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Conserved domains on  [gi|748779139|ref|WP_040030568|]
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MULTISPECIES: SDR family oxidoreductase [Staphylococcus]

Protein Classification

SDR family oxidoreductase( domain architecture ID 11431150)

SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to the N-terminal domain of Ybjt, an atypical short chain dehydrogenase that has an HXXXR motif in place of the classical active site motif YXXXK; the NAD(P)-binding motif is similar to that of extended short chain dehydrogenases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
1-214 4.87e-42

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


:

Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 143.45  E-value: 4.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   1 MILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYYiCSAANPKED 80
Cdd:COG0702    1 KILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAAGV-EVVQGDLDDPESLAAALAGVDAVFL-LVPSGPGGD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  81 -----EIGEQMIQIAKKVGNIYFVYHSVLH-SVLQDMPHHKRKLHTEQLVVDSGLDFAIIQPAVFMQMLMPAVKSVQSGG 154
Cdd:COG0702   79 favdvEGARNLADAAKAAGVKRIVYLSALGaDRDSPSPYLRAKAAVEEALRASGLPYTILRPGWFMGNLLGFFERLRERG 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139 155 PMlqkFFTSDETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQNMEAVFSEV 214
Cdd:COG0702  159 VL---PLPAGDGRVQPIAVRDVAEAAAAALTDPGHAGRTYELGGPEALTYAELAAILSEA 215
 
Name Accession Description Interval E-value
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
1-214 4.87e-42

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 143.45  E-value: 4.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   1 MILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYYiCSAANPKED 80
Cdd:COG0702    1 KILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAAGV-EVVQGDLDDPESLAAALAGVDAVFL-LVPSGPGGD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  81 -----EIGEQMIQIAKKVGNIYFVYHSVLH-SVLQDMPHHKRKLHTEQLVVDSGLDFAIIQPAVFMQMLMPAVKSVQSGG 154
Cdd:COG0702   79 favdvEGARNLADAAKAAGVKRIVYLSALGaDRDSPSPYLRAKAAVEEALRASGLPYTILRPGWFMGNLLGFFERLRERG 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139 155 PMlqkFFTSDETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQNMEAVFSEV 214
Cdd:COG0702  159 VL---PLPAGDGRVQPIAVRDVAEAAAAALTDPGHAGRTYELGGPEALTYAELAAILSEA 215
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
2-275 3.54e-38

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 135.48  E-value: 3.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYYICSAANPKEDE 81
Cdd:cd05269    1 ILVTGATGKLGTAVVELLLAKVASVVALVRNPEKAKAFAADGV-EVRQGDYDDPETLERAFEGVDRLLLISPSDLEDRIQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  82 IGEQMIQIAKKVGNIYFVYHSVLH----SVLQDMPHHkrkLHTEQLVVDSGLDFAIIQPAVFMQMLMPAVKSVQSGGpml 157
Cdd:cd05269   80 QHKNFIDAAKQAGVKHIVYLSASGadedSPFLLARDH---GATEKYLEASGIPYTILRPGWFMDNLLEFLPSILEEG--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139 158 qKFFTSD-ETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQNMEAVFSEVAGREVKsaYI---TDEAFIGQM 233
Cdd:cd05269  154 -TIYGPAgDGKVAFVDRRDIAEAAAAALTEPGHEGKVYNLTGPEALSYAELAAILSEALGKPVR--YVpvsPDEAARELL 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 748779139 234 KIDASSYQAQTLLTMFRHYNEHSFRGNSVVLSQILRRDPHTL 275
Cdd:cd05269  231 AAGLPEGFAALLASLYAAIRKGELAVVSDDVEKLTGRPPRSL 272
NmrA pfam05368
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ...
2-220 2.06e-23

NmrA-like family; NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.


Pssm-ID: 398829 [Multi-domain]  Cd Length: 236  Bit Score: 95.49  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139    2 ILITGASGQVGCAVIRALSKVGIETKAFIHSAS--NIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYYICSAANPKE 79
Cdd:pfam05368   1 ILVFGATGQQGGSVVRASLKAGHKVRALVRDPKseLAKSLKEAGV-ELVKGDLDDKESLVEALKGVDVVFSVTGFWAGKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   80 DEIGEQMIQIAKKVGNIYFVYHSVL------HSVLQDMPHHKRKLHTEQLVVDSGLDFAIIQPAVFMQML--MPAVKSVQ 151
Cdd:pfam05368  80 IEDGKKLADAAKEAGVKHFIPSSFGndndisNGVEPAVPHFDSKAEIERYIRALGIPYTFVYAGFFMQNFlsLLAPLFPG 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748779139  152 SGGPMLQKF-----FTSDETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQNMEAVFSEVAGREVK 220
Cdd:pfam05368 160 DLSPPEDKFtllgpGNPKAVPLWMDDEHDIGTFVIAILDDPRKLKGKRIKLAGNTLSGNEIAELFSKKTGKTVK 233
ycf39 CHL00194
Ycf39; Provisional
2-203 1.12e-09

Ycf39; Provisional


Pssm-ID: 177093  Cd Length: 317  Bit Score: 58.09  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIR-ALSKvGIETKAFIHsasNIEK---VKEAGATEVFvGDMSEEKDLREALHGVdTVYYICSAANP 77
Cdd:CHL00194   3 LLVIGATGTLGRQIVRqALDE-GYQVRCLVR---NLRKasfLKEWGAELVY-GDLSLPETLPPSFKGV-TAIIDASTSRP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  78 KEDEIGEQ--------MIQIAKKVGNIYFVYHSVLHSVL-QDMPHHKRKLHTEQLVVDSGLDFAIIQPAVFMQMLMpavk 148
Cdd:CHL00194  77 SDLYNAKQidwdgklaLIEAAKAAKIKRFIFFSILNAEQyPYIPLMKLKSDIEQKLKKSGIPYTIFRLAGFFQGLI---- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 748779139 149 sVQSGGPMLQK---FFTSDETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYS 203
Cdd:CHL00194 153 -SQYAIPILEKqpiWITNESTPISYIDTQDAAKFCLKSLSLPETKNKTFPLVGPKSWN 209
 
Name Accession Description Interval E-value
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
1-214 4.87e-42

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 143.45  E-value: 4.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   1 MILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYYiCSAANPKED 80
Cdd:COG0702    1 KILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAAGV-EVVQGDLDDPESLAAALAGVDAVFL-LVPSGPGGD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  81 -----EIGEQMIQIAKKVGNIYFVYHSVLH-SVLQDMPHHKRKLHTEQLVVDSGLDFAIIQPAVFMQMLMPAVKSVQSGG 154
Cdd:COG0702   79 favdvEGARNLADAAKAAGVKRIVYLSALGaDRDSPSPYLRAKAAVEEALRASGLPYTILRPGWFMGNLLGFFERLRERG 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139 155 PMlqkFFTSDETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQNMEAVFSEV 214
Cdd:COG0702  159 VL---PLPAGDGRVQPIAVRDVAEAAAAALTDPGHAGRTYELGGPEALTYAELAAILSEA 215
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
2-275 3.54e-38

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 135.48  E-value: 3.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYYICSAANPKEDE 81
Cdd:cd05269    1 ILVTGATGKLGTAVVELLLAKVASVVALVRNPEKAKAFAADGV-EVRQGDYDDPETLERAFEGVDRLLLISPSDLEDRIQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  82 IGEQMIQIAKKVGNIYFVYHSVLH----SVLQDMPHHkrkLHTEQLVVDSGLDFAIIQPAVFMQMLMPAVKSVQSGGpml 157
Cdd:cd05269   80 QHKNFIDAAKQAGVKHIVYLSASGadedSPFLLARDH---GATEKYLEASGIPYTILRPGWFMDNLLEFLPSILEEG--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139 158 qKFFTSD-ETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQNMEAVFSEVAGREVKsaYI---TDEAFIGQM 233
Cdd:cd05269  154 -TIYGPAgDGKVAFVDRRDIAEAAAAALTEPGHEGKVYNLTGPEALSYAELAAILSEALGKPVR--YVpvsPDEAARELL 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 748779139 234 KIDASSYQAQTLLTMFRHYNEHSFRGNSVVLSQILRRDPHTL 275
Cdd:cd05269  231 AAGLPEGFAALLASLYAAIRKGELAVVSDDVEKLTGRPPRSL 272
NmrA_like_SDR_a cd05251
NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) ...
2-230 4.52e-37

NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) SDRs; NmrA and HSCARG like proteins. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187561 [Multi-domain]  Cd Length: 242  Bit Score: 131.63  E-value: 4.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKV-GIETKAFIHSASNiEKVKE--AGATEVFVGDMSEEKDLREALHGVDTVYYIC---SAA 75
Cdd:cd05251    1 ILVFGATGKQGGSVVRALLKDpGFKVRALTRDPSS-PAAKAlaAPGVEVVQGDLDDPESLEAALKGVYGVFLVTdfwEAG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  76 NPKEDEIGEQMIQIAKKVGNIYFVYHSVLHSVLQ--DMPHHKRKLHTEQLVVDSGLDFAIIQPAVFMQM-LMPAVKSVQS 152
Cdd:cd05251   80 GEDEIAQGKNVVDAAKRAGVQHFVFSSVPDVEKLtlAVPHFDSKAEVEEYIRASGLPATILRPAFFMENfLTPPAPQKME 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748779139 153 GGPMLQKFFTSDETQMSLVDMEDFAEAAAVILSN-KDYANGTFELCGkGSYSLQNMEAVFSEVAGREVksAYITDEAFI 230
Cdd:cd05251  160 DGTLTLVLPLDPDTKLPMIDVADIGPAVAAIFKDpAKFNGKTIELAG-DELTPEEIAAAFSKVLGKPV--TYVQVEEWL 235
NmrA_TMR_like_1_SDR_a cd05231
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ...
2-254 1.61e-27

NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187542 [Multi-domain]  Cd Length: 259  Bit Score: 107.03  E-value: 1.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYYICSAA--NPKE 79
Cdd:cd05231    1 ILVTGATGRIGSKVATTLLEAGRPVRALVRSDERAAALAARGA-EVVVGDLDDPAVLAAALAGVDAVFFLAPPAptADAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  80 D---EIGEQMIQIAKKVGNIYFVYHSVLHSVLQDMPHHKRKLH-TEQLVVDSGLDFAIIQPAVFMQMLMPAVKSVQSGGp 155
Cdd:cd05231   80 PgyvQAAEAFASALREAGVKRVVNLSSVGADPESPSGLIRGHWlMEQVLNWAGLPVVHLRPAWFMENLLSQAPSIRKAG- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139 156 MLQKFFTSDeTQMSLVDMEDFAEAAAVILSNKDYANG-TFELCGKGSYSLQNMEAVFSEVAGREVKSAYITDEAFIGQM- 233
Cdd:cd05231  159 VLALPFPGD-GRLPPIATDDIARVAAKLLLDPEWHGHrVYELTGPEDLTMNEIAAALSRVLGRPVRYVPVPEEQWEATLl 237
                        250       260
                 ....*....|....*....|.
gi 748779139 234 KIDASSYQAQTLLTMFRHYNE 254
Cdd:cd05231  238 SLGFSPEMAQHLSEMARAFNE 258
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
1-196 1.80e-23

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 94.61  E-value: 1.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   1 MILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVyYICSAANPKED 80
Cdd:cd05243    1 KVLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAAGA-EVVVGDLTDAESLAAALEGIDAV-ISAAGSGGKGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  81 EIGEQ--------MIQIAKKVGNIYFVYHSVL------HSVLQDMPHHKRKLHTEQLVVDSGLDFAIIQPAVFMQmLMPA 146
Cdd:cd05243   79 PRTEAvdydgninLIDAAKKAGVKRFVLVSSIgadkpsHPLEALGPYLDAKRKAEDYLRASGLDYTIVRPGGLTD-DPAG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 748779139 147 VKSVQsggpmlqkFFTSDETQMSLVDMEDFAEAAAVILSNKDYANGTFEL 196
Cdd:cd05243  158 TGRVV--------LGGDGTRLDGPISRADVAEVLAEALDTPAAIGKTFEL 199
NmrA pfam05368
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ...
2-220 2.06e-23

NmrA-like family; NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.


Pssm-ID: 398829 [Multi-domain]  Cd Length: 236  Bit Score: 95.49  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139    2 ILITGASGQVGCAVIRALSKVGIETKAFIHSAS--NIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYYICSAANPKE 79
Cdd:pfam05368   1 ILVFGATGQQGGSVVRASLKAGHKVRALVRDPKseLAKSLKEAGV-ELVKGDLDDKESLVEALKGVDVVFSVTGFWAGKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   80 DEIGEQMIQIAKKVGNIYFVYHSVL------HSVLQDMPHHKRKLHTEQLVVDSGLDFAIIQPAVFMQML--MPAVKSVQ 151
Cdd:pfam05368  80 IEDGKKLADAAKEAGVKHFIPSSFGndndisNGVEPAVPHFDSKAEIERYIRALGIPYTFVYAGFFMQNFlsLLAPLFPG 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748779139  152 SGGPMLQKF-----FTSDETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQNMEAVFSEVAGREVK 220
Cdd:pfam05368 160 DLSPPEDKFtllgpGNPKAVPLWMDDEHDIGTFVIAILDDPRKLKGKRIKLAGNTLSGNEIAELFSKKTGKTVK 233
NmrA_TMR_like_SDR_a cd08947
NmrA (a transcriptional regulator), HSCARG (an NADPH sensor), and triphenylmethane reductase ...
2-222 1.37e-19

NmrA (a transcriptional regulator), HSCARG (an NADPH sensor), and triphenylmethane reductase (TMR) like proteins, atypical (a) SDRs; Atypical SDRs belonging to this subgroup include NmrA, HSCARG, and TMR, these proteins bind NAD(P) but they lack the usual catalytic residues of the SDRs. Atypical SDRs are distinct from classical SDRs. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. TMR, an NADP-binding protein, lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187651 [Multi-domain]  Cd Length: 224  Bit Score: 84.90  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGI-ETKAFIHSASNIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYYICS--AANPK 78
Cdd:cd08947    1 IAVTGATGQQGGSVIRHLLAKGAsQVRAVVRNVEKAATLADQGV-EVRQGDYNQPELLQKAFAGASKLFIITGphYDNTL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  79 EDEIGEQMIQIAKKVGNIYFVYHSVLHSVLQDMPHHKRKLHTEQLVVDSGLDFAIIQPAVFMQMLMPAVKSVQSGGPMLQ 158
Cdd:cd08947   80 EIKQGKNVADAARRAGVKHIYSTGYAFAEESAIPLAHVKLAVEYAIRTTGIPYTFLRNGLYTENFVSEGLPAADTGSGAI 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748779139 159 KFFTSDETqMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQNMEAVFSEVAGREVKSA 222
Cdd:cd08947  160 VLPAGDGP-VPSVTRNDLGPAAAQLLKEEGHEGKTINLVSNCRWTPDELAAALSRVLGKKVVHQ 222
NAD_binding_10 pfam13460
NAD(P)H-binding;
6-139 4.15e-19

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 82.65  E-value: 4.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139    6 GASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGATEVFVGDMSEEKDLREALHGVDTVyYICSAANPKEDEIGEQ 85
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALVRNPEKLADLEDHPGVEVVDGDVLDPDDLAEALAGQDAV-ISALGGGGTDETGAKN 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748779139   86 MIQIAKKVG----------NIYFVYHSVLHSVLQDMPHH--KRKLHTEQLVVDSGLDFAIIQPAVF 139
Cdd:pfam13460  80 IIDAAKAAGvkrfvlvsslGVGDEVPGPFGPWNKEMLGPylAAKRAAEELLRASGLDYTIVRPGWL 145
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
1-220 2.53e-18

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 82.72  E-value: 2.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   1 MILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGATEVFVGDMSEEKDLREALHGVDTVYYICSAANPKED 80
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFVRGDLRDPEALAAALAGVDAVVHLAAPAGVGEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  81 E---------IG-EQMIQIAKKVGNIYFVYHS---VL----------HSVLQDMPHHKRKLHTEQLVVD----SGLDFAI 133
Cdd:COG0451   81 DpdetlevnvEGtLNLLEAARAAGVKRFVYASsssVYgdgegpidedTPLRPVSPYGASKLAAELLARAyarrYGLPVTI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139 134 IQPAVF----MQMLMPA-VKSVQSGGPMlqKFFTSDETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQNME 208
Cdd:COG0451  161 LRPGNVygpgDRGVLPRlIRRALAGEPV--PVFGDGDQRRDFIHVDDVARAIVLALEAPAAPGGVYNVGGGEPVTLRELA 238
                        250
                 ....*....|..
gi 748779139 209 AVFSEVAGREVK 220
Cdd:COG0451  239 EAIAEALGRPPE 250
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
1-220 4.91e-12

