltqklmpLLIKASSKVSGDQLSASRAAVVTISSglasmtdf 160
Cdd:cd05326  81 DIMFNNAG-VLGAPCYSILETSLeeFERVLDVNVYGAF--------LGTKHAARVMIPAKKGSIVSVASVAG-------- 143

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558990 161 ATGGHAPNafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKALLTVEQSTAELVASFNKL 232
Cdd:cd05326 144 VVGGLGPH--AYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEDEAIEEAVRGAANLK 213
PRK09186 PRK09186
flagellin modification protein A; Provisional
 4-206 1.20e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 45.37  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNIrhIIATARDVEKATDLK-----AISDPRVTALQLEVTCDKSMDTFVSKVEEIVG 78
Cdd:PRK09186   5 KTILITGAGGLIGSALVKAILEAGGI--VIAADIDKEALNELLeslgkEFKSKKLSLVELDITDQESLEEFLSKSAEKYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 SdgLNLLVNNAgnavdYP-CKAKPNRAL------FAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTIS 151
Cdd:PRK09186  83 K--IDGAVNCA-----YPrNKDYGKKFFdvslddFNENLSLHLGSSFLFSQQFAKYFKKQGG-----------GNLVNIS 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990  152 S--GLA----------SMTdfatgghapNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVK 206
Cdd:PRK09186 145 SiyGVVapkfeiyegtSMT---------SPVEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGIL 202
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-210 1.29e-05

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 45.10  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKNIRHIIATARDVEKATDLKAISDPRVTAL--QLEVTCDKSMDTFVSKVEEIVG 78
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIgvLADVSTREGCETLAKATIDRYG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 sdGLNLLVNNAGNAVDYPCKAKPNRaLFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasraaVVTISSgLASMT 158
Cdd:PRK06077  84 --VADILVNNAGLGLFSPFLNVDDK-LIDKHISTDFKSVIYCSQELAKEMREGGA-------------IVNIAS-VAGIR 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17558990  159 DFatgghaPNAFAYRISKAAINMFGRALANDMKDdHILVASIGPGWVKTDMG 210
Cdd:PRK06077 147 PA------YGLSIYGAMKAAVINLTKYLALELAP-KIRVNAIAPGFVKTKLG 191
PRK07069 PRK07069
short chain dehydrogenase; Validated
 8-226 1.33e-05

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 45.09  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    8 ITGANRGIGLG----LVQE----FVKDKNIRHIIAtardvEKATDLKAISDPRVT-ALQLEVTCDKSMDTFVSKVEEIVG 78
Cdd:PRK07069   4 ITGAAGGLGRAiarrMAEQgakvFLTDINDAAGLD-----AFAAEINAAHGEGVAfAAVQDVTDEAQWQALLAQAADAMG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 sdGLNLLVNNAGNAVDYP---CKAKPNRALFAeqlnVNTTSVVILTQKLMPLlikasskvsgdqLSASR-AAVVTISSgl 154
Cdd:PRK07069  79 --GLSVLVNNAGVGSFGAieqIELDEWRRVMA----INVESIFLGCKHALPY------------LRASQpASIVNISS-- 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  155 asmtdFATGGHAPNAFAYRISKAAINMFGRALANDMKDDHILVA--SIGPGWVKTDM-GGEKALLTVEQSTAELV 226
Cdd:PRK07069 139 -----VAAFKAEPDYTAYNASKAAVASLTKSIALDCARRGLDVRcnSIHPTFIRTGIvDPIFQRLGEEEATRKLA 208
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 2-236 1.73e-05

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 44.54  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    2 SPKSVVITGANRGIGLGLVQEFVKDKniRHIIATARdvekaTDLKAISDPR---VTALQLEVTCDKSMDTFVSKVEEIVg 78
Cdd:PRK06483   1 MPAPILITGAGQRIGLALAWHLLAQG--QPVIVSYR-----THYPAIDGLRqagAQCIQADFSTNAGIMAFIDELKQHT- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 sDGLNLLVNNAGNAVDYPCKAKPnRALFAEQLNVNTTSVVILTQKLMPLLIKASSKVsgdqlsasrAAVVTIssglasmT 158
Cdd:PRK06483  73 -DGLRAIIHNASDWLAEKPGAPL-ADVLARMMQIHVNAPYLLNLALEDLLRGHGHAA---------SDIIHI-------T 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  159 DFATGGHAPNAFAYRISKAAI-NM---FGRALANDMKddhilVASIGPGWVKTDMGG---------EKALLTVEQSTAEL 225
Cdd:PRK06483 135 DYVVEKGSDKHIAYAASKAALdNMtlsFAAKLAPEVK-----VNSIAPALILFNEGDdaayrqkalAKSLLKIEPGEEEI 209

                        250
                 ....*....|.
gi 17558990  226 VASFNKLNNSH 236
Cdd:PRK06483 210 IDLVDYLLTSC 220
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 4-202 2.00e-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: 44.36  E-value: 2.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKD-KNI--------RH------IIATARDVEKA--TDLKAISDPRVTAlQLEVTCDKSM 66
Cdd:cd09762   4 KTLFITGASRGIGKAIALKAARDgANVviaaktaePHpklpgtIYTAAEEIEAAggKALPCIVDIRDED-QVRAAVEKAV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  67 DTFvskveeivgsDGLNLLVNNA-----GNAVDYPCKAkpnralFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqls 141
Cdd:cd09762  83 EKF----------GGIDILVNNAsaislTGTLDTPMKR------YDLMMGVNTRGTYLCSKACLPYLKKSKN-------- 138

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558990 142 asrAAVVTISSGLaSMTDFATGGHApnafAYRISKAAINMFGRALANDMKDDHILVASIGP 202
Cdd:cd09762 139 ---PHILNLSPPL-NLNPKWFKNHT----AYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 4-215 2.86e-05

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 44.18  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVkDKNIRhIIATARDVEKATDLKAISDPRVTALQLEVTcdkSMDTFVSKVEEIVGSDG-L 82
Cdd:PRK06200   7 QVALITGGGSGIGRALVERFL-AEGAR-VAVLERSAEKLASLRQRFGDHVLVVEGDVT---SYADNQRAVDQTVDAFGkL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   83 NLLVNNAG------NAVDYPckakPNR--ALFAEQLNVNTTSVVIltqklmpllikaSSKVSGDQLSASRAAVV-TIS-S 152
Cdd:PRK06200  82 DCFVGNAGiwdyntSLVDIP----AETldTAFDEIFNVNVKGYLL------------GAKAALPALKASGGSMIfTLSnS 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17558990  153 GlasmtdFATGGHAPnafAYRISKAAINMFGRALANDMKDDhILVASIGPGWVKTDMGGEKAL 215
Cdd:PRK06200 146 S------FYPGGGGP---LYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLRGPASL 198
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 6-209 3.24e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 44.25  E-value: 3.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    6 VVITGANRGIGLGLVQEFVkDKNIRHIIAtARDVEKATD-----LKAISDPRVTALQLEVTcdkSMDTFVSKVEEIVGS- 79
Cdd:PRK06197  19 AVVTGANTGLGYETAAALA-AKGAHVVLA-VRNLDKGKAaaariTAATPGADVTLQELDLT---SLASVRAAADALRAAy 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   80 DGLNLLVNNAGnaVDYPCKAKpNRALFAEQLNVNTTSVVILTQKLMPLLIkassKVSGdqlsaSRaaVVTISSglasmtd 159
Cdd:PRK06197  94 PRIDLLINNAG--VMYTPKQT-TADGFELQFGTNHLGHFALTGLLLDRLL----PVPG-----SR--VVTVSS------- 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17558990  160 fatGGHAPNA---F-------------AYRISKAAINMFGRALANDMKDDH---ILVASiGPGWVKTDM 209
Cdd:PRK06197 153 ---GGHRIRAaihFddlqwerrynrvaAYGQSKLANLLFTYELQRRLAAAGattIAVAA-HPGVSNTEL 217
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-209 3.29e-05

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 43.80  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDK-NIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSdgL 82
Cdd:PRK08217   6 KVIVITGGAQGLGRAMAEYLAQKGaKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQ--L 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   83 NLLVNNAG--------NAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSKvsgdqlsasrAAVVTISSgl 154
Cdd:PRK08217  84 NGLINNAGilrdgllvKAKDGKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSK----------GVIINISS-- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  155 asmtdFATGGHAPNAfAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK08217 152 -----IARAGNMGQT-NYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEM 200
PRK05650 PRK05650
SDR family oxidoreductase;
4-210 3.62e-05

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 43.88  E-value: 3.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDkNIRHIIAtarDVEKAT---DLKAISDPRVTA--LQLEVTCDKSMDTFVSKVEEIVG 78
Cdd:PRK05650   1 NRVMITGAASGLGRAIALRWARE-GWRLALA---DVNEEGgeeTLKLLREAGGDGfyQRCDVRDYSQLTALAQACEEKWG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 sdGLNLLVNNAGNAvdypckakpNRALFAE--------QLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTI 150
Cdd:PRK05650  77 --GIDVIVNNAGVA---------SGGFFEElsledwdwQIAINLMGVVKGCKAFLPLFKRQKS-----------GRIVNI 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  151 SSGLASMtdfatggHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMG 210
Cdd:PRK05650 135 ASMAGLM-------QGPAMSSYNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLL 187
PRK05866 PRK05866
SDR family oxidoreductase;
4-209 3.88e-05

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 43.96  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARdveKATDLKAISDpRVTALQLE---VTCD----KSMDTFVSKVEEI 76
Cdd:PRK05866  41 KRILLTGASSGIGEAAAEQFARRG--ATVVAVAR---REDLLDAVAD-RITRAGGDamaVPCDlsdlDAVDALVADVEKR 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   77 VGsdGLNLLVNNAGNAVDYPCKAKPNRALFAEQ-LNVNTTSVVILTQKLMPLLIKASskvSGDQLSASRAAVVTISSGLA 155
Cdd:PRK05866 115 IG--GVDILINNAGRSIRRPLAESLDRWHDVERtMVLNYYAPLRLIRGLAPGMLERG---DGHIINVATWGVLSEASPLF 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17558990  156 SmtdfatgghapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK05866 190 S--------------VYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229
PRK06398 PRK06398
aldose dehydrogenase; Validated
 4-189 4.34e-05

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 43.67  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVkDKNIRHIiatardvekATDLKAISDPRVTALQLEVTcdkSMDTFVSKVEEIVGSDG-L 82
Cdd:PRK06398   7 KVAIVTGGSQGIGKAVVNRLK-EEGSNVI---------NFDIKEPSYNDVDYFKVDVS---NKEQVIKGIDYVISKYGrI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   83 NLLVNNAGNAVDYPCKAKPNRAlFAEQLNVNTTSVVILTQKLMPLLIKASSKVsgdqlsasraaVVTISSGLASMTdfat 162
Cdd:PRK06398  74 DILVNNAGIESYGAIHAVEEDE-WDRIINVNVNGIFLMSKYTIPYMLKQDKGV-----------IINIASVQSFAV---- 137

                        170       180
                 ....*....|....*....|....*..
gi 17558990  163 gghAPNAFAYRISKAAINMFGRALAND 189
Cdd:PRK06398 138 ---TRNAAAYVTSKHAVLGLTRSIAVD 161
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 4-213 5.12e-05

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: 43.34  E-value: 5.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVK--------DKNIRHIIATARDVEKATDLKAISdprvtalqleVTCDKSMDTFVSK-VE 74
Cdd:cd05369   4 KVAFITGGGTGIGKAIAKAFAElgasvaiaGRKPEVLEAAAEEISSATGGRAHP----------IQCDVRDPEAVEAaVD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  75 EIVGSDG-LNLLVNNA-GNavdYPCKAkpnralfaEQLNVNTTSVVI---------LTQKLMPLLIKASSKvsgdqlsas 143
Cdd:cd05369  74 ETLKEFGkIDILINNAaGN---FLAPA--------ESLSPNGFKTVIdidlngtfnTTKAVGKRLIEAKHG--------- 133

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 144 rAAVVTISSGLASmtdFATGGHAPNAFAyrisKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEK 213
Cdd:cd05369 134 -GSILNISATYAY---TGSPFQVHSAAA----KAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMER 195
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-226 5.29e-05

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 43.32  E-value: 5.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIG----LGLVQEFVKDKNIrHIIATARDVEKatdlkaisdprVTALQ---LEVTCD-KSMDTFVSKVEE 75
Cdd:PRK08993  11 KVAVVTGCDTGLGqgmaLGLAEAGCDIVGI-NIVEPTETIEQ-----------VTALGrrfLSLTADlRKIDGIPALLER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   76 IVGSDG-LNLLVNNAG-----NAVDypckakpnralFAEQ-----LNVNTTSVVILTQKLMPLLIKasskvsgdqlSASR 144
Cdd:PRK08993  79 AVAEFGhIDILVNNAGlirreDAIE-----------FSEKdwddvMNLNIKSVFFMSQAAAKHFIA----------QGNG 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  145 AAVVTIssglASMTDFATGGHAPnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDmgGEKALLTVEQSTAE 224
Cdd:PRK08993 138 GKIINI----ASMLSFQGGIRVP---SYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATN--NTQQLRADEQRSAE 208


                 ..
gi 17558990  225 LV 226
Cdd:PRK08993 209 IL 210
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 1-207 6.07e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 43.22  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEK----ATDLKAiSDPRVTALQLEVTCDKSMDTFVSKVEEI 76
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAG--AEVILNGRDPAKlaaaAESLKG-QGLSAHALAFDVTDHDAVRAAIDAFEAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   77 VGSdgLNLLVNNAGNAVDYPCKAKPNRAlFAEQLNVNTTSVVILTQKLMPLLIKasskvsgdqlsASRAAVVTISSglaS 156
Cdd:PRK07523  85 IGP--IDILVNNAGMQFRTPLEDFPADA-FERLLRTNISSVFYVGQAVARHMIA-----------RGAGKIINIAS---V 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17558990  157 MTDFATGGHAPnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK07523 148 QSALARPGIAP----YTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 1-207 6.44e-05

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 42.95  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKD-KNIrhIIATARDVEKATDLKAISDP--RVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEgAKV--VIADLNDEAAAAAAEALQKAggKAIGVAMDVTDEEAINAGIDYAVETF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   78 GsdGLNLLVNNAG-----NAVDYPCkakpnrALFAEQLNVNTTSVVILTQKLMPLLIKAS-------SKVSGDQLSASRA 145
Cdd:PRK12429  80 G--GVDILVNNAGiqhvaPIEDFPT------EKWKKMIAIMLDGAFLTTKAALPIMKAQGggriinmASVHGLVGSAGKA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17558990  146 AVVTISSGLASMTdfatgghapnafayriskaainmfgRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK12429 152 AYVSAKHGLIGLT-------------------------KVVALEGATHGVTVNAICPGYVDT 188
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 4-209 6.52e-05

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 43.17  E-value: 6.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKN-----IRHIIATARDVEKATDLKAISDPRVTALQLEVTcdkSMDTFVSKVEEIVG 78
Cdd:PRK12827   7 RRVLITGGSGGLGRAIAVRLAADGAdvivlDIHPMRGRAEADAVAAGIEAAGGKALGLAFDVR---DFAATRAALDAGVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 SDG-LNLLVNNAGNAVDypckaKPNRALFAEQ----LNVNTTSVVILTQKLMPLLIKASSKvsgdqlsasrAAVVTISSg 153
Cdd:PRK12827  84 EFGrLDILVNNAGIATD-----AAFAELSIEEwddvIDVNLDGFFNVTQAALPPMIRARRG----------GRIVNIAS- 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990  154 lasmtDFATGGHAPNAfAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK12827 148 -----VAGVRGNRGQV-NYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPM 197
PRK08340 PRK08340
SDR family oxidoreductase;
6-97 8.46e-05

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 42.87  E-value: 8.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    6 VVITGANRGIGLGLVQEFVKdKNIRHIIATA--RDVEKATD-LKAISDprVTALQLEVTCDKSMDTFVSKVEEIVGsdGL 82
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLK-KGARVVISSRneENLEKALKeLKEYGE--VYAVKADLSDKDDLKNLVKEAWELLG--GI 77

                         90
                 ....*....|....*
gi 17558990   83 NLLVNNAGNAVDYPC 97
Cdd:PRK08340  78 DALVWNAGNVRCEPC 92
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 4-209 8.56e-05

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: 42.82  E-value: 8.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKD-KNIrhiiaTARDVEKATDLKAISDP-------RVTALQLEVTCDKSMDTFVSKVEE 75
Cdd:cd08940   3 KVALVTGSTSGIGLGIARALAAAgANI-----VLNGFGDAAEIEAVRAGlaakhgvKVLYHGADLSKPAAIEDMVAYAQR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  76 IVGsdGLNLLVNNAGNAVDYPCKAKPnralfAEQLN----VNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTIS 151
Cdd:cd08940  78 QFG--GVDILVNNAGIQHVAPIEDFP-----TEKWDaiiaLNLSAVFHTTRLALPHMKKQGW-----------GRIINIA 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990 152 S--GLASmtdfatgghAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:cd08940 140 SvhGLVA---------SANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPL 190
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
1-209 1.31e-04

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 42.31  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKNIrhIIA-----TARDVEKATDLKAISDPRVtALQLEVTCDKSMDTFVSKVEE 75
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFK--VVAgcgpnSPRRVKWLEDQKALGFDFI-ASEGNVGDWDSTKAAFDKVKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   76 IVGSdgLNLLVNNAGNAVDYPCKaKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSGLA 155
Cdd:PRK12938  78 EVGE--IDVLVNNAGITRDVVFR-KMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGW-----------GRIINISSVNG 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17558990  156 SMTDFATGGhapnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK12938 144 QKGQFGQTN-------YSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDM 190
PRK08251 PRK08251
SDR family oxidoreductase;
4-209 1.42e-04

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 41.84  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKA-----ISDPRVTALQLEVTCDKSMDTFVSKVEEIVG 78
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKG--RDLALCARRTDRLEELKAellarYPGIKVAVAALDVNDHDQVFEVFAEFRDELG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   79 sdGLNLLVNNAGNAVDYPC---KAKPNRALfAEqlnvnTTSVVILTQklmpllIKASSKVSGDQlsaSRAAVVTISSGLA 155
Cdd:PRK08251  81 --GLDRVIVNAGIGKGARLgtgKFWANKAT-AE-----TNFVAALAQ------CEAAMEIFREQ---GSGHLVLISSVSA 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17558990  156 SMtdfatgGHAPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK08251 144 VR------GLPGVKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEM 191
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 4-89 1.53e-04

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: 41.83  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDkNIRHIIATARdVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd05363   4 KTALITGSARGIGRAFAQAYVRE-GARVAIADIN-LEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SID 79


                ....*.
gi 17558990  84 LLVNNA 89
Cdd:cd05363  80 ILVNNA 85
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-207 1.83e-04

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 41.61  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKdKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSd 80
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAR-EGARVVVNYHQSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGK- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAgnAVDY---PCKAKPNRALFAE----QLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSG 153
Cdd:PRK08642  81 PITTVVNNA--LADFsfdGDARKKADDITWEdfqqQLEGSVKGALNTIQAALPGMREQGF-----------GRIINIGTN 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17558990  154 LasMTDFATGGHapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK08642 148 L--FQNPVVPYH-----DYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 4-207 1.89e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 41.94  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKD-KNIrhIIATARDVEKATDLKAisdprvtALQLE-VTC-----DKSMDTFVSK-VEE 75
Cdd:PRK06701  47 KVALITGGDSGIGRAVAVLFAKEgADI--AIVYLDEHEDANETKQ-------RVEKEgVKCllipgDVSDEAFCKDaVEE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   76 IVGSDG-LNLLVNNAgnAVDYPckAKPNRALFAEQLN----VNTTSVVILTQKLMPLLIKASSKVSgdqlSASraavVTI 150
Cdd:PRK06701 118 TVRELGrLDILVNNA--AFQYP--QQSLEDITAEQLDktfkTNIYSYFHMTKAALPHLKQGSAIIN----TGS----ITG 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990  151 SSGLASMTDfatgghapnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK06701 186 YEGNETLID------------YSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWT 230
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 4-205 1.90e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 41.48  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARDVEKATDLKAISDP---RVTALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:PRK07890   6 KVVVVSGVGPGLGRTLAVRAARAGA--DVVLAARTAERLDEVAAEIDDlgrRALAVPTDITDEDQCANLVALALERFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAgnAVDYPCK--AKPNRALFAEQLNVNTTSVVILTQKLMPLLIKasskvsgdqlsaSRAAVVTISSGLA--S 156
Cdd:PRK07890  82 RVDALVNNA--FRVPSMKplADADFAHWRAVIELNVLGTLRLTQAFTPALAE------------SGGSIVMINSMVLrhS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17558990  157 MTDFAtgghapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWV 205
Cdd:PRK07890 148 QPKYG---------AYKMAKGALLAASQSLATELGPQGIRVNSVAPGYI 187
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 4-207 2.13e-04

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: 41.36  E-value: 2.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKDKNirHIIATARD---VEKATDLKAISDpRVTALQLEVTCDKSMDTFVSKVEEIVGSd 80
Cdd:cd08937   5 KVVVVTGAAQGIGRGVAERLAGEGA--RVLLVDRSelvHEVLAEILAAGD-AAHVHTADLETYAGAQGVVRAAVERFGR- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  81 gLNLLVNNAGNAVdypcKAKPNRALFAEQLNVNttsvviLTQKLMPLLIkASSKVSGDQLSASRAAVVTISSglasmtdF 160
Cdd:cd08937  81 -VDVLINNVGGTI----WAKPYEHYEEEQIEAE------IRRSLFPTLW-CCRAVLPHMLERQQGVIVNVSS-------I 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17558990 161 ATGG--HAPnafaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:cd08937 142 ATRGiyRIP----YSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEA 186
PRK06949 PRK06949
SDR family oxidoreductase;
1-209 2.36e-04

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 41.29  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQefVKDKNIRHIIATARDVEKATDLKA---ISDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQ--VLAQAGAKVVLASRRVERLKELRAeieAEGGAAHVVSLDVTDYQSIKAAVAHAETEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   78 GSdgLNLLVNNAG-NAVDYPCKAKPNRalFAEQLNVNTTSVVILTQKLMPLLIkASSKVSGDQLSASRaaVVTISS--GL 154
Cdd:PRK06949  85 GT--IDILVNNSGvSTTQKLVDVTPAD--FDFVFDTNTRGAFFVAQEVAKRMI-ARAKGAGNTKPGGR--IINIASvaGL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17558990  155 ASMtdfatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK06949 158 RVL---------PQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
4-209 3.44e-04

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 40.86  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDK--------NIRHIIATARDVEKATDlKAIsdprvtALQLEVTcdkSMDTFVSKVEE 75
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGfkvaivdyNEETAQAAADKLSKDGG-KAI------AVKADVS---DRDQVFAAVRQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   76 IVGSDG-LNLLVNNAGNAVDYPCKAKpNRALFAEQLNVNTTSVVILTQKlmplLIKASSKVS--GDQLSASRAAVVTISS 152
Cdd:PRK08643  73 VVDTFGdLNVVVNNAGVAPTTPIETI-TEEQFDKVYNINVGGVIWGIQA----AQEAFKKLGhgGKIINATSQAGVVGNP 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558990  153 GLAsmtdfatgghapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDM 209
Cdd:PRK08643 148 ELA---------------VYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPM 189
PRK07814 PRK07814
SDR family oxidoreductase;
7-222 3.73e-04

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 40.92  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    7 VITGANRGIGLGLVQEFVKDKNirHIIATARDVEkatDLKAISDpRVTAL---QLEVTCDKS-MDTFVSKVEEIVGSDG- 81
Cdd:PRK07814  14 VVTGAGRGLGAAIALAFAEAGA--DVLIAARTES---QLDEVAE-QIRAAgrrAHVVAADLAhPEATAGLAGQAVEAFGr 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAVDYPCKAKPNRALfAEQLNVNTTSVVILTQKLMPLLIKASSKVSgdqlsasraaVVTISSglaSMTDFA 161
Cdd:PRK07814  88 LDIVVNNVGGTMPNPLLSTSTKDL-ADAFTFNVATAHALTVAAVPLMLEHSGGGS----------VINISS---TMGRLA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17558990  162 TGGHApnafAYRISKAAINMFGRALANDMKdDHILVASIGPGWVKTD-----MGGEKALLTVEQST 222
Cdd:PRK07814 154 GRGFA----AYGTAKAALAHYTRLAALDLC-PRIRVNAIAPGSILTSalevvAANDELRAPMEKAT 214
PRK07062 PRK07062
SDR family oxidoreductase;
1-207 4.35e-04

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 40.80  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDLKA-----ISDPRVTALQLEVTCDKSMDTFVSKVEE 75
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAG--ASVAICGRDEERLASAEArlrekFPGARLLAARCDVLDEADVAAFAAAVEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   76 IVGsdGLNLLVNNAGNAVDYPCKAKPNRALFAEqLNVNTTSVVILTQKLMPLLiKASSKvsgdqlsasrAAVVTISSGLA 155
Cdd:PRK07062  84 RFG--GVDMLVNNAGQGRVSTFADTTDDAWRDE-LELKYFSVINPTRAFLPLL-RASAA----------ASIVCVNSLLA 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17558990  156 SMTDfatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:PRK07062 150 LQPE-------PHMVATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVES 194
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 4-90 5.33e-04

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 40.45  E-value: 5.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLG----LVQEFVKDKNIrHIIATARDVEKATD----LKAI---SDPRVTALQLEVTcdkSMDTFVSK 72
Cdd:cd08941   2 KVVLVTGANSGLGLAicerLLAEDDENPEL-TLILACRNLQRAEAacraLLAShpdARVVFDYVLVDLS---NMVSVFAA 77

                        90
                ....*....|....*....
gi 17558990  73 VEEIVGS-DGLNLLVNNAG 90
Cdd:cd08941  78 AKELKKRyPRLDYLYLNAG 96
PRK07856 PRK07856
SDR family oxidoreductase;
4-221 6.35e-04

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 39.92  E-value: 6.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKdknirhiiATARDVEKATDLKAISDPRVTALqleVTCD-KSMDTFVSKVEEIVGSDG- 81
Cdd:PRK07856   7 RVVLVTGGTRGIGAGIARAFLA--------AGATVVVCGRRAPETVDGRPAEF---HAADvRDPDQVAALVDAIVERHGr 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 LNLLVNNAGNAVDYPC-KAKPNraLFAEQLNVNTTSVVILTQKLMPLLikasskvsgdQLSASRAAVVTISSglasmtdf 160
Cdd:PRK07856  76 LDVLVNNAGGSPYALAaEASPR--FHEKIVELNLLAPLLVAQAANAVM----------QQQPGGGSIVNIGS-------- 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990  161 aTGGH--APNAFAYRISKAAINMFGRALANDMKDDhILVASIGPGWVKTDM-----GGEKALLTVEQS 221
Cdd:PRK07856 136 -VSGRrpSPGTAAYGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQselhyGDAEGIAAVAAT 201
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 4-210 1.30e-03

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: 39.19  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   4 KSVVITGANRGIGLGLVQEFVKdKNIRHIIATARDVEKATDLKAIsdPRVTALQLEVTCDKSMDTFVSKVEEIVGsdGLN 83
Cdd:cd05371   3 LVAVVTGGASGLGLATVERLLA-QGAKVVILDLPNSPGETVAKLG--DNCRFVPVDVTSEKDVKAALALAKAKFG--RLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  84 LLVNNAGNAV---DYPCKAKP--NRALFAEQLNVNttsvVILTQKLMPLLIKASSKVSGDQlSASRAAVVTIssglASMT 158
Cdd:cd05371  78 IVVNCAGIAVaakTYNKKGQQphSLELFQRVINVN----LIGTFNVIRLAAGAMGKNEPDQ-GGERGVIINT----ASVA 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17558990 159 DFAtgGHAPNAfAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMG 210
Cdd:cd05371 149 AFE--GQIGQA-AYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLL 197
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 1-212 1.71e-03

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 38.74  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEFVKDKNIRHIIATArdVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGsd 80
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTR--VEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLE-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   81 GLNLLVNNAGNAVDypckakpnrALFAEQ--------LNVNTTSVVILTQKLM-PLLIKASSKVsgdqlsasraavVTIS 151
Cdd:PRK12936  80 GVDILVNNAGITKD---------GLFVRMsdedwdsvLEVNLTATFRLTRELThPMMRRRYGRI------------INIT 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558990  152 SGLAsmtdfATGGhaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGE 212
Cdd:PRK12936 139 SVVG-----VTGN--PGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGK 192
PRK08278 PRK08278
SDR family oxidoreductase;
4-202 1.91e-03

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 38.73  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDK-NI--------RH------IIATARDVEKATDlKAIsdprvtALQLEVTCDKSMDT 68
Cdd:PRK08278   7 KTLFITGASRGIGLAIALRAARDGaNIviaaktaePHpklpgtIHTAAEEIEAAGG-QAL------PLVGDVRDEDQVAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   69 FVSKVEEIVGsdGLNLLVNNAG-----NAVDYPckakPNRalFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsas 143
Cdd:PRK08278  80 AVAKAVERFG--GIDICVNNASainltGTEDTP----MKR--FDLMQQINVRGTFLVSQACLPHLKKSEN---------- 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17558990  144 rAAVVTISSGLaSMTDFATGGHAPnafaYRISKAAINMFGRALANDMKDDHILVASIGP 202
Cdd:PRK08278 142 -PHILTLSPPL-NLDPKWFAPHTA----YTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 1-207 2.03e-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: 38.68  E-value: 2.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   1 MSPKSVVITGANRGIGLGLVQEFVKDKniRHIIATAR---DVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIV 77
Cdd:cd08936   8 LANKVALVTASTDGIGLAIARRLAQDG--AHVVVSSRkqqNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLH 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  78 GsdGLNLLVNNAGNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTISSgLASM 157
Cdd:cd08936  86 G--GVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGG-----------GSVVIVSS-VAAF 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17558990 158 TDFatgghaPNAFAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKT 207
Cdd:cd08936 152 HPF------PGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKT 195
PRK05717 PRK05717
SDR family oxidoreductase;
4-207 2.04e-03

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 38.72  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKniRHIIATARDVEKATDL-KAISDPrvtalQLEVTCDKSMDTFVSK-VEEIVGSDG 81
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEG--WQVVLADLDRERGSKVaKALGEN-----AWFIAMDVADEAQVAAgVAEVLGQFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   82 -LNLLVNNAGNAVDYpckakpNRALfaEQLNVNTTSVVILTQKLMPLLIkasSKVSGDQLSASRAAVVTISSGLASMTDf 160
Cdd:PRK05717  84 rLDALVCNAAIADPH------NTTL--ESLSLAHWNRVLAVNLTGPMLL---AKHCAPYLRAHNGAIVNLASTRARQSE- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17558990  161 atgghaPNAFAYRISKAAINMFGRALANDMKDDhILVASIGPGWVKT 207
Cdd:PRK05717 152 ------PDTEAYAASKGGLLALTHALAISLGPE-IRVNAVSPGWIDA 191
PRK09134 PRK09134
SDR family oxidoreductase;
2-203 2.30e-03

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 38.37  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    2 SPKSVVITGANRGIGLGLVQEFVK---DKNI--RHIIATARDVekATDLKAiSDPRVTALQLEVTCDKSMDTFVSKVEEI 76
Cdd:PRK09134   8 APRAALVTGAARRIGRAIALDLAAhgfDVAVhyNRSRDEAEAL--AAEIRA-LGRRAVALQADLADEAEVRALVARASAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   77 VGSdgLNLLVNNAgNAVDYPCKAKPNRALFAEQLNVNTTSVVILTQKLmpllikasskvsGDQLSASRAAVVT--ISSGL 154
Cdd:PRK09134  85 LGP--ITLLVNNA-SLFEYDSAASFTRASWDRHMATNLRAPFVLAQAF------------ARALPADARGLVVnmIDQRV 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17558990  155 ASMTdfatgghaPNAFAYRISKAAINMFGRALANDMKDDhILVASIGPG 203
Cdd:PRK09134 150 WNLN--------PDFLSYTLSKAALWTATRTLAQALAPR-IRVNAIGPG 189
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 4-158 2.61e-03

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 38.34  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGLGLVQEFVKDKNIRHIIATARD-VEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVGSdgL 82
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAGAAVAIADLNQDgANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGS--V 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   83 NLLVNNAGNAVDYPCKAKPnRALFAEQLNVNTTSVVILTQKLMPLLIKAS--------SKVSGDQLSASRAAVVTISSGL 154
Cdd:PRK13394  86 DILVSNAGIQIVNPIENYS-FADWKKMQAIHVDGAFLTTKAALKHMYKDDrggvviymGSVHSHEASPLKSAYVTAKHGL 164


                 ....
gi 17558990  155 ASMT 158
Cdd:PRK13394 165 LGLA 168
KR_fFAS_like_SDR_c_like cd08928
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c) ...
 6-220 3.26e-03

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c)-like SDRs; KR domain of FAS, including the fungal-type multidomain FAS alpha chain, and the single domain daunorubicin C-13 ketoreductase. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD(P)-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Single domain 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: 187633 [Multi-domain]  Cd Length: 248  Bit Score: 38.04  E-value: 3.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   6 VVITGANRG-IGLGLVQEFVkDKNIRHIIATARDVEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEEIVgsDGLNL 84
Cdd:cd08928   1 VLITGAGDGsIGAEVLQGLL-NGGAKVYVTTSRFSRQVTKYYQDIYAACGAAGSVLIVVPFNQGSKQDVEALA--IGIYD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990  85 LVNNAGNAVDY--PCKAKPNRALFAEQLN-VNTTSVVILTQKLMPL--LIKASSKVSGdQLSASRAAVVTISSGLASMTD 159
Cdd:cd08928  78 TVNGLGWDLDLygPFAAIPETGIEIPAIDsKSEVAHRIMLTNLLRPkgLVKIQKQLRG-QETRPAQVILPFSPNHGTFGD 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558990 160 FAtgghapnafAYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTDMGGEKALLTVEQ 220
Cdd:cd08928 157 DG---------AYSESKLHLETLFNRWASESWGNDLTVCGAHIGWTRGTLGGEAAPEGLEK 208
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 5-94 4.18e-03

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 37.75  E-value: 4.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   5 SVVITGANRGIGLGLVQEFVkDKNIRHIIATAR-----DVEKATDLKAISDPRVTALQLEVTCDKSMDTFvskVEEIVGS 79
Cdd:cd05274 152 TYLITGGLGGLGLLVARWLA-ARGARHLVLLSRrgpapRAAARAALLRAGGARVSVVRCDVTDPAALAAL---LAELAAG 227

                        90
                ....*....|....*
gi 17558990  80 DGLNLLVNNAGNAVD 94
Cdd:cd05274 228 GPLAGVIHAAGVLRD 242
PRK09135 PRK09135
pteridine reductase; Provisional
 1-203 5.47e-03

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 37.22  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    1 MSPKSVVITGANRGIGLGLVQEF-VKDKNI----RHIIATARdvEKATDLKAISDPRVTALQLEVTCDKSMDTFVSKVEE 75
Cdd:PRK09135   4 DSAKVALITGGARRIGAAIARTLhAAGYRVaihyHRSAAEAD--ALAAELNALRPGSAAALQADLLDPDALPELVAACVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   76 IVGsdGLNLLVNNAGNAVDYPCkAKPNRALFAEQLNVNTTSVVILTQKLMPllikasskvsgdQLSASRAAVVTIssgla 155
Cdd:PRK09135  82 AFG--RLDALVNNASSFYPTPL-GSITEAQWDDLFASNLKAPFFLSQAAAP------------QLRKQRGAIVNI----- 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17558990  156 smTDFatggHAPNAFA----YRISKAAINMFGRALANDMKdDHILVASIGPG 203
Cdd:PRK09135 142 --TDI----HAERPLKgypvYCAAKAALEMLTRSLALELA-PEVRVNAVAPG 186
PRK07774 PRK07774
SDR family oxidoreductase;
4-208 8.55e-03

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 36.65  E-value: 8.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990    4 KSVVITGANRGIGL----GLVQE----FVKDKNIRHIIATArdvekatdlKAISDPRVTAL--QLEVTCDKSMDTFVSKV 73
Cdd:PRK07774   7 KVAIVTGAAGGIGQayaeALAREgasvVVADINAEGAERVA---------KQIVADGGTAIavQVDVSDPDSAKAMADAT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558990   74 EEIVGsdGLNLLVNNA---GNAVDYPCKAKPNRaLFAEQLNVNTTSVVILTQKLMPLLIKASSkvsgdqlsasrAAVVTI 150
Cdd:PRK07774  78 VSAFG--GIDYLVNNAaiyGGMKLDLLITVPWD-YYKKFMSVNLDGALVCTRAVYKHMAKRGG-----------GAIVNQ 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17558990  151 SSglasmtdfaTGGHAPNAFaYRISKAAINMFGRALANDMKDDHILVASIGPGWVKTD 208
Cdd:PRK07774 144 SS---------TAAWLYSNF-YGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTE 191
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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