|
Name |
Accession |
Description |
Interval |
E-value |
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
4-338 |
0e+00 |
|
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.
Pssm-ID: 239242 [Multi-domain] Cd Length: 336 Bit Score: 539.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLRGLTVRNRVWLPPMCQYSCEnrDGVPGQWHLTHLGARAAGGFGLIITEASAVVPEGRISPQDAGIWNDEQAQA 83
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMCQYSAE--DGVATDWHLVHYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDEQIEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 84 WKPIVDFVHSQGAAIGIQLAHAGRKASTHRPFPGeGKGTVSKDAGGWPTLGPSSLAY-PGLAEPTAMSVEEIRDVVEAFG 162
Cdd:cd02932 79 LKRIVDFIHSQGAKIGIQLAHAGRKASTAPPWEG-GGPLLPPGGGGWQVVAPSAIPFdEGWPTPRELTREEIAEVVDAFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 163 AAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEYG-SGTGRWKLLRDILAAVRSRVPDDFPVLVRISADEWAEGG 241
Cdd:cd02932 158 AAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGgSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVEGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 242 FGIDEAVELSRVLHEEGCDLVDVSGGGNTP-ADIPVGPGYQTGFAQRIR-EAGVPTAAVGLITDPVQAQTILTTGQADAV 319
Cdd:cd02932 238 WDLEDSVELAKALKELGVDLIDVSSGGNSPaQKIPVGPGYQVPFAERIRqEAGIPVIAVGLITDPEQAEAILESGRADLV 317
|
330
....*....|....*....
gi 518005299 320 LIGRAALREPSWSLRAAHE 338
Cdd:cd02932 318 ALGRELLRNPYWPLHAAAE 336
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
1-340 |
1.13e-152 |
|
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];
Pssm-ID: 441506 [Multi-domain] Cd Length: 365 Bit Score: 433.83 E-value: 1.13e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 1 MTQLFSPMTLRGLTVRNRVWLPPMCQYSCeNRDGVPGQWHLTHLGARAAGGFGLIITEASAVVPEGRISPQDAGIWNDEQ 80
Cdd:COG1902 4 MPKLFSPLTLGGLTLKNRIVMAPMTRGRA-DEDGVPTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDEQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 81 AQAWKPIVDFVHSQGAAIGIQLAHAGRKASTHRPfpgegkgtvskdaGGWPTLGPSSLAYPGL-AEPTAMSVEEIRDVVE 159
Cdd:COG1902 83 IAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLP-------------GGWPPVAPSAIPAPGGpPTPRALTTEEIERIIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 160 AFGAAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEYGsGT--GRWKLLRDILAAVRSRVPDDFPVLVRISADEW 237
Cdd:COG1902 150 DFAAAARRAKEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYG-GSleNRARFLLEVVEAVRAAVGPDFPVGVRLSPTDF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 238 AEGGFGIDEAVELSRVLHEEGCDLVDVSGGGN-TPADIP--VGPGYQTGFAQRIREA-GVPTAAVGLITDPVQAQTILTT 313
Cdd:COG1902 229 VEGGLTLEESVELAKALEEAGVDYLHVSSGGYePDAMIPtiVPEGYQLPFAARIRKAvGIPVIAVGGITTPEQAEAALAS 308
|
330 340
....*....|....*....|....*..
gi 518005299 314 GQADAVLIGRAALREPSWSLRAAHELG 340
Cdd:COG1902 309 GDADLVALGRPLLADPDLPNKAAAGRG 335
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
2-355 |
6.41e-145 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 413.33 E-value: 6.41e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 2 TQLFSPMTLRGLTVRNRVWLPPMCQYSCENRDGVPGQWHLTHLGARAAGGFGLIITEASAVVPEGRISPQDAGIWNDEQA 81
Cdd:PRK13523 1 SKLFSPYTIKDVTLKNRIVMSPMCMYSSENKDGKVTNFHLIHYGTRAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 82 QAWKPIVDFVHSQGAAIGIQLAHAGRKASThrpfPGEgkgtvskdaggwpTLGPSSLAY-PGLAEPTAMSVEEIRDVVEA 160
Cdd:PRK13523 81 EGLHKLVTFIHDHGAKAAIQLAHAGRKAEL----EGD-------------IVAPSAIPFdEKSKTPVEMTKEQIKETVLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 161 FGAAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEYG-SGTGRWKLLRDILAAVRSrVPDDfPVLVRISADEWAE 239
Cdd:PRK13523 144 FKQAAVRAKEAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGgSPENRYRFLREIIDAVKE-VWDG-PLFVRISASDYHP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 240 GGFGIDEAVELSRVLHEEGCDLVDVSGGGNTPADIPVGPGYQTGFAQRIRE-AGVPTAAVGLITDPVQAQTILTTGQADA 318
Cdd:PRK13523 222 GGLTVQDYVQYAKWMKEQGVDLIDVSSGAVVPARIDVYPGYQVPFAEHIREhANIATGAVGLITSGAQAEEILQNNRADL 301
|
330 340 350
....*....|....*....|....*....|....*..
gi 518005299 319 VLIGRAALREPSWSLRAAHELGLnprEIPYPPQYVRG 355
Cdd:PRK13523 302 IFIGRELLRNPYFPRIAAKELGF---EIEAPKQYERA 335
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
4-356 |
2.15e-130 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 390.84 E-value: 2.15e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLRGLTVRNRVWLPPMCQYSCEnrDGVPGQWHLTHLGARAAGGFGLIITEASAVVPEGRISPQDAGIWNDEQAQA 83
Cdd:PRK08255 399 MFTPFRLRGLTLKNRVVVSPMAMYSAV--DGVPGDFHLVHLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDEQEAA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 84 WKPIVDFVHSQG-AAIGIQLAHAGRKASTHRPFPGEGKgtvSKDAGGWPTLGPSSLAY-PGLAEPTAMSVEEIRDVVEAF 161
Cdd:PRK08255 477 WKRIVDFVHANSdAKIGIQLGHSGRKGSTRLGWEGIDE---PLEEGNWPLISASPLPYlPGSQVPREMTRADMDRVRDDF 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 162 GAAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEY-GSGTGRWKLLRDILAAVRSRVPDDFPVLVRISADEWAEG 240
Cdd:PRK08255 554 VAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYgGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVEG 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 241 GFGIDEAVELSRVLHEEGCDLVDVSGGGNTPADIPV-GPGYQTGFAQRIR-EAGVPTAAVGLITDPVQAQTILTTGQADA 318
Cdd:PRK08255 634 GNTPDDAVEIARAFKAAGADLIDVSSGQVSKDEKPVyGRMYQTPFADRIRnEAGIATIAVGAISEADHVNSIIAAGRADL 713
|
330 340 350
....*....|....*....|....*....|....*...
gi 518005299 319 VLIGRAALREPSWSLRAAHELGLnpREIPYPPQYVRGR 356
Cdd:PRK08255 714 CALARPHLADPAWTLHEAAEIGY--RDVAWPKQYLAGK 749
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
5-331 |
3.86e-119 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 347.25 E-value: 3.86e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 5 FSPMTLRGLTVRNRVWLPPMCQYSCeNRDGVPGQWHLTHLGARAAGGFGLIITEASAVVPEGRISPQDAGIWNDEQAQAW 84
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTENMA-TEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 85 KPIVDFVHSQGAAIGIQLAHAGRKAstHRPFPGEGKGTVSKDAGGWPTlgpsslaypglAEPTAMSVEEIRDVVEAFGAA 164
Cdd:cd02803 80 RKLTEAVHAHGAKIFAQLAHAGRQA--QPNLTGGPPPAPSAIPSPGGG-----------EPPREMTKEEIEQIIEDFAAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 165 AERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEYG-SGTGRWKLLRDILAAVRSRVPDDFPVLVRISADEWAEGGFG 243
Cdd:cd02803 147 ARRAKEAGFDGVEIHGAHGYLLSQFLSPYTNKRTDEYGgSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 244 IDEAVELSRVLHEEGCDLVDVSGG-----GNTPADIPVGPGYQTGFAQRIREA-GVPTAAVGLITDPVQAQTILTTGQAD 317
Cdd:cd02803 227 LEEAIEIAKALEEAGVDALHVSGGsyespPPIIPPPYVPEGYFLELAEKIKKAvKIPVIAVGGIRDPEVAEEILAEGKAD 306
|
330
....*....|....
gi 518005299 318 AVLIGRAALREPSW 331
Cdd:cd02803 307 LVALGRALLADPDL 320
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
4-342 |
4.20e-80 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 248.13 E-value: 4.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLRGLTVRNRVWLPPMCQYSCENRDGVPGQWHLTHLGARAAGGFGLIITEASAVVPEGRISPQDAGIWNDEQAQA 83
Cdd:pfam00724 2 LFEPIKIGNTTLKNRIVMAPMTRLRSLDDGTKATGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 84 WKPIVDFVHSQGAAIGIQLAHAGRKAsthrpfPGEGKGTVSKDAGGWPTLGPSSLAYPGlAEPTAMSVEEIRDVVEAFGA 163
Cdd:pfam00724 82 WRKLTEAVHKNGSKAGVQLWHLGREA------PMEYRPDLEVDGPSDPFALGAQEFEIA-SPRYEMSKEEIKQHIQDFVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 164 AAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEY-GSGTGRWKLLRDILAAVRSRVPDDFPVLVRISADEWAEGGF 242
Cdd:pfam00724 155 AAKRAREAGFDGVEIHGANGYLINQFLSPGTNQRTDEYgGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 243 GIDEAVELSRVLHEEGCDLVDVSGGGNTPADIPVGPG------YQTGFAQRIRE-AGVPTAAVGLITDPVQAQTILTTGQ 315
Cdd:pfam00724 235 DFAETAQFIYLLAELGVRLPDGWHLAYIHAIEPRPRGagpvrtRQQHNTLFVKGvWKGPLITVGRIDDPSVAAEIVSKGR 314
|
330 340
....*....|....*....|....*..
gi 518005299 316 ADAVLIGRAALREPSWSLRAAHELGLN 342
Cdd:pfam00724 315 ADLVAMGRPFLADPDLPFKAKKGRPLN 341
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
4-329 |
2.66e-78 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase.
Pssm-ID: 240085 [Multi-domain] Cd Length: 343 Bit Score: 243.67 E-value: 2.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLRGLTVRNRVWLPP-MCQYScenRDGVPGQWHLTHLGARAAGGFGLIITEASAVVPEGRISPQDAGIWNDEQAQ 82
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAhATNYA---EDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 83 AWKPIVDFVHSQGAAIGIQLAHAGRKASthrpfpgegkgtvskDAGGW-PTLGPSSLAYPGLAE-PTAMSVEEIRDVVEA 160
Cdd:cd04734 78 GFRRLAEAVHAHGAVIMIQLTHLGRRGD---------------GDGSWlPPLAPSAVPEPRHRAvPKAMEEEDIEEIIAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 161 FGAAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEY-GSGTGRWKLLRDILAAVRSRVPDDFPVLVRISADEWAE 239
Cdd:cd04734 143 FADAARRCQAGGLDGVELQAAHGHLIDQFLSPLTNRRTDEYgGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 240 GGFGIDEAVELSRVLHEEGC-DLVDVSGGG--------NTPADIPVGPGYQTGFAQRIREA-GVPTAAVGLITDPVQAQT 309
Cdd:cd04734 223 GGLSPDEALEIAARLAAEGLiDYVNVSAGSyytllglaHVVPSMGMPPGPFLPLAARIKQAvDLPVFHAGRIRDPAEAEQ 302
|
330 340
....*....|....*....|
gi 518005299 310 ILTTGQADAVLIGRAALREP 329
Cdd:cd04734 303 ALAAGHADMVGMTRAHIADP 322
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
4-330 |
7.93e-65 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240084 [Multi-domain] Cd Length: 338 Bit Score: 208.98 E-value: 7.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLR-GLTVRNRVWLPPMCQYSCeNRDGVPGQWHLTHLGARAAGGFGLIITEASAVVPEGRISPQDAG---IWNDE 79
Cdd:cd04733 1 LGQPLTLPnGATLPNRLAKAAMSERLA-DGRGLPTPELIRLYRRWAEGGIGLIITGNVMVDPRHLEEPGIIGnvvLESGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 80 QAQAWKPIVDFVHSQGAAIGIQLAHAGRKASTHRpfpgeGKGTVSKDAggwpTLGPSSLAyPGLAEPTAMSVEEIRDVVE 159
Cdd:cd04733 80 DLEAFREWAAAAKANGALIWAQLNHPGRQSPAGL-----NQNPVAPSV----ALDPGGLG-KLFGKPRAMTEEEIEDVID 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 160 AFGAAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEY-GSGTGRWKLLRDILAAVRSRVPDDFPVLVRISADEWA 238
Cdd:cd04733 150 RFAHAARLAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYgGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 239 EGGFGIDEAVELSRVLHEEGCDLVDVSGG--------GNTPADIPVGPGYQTGFAQRIREA-GVPTAAVGLITDPVQAQT 309
Cdd:cd04733 230 RGGFTEEDALEVVEALEEAGVDLVELSGGtyespamaGAKKESTIAREAYFLEFAEKIRKVtKTPLMVTGGFRTRAAMEQ 309
|
330 340
....*....|....*....|.
gi 518005299 310 ILTTGQADAVLIGRAALREPS 330
Cdd:cd04733 310 ALASGAVDGIGLARPLALEPD 330
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
4-343 |
4.20e-64 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include 12-oxophytodienoate reductase, pentaerythritol tetranitrate reductase, morphinone reductase, and related enzymes.
Pssm-ID: 239243 [Multi-domain] Cd Length: 338 Bit Score: 206.94 E-value: 4.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLRGLTVRNRVWLPPMCQYSCENrDGVPGQWHLTHLGARAagGFGLIITEASAVVPEGRISPQDAGIWNDEQAQA 83
Cdd:cd02933 2 LFSPLKLGNLTLKNRIVMAPLTRSRADP-DGVPTDLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIYTDEQVEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 84 WKPIVDFVHSQGAAIGIQLAHAGRKAstHRPFPGEGKgtvskdaggwPTLGPSSLAYPGLA----------EPTAMSVEE 153
Cdd:cd02933 79 WKKVTDAVHAKGGKIFLQLWHVGRVS--HPSLLPGGA----------PPVAPSAIAAEGKVftpagkvpypTPRALTTEE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 154 IRDVVEAFGAAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEYG-SGTGRWKLLRDILAAVRSRVPDDFpVLVRI 232
Cdd:cd02933 147 IPGIVADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGgSIENRARFLLEVVDAVAEAIGADR-VGIRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 233 SAdeWAE-GGFGIDEAVEL-SRVLHE-EGCDL--VDVSGGGNTPADIPVGPgyqtGFAQRIREA--GVPTAAVGLitDPV 305
Cdd:cd02933 226 SP--FGTfNDMGDSDPEATfSYLAKElNKRGLayLHLVEPRVAGNPEDQPP----DFLDFLRKAfkGPLIAAGGY--DAE 297
|
330 340 350
....*....|....*....|....*....|....*...
gi 518005299 306 QAQTILTTGQADAVLIGRAALREPSWSLRAAHELGLNP 343
Cdd:cd02933 298 SAEAALADGKADLVAFGRPFIANPDLVERLKNGAPLNE 335
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
4-331 |
9.99e-64 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240086 [Multi-domain] Cd Length: 353 Bit Score: 206.29 E-value: 9.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLR-GLTVRNRVWLPPMCQYScENRDGVPGQWHLTHLGARAaGGFGLIITEASAVVPEGRISPQDAGIWNDEQAQ 82
Cdd:cd04735 1 LFEPFTLKnGVTLKNRFVMAPMTTYS-SNPDGTITDDELAYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 83 AWKPIVDFVHSQGA-AIgIQLAHAGRKAsthrpfpgegkgtVSKDAGGWPTLGPSSLA--YPGLAEPTAMSVEEIRDVVE 159
Cdd:cd04735 79 GLRKLAQAIKSKGAkAI-LQIFHAGRMA-------------NPALVPGGDVVSPSAIAafRPGAHTPRELTHEEIEDIID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 160 AFGAAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEYGsGT--GRWKLLRDILAAVRSRV----PDDFPVLVRIS 233
Cdd:cd04735 145 AFGEATRRAIEAGFDGVEIHGANGYLIQQFFSPHSNRRTDEWG-GSleNRMRFPLAVVKAVQEVIdkhaDKDFILGYRFS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 234 ADEWAEGGFGIDEAVELSRVLHEEGCDLVDVSGGG---NTPADIPVGPGYQTGFAQRIreAG-VPTAAVGLITDPVQAQT 309
Cdd:cd04735 224 PEEPEEPGIRMEDTLALVDKLADKGLDYLHISLWDfdrKSRRGRDDNQTIMELVKERI--AGrLPLIAVGSINTPDDALE 301
|
330 340
....*....|....*....|..
gi 518005299 310 ILTTGqADAVLIGRAALREPSW 331
Cdd:cd04735 302 ALETG-ADLVAIGRGLLVDPDW 322
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
4-336 |
2.64e-58 |
|
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.
Pssm-ID: 239240 [Multi-domain] Cd Length: 353 Bit Score: 192.50 E-value: 2.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLRGLTVRNRVWLPPMCQYSCENRDGVPGQwhLTHLGARAAGGFGLIITEASAVVPEGRISPQDAGIWNDEQAQA 83
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRL--AAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 84 WKPIVDFVHSQGAAIGIQLAHAGRKAstHRPFPgegkgtvskdaggwptLGPSSLAYP-GLAEPTAMSVEEIRDVVEAFG 162
Cdd:cd02930 79 HRLITDAVHAEGGKIALQILHAGRYA--YHPLC----------------VAPSAIRAPiNPFTPRELSEEEIEQTIEDFA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 163 AAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEY-GSGTGRWKLLRDILAAVRSRVPDDFPVLVRISADEWAEGG 241
Cdd:cd02930 141 RCAALAREAGYDGVEIMGSEGYLINQFLAPRTNKRTDEWgGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 242 FGIDEAVELSRVLHEEGCDLVDvSGGGNTPADIP-----VGPGYQTGFAQRIREA-GVPTAAVGLITDPVQAQTILTTGQ 315
Cdd:cd02930 221 STWEEVVALAKALEAAGADILN-TGIGWHEARVPtiatsVPRGAFAWATAKLKRAvDIPVIASNRINTPEVAERLLADGD 299
|
330 340
....*....|....*....|.
gi 518005299 316 ADAVLIGRAALREPSWSLRAA 336
Cdd:cd02930 300 ADMVSMARPFLADPDFVAKAA 320
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
4-335 |
4.40e-58 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240095 [Multi-domain] Cd Length: 361 Bit Score: 192.15 E-value: 4.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLRGLTVRNRVWLPPMCQYSCENrdGVPGQWHLTHLGARAAGGFGLIITEASAVV-PEGRISPQDAGIWNDEQAQ 82
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPMTRSFSPG--GVPGQDVAAYYRRRAAGGVGLIITEGTAVDhPAASGDPNVPRFHGEDALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 83 AWKPIVDFVHSQGAAIGIQLAHAGRKASTHRPFPGEGkgtvskdaggwPTLGPSSLAYPGLAEPTAMSVEEIRDVVEAFG 162
Cdd:cd04747 79 GWKKVVDEVHAAGGKIAPQLWHVGAMRKLGTPPFPDV-----------PPLSPSGLVGPGKPVGREMTEADIDDVIAAFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 163 AAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEYG-SGTGRWKLLRDILAAVRSRVPDDFPVLVRISadEWAEGG 241
Cdd:cd04747 148 RAAADARRLGFDGIELHGAHGYLIDQFFWAGTNRRADGYGgSLAARSRFAAEVVKAIRAAVGPDFPIILRFS--QWKQQD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 242 FGI------DEAVELSRVLHEEGCDLVDVSgggNTPADIPVGPGYQ---TGFAQRIreAGVPTAAVGLI----------- 301
Cdd:cd04747 226 YTArladtpDELEALLAPLVDAGVDIFHCS---TRRFWEPEFEGSElnlAGWTKKL--TGLPTITVGSVgldgdfigafa 300
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 518005299 302 TDPVQAQTILT-------TGQADAVLIGRAALREPSWSLRA 335
Cdd:cd04747 301 GDEGASPASLDrllerleRGEFDLVAVGRALLSDPAWVAKV 341
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
4-324 |
2.66e-42 |
|
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. TMADH is an iron-sulfur flavoprotein that catalyzes the oxidative demethylation of trimethylamine to form dimethylamine and formaldehyde. The protein forms a symetrical dimer with each subunit containing one 4Fe-4S cluster and one FMN cofactor. It contains a unique flavin, in the form of a 6-S-cysteinyl FMN which is bent by ~25 degrees along the N5-N10 axis of the flavin isoalloxazine ring. This modification of the conformation of the flavin is thought to facilitate catalysis.The closely related histamine dehydrogenase catalyzes oxidative deamination of histamine.
Pssm-ID: 239239 [Multi-domain] Cd Length: 370 Bit Score: 150.97 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLRGLTVRNRVWLPPMCQYSCENRdgvPGQWhLTHLGARAAGGFGLIITEASAVVPEGRISPQ-DAGIWNDEQAQ 82
Cdd:cd02929 8 LFEPIKIGPVTARNRFYQVPHCNGMGYRK---PSAQ-AAMRGIKAEGGWGVVNTEQCSIHPSSDDTPRiSARLWDDGDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 83 AWKPIVDFVHSQGAAIGIQLAHAGRKAS--THRPFPgegkgtvskdaggwptLGPSSLA----YPGLAEPTAMSVEEIRD 156
Cdd:cd02929 84 NLAAMTDAVHKHGALAGIELWHGGAHAPnrESRETP----------------LGPSQLPsefpTGGPVQAREMDKDDIKR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 157 VVEAFGAAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEY-GSGTGRWKLLRDILAAVRSRVPDDFPVLVRISAD 235
Cdd:cd02929 148 VRRWYVDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYgGSLENRARFWRETLEDTKDAVGDDCAVATRFSVD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 236 EWA--EGGFGIDEAVELSRVLhEEGCDLVDVSGG--GNTPADIPVGP-GYQTGFAQRIREA-GVPTAAVGLITDPVQAQT 309
Cdd:cd02929 228 ELIgpGGIESEGEGVEFVEML-DELPDLWDVNVGdwANDGEDSRFYPeGHQEPYIKFVKQVtSKPVVGVGRFTSPDKMVE 306
|
330
....*....|....*
gi 518005299 310 ILTTGQADavLIGRA 324
Cdd:cd02929 307 VVKSGILD--LIGAA 319
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
2-233 |
2.92e-42 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 151.55 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 2 TQLFSPMTLRGLTVRNRVWLPPMCQysCENRDGVPGQWHLTHLGARAAGGfGLIITEASAVVPEGRISPQDAGIWNDEQA 81
Cdd:PLN02411 10 ETLFSPYKMGRFDLSHRVVLAPMTR--CRALNGIPNAALAEYYAQRSTPG-GFLISEGTLISPTAPGFPHVPGIYSDEQV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 82 QAWKPIVDFVHSQGAAIGIQLAHAGRkaSTHRPF-PGEGKGTVSKD---AGGWPTLGP--SSLAYPglaEPTAMSVEEIR 155
Cdd:PLN02411 87 EAWKKVVDAVHAKGSIIFCQLWHVGR--ASHQVYqPGGAAPISSTNkpiSERWRILMPdgSYGKYP---KPRALETSEIP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518005299 156 DVVEAFGAAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEY-GSGTGRWKLLRDILAAVRSRVPDDfPVLVRIS 233
Cdd:PLN02411 162 EVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYgGSIENRCRFLMQVVQAVVSAIGAD-RVGVRVS 239
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
3-343 |
7.62e-41 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 146.79 E-value: 7.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 3 QLFSPMTLRGLTVRNRVWLPPMCQY-SCENRDgVPGQWHLTHLGARAAGGfgLIITEASAVVPEGRISPQDAGIWNDEQA 81
Cdd:PRK10605 2 KLFSPLKVGAITAPNRVFMAPLTRLrSIEPGD-IPTPLMAEYYRQRASAG--LIISEATQISAQAKGYAGAPGLHSPEQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 82 QAWKPIVDFVHSQGAAIGIQLAHAGRKAstHRPFPGEGKGTVS------------KDAGGWPTLGPSSLaypglaePTAM 149
Cdd:PRK10605 79 AAWKKITAGVHAEGGHIAVQLWHTGRIS--HASLQPGGQAPVApsainagtrtslRDENGQAIRVETST-------PRAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 150 SVEEIRDVVEAFGAAAERAVTAGFDTVEIHGAHGYLIHSFLSPLSNNRDDEY-GSGTGRWKLLRDIL-AAVRSRVPDDfp 227
Cdd:PRK10605 150 ELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYgGSVENRARLVLEVVdAGIAEWGADR-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 228 VLVRISadewAEGGF-----GIDE---AVELSRVLHEEGCDLVDVSgggntPADIPVGPGYQTGFAQRIREA--GVPTAA 297
Cdd:PRK10605 228 IGIRIS----PLGTFnnvdnGPNEeadALYLIEQLGKRGIAYLHMS-----EPDWAGGEPYSDAFREKVRARfhGVIIGA 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 518005299 298 VGLitDPVQAQTILTTGQADAVLIGRAALREPSWSLRAAHELGLNP 343
Cdd:PRK10605 299 GAY--TAEKAETLIGKGLIDAVAFGRDYIANPDLVARLQRKAELNP 342
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
4-331 |
9.27e-38 |
|
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent reduction of carbon-carbon double bonds of several molecules, including nonactivated 2-enoates, alpha,beta-unsaturated aldehydes, cyclic ketones, and methylketones. ERs are similar to 2,4-dienoyl-CoA reductase from E. coli and to the old yellow enzyme from Saccharomyces cerevisiae.