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 65.04  E-value: 4.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   1 MILITGASGQVGCAVIRALSKVGIETKAFIHSASnieKVKEAGATEVFVGDMSEEKDLREALHGVDTVYYicsAANPKED 80
Cdd:cd05229    1 TAHVLGASGPIGREVARELRRRGWDVRLVSRSGS---KLAWLPGVEIVAADAMDASSVIAAARGADVIYH---CANPAYT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  81 EIGEQMIQIAKKV--------------GNIYfVYHSVLHSVLQ-DMPH----HKRKLHTEQ---------------LVVD 126
Cdd:cd05229   75 RWEELFPPLMENVvaaaeangaklvlpGNVY-MYGPQAGSPITeDTPFqpttRKGRIRAEMeerllaahakgdiraLIVR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139 127 SGlDFaiIQPAVFMQMLMPAVKSVQSGGPMLqkfFTSD-ETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQ 205
Cdd:cd05229  154 AP-DF--YGPGAINSWLGAALFAILQGKTAV---FPGNlDTPHEWTYLPDVARALVTLAEEPDAFGEAWHLPGAGAITTR 227
                        250
                 ....*....|....*
gi 748779139 206 NMEAVFSEVAGREVK 220
Cdd:cd05229  228 ELIAIAARAAGRPPK 242
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
2-139 7.38e-12

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 62.42  E-value: 7.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGATEVfVGDMSEEKDLREALHGVDTVYYiCSAANPKEDE 81
Cdd:cd05226    1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKRLSKEDQEPVAVV-EGDLRDLDSLSDAVQGVDVVIH-LAGAPRDTRD 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748779139  82 IGEQMIQIAKKVGNI---YFVYHSVLHSVLQDMPHH-------------KRKLHTEQLVVDSGLDFAIIQPAVF 139
Cdd:cd05226   79 FCEVDVEGTRNVLEAakeAGVKHFIFISSLGAYGDLheetepspsspylAVKAKTEAVLREASLPYTIVRPGVI 152
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
2-217 2.37e-11

atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187556 [Multi-domain]  Cd Length: 293  Bit Score: 62.75  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGATEVFVGDMSEEKDLREALHGVDTVYYICSAANPKED- 80
Cdd:cd05245    1 VLVTGATGYVGGRLVPRLLQEGHQVRALVRSPEKLADRPWSERVTVVRGDLEDPESLRAALEGIDTAYYLVHSMGSGGDf 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  81 -----EIGEQMIQIAKKVGNIYFVYHSVLHSVLQDMPHHKR-KLHTEQLVVDSGLDFAIIQPAVFM-------QMLMPAV 147
Cdd:cd05245   81 eeadrRAARNFARAARAAGVKRIIYLGGLIPKGEELSPHLRsRAEVGEILRAGGVPVTELRAAVIIgsgsasfEMVRYLV 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748779139 148 KSVqsggP-MLQKFFTSDETQMslVDMEDFAEAAAVILSNKDYANGTFELCGKGSYSLQNMEAVFSEVAGR 217
Cdd:cd05245  161 ERL----PvMITPRWVNTPCQP--IAIRDVLEYLVAALDRPATAGETFEIGGPDVLSYKDMMERFAEVRGL 225
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
2-233 1.32e-10

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187569 [Multi-domain]  Cd Length: 282  Bit Score: 60.39  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSK-VGIETKAFIHSASNIEKVKEAGATEVFVGDMSEEKDLREALHGVDTVyyICSAANPked 80
Cdd:cd05259    2 IAIAGATGTLGGPIVSALLAsPGFTVTVLTRPSSTSSNEFQPSGVKVVPVDYASHESLVAALKGVDAV--ISALGGA--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  81 EIGEQM--IQIAKKVGNIYF-------VYHSVLHSVLQDMPHHKRKLHteQLVVDS--GLDFAIIQPAVFMQ-MLMPAVk 148
Cdd:cd05259   77 AIGDQLklIDAAIAAGVKRFipsefgvDYDRIGALPLLDLFDEKRDVR--RYLRAKnaGLPWTYVSTGMFLDyLLEPLF- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139 149 svqSGGPMLQKFFT---SDETQMSLVDMEDFAEAAAVILSNKDY-ANGTFELcgKGSYSLQN-MEAVFSEVAGREVKSAY 223
Cdd:cd05259  154 ---GVVDLANRTATiygDGETKFAFTTLEDIGRAVARALTHPDRtLNRVVFV--AGDVVTQNeLIALVERVTGRKFERTY 228
                        250
                 ....*....|
gi 748779139 224 ITDEAFIGQM 233
Cdd:cd05259  229 VSEEELLEEL 238
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
2-196 2.40e-10

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 58.71  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEkVKEAGATeVFVGDMSEEKDLREALHGVDTVYyicSAANPKEDE 81
Cdd:COG2910    2 IAVIGATGRVGSLIVREALARGHEVTALVRNPEKLP-DEHPGLT-VVVGDVLDPAAVAEALAGADAVV---SALGAGGGN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  82 IGEQ-------MIQIAKKVGNIYFVYHS---VLHS---VLQDMPHHKRKLHT--------EQLVVDSGLDFAIIQPAVFM 140
Cdd:COG2910   77 PTTVlsdgaraLIDAMKAAGVKRLIVVGgagSLDVapgLGLDTPGFPAALKPaaaakaaaEELLRASDLDWTIVRPAALT 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 748779139 141 QmlMPAVKSVQSGGPMLqkffTSDETQMSlvdMEDFAEAAAVILSNKDYANGTFEL 196
Cdd:COG2910  157 D--GERTGRYRLGGDGL----LVDASSIS---RADVAVALLDELEDPAHIRQRFTV 203
ycf39 CHL00194
Ycf39; Provisional
2-203 1.12e-09

Ycf39; Provisional


Pssm-ID: 177093  Cd Length: 317  Bit Score: 58.09  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIR-ALSKvGIETKAFIHsasNIEK---VKEAGATEVFvGDMSEEKDLREALHGVdTVYYICSAANP 77
Cdd:CHL00194   3 LLVIGATGTLGRQIVRqALDE-GYQVRCLVR---NLRKasfLKEWGAELVY-GDLSLPETLPPSFKGV-TAIIDASTSRP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  78 KEDEIGEQ--------MIQIAKKVGNIYFVYHSVLHSVL-QDMPHHKRKLHTEQLVVDSGLDFAIIQPAVFMQMLMpavk 148
Cdd:CHL00194  77 SDLYNAKQidwdgklaLIEAAKAAKIKRFIFFSILNAEQyPYIPLMKLKSDIEQKLKKSGIPYTIFRLAGFFQGLI---- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 748779139 149 sVQSGGPMLQK---FFTSDETQMSLVDMEDFAEAAAVILSNKDYANGTFELCGKGSYS 203
Cdd:CHL00194 153 -SQYAIPILEKqpiWITNESTPISYIDTQDAAKFCLKSLSLPETKNKTFPLVGPKSWN 209
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
2-179 1.37e-09

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 57.68  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYY---ICSAANPK 78
Cdd:cd05228    1 ILVTGATGFLGSNLVRALLAQGYRVRALVRSGSDAVLLDGLPV-EVVEGDLTDAASLAAAMKGCDRVFHlaaFTSLWAKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  79 EDEI------GEQ-MIQIAKKVGNIYFVYHS---VL----------HSVLQDMPHH----KRKLHTEQLV---VDSGLDF 131
Cdd:cd05228   80 RKELyrtnveGTRnVLDAALEAGVRRVVHTSsiaALggppdgrideTTPWNERPFPndyyRSKLLAELEVleaAAEGLDV 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748779139 132 AIIQPAV------------------FMQMLMPAVksVQSGGpmlqkfftsdetqmSLVDMEDFAEA 179
Cdd:cd05228  160 VIVNPSAvfgpgdegptstgldvldYLNGKLPAY--PPGGT--------------SFVDVRDVAEG 209
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
1-81 1.94e-07

UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 51.16  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   1 MILITGASGQVGCAVIRALSKVGIETKAFIHSASNiEKVKEAGAtEVFVGDMSEEKDLREALHGVDTVYYICSAANPKED 80
Cdd:cd05264    1 RVLIVGGNGFIGSHLVDALLEEGPQVRVFDRSIPP-YELPLGGV-DYIKGDYENRADLESALVGIDTVIHLASTTNPATS 78

                 .
gi 748779139  81 E 81
Cdd:cd05264   79 N 79
SDR_a6 cd05267
atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only ...
2-139 2.01e-07

atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only a partial match to a prototypical glycine-rich NAD(P)-binding motif consensus, GXXG, which conserves part of the motif of extended SDR. Furthermore, they lack the characteristic active site residues of the SDRs. This subgroup is related to phenylcoumaran benzylic ether reductase, an NADPH-dependent aromatic alcohol reductase. One member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187577 [Multi-domain]  Cd Length: 203  Bit Score: 50.44  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVI-RALSKVGIETKAFIHSASNIEKVKEAGATeVFVGDMSEEKDLREALHGVDTVYyiCSAANPKED 80
Cdd:cd05267    3 VLILGANGEIAREATtMLLENSNVELTLFLRNAHRLLHLKSARVT-VVEGDALNSDDLKAAMRGQDVVY--ANLGGTDLD 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748779139  81 EIGEQMIQIAKKVG-------NIYFVYHSV--------LHSVLQDMPHHKRklhTEQLVVDSGLDFAIIQPAVF 139
Cdd:cd05267   80 QQAENVVQAMKAVGvkrliwtTSLGIYDEVpgkfgewnKEFIGNYLAPYRK---SAAVIENSDLDYTLLRPAWL 150
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
2-204 4.20e-07

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


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 49.94  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVK---EAGATEVFVGDMSEEKDLREALHGVDTVYYICSAANPK 78
Cdd:cd05271    3 VTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEAYARRLLvmgDLGQVLFVEFDLRDDESIRKALEGSDVVINLVGRLYET 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  79 -----ED---EIGEQMIQIAKKVGNIYFVYHSVL----HSVLQDMphhKRKLHTEQLVVDSGLDFAIIQPAV-------- 138
Cdd:cd05271   83 knfsfEDvhvEGPERLAKAAKEAGVERLIHISALgadaNSPSKYL---RSKAEGEEAVREAFPEATIVRPSVvfgredrf 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748779139 139 ---FMQML--MPAVKSVQSGGPMLQKFFTSDetqmslvdmedFAEAAAVILSNKDYANGTFELCGKGSYSL 204
Cdd:cd05271  160 lnrFAKLLafLPFPPLIGGGQTKFQPVYVGD-----------VAEAIARALKDPETEGKTYELVGPKVYTL 219
PLN02657 PLN02657
3,8-divinyl protochlorophyllide a 8-vinyl reductase
2-155 1.10e-06

3,8-divinyl protochlorophyllide a 8-vinyl reductase


Pssm-ID: 178263 [Multi-domain]  Cd Length: 390  Bit Score: 49.38  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEA--------GATEVFvGDMSEEKDLREALHG----VDTVy 69
Cdd:PLN02657  63 VLVVGATGYIGKFVVRELVRRGYNVVAVAREKSGIRGKNGKedtkkelpGAEVVF-GDVTDADSLRKVLFSegdpVDVV- 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  70 yICSAANP---KED------EIGEQMIQIAKKVGNIYFVYHS---VLHSVLQdMPHHKRKLHTEQLVVDSGLDFAIIQPA 137
Cdd:PLN02657 141 -VSCLASRtggVKDswkidyQATKNSLDAGREVGAKHFVLLSaicVQKPLLE-FQRAKLKFEAELQALDSDFTYSIVRPT 218
                        170
                 ....*....|....*...
gi 748779139 138 VFMQMLMPAVKSVQSGGP 155
Cdd:PLN02657 219 AFFKSLGGQVEIVKDGGP 236
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
2-197 1.18e-06

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 48.45  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139    2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGATEVFvGDMSEEKDLREAL--HGVDTVYYICSAANPKE 79
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLRFVE-GDLTDRDALEKLLadVRPDAVIHLAAVGGVGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   80 D------------EIGEQMIQIAKKVGNIYFVY-----------HSVLHSVLQDMPHHKR------KLHTEQLVVDS--- 127
Cdd:pfam01370  80 SiedpedfieanvLGTLNLLEAARKAGVKRFLFasssevygdgaEIPQEETTLTGPLAPNspyaaaKLAGEWLVLAYaaa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  128 -GLDFAII---------QPAVFMQMLMPA-VKSVQSGGPMLqkFFTSDETQMSLVDMEDFAEAAAVILSNKDYANGTFEL 196
Cdd:pfam01370 160 yGLRAVILrlfnvygpgDNEGFVSRVIPAlIRRILEGKPIL--LWGDGTQRRDFLYVDDVARAILLALEHGAVKGEIYNI 237

                  .
gi 748779139  197 C 197
Cdd:pfam01370 238 G 238
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
1-194 3.04e-06

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 47.73  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   1 MILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVkeagateVFVGDMSEEKDLREALHGVDTVYYICS------- 73
Cdd:cd05232    1 KVLVTGANGFIGRALVDKLLSRGEEVRIAVRNAENAEPS-------VVLAELPDIDSFTDLFLGVDAVVHLAArvhvmnd 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  74 -AANPKED------EIGEQMIQIAKKVGNIYFVYHSV--------LHSVL--------QDmPHHKRKLHTEQLVVD---- 126
Cdd:cd05232   74 qGADPLSDyrkvntELTRRLARAAARQGVKRFVFLSSvkvngegtVGAPFdetdppapQD-AYGRSKLEAERALLElgas 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748779139 127 SGLDFAIIQPAVF--------MQMLMPAVKsvqSGGPMlqkFFTSDETQMSLVDMEDFAEAAAVILSNKDYANGTF 194
Cdd:cd05232  153 DGMEVVILRPPMVygpgvrgnFARLMRLID---RGLPL---PPGAVKNRRSLVSLDNLVDAIYLCISLPKAANGTF 222
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
2-122 6.20e-05

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 43.80  E-value: 6.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEA-------GATEVFVGDMSEEKD-LREALHGVDTVYYICS 73
Cdd:cd05227    2 VLVTGATGFIASHIVEQLLKAGYKVRGTVRSLSKSAKLKALlkaagynDRLEFVIVDDLTAPNaWDEALKGVDYVIHVAS 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748779139  74 AANPKEDEIGEQMIQIA-----------KKVGNI-YFVYHSVLHSVLQDMPHHKRKLHTEQ 122
Cdd:cd05227   82 PFPFTGPDAEDDVIDPAvegtlnvleaaKAAGSVkRVVLTSSVAAVGDPTAEDPGKVFTEE 142
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
2-137 6.31e-05

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 43.57  E-value: 6.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKvgiETKAFIHS---ASNIEKVKEAGAT--EVFVGDMSEEKDLREALHGVDTVYYICSA-- 74
Cdd:cd05241    2 VLVTGGSGFFGERLVKQLLE---RGGTYVRSfdiAPPGEALSAWQHPniEFLKGDITDRNDVEQALSGADCVFHTAAIvp 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  75 -ANPKE--DEI---GEQMI-QIAKKVGNIYFVYHS---------VLHSVLQDMPHHKR--------KLHTEQLVVD---- 126
Cdd:cd05241   79 lAGPRDlyWEVnvgGTQNVlDACQRCGVQKFVYTSsssvifggqNIHNGDETLPYPPLdsdmyaetKAIAEIIVLEangr 158
                        170
                 ....*....|.
gi 748779139 127 SGLDFAIIQPA 137
Cdd:cd05241  159 DDLLTCALRPA 169
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
2-141 8.75e-05

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187555 [Multi-domain]  Cd Length: 207  Bit Score: 42.61  E-value: 8.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIR-ALSKvGIETKAFIHSASNIEKvkEAGATEVFVGDMSEEKDLREALHGVDTVyyiCSAANPKED 80
Cdd:cd05244    2 IAIIGATGRTGSAIVReALAR-GHEVTALVRDPAKLPA--EHEKLKVVQGDVLDLEDVKEALEGQDAV---ISALGTRND 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  81 E------------IGEQM--------IQI----------AKKVGNIYFVYHSVLHSVLQDmphHKRklhTEQLVVDSGLD 130
Cdd:cd05244   76 LspttlhsegtrnIVSAMkaagvkrlIVVggagslddrpKVTLVLDTLLFPPALRRVAED---HAR---MLKVLRESGLD 149
                        170
                 ....*....|.
gi 748779139 131 FAIIQPAVFMQ 141
Cdd:cd05244  150 WTAVRPPALFD 160
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
2-68 1.33e-04

Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 42.53  E-value: 1.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGATEVF----VGDMSEEKDLREALHG-VDTV 68
Cdd:cd05280  150 VLVTGATGGVGSIAVAILAKLGYTVVALTGKEEQADYLKSLGASEVLdredLLDESKKPLLKARWAGaIDTV 221
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
3-74 4.20e-04

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 41.20  E-value: 4.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748779139    3 LITGASGQVGCAVIRALSKVG--IETKAF--IHSASNIEKVKEAGATEVFVGDMSEEKDLREALHGVDTVYYICSA 74
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGelKEVRVFdlRESPELLEDFSKSNVIKYIQGDVTDKDDLDNALEGVDVVIHTASA 76
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
2-73 4.77e-04

aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187536 [Multi-domain]  Cd Length: 295  Bit Score: 41.06  E-value: 4.77e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKV-------KEAGATEVFVGDMSEEKDLREALHGVDTVYYICS 73
Cdd:cd05193    1 VLVTGASGFVASHVVEQLLERGYKVRATVRDPSKVKKVnhlldldAKPGRLELAVADLTDEQSFDEVIKGCAGVFHVAT 79
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
2-194 5.40e-04

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 40.36  E-value: 5.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAF------IHSAsniekvkeagatevfvgdmseekdlreALHGVDtvyyiCSAA 75
Cdd:cd08946    1 ILVTGGAGFIGSHLVRRLLERGHEVVVIdrldvvVHLA---------------------------ALVGVP-----ASWD 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  76 NPKEDE-----IGEQMIQIAKKVGNIYFVYHS------VLHSVLQDMPHHKR--------KLHTEQLVVD----SGLDFA 132
Cdd:cd08946   49 NPDEDFetnvvGTLNLLEAARKAGVKRFVYASsasvygSPEGLPEEEETPPRplspygvsKLAAEHLLRSygesYGLPVV 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748779139 133 IIQPA-VF-------MQMLMPAV-KSVQSGGPMlqKFFTSDETQMSLVDMEDFAEAAAVILSNKDYANGTF 194
Cdd:cd08946  129 ILRLAnVYgpgqrprLDGVVNDFiRRALEGKPL--TVFGGGNQTRDFIHVDDVVRAILHALENPLEGGGVY 197
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
2-69 9.06e-04

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


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 40.13  E-value: 9.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGATEVFVgdmSEEKDLREAL------HGVDTVY 69
Cdd:COG0604  143 VLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRALGADHVID---YREEDFAERVraltggRGVDVVL 213
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
2-100 9.50e-04

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 40.27  E-value: 9.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGATEVFVgdmSEEKDLREALH------GVDTVYyicsaa 75
Cdd:cd08268  148 VLITAASSSVGLAAIQIANAAGATVIATTRTSEKRDALLALGAAHVIV---TDEEDLVAEVLritggkGVDVVF------ 218
                         90       100
                 ....*....|....*....|....*...
gi 748779139  76 npkeDEI-GEQMIQIAKKV--GNIYFVY 100
Cdd:cd08268  219 ----DPVgGPQFAKLADALapGGTLVVY 242
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
2-68 1.20e-03

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 39.64  E-value: 1.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGAtEVFVGDMSEEKDLREALHGVDTV 68
Cdd:cd05262    3 VFVTGATGFIGSAVVRELVAAGHEVVGLARSDAGAAKLEAAGA-QVHRGDLEDLDILRKAAAEADAV 68
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
2-97 1.23e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 39.66  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGAsGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGaTEVFVGDMSEEKDLREAlhGVDTVYYICSAANpkEDE 81
Cdd:COG0569   98 VIIIGA-GRVGRSLARELEEEGHDVVVIDKDPERVERLAEED-VLVIVGDATDEEVLEEA--GIEDADAVIAATG--DDE 171
                         90
                 ....*....|....*.
gi 748779139  82 IGEQMIQIAKKVGNIY 97
Cdd:COG0569  172 ANILACLLAKELGVPR 187
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
1-39 1.31e-03

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


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 39.53  E-value: 1.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 748779139   1 MILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKV 39
Cdd:cd05254    1 KILITGATGMLGRALVRLLKERGYEVIGTGRSRASLFKL 39
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
2-48 1.37e-03

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 39.56  E-value: 1.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 748779139    2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEkvKEAGATEVF 48
Cdd:pfam04321   1 ILITGANGQLGTELRRLLAERGIEVVALTRAELDLT--DPEAVARLL 45
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
2-68 1.70e-03

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 39.20  E-value: 1.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 748779139   2 ILITGASGQVGCAVIrALSKVGIETKAFIHSASNIEKVKEAGATEVFVGDMSEEKDLREAL-HGVDTV 68
Cdd:cd08274  181 VLVTGASGGVGSALV-QLAKRRGAIVIAVAGAAKEEAVRALGADTVILRDAPLLADAKALGgEPVDVV 247
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
2-65 1.81e-03

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: 38.99  E-value: 1.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEK-VKEAGATEVFVGDMSEEKDLREALHGV 65
Cdd:cd05351   10 ALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSlVRECPGIEPVCVDLSDWDATEEALGSV 74
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
2-42 1.84e-03

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 38.96  E-value: 1.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSA---SNIEKVKEA 42
Cdd:COG1091    2 ILVTGANGQLGRALVRLLAERGYEVVALDRSEldiTDPEAVAAL 45
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
3-96 2.09e-03

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 38.89  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   3 LITGASGQVGCAVIRALSKvgietkafihsasniekvkeAGATEVFvGDMSEEKdLREAL-----HGVDTVYYICSAANp 77
Cdd:PRK07097  14 LITGASYGIGFAIAKAYAK--------------------AGATIVF-NDINQEL-VDKGLaayreLGIEAHGYVCDVTD- 70
                         90
                 ....*....|....*....
gi 748779139  78 kEDEIGEQMIQIAKKVGNI 96
Cdd:PRK07097  71 -EDGVQAMVSQIEKEVGVI 88
CAPF_like_SDR_e cd05261
capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of ...
2-194 2.29e-03

capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of extended SDRs, includes some members which have been identified as capsular polysaccharide assembling proteins, such as Staphylococcus aureus Cap5F which is involved in the biosynthesis of N-acetyl-l-fucosamine, a constituent of surface polysaccharide structures of S. aureus. This subgroup has the characteristic active site tetrad and NAD-binding motif of extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187571 [Multi-domain]  Cd Length: 248  Bit Score: 38.49  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGQVGCAVIRALskvgietkafihsasniekvKEAGATEVF-VGDMSEEKDLREALHGVDTVYYICSAANPKED 80
Cdd:cd05261    3 ILITGAKGFIGKNLIARL--------------------KEQKDDDIFfYDRESDESELDDFLQGADFIFHLAGVNRPKDE 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139  81 ---EIG-----EQMIQIAKKVGN-IYFVYHSVLHSVLqDMPHHKRKLHTEQLVV----DSGLDFAI-IQPAVFMQMLMPA 146
Cdd:cd05261   63 aefESGnvgltERLLDALTRNGKkPPILLSSSIQAAL-DNPYGKSKLAAEELLQeyarETGAPVYIyRLPNVFGKWCRPN 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 748779139 147 VKSVQS--------GGPMLQKfftSDETQMSLVDMEDFAEAAAVILSNKDYANGTF 194
Cdd:cd05261  142 YNSAVAtfcyniarDLPIQIN---DPAAELTLVYIDDVVDELIQLLEGAPTYSGGF 194
PLN02650 PLN02650
dihydroflavonol-4-reductase
2-71 2.41e-03

dihydroflavonol-4-reductase


Pssm-ID: 178256 [Multi-domain]  Cd Length: 351  Bit Score: 39.04  E-value: 2.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKE----AGATE---VFVGDMSEEKDLREALHGVDTVYYI 71
Cdd:PLN02650   8 VCVTGASGFIGSWLVMRLLERGYTVRATVRDPANVKKVKHlldlPGATTrltLWKADLAVEGSFDDAIRGCTGVFHV 84
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
2-96 2.78e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 38.46  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748779139   2 ILITGASGqVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGATEVFVgdmSEEKDLREAL-----HGVDTVyyICSAAN 76
Cdd:cd05188  138 VLVLGAGG-VGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHVID---YKEEDLEEELrltggGGADVV--IDAVGG 211
                         90       100
                 ....*....|....*....|
gi 748779139  77 PkedEIGEQMIQIAKKVGNI 96
Cdd:cd05188  212 P---ETLAQALRLLRPGGRI 228
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
2-69 3.11e-03

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 38.45  E-value: 3.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASNIEKVKEAGATEVFVG-DMSEEKDlreALHGVDTVY 69
Cdd:cd08259  166 VLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKILKELGADYVIDGsKFSEDVK---KLGGADVVI 231
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
41-103 3.87e-03

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 38.17  E-value: 3.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 748779139  41 EAGATEVF--VGDMSEE--KDLREALHGVDTVYYICSAANpkEDEIGEQMIQIAKKVGNIYFVYHSV 103
Cdd:PRK08594  31 NAGAKLVFtyAGERLEKevRELADTLEGQESLLLPCDVTS--DEEITACFETIKEEVGVIHGVAHCI 95
YfcH COG1090
NAD dependent epimerase/dehydratase family enzyme [General function prediction only];
2-68 5.46e-03

NAD dependent epimerase/dehydratase family enzyme [General function prediction only];


Pssm-ID: 440707 [Multi-domain]  Cd Length: 298  Bit Score: 37.74  E-value: 5.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIETKAFIHSASniekvKEAGATEVFVGDMSEEKDLREALHGVDTV 68
Cdd:COG1090    2 ILITGGTGFIGSALVAALLARGHEVVVLTRRPP-----KAPDEVTYVAWDPETGGIDAAALEGADAV 63
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
2-68 6.98e-03

enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 37.56  E-value: 6.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 748779139   2 ILITGASGQVGCAVIRALSKVGIE--TKAfihSASNIEKVKEAGATEVF------VGDMSEEKDLREALHGVDTV 68
Cdd:cd08249  158 VLIWGGSSSVGTLAIQLAKLAGYKviTTA---SPKNFDLVKSLGADAVFdyhdpdVVEDIRAATGGKLRYALDCI 229
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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