|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
43-793 |
0e+00 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 1321.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 43 RIAVVGGGPGGLYTAALLKRLAPDREITVHERNAPDDTFGFGVVLSDETLGGIEHADADVYAALKAHFVRWDDIDIVHRG 122
Cdd:PRK08255 2 RIVCIGGGPAGLYFALLMKLLDPAHEVTVVERNRPYDTFGWGVVFSDATLGNLRAADPVSAAAIGDAFNHWDDIDVHFKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 123 HRHTSGGHRFAALGRRRLLEILHERCRALGVGLRFGAEAPDPAELARTHDLVVAADGVHSATREAFRDVFRPHVTGHRCR 202
Cdd:PRK08255 82 RRIRSGGHGFAGIGRKRLLNILQARCEELGVKLVFETEVPDDQALAADADLVIASDGLNSRIRTRYADTFQPDIDTRRCR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 203 YIWLAADFALDAFRFEIAETEHGVMQLHGYPYAADASTVIVEMREEVWRAAGFDELGEEESTARCAKIFADALGGRPLRS 282
Cdd:PRK08255 162 FVWLGTHKVFDAFTFAFEETEHGWFQAHAYRFDDDTSTFIVETPEEVWRAAGLDEMSQEESIAFCEKLFADYLDGHPLMS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 283 NN-----SAWTTFRTVVNERWSHGNT----VLLGDAAHTAHFSIGSGTKLAVEDALALAACLEERPSLAEALAAY-EEER 352
Cdd:PRK08255 242 NAshlrgSAWINFPRVVCERWVHWNRrvpvVLMGDAAHTAHFSIGSGTKLALEDAIELARCLHEHPGDLPAALAAyEEER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 353 RPVVASTQRAAKASMEWFEDLARYVDQPPRQFAFNLLTRSRRVTHDNLRLRDAGFTGSVEREF----GCAVG--TPPMFT 426
Cdd:PRK08255 322 RVEVLRIQNAARNSTEWFENVERYAGLEPEQFAYSLLTRSQRISHENLRLRDAAWLEGYERWFarraGAPVArpPPPMFT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 427 PFRLRDLTLRNRVVVSPMDMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGEAWRRIT 506
Cdd:PRK08255 402 PFRLRGLTLKNRVVVSPMAMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDEQEAAWKRIV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 507 DFVHASAPgTAIGVQLGHSGRKGSTRLMWEGMDEPLPDGNWPLVAPSPLPYRPDGQTPRELSRAQLTDIREQFTSAAVRA 586
Cdd:PRK08255 482 DFVHANSD-AKIGIQLGHSGRKGSTRLGWEGIDEPLEEGNWPLISASPLPYLPGSQVPREMTRADMDRVRDDFVAAARRA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 587 ARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSATDWAEGGTAPEEA 666
Cdd:PRK08255 561 AEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVEGGNTPDDA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 667 VAIARAFAAHGVDAVDVSTGQVVADERPEFGRSYQTPYADRIRHEAGVPVIAVGAISSWDDVNSLILAGRADLCALARPH 746
Cdd:PRK08255 641 VEIARAFKAAGADLIDVSSGQVSKDEKPVYGRMYQTPFADRIRNEAGIATIAVGAISEADHVNSIIAAGRADLCALARPH 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1036854380 747 LYDPHWTLHAAAEQGYEgpGARWPAPYRAGSRPPRTGRTDAPRPRLT 793
Cdd:PRK08255 721 LADPAWTLHEAAEIGYR--DVAWPKQYLAGKRQLERNLERAAAPALQ 765
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
424-759 |
3.89e-180 |
|
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: 519.36 E-value: 3.89e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 424 MFTPFRLRDLTLRNRVVVSPMDMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGEAWR 503
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMCQYSAEDGVATDWHLVHYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDEQIEALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 504 RITDFVHASapGTAIGVQLGHSGRKGSTRLMWEGMDEPLPD--GNWPLVAPSPLPYRPDGQTPRELSRAQLTDIREQFTS 581
Cdd:cd02932 81 RIVDFIHSQ--GAKIGIQLAHAGRKASTAPPWEGGGPLLPPggGGWQVVAPSAIPFDEGWPTPRELTREEIAEVVDAFVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 582 AAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSATDWAEGGT 661
Cdd:cd02932 159 AARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVEGGW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 662 APEEAVAIARAFAAHGVDAVDVSTGQVVADERPEFGRSYQTPYADRIRHEAGVPVIAVGAISSWDDVNSLILAGRADLCA 741
Cdd:cd02932 239 DLEDSVELAKALKELGVDLIDVSSGGNSPAQKIPVGPGYQVPFAERIRQEAGIPVIAVGLITDPEQAEAILESGRADLVA 318
|
330
....*....|....*...