Pssm-ID: 239241 [Multi-domain] Cd Length: 382 Bit Score: 139.18 E-value: 9.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 4 LFSPMTLRGLTVRNRVWLPPMCQYSCENRDGVPGQWHLTHLGARAAGGFGLIITEASAVVPEGRISPQDAGIWNDEQAQA 83
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPLGLADNDGAFNQRGIDYYVERAKGGTGLIITGVTMVDNEIEQFPMPSLPCPTYNPTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 84 W----KPIVDFVHSQGAAIGIQLAhagrkasthrpfPGEGKGTVSKDAGGWPTLGPSSLAYPGLAEPTA--MSVEEIRDV 157
Cdd:cd02931 81 FirtaKEMTERVHAYGTKIFLQLT------------AGFGRVCIPGFLGEDKPVAPSPIPNRWLPEITCreLTTEEVETF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 158 VEAFGAAAERAVTAGFDTVEIHGAH-GYLIHSFLSPLSNNRDDEY-GSGTGRWKLLRDILAAVRSRVPDDFPVLVRIS-- 233
Cdd:cd02931 149 VGKFGESAVIAKEAGFDGVEIHAVHeGYLLDQFTISLFNKRTDKYgGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSvk 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 234 ------------ADEWAEGGFGIDEAVELSRVLHEEGCDLVDVSGGG------NTPadiPV--GPGYQTGFAQRIREA-G 292
Cdd:cd02931 229 syikdlrqgalpGEEFQEKGRDLEEGLKAAKILEEAGYDALDVDAGSydawywNHP---PMyqKKGMYLPYCKALKEVvD 305
|
330 340 350
....*....|....*....|....*....|....*....
gi 518005299 293 VPTAAVGLITDPVQAQTILTTGQADAVLIGRAALREPSW 331
Cdd:cd02931 306 VPVIMAGRMEDPELASEAINEGIADMISLGRPLLADPDV 344
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
138-354 |
9.92e-09 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 55.79 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 138 LAYPGLAEPTAMSVEEIRDVVEAFGAAAERAVTAGFDTVEIH-GAHgylihsflSPLSNNRDdeYGSGTGR-WKLLRDIL 215
Cdd:pfam01207 45 RMLSELEEPTPLAVQLGGSDPALLAEAAKLVEDRGADGIDINmGCP--------SKKVTRGG--GGAALLRnPDLVAQIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 216 AAVRSRVpdDFPVLVRISadewaeggFGIDE----AVELSRVLHEEGCDLVDVSGggNTPADIPVGPGYQTGFAQRIREA 291
Cdd:pfam01207 115 KAVVKAV--GIPVTVKIR--------IGWDDshenAVEIAKIVEDAGAQALTVHG--RTRAQNYEGTADWDAIKQVKQAV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518005299 292 GVPTAAVGLITDPVQAQTILTTGQADAVLIGRAALREPsWSLRAAHelgLNPREIPYPPQYVR 354
Cdd:pfam01207 183 SIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNP-WLFAEQH---TVKTGEFGPSPPLA 241
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
154-323 |
8.42e-07 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 49.12 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 154 IRDVVEAFGAAAERAVTAGFDTVEIHGAHGYLIhsflsplsnnrddeygsgtgrwKLLRDILAAVRSRVPdDFPVLVRIS 233
Cdd:cd04722 66 INDAAAAVDIAAAAARAAGADGVEIHGAVGYLA----------------------REDLELIRELREAVP-DVKVVVKLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 234 ADEwaeggfgideaVELSRVLHEEGCDLVDVSGGGNTPADIPVGPGYQTGFAQRIREAGVPTAAVGLITDPVQAQTILTT 313
Cdd:cd04722 123 PTG-----------ELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALAL 191
|
170
....*....|
gi 518005299 314 GqADAVLIGR 323
Cdd:cd04722 192 G-ADGVIVGS 200
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
158-330 |
8.53e-07 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 49.42 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 158 VEAFGAAAERAVTAGFDTVEIHgahgylihsfL---SPLSNNRDdeYGSG-TGRWKLLRDILAAVRSRVPddFPVLV--R 231
Cdd:cd02801 66 PETLAEAAKIVEELGADGIDLN----------MgcpSPKVTKGG--AGAAlLKDPELVAEIVRAVREAVP--IPVTVkiR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 232 IsadewaeggfGIDE---AVELSRVLHEEGCDLVDVSGggNTPADIPVGPGYQTGFAqRIREA-GVPTAAVGLITDPVQA 307
Cdd:cd02801 132 L----------GWDDeeeTLELAKALEDAGASALTVHG--RTREQRYSGPADWDYIA-EIKEAvSIPVIANGDIFSLEDA 198
|
170 180
....*....|....*....|...
gi 518005299 308 QTILTTGQADAVLIGRAALREPS 330
Cdd:cd02801 199 LRCLEQTGVDGVMIGRGALGNPW 221
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
159-347 |
1.48e-06 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 49.32 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 159 EAFGAAAERAVTAGFDTVEI-----------HGAhgylihsflsplsnnrddeyGSGtgrwkLLRD------ILAAVRSR 221
Cdd:COG0042 74 EELAEAARIAEELGADEIDInmgcpvkkvtkGGA--------------------GAA-----LLRDpelvaeIVKAVVEA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 222 VpdDFPVLV--RIsadewaeggfGIDE----AVELSRVLHEEGCDLVDV---------SGggntPADipvgpgYQTgfAQ 286
Cdd:COG0042 129 V--DVPVTVkiRL----------GWDDddenALEFARIAEDAGAAALTVhgrtreqryKG----PAD------WDA--IA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518005299 287 RIREA-GVPTAAVGLITDPVQAQTILTTGQADAVLIGRAALREPSWSLRAAHELGLNPREIP 347
Cdd:COG0042 185 RVKEAvSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDAYLAGGEAPPP 246
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
158-321 |
2.30e-05 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 45.58 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 158 VEAFGAAAERAVTAGFDTVEIHGahgylihsflsplsnnrddeygsGTGRWKLLRDILAAVRSRVPDDfpvlVRISADew 237
Cdd:COG4948 138 PEEMAEEAREAVARGFRALKLKV-----------------------GGPDPEEDVERVRAVREAVGPD----ARLRVD-- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 238 AEGGFGIDEAVELSRVLHEEGCDLVdvsgggntpaDIPVGPGYQTGFAqRIREA-GVPTAAVGLITDPVQAQTILTTGQA 316
Cdd:COG4948 189 ANGAWTLEEAIRLLRALEDLGLEWI----------EQPLPAEDLEGLA-ELRRAtPVPIAADESLTSRADFRRLIEAGAV 257
|
....*
gi 518005299 317 DAVLI 321
Cdd:COG4948 258 DIVNI 262
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
210-334 |
3.19e-05 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 45.35 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 210 LLRDILAAVRSRVpdDFPVLVRISADeWAEGGFGIDEAVELSrvlheEGCDLVDVSGGGNTPADIPVGPGYQTGFAQRIR 289
Cdd:PRK10415 120 LVKSILTEVVNAV--DVPVTLKIRTG-WAPEHRNCVEIAQLA-----EDCGIQALTIHGRTRACLFNGEAEYDSIRAVKQ 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 518005299 290 EAGVPTAAVGLITDPVQAQTILTTGQADAVLIGRAALREPsWSLR 334
Cdd:PRK10415 192 KVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRP-WIFR 235
|
|
| PRK10550 |
PRK10550 |
tRNA dihydrouridine(16) synthase DusC; |
202-332 |
8.08e-04 |
|
tRNA dihydrouridine(16) synthase DusC;
Pssm-ID: 236713 Cd Length: 312 Bit Score: 40.95 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 202 GSGTGRwKLLRDI------LAAVRSRVPDDFPVLVRISADeWAEGgfgiDEAVELSRVLHEEGCDLVDVSGggNTPADip 275
Cdd:PRK10550 105 GSGGGA-TLLKDPeliyqgAKAMREAVPAHLPVTVKVRLG-WDSG----ERKFEIADAVQQAGATELVVHG--RTKED-- 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518005299 276 vgpGYQtgfAQRI---------REAGVPTAAVGLITDPVQAQTILTTGQADAVLIGRAALREPSWS 332
Cdd:PRK10550 175 ---GYR---AEHInwqaigeirQRLTIPVIANGEIWDWQSAQQCMAITGCDAVMIGRGALNIPNLS 234
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
158-322 |
9.00e-03 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).
Pssm-ID: 239432 [Multi-domain] Cd Length: 357 Bit Score: 37.59 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 158 VEAFGAAAERAVTAGFDTVEIHGAHgylihsflsplsnnrddeYGSGTGRWKLLRDILAAVRSRVPDDFPVLVrisaDew 237
Cdd:cd03316 140 PEELAEEAKRAVAEGFTAVKLKVGG------------------PDSGGEDLREDLARVRAVREAVGPDVDLMV----D-- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518005299 238 AEGGFGIDEAVELSRVLHEEGCDLVdvsgggntpaDIPVGPGYQTGFAqRIREA-GVPTAAVGLITDPVQAQTILTTG-- 314
Cdd:cd03316 196 ANGRWDLAEAIRLARALEEYDLFWF----------EEPVPPDDLEGLA-RLRQAtSVPIAAGENLYTRWEFRDLLEAGav 264
|
170
....*....|.
gi 518005299 315 ---QADAVLIG 322
Cdd:cd03316 265 diiQPDVTKVG 275
|
|
| |
