|
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: 552.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQLTLDNRIVIAPMCQYSADEGKATSWHRIHLGQLAFSGAGLLILEATAVEPAGRISPGDLGLWDDETENALR 83
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMCQYSAEDGVATDWHLVHYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDEQIEALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 84 GVVEDIRAwSPIRLGIQLGHAGRKASCAAPWQGGHQ-LALNDGGWQTVAPSAVAFHDGDRAPAELSHADLARIKAAFVAS 162
Cdd:cd02932 81 RIVDFIHS-QGAKIGIQLAHAGRKASTAPPWEGGGPlLPPGGGGWQVVAPSAIPFDEGWPTPRELTREEIAEVVDAFVAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 163 ALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSATDWVEGGWD 242
Cdd:cd02932 160 ARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVEGGWD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 243 CEQSIKFSQQLETLGSDYIHVSSGGLSPQQAITVGPGYQLPFARDIRQQVAIPVIGVGLITDPQQAEAALENGDADLIAL 322
Cdd:cd02932 240 LEDSVELAKALKELGVDLIDVSSGGNSPAQKIPVGPGYQVPFAERIRQEAGIPVIAVGLITDPEQAEAILESGRADLVAL 319
|
330
....*....|....*.
gi 488994502 323 ARAVLYDPHWPWHAAA 338
Cdd:cd02932 320 GRELLRNPYWPLHAAA 335
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
1-361 |
6.46e-160 |
|
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: 452.70 E-value: 6.46e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 1 MSHLFSATRIGQLTLDNRIVIAPMCQYSADE-GKATSWHRIHLGQLAFSGAGLLILEATAVEPAGRISPGDLGLWDDETE 79
Cdd:COG1902 4 MPKLFSPLTLGGLTLKNRIVMAPMTRGRADEdGVPTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDEQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 80 NALRGVVEDIRAWSPiRLGIQLGHAGRKASCAAPwqgghqlalndGGWQTVAPSAVAFHDGDRAPAELSHADLARIKAAF 159
Cdd:COG1902 84 AGLRRVTDAVHAAGG-KIFIQLWHAGRKAHPDLP-----------GGWPPVAPSAIPAPGGPPTPRALTTEEIERIIEDF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 160 VASALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSATDWVEG 239
Cdd:COG1902 152 AAAARRAKEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 240 GWDCEQSIKFSQQLETLGSDYIHVSSGGLSPQQAI--TVGPGYQLPFARDIRQQVAIPVIGVGLITDPQQAEAALENGDA 317
Cdd:COG1902 232 GLTLEESVELAKALEEAGVDYLHVSSGGYEPDAMIptIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDA 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 488994502 318 DLIALARAVLYDPHWPWHAAASLGAQVRVPSQYLRSEPHGLKGT 361
Cdd:COG1902 312 DLVALGRPLLADPDLPNKAAAGRGDEIRPCIGCNQCLPTFYGGA 355
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
4-351 |
1.68e-129 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 388.91 E-value: 1.68e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQLTLDNRIVIAPMCQYSADEGKATSWHRIHLGQLAFSGAGLLILEATAVEPAGRISPGDLGLWDDETENALR 83
Cdd:PRK08255 399 MFTPFRLRGLTLKNRVVVSPMAMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDEQEAAWK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 84 GVVEDIRAWSPIRLGIQLGHAGRKASCAAPWQGGHQlALNDGGWQTVAPSAVAFHDGDRAPAELSHADLARIKAAFVASA 163
Cdd:PRK08255 479 RIVDFVHANSDAKIGIQLGHSGRKGSTRLGWEGIDE-PLEEGNWPLISASPLPYLPGSQVPREMTRADMDRVRDDFVAAA 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 164 LRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSATDWVEGGWDC 243
Cdd:PRK08255 558 RRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVEGGNTP 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 244 EQSIKFSQQLETLGSDYIHVSSGGLSPQQAITVGPGYQLPFARDIRQQVAIPVIGVGLITDPQQAEAALENGDADLIALA 323
Cdd:PRK08255 638 DDAVEIARAFKAAGADLIDVSSGQVSKDEKPVYGRMYQTPFADRIRNEAGIATIAVGAISEADHVNSIIAAGRADLCALA 717
|
330 340
....*....|....*....|....*....
gi 488994502 324 RAVLYDPHWPWHAAASLG-AQVRVPSQYL 351
Cdd:PRK08255 718 RPHLADPAWTLHEAAEIGyRDVAWPKQYL 746
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
2-352 |
1.74e-124 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 361.71 E-value: 1.74e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 2 SHLFSATRIGQLTLDNRIVIAPMCQYSADE--GKATSWHRIHLGQLAFSGAGLLILEATAVEPAGRISPGDLGLWDDETE 79
Cdd:PRK13523 1 SKLFSPYTIKDVTLKNRIVMSPMCMYSSENkdGKVTNFHLIHYGTRAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 80 NALRGVVEDIRAWSPiRLGIQLGHAGRKASCAApwqgghqlalndggwQTVAPSAVAFHDGDRAPAELSHADLARIKAAF 159
Cdd:PRK13523 81 EGLHKLVTFIHDHGA-KAAIQLAHAGRKAELEG---------------DIVAPSAIPFDEKSKTPVEMTKEQIKETVLAF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 160 VASALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVgnTMAVGVRLSATDWVEG 239
Cdd:PRK13523 145 KQAAVRAKEAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVW--DGPLFVRISASDYHPG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 240 GWDCEQSIKFSQQLETLGSDYIHVSSGGLSPqQAITVGPGYQLPFARDIRQQVAIPVIGVGLITDPQQAEAALENGDADL 319
Cdd:PRK13523 223 GLTVQDYVQYAKWMKEQGVDLIDVSSGAVVP-ARIDVYPGYQVPFAEHIREHANIATGAVGLITSGAQAEEILQNNRADL 301
|
330 340 350
....*....|....*....|....*....|...
gi 488994502 320 IALARAVLYDPHWPWHAAASLGAQVRVPSQYLR 352
Cdd:PRK13523 302 IFIGRELLRNPYFPRIAAKELGFEIEAPKQYER 334
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
5-338 |
2.63e-115 |
|
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: 338.01 E-value: 2.63e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 5 FSATRIGQLTLDNRIVIAPMC-QYSADEGKATSWHRIHLGQLAFSGAGLLILEATAVEPAGRISPGDLGLWDDETENALR 83
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTeNMATEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 84 GVVEDIRAW-SPIrlGIQLGHAGRKAscaapwqgghqlALNDGGWQTVAPSAVAFHDGDRAPAELSHADLARIKAAFVAS 162
Cdd:cd02803 81 KLTEAVHAHgAKI--FAQLAHAGRQA------------QPNLTGGPPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 163 ALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSATDWVEGGWD 242
Cdd:cd02803 147 ARRAKEAGFDGVEIHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 243 CEQSIKFSQQLETLGSDYIHVSSGGLSPQQAIT----VGPGYQLPFARDIRQQVAIPVIGVGLITDPQQAEAALENGDAD 318
Cdd:cd02803 227 LEEAIEIAKALEEAGVDALHVSGGSYESPPPIIpppyVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKAD 306
|
330 340
....*....|....*....|
gi 488994502 319 LIALARAVLYDPHWPWHAAA 338
Cdd:cd02803 307 LVALGRALLADPDLPNKARE 326
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
4-345 |
2.86e-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: 244.06 E-value: 2.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQLTLDNRIVIAPMCQYSADEGKATSWHRIHLGQLAFSGAGLLILEATAVEPAGRISPGDLGLWDDETENALR 83
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPGFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 84 GVVEDIRAWSpIRLGIQLGHAGRKAScaapwqgghqlalNDGGWQTV-APSAVAFHDGDRAPAELSHADLARIKAAFVAS 162
Cdd:cd04734 81 RLAEAVHAHG-AVIMIQLTHLGRRGD-------------GDGSWLPPlAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 163 ALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSATDWVEGGWD 242
Cdd:cd04734 147 ARRCQAGGLDGVELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 243 CEQSIKFSQQLETLGS-DYIHVSSGGLSPQQA-------ITVGPGYQLPFARDIRQQVAIPVIGVGLITDPQQAEAALEN 314
Cdd:cd04734 227 PDEALEIAARLAAEGLiDYVNVSAGSYYTLLGlahvvpsMGMPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAA 306
|
330 340 350
....*....|....*....|....*....|.
gi 488994502 315 GDADLIALARAVLYDPHWPWHAAASLGAQVR 345
Cdd:cd04734 307 GHADMVGMTRAHIADPHLVAKAREGREDDIR 337
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
4-333 |
8.57e-71 |
|
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: 225.17 E-value: 8.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQ-LTLDNRIVIAPMCQYSA-DEGKAT----SWHRIHlgqlaFSGAGLLILEATAVEPAGRISPGDLGLWDDE 77
Cdd:cd04735 1 LFEPFTLKNgVTLKNRFVMAPMTTYSSnPDGTITddelAYYQRR-----AGGVGMVITGATYVSPSGIGFEGGFSADDDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 78 TENALRGVVEDIRAWSPIRLgIQLGHAGRKAscaAPwqgghqlALNDGGwQTVAPSAV-AFHDGDRAPAELSHADLARIK 156
Cdd:cd04735 76 DIPGLRKLAQAIKSKGAKAI-LQIFHAGRMA---NP-------ALVPGG-DVVSPSAIaAFRPGAHTPRELTHEEIEDII 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 157 AAFVASALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGN----TMAVGVRLS 232
Cdd:cd04735 144 DAFGEATRRAIEAGFDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDKhadkDFILGYRFS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 233 ATDWVEGGWDCEQSIKFSQQLETLGSDYIHVSSGGLSpQQAITVGPGYQlPFARDIRQQVA--IPVIGVGLITDPQQAEA 310
Cdd:cd04735 224 PEEPEEPGIRMEDTLALVDKLADKGLDYLHISLWDFD-RKSRRGRDDNQ-TIMELVKERIAgrLPLIAVGSINTPDDALE 301
|
330 340
....*....|....*....|...
gi 488994502 311 ALENGdADLIALARAVLYDPHWP 333
Cdd:cd04735 302 ALETG-ADLVAIGRGLLVDPDWV 323
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
4-333 |
9.48e-70 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 221.94 E-value: 9.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQLTLDNRIVIAPMCQYSA--DEGKATSWHRIHLGQLAFSGAGLLILEATAVEPAGRISPGDLGLWDDETENA 81
Cdd:pfam00724 2 LFEPIKIGNTTLKNRIVMAPMTRLRSldDGTKATGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 82 LRGVVEDIRAWSPiRLGIQLGHAGRKAscaaPWQGGHQLALndggwqtVAPSAVAFHDGDRAPA-----ELSHADLARIK 156
Cdd:pfam00724 82 WRKLTEAVHKNGS-KAGVQLWHLGREA----PMEYRPDLEV-------DGPSDPFALGAQEFEIaspryEMSKEEIKQHI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 157 AAFVASALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSATDW 236
Cdd:pfam00724 150 QDFVDAAKRAREAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 237 VEGGWDCEQSIKFSQQLETLGSDYIHVSSGGL------SPQQAITVGPGYQLpFARDIRQQVAIPVIGVGLITDPQQAEA 310
Cdd:pfam00724 230 VGPGLDFAETAQFIYLLAELGVRLPDGWHLAYihaiepRPRGAGPVRTRQQH-NTLFVKGVWKGPLITVGRIDDPSVAAE 308
|
330 340
....*....|....*....|...
gi 488994502 311 ALENGDADLIALARAVLYDPHWP 333
Cdd:pfam00724 309 IVSKGRADLVAMGRPFLADPDLP 331
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
3-325 |
3.23e-62 |
|
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: 202.32 E-value: 3.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 3 HLFSATRIGQLTLDNRIVIAPM--CQySADEGKATSWHRIHLGQLAfsGAGLLILEATAVEPAGRISPGDLGLWDDETEN 80
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIVMAPLtrSR-ADPDGVPTDLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIYTDEQVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 81 ALRGVVEDIRAwspiRLG---IQLGHAGRKAscaapwqggHQlALNDGGWQTVAPSAVA-----FHDGDRA----PAELS 148
Cdd:cd02933 78 GWKKVTDAVHA----KGGkifLQLWHVGRVS---------HP-SLLPGGAPPVAPSAIAaegkvFTPAGKVpyptPRALT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 149 HADLARIKAAFVASALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTmAVG 228
Cdd:cd02933 144 TEEIPGIVADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGAD-RVG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 229 VRLS--ATDWVEGGWDCEQSIK-FSQQLETLGSDYIHVSSGGLSPQqaitvGPGYQLPFARDIRQQVAIPVIGVGLItDP 305
Cdd:cd02933 223 IRLSpfGTFNDMGDSDPEATFSyLAKELNKRGLAYLHLVEPRVAGN-----PEDQPPDFLDFLRKAFKGPLIAAGGY-DA 296
|
330 340
....*....|....*....|
gi 488994502 306 QQAEAALENGDADLIALARA 325
Cdd:cd02933 297 ESAEAALADGKADLVAFGRP 316
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
13-333 |
7.19e-62 |
|
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: 201.66 E-value: 7.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 13 LTLDNRIVIAPM--CQYSADeGKATSWHrIHL-GQLAFSGAGLLILEATAVEPAGRISPGDLGLwdDETENALRgvVEDI 89
Cdd:cd04733 11 ATLPNRLAKAAMseRLADGR-GLPTPEL-IRLyRRWAEGGIGLIITGNVMVDPRHLEEPGIIGN--VVLESGED--LEAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 90 RAW--------SPIRLgiQLGHAGRKAscaapwqgghQLALNDGGWqtvAPSAVAFHDGDR----APAELSHADLARIKA 157
Cdd:cd04733 85 REWaaaakangALIWA--QLNHPGRQS----------PAGLNQNPV---APSVALDPGGLGklfgKPRAMTEEEIEDVID 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 158 AFVASALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSATDWV 237
Cdd:cd04733 150 RFAHAARLAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 238 EGGWDCEQSIKFSQQLETLGSDYIHVSSG------GLSPQQAITVGPG-YQLPFARDIRQQVAIPVIGVGLITDPQQAEA 310
Cdd:cd04733 230 RGGFTEEDALEVVEALEEAGVDLVELSGGtyespaMAGAKKESTIAREaYFLEFAEKIRKVTKTPLMVTGGFRTRAAMEQ 309
|
330 340
....*....|....*....|...
gi 488994502 311 ALENGDADLIALARAVLYDPHWP 333
Cdd:cd04733 310 ALASGAVDGIGLARPLALEPDLP 332
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
4-332 |
4.13e-60 |
|
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: 197.51 E-value: 4.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQLTLDNRIVIAPMcqYSADEGKATSWHRIHL--GQLAFSGAGLLILEATAVEPAGRISPGDLGLWDDETENA 81
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSM--HTGLEELDDGIDRLAAfyAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 82 LRGVVEDIRAwSPIRLGIQLGHAGRKASCAAPwqgghqlalndggwqtVAPSAVAFHDGDRAPAELSHADLARIKAAFVA 161
Cdd:cd02930 79 HRLITDAVHA-EGGKIALQILHAGRYAYHPLC----------------VAPSAIRAPINPFTPRELSEEEIEQTIEDFAR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 162 SALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSATDWVEGGW 241
Cdd:cd02930 142 CAALAREAGYDGVEIMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 242 DCEQSIKFSQQLETLGSDYIHVSSG---GLSPQQAITVGPGYQLPFARDIRQQVAIPVIGVGLITDPQQAEAALENGDAD 318
Cdd:cd02930 222 TWEEVVALAKALEAAGADILNTGIGwheARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDAD 301
|
330
....*....|....
gi 488994502 319 LIALARAVLYDPHW 332
Cdd:cd02930 302 MVSMARPFLADPDF 315
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
4-333 |
1.47e-47 |
|
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: 164.80 E-value: 1.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQLTLDNRIVIAPMCQYSADEGKAT----SWHRihlgQLAFSGAGLLILEATAV-EPAGRISPGDLGLWDDET 78
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPMTRSFSPGGVPGqdvaAYYR----RRAAGGVGLIITEGTAVdHPAASGDPNVPRFHGEDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 79 ENALRGVVEDIRAwSPIRLGIQLGHAGRKASCAAPWqgghqlalnDGGWQTVAPSAVaFHDGDRAPAELSHADLARIKAA 158
Cdd:cd04747 77 LAGWKKVVDEVHA-AGGKIAPQLWHVGAMRKLGTPP---------FPDVPPLSPSGL-VGPGKPVGREMTEADIDDVIAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 159 FVASALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSatDWVE 238
Cdd:cd04747 146 FARAAADARRLGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFS--QWKQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 239 GgwDCEQSIKFS-QQLETL-------GSDYIHVSSGGL-SPQqaitvGPGYQLPFARDIRQQVAIPVIGVGLI------- 302
Cdd:cd04747 224 Q--DYTARLADTpDELEALlaplvdaGVDIFHCSTRRFwEPE-----FEGSELNLAGWTKKLTGLPTITVGSVgldgdfi 296
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 488994502 303 -----------TDPQQAEAALENGDADLIALARAVLYDPHWP 333
Cdd:cd04747 297 gafagdegaspASLDRLLERLERGEFDLVAVGRALLSDPAWV 338
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
4-333 |
5.17e-46 |
|
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: 160.98 E-value: 5.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQLTLDNRIVIAPMCQ-YSADEGKATSWHRihlGQLAFSGAGLLILEATAVEPAGRISP-GDLGLWDDETENA 81
Cdd:cd02929 8 LFEPIKIGPVTARNRFYQVPHCNgMGYRKPSAQAAMR---GIKAEGGWGVVNTEQCSIHPSSDDTPrISARLWDDGDIRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 82 LRGVVEDIRAWSPIRlGIQLGHAGRKASCaapwQGGHQLALndggwqtvAPSAVAFHDGDRAPA---ELSHADLARIKAA 158
Cdd:cd02929 85 LAAMTDAVHKHGALA-GIELWHGGAHAPN----RESRETPL--------GPSQLPSEFPTGGPVqarEMDKDDIKRVRRW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 159 FVASALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSATDwvE 238
Cdd:cd02929 152 YVDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDE--L 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 239 GGWDCEQSIKFSQQLETLGSDY-----IHVSSGGLSPQQAITVGPGYQLPFARDIRQQVAIPVIGVGLITDPQQAEAALE 313
Cdd:cd02929 230 IGPGGIESEGEGVEFVEMLDELpdlwdVNVGDWANDGEDSRFYPEGHQEPYIKFVKQVTSKPVVGVGRFTSPDKMVEVVK 309
|
330 340
....*....|....*....|
gi 488994502 314 NGDADLIALARAVLYDPHWP 333
Cdd:cd02929 310 SGILDLIGAARPSIADPFLP 329
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
4-333 |
9.50e-42 |
|
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: 149.97 E-value: 9.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQLTLDNRIVIAPMCQYS-ADEGKATSWHRI-HLGQLAFSGAGLLILEATAVEpaGRISPGDLGLWDDETENA 81
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPLGlADNDGAFNQRGIdYYVERAKGGTGLIITGVTMVD--NEIEQFPMPSLPCPTYNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 82 L------RGVVEDIRAWSPiRLGIQLGhAGRKASCAApwqgghqlaLNDGGWQTVAPSAVA-FHDGDRAPAELSHADLAR 154
Cdd:cd02931 79 TafirtaKEMTERVHAYGT-KIFLQLT-AGFGRVCIP---------GFLGEDKPVAPSPIPnRWLPEITCRELTTEEVET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 155 IKAAFVASALRAQRLGFELIELHAAH-GYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTMAVGVRLSA 233
Cdd:cd02931 148 FVGKFGESAVIAKEAGFDGVEIHAVHeGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 234 TDWVEG--------------GWDCEQSIKFSQQLETLGSDYIHVSSGGLSP----QQAITVGPGYQLPFARDIRQQVAIP 295
Cdd:cd02931 228 KSYIKDlrqgalpgeefqekGRDLEEGLKAAKILEEAGYDALDVDAGSYDAwywnHPPMYQKKGMYLPYCKALKEVVDVP 307
|
330 340 350
....*....|....*....|....*....|....*...
gi 488994502 296 VIGVGLITDPQQAEAALENGDADLIALARAVLYDPHWP 333
Cdd:cd02931 308 VIMAGRMEDPELASEAINEGIADMISLGRPLLADPDVV 345
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
4-330 |
6.94e-39 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 141.79 E-value: 6.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQLTLDNRIVIAPMCQY-SADEGK-----ATSWHRihlgQLAfsGAGLLILEATAVEPAGRISPGDLGLWDDE 77
Cdd:PRK10605 3 LFSPLKVGAITAPNRVFMAPLTRLrSIEPGDiptplMAEYYR----QRA--SAGLIISEATQISAQAKGYAGAPGLHSPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 78 TENALRGVVEDIRAWSPiRLGIQLGHAGRKAscaapwqggHQlALNDGGWQTVAPSAVafHDGDR--------------- 142
Cdd:PRK10605 77 QIAAWKKITAGVHAEGG-HIAVQLWHTGRIS---------HA-SLQPGGQAPVAPSAI--NAGTRtslrdengqairvet 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 143 -APAELSHADLARIKAAFVASALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAV 221
Cdd:PRK10605 144 sTPRALELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 222 GNTMaVGVRLSAT---DWVEGGWDCEQ-SIKFSQQLETLGSDYIHVSsgglSPQQAitVGPGYQLPFARDIRQQVAIPVI 297
Cdd:PRK10605 224 GADR-IGIRISPLgtfNNVDNGPNEEAdALYLIEQLGKRGIAYLHMS----EPDWA--GGEPYSDAFREKVRARFHGVII 296
|
330 340 350
....*....|....*....|....*....|...
gi 488994502 298 GVGLITdPQQAEAALENGDADLIALARAVLYDP 330
Cdd:PRK10605 297 GAGAYT-AEKAETLIGKGLIDAVAFGRDYIANP 328
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
4-330 |
2.35e-31 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 122.27 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 4 LFSATRIGQLTLDNRIVIAPMCQYSADEGKATSWHRIHLGQLAFSGaGLLILEATAVEPAGRISPGDLGLWDDETENALR 83
Cdd:PLN02411 12 LFSPYKMGRFDLSHRVVLAPMTRCRALNGIPNAALAEYYAQRSTPG-GFLISEGTLISPTAPGFPHVPGIYSDEQVEAWK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 84 GVVEDIRAWSPIrLGIQLGHAGRkAScaapwqggHQLALNDGG-------------WQTVAPSAVafHDGDRAPAELSHA 150
Cdd:PLN02411 91 KVVDAVHAKGSI-IFCQLWHVGR-AS--------HQVYQPGGAapisstnkpiserWRILMPDGS--YGKYPKPRALETS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 151 DLARIKAAFVASALRAQRLGFELIELHAAHGYLLHQFLSPLSNQRRDEYGGSLENRMRYPLEVFKAIREAVGNTmAVGVR 230
Cdd:PLN02411 159 EIPEVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGAD-RVGVR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 231 LS-ATDWVE---------GGWDCEQSIKFSQQletLGSD--YIHVSSGGLSPQQAITVG-PGY---QLPFARDIRQQVAI 294
Cdd:PLN02411 238 VSpAIDHLDatdsdplnlGLAVVERLNKLQLQ---NGSKlaYLHVTQPRYTAYGQTESGrHGSeeeEAQLMRTLRRAYQG 314
|
330 340 350
....*....|....*....|....*....|....*.
gi 488994502 295 PVIGVGLITDPQQAEaALENGDADLIALARAVLYDP 330
Cdd:PLN02411 315 TFMCSGGFTRELGMQ-AVQQGDADLVSYGRLFISNP 349
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
199-330 |
4.50e-08 |
|
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: 53.87 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 199 YGGSLenrMRYP---LEVFKAIREAVGNTMAVGVRLsatdwvegGWD--CEQSIKFSQQLETLGSDYIHVSsgGLSPQQa 273
Cdd:pfam01207 99 GGAAL---LRNPdlvAQIVKAVVKAVGIPVTVKIRI--------GWDdsHENAVEIAKIVEDAGAQALTVH--GRTRAQ- 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488994502 274 itvgpGYQLP----FARDIRQQVAIPVIGVGLITDPQQAEAALENGDADLIALARAVLYDP 330
Cdd:pfam01207 165 -----NYEGTadwdAIKQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNP 220
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
128-324 |
2.49e-06 |
|
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: 47.58 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 128 QTVAPSAVAFHDGDRApAELSHADlarIKAAFVASALRAQRLGFELIELHAAHGYllhqflsplsnqrrdeyggslenRM 207
Cdd:cd04722 46 KEVLKEVAAETDLPLG-VQLAIND---AAAAVDIAAAAARAAGADGVEIHGAVGY-----------------------LA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 208 RYPLEVFKAIREAVGNtMAVGVRLSATdwveggWDCEQSikfsqQLETLGSDYIHVSSGGLSpqQAITVGPGYQLPFARD 287
Cdd:cd04722 99 REDLELIRELREAVPD-VKVVVKLSPT------GELAAA-----AAEEAGVDEVGLGNGGGG--GGGRDAVPIADLLLIL 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 488994502 288 IRQQVAIPVIGVGLITDPQQAEAALENGdADLIALAR 324
Cdd:cd04722 165 AKRGSKVPVIAGGGINDPEDAAEALALG-ADGVIVGS 200
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
199-330 |
4.77e-06 |
|
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: 47.10 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 199 YGGSLenrMRYP---LEVFKAIREAVGNTMAVGVRLsatdwvegGWDCE-QSIKFSQQLETLGSDYI--HvssgGLSPQQ 272
Cdd:cd02801 100 AGAAL---LKDPelvAEIVRAVREAVPIPVTVKIRL--------GWDDEeETLELAKALEDAGASALtvH----GRTREQ 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994502 273 aitvgpGYQLP----FARDIRQQVAIPVIGVGLITDPQQAEAALENGDADLIALARAVLYDP 330
Cdd:cd02801 165 ------RYSGPadwdYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNP 220
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
207-325 |
7.35e-06 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 47.27 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 207 MRYPlEVFKAIREAVGNTMAVGVRLSatdwVEGGWDCEQS--IKFSQQLETLGSDYIHVSSgglsPQQAITVGPGYQLPF 284
Cdd:PRK10415 115 LQYP-DLVKSILTEVVNAVDVPVTLK----IRTGWAPEHRncVEIAQLAEDCGIQALTIHG----RTRACLFNGEAEYDS 185
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488994502 285 ARDIRQQVAIPVIGVGLITDPQQAEAALENGDADLIALARA 325
Cdd:PRK10415 186 IRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRA 226
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
207-330 |
6.90e-05 |
|
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: 44.31 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 207 MRYP---LEVFKAIREAVGntMAVGV--RLsatdwvegGWDcEQSIKFsqqLETLGsdyiHVSSGGLspqQAITVGP--- 278
Cdd:COG0042 112 LRDPelvAEIVKAVVEAVD--VPVTVkiRL--------GWD-DDDENA---LEFAR----IAEDAGA---AALTVHGrtr 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488994502 279 --GYQ----LPFARDIRQQVAIPVIGVGLITDPQQAEAALENGDADLIALARAVLYDP 330
Cdd:COG0042 171 eqRYKgpadWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEETGCDGVMIGRGALGNP 228
|
|
| G3P_antiterm |
pfam04309 |
Glycerol-3-phosphate responsive antiterminator; Intracellular glycerol is usually converted to ... |
273-315 |
2.79e-04 |
|
Glycerol-3-phosphate responsive antiterminator; Intracellular glycerol is usually converted to glycerol-3-phosphate in an ATP-requiring phosphorylation reaction catalyzed by glycerol kinase (GlpK) glycerol-3-phosphate activates the antiterminator GlpP.
Pssm-ID: 427855 Cd Length: 173 Bit Score: 41.23 E-value: 2.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488994502 273 AITVGPGYQLPFARDIRQQVAIPVIGVGLITDPQQAEAALENG 315
Cdd:pfam04309 119 AVEILPGLMPKVIKEIKEELGIPIIAGGLIRTKEDVEEALKAG 161
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
256-315 |
5.97e-04 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 40.64 E-value: 5.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 256 LGSDYIHVSSGGLSPQQAITVGPGYQLpfARDIRQQVAIPVIGVGLITDPQQAEAALENG 315
Cdd:cd04729 142 LGFDIIGTTLSGYTEETAKTEDPDFEL--LKELRKALGIPVIAEGRINSPEQAAKALELG 199
|
|
| GlpP |
COG1954 |
Glycerol-3-phosphate responsive antiterminator (mRNA-binding) [Transcription]; |
273-315 |
1.33e-03 |
|
Glycerol-3-phosphate responsive antiterminator (mRNA-binding) [Transcription];
Pssm-ID: 441557 Cd Length: 178 Bit Score: 39.31 E-value: 1.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488994502 273 AITVGPGYQLPFARDIRQQVAIPVIGVGLITDPQQAEAALENG 315
Cdd:COG1954 124 AIEILPGIMPKVIKEIKKETGIPIIAGGLIRTKEDVEAALAAG 166
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
211-322 |
2.02e-03 |
|
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.
Pssm-ID: 238188 [Multi-domain] Cd Length: 229 Bit Score: 39.23 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 211 LEVFKAIREAVGNTMAVGVrlsatDWvEGGWDCEQSIKFSQQLETLGSDYIHvssgglSPqqaitvGPGYQLPFARDIRQ 290
Cdd:cd00308 81 IERVRAVREAFGPDARLAV-----DA-NGAWTPKEAIRLIRALEKYGLAWIE------EP------CAPDDLEGYAALRR 142
|
90 100 110
....*....|....*....|....*....|..
gi 488994502 291 QVAIPVIGVGLITDPQQAEAALENGDADLIAL 322
Cdd:cd00308 143 RTGIPIAADESVTTVDDALEALELGAVDILQI 174
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
211-349 |
3.85e-03 |
|
Muconate lactonizing enzyme (MLE) like subgroup 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 residues that can function as general acid/base catalysts, a Lys-X-Lys motif and another conserved lysine. Despite these conserved residues, the members of the MLE subgroup, like muconate lactonizing enzyme, o-succinylbenzoate synthase (OSBS) and N-acylamino acid racemase (NAAAR), catalyze different reactions.
Pssm-ID: 239431 [Multi-domain] Cd Length: 265 Bit Score: 38.48 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994502 211 LEVFKAIREAVGNtmAVGVRLSATdwveGGWDCEQSIKFSQQLETLGSDYIhvssgglspQQAItvgPGYQLPFARDIRQ 290
Cdd:cd03315 116 VAVVAALREAVGD--DAELRVDAN----RGWTPKQAIRALRALEDLGLDYV---------EQPL---PADDLEGRAALAR 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488994502 291 QVAIPVIGVGLITDPQQAEAALENGDADLIAL--ARA-VLYDPHWPWHAAASLGAQVRVPSQ 349
Cdd:cd03315 178 ATDTPIMADESAFTPHDAFRELALGAADAVNIktAKTgGLTKAQRVLAVAEALGLPVMVGSM 239
|
|
| |