gi 1036854380 742 LARPHLYDPHWTLHAAAE 759
Cdd:cd02932 319 LGRELLRNPYWPLHAAAE 336
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
421-784 |
1.16e-135 |
|
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: 406.48 E-value: 1.16e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 421 TPPMFTPFRLRDLTLRNRVVVSPMDMYSA-VDGVPGDFHLVHLGARALGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQG 499
Cdd:COG1902 4 MPKLFSPLTLGGLTLKNRIVMAPMTRGRAdEDGVPTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDEQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 500 EAWRRITDFVHASapGTAIGVQLGHSGRKGSTRLMwegmdeplpdGNWPLVAPSPLPYRPDGQTPRELSRAQLTDIREQF 579
Cdd:COG1902 84 AGLRRVTDAVHAA--GGKIFIQLWHAGRKAHPDLP----------GGWPPVAPSAIPAPGGPPTPRALTTEEIERIIEDF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 580 TSAAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSATDWAEG 659
Cdd:COG1902 152 AAAARRAKEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 660 GTAPEEAVAIARAFAAHGVDAVDVSTGQVVADERP--EFGRSYQTPYADRIRHEAGVPVIAVGAISSWDDVNSLILAGRA 737
Cdd:COG1902 232 GLTLEESVELAKALEEAGVDYLHVSSGGYEPDAMIptIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDA 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1036854380 738 DLCALARPHLYDPHWTLHAAAEQGYE-----GPGARWPAPYR--AGSRPPRTGR 784
Cdd:COG1902 312 DLVALGRPLLADPDLPNKAAAGRGDEirpciGCNQCLPTFYGgaSCYVDPRLGR 365
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
424-776 |
1.03e-106 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 330.51 E-value: 1.03e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 424 MFTPFRLRDLTLRNRVVVSPMDMYSA--VDGVPGDFHLVHLGARALGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGEA 501
Cdd:PRK13523 3 LFSPYTIKDVTLKNRIVMSPMCMYSSenKDGKVTNFHLIHYGTRAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHIEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 502 WRRITDFVHASapGTAIGVQLGHSGRKGSTrlmwEGmdeplpdgnwPLVAPSPLPYRPDGQTPRELSRAQLTDIREQFTS 581
Cdd:PRK13523 83 LHKLVTFIHDH--GAKAAIQLAHAGRKAEL----EG----------DIVAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 582 AAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGerPMTVRVSATDWAEGGT 661
Cdd:PRK13523 147 AAVRAKEAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVWDG--PLFVRISASDYHPGGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 662 APEEAVAIARAFAAHGVDAVDVSTGQVVADERPEFgRSYQTPYADRIRHEAGVPVIAVGAISSWDDVNSLILAGRADLCA 741
Cdd:PRK13523 225 TVQDYVQYAKWMKEQGVDLIDVSSGAVVPARIDVY-PGYQVPFAEHIREHANIATGAVGLITSGAQAEEILQNNRADLIF 303
|
330 340 350
....*....|....*....|....*....|....*
gi 1036854380 742 LARPHLYDPHWTLHAAAEQGYEGPGarwPAPYRAG 776
Cdd:PRK13523 304 IGRELLRNPYFPRIAAKELGFEIEA---PKQYERA 335
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
425-752 |
5.57e-95 |
|
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: 299.49 E-value: 5.57e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 425 FTPFRLRDLTLRNRVVVSPMD-MYSAVDGVPGDFHLVHLGARALGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGEAWR 503
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTeNMATEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 504 RITDFVHASapGTAIGVQLGHSGRKgsTRLMWEGMdeplpdgnwPLVAPSPLPYRPDGQTPRELSRAQLTDIREQFTSAA 583
Cdd:cd02803 81 KLTEAVHAH--GAKIFAQLAHAGRQ--AQPNLTGG---------PPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 584 VRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSATDWAEGGTAP 663
Cdd:cd02803 148 RRAKEAGFDGVEIHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 664 EEAVAIARAFAAHGVDAVDVSTGQVVADE----RPEFGRSYQTPYADRIRHEAGVPVIAVGAISSWDDVNSLILAGRADL 739
Cdd:cd02803 228 EEAIEIAKALEEAGVDALHVSGGSYESPPpiipPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADL 307
|
330
....*....|...
gi 1036854380 740 CALARPHLYDPHW 752
Cdd:cd02803 308 VALGRALLADPDL 320
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
424-751 |
3.55e-68 |
|
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: 229.04 E-value: 3.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 424 MFTPFRLRDLTLRNRVVVSPMDMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGEAWR 503
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPGFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 504 RITDFVHASapGTAIGVQLGHSGRKGSTrlmwegmdeplpDGNW-PLVAPSPLPYRPDGQTPRELSRAQLTDIREQFTSA 582
Cdd:cd04734 81 RLAEAVHAH--GAVIMIQLTHLGRRGDG------------DGSWlPPLAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 583 AVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSATDWAEGGTA 662
Cdd:cd04734 147 ARRCQAGGLDGVELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 663 PEEAVAIARAFAAHG-VDAVDVSTGQVVADERPE-------FGRSYQTPYADRIRHEAGVPVIAVGAISSWDDVNSLILA 734
Cdd:cd04734 227 PDEALEIAARLAAEGlIDYVNVSAGSYYTLLGLAhvvpsmgMPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAA 306
|
330
....*....|....*..
gi 1036854380 735 GRADLCALARPHLYDPH 751
Cdd:cd04734 307 GHADMVGMTRAHIADPH 323
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
423-753 |
1.55e-60 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 208.46 E-value: 1.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 423 PMFTPFRLRDLTLRNRVVVSPMDMYSAVD--GVPGDFHLVHLGARALGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGE 500
Cdd:pfam00724 1 KLFEPIKIGNTTLKNRIVMAPMTRLRSLDdgTKATGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 501 AWRRITDFVHASapGTAIGVQLGHSGRkgstrlmwEGMDEPLPDGnwPLVAPSPLPYRPDGQ----TPR-ELSRAQLTDI 575
Cdd:pfam00724 81 GWRKLTEAVHKN--GSKAGVQLWHLGR--------EAPMEYRPDL--EVDGPSDPFALGAQEfeiaSPRyEMSKEEIKQH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 576 REQFTSAAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSATD 655
Cdd:pfam00724 149 IQDFVDAAKRAREAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 656 WAEGGTAPEEAVAIARAFAAHGVDAVDVSTGQVV-ADERPEFG----RSYQTPYADRIRHEAGVPVIAVGAISSwDDVNS 730
Cdd:pfam00724 229 VVGPGLDFAETAQFIYLLAELGVRLPDGWHLAYIhAIEPRPRGagpvRTRQQHNTLFVKGVWKGPLITVGRIDD-PSVAA 307
|
330 340
....*....|....*....|....
gi 1036854380 731 LILA-GRADLCALARPHLYDPHWT 753
Cdd:pfam00724 308 EIVSkGRADLVAMGRPFLADPDLP 331
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
423-652 |
8.33e-60 |
|
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: 206.17 E-value: 8.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 423 PMFTPFRLRDLTLRNRVVVSPMD-MYSAVDGVPGDFHLVHLGARAlgGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGEA 501
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIVMAPLTrSRADPDGVPTDLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIYTDEQVEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 502 WRRITDFVHASapGTAIGVQLGHSGRKGSTRLmwegmdepLPDGNwPLVAPSPLP-----YRPDGQ----TPRELSRAQL 572
Cdd:cd02933 79 WKKVTDAVHAK--GGKIFLQLWHVGRVSHPSL--------LPGGA-PPVAPSAIAaegkvFTPAGKvpypTPRALTTEEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 573 TDIREQFTSAAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERpMTVRVS 652
Cdd:cd02933 148 PGIVADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADR-VGIRLS 226
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
424-760 |
1.82e-55 |
|
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: 194.81 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 424 MFTPFRLRDLTLRNRVVVSpmDMYSAVDGVPGDFHLVHL--GARALGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGEA 501
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMG--SMHTGLEELDDGIDRLAAfyAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 502 WRRITDFVHASapGTAIGVQLGHSGRKGSTRLMwegmdeplpdgnwplVAPSPLPYRPDGQTPRELSRAQLTDIREQFTS 581
Cdd:cd02930 79 HRLITDAVHAE--GGKIALQILHAGRYAYHPLC---------------VAPSAIRAPINPFTPRELSEEEIEQTIEDFAR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 582 AAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSATDWAEGGT 661
Cdd:cd02930 142 CAALAREAGYDGVEIMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 662 APEEAVAIARAFAAHGVDAVDVSTG------QVVADERPefgRSYQTPYADRIRHEAGVPVIAVGAISSWDDVNSLILAG 735
Cdd:cd02930 222 TWEEVVALAKALEAAGADILNTGIGwhearvPTIATSVP---RGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADG 298
|
330 340
....*....|....*....|....*
gi 1036854380 736 RADLCALARPHLYDPHWTLHAAAEQ 760
Cdd:cd02930 299 DADMVSMARPFLADPDFVAKAAAGR 323
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
424-760 |
5.90e-55 |
|
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: 193.20 E-value: 5.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 424 MFTPFRLR-DLTLRNRVVVSPMDMYSAV-DGVPGDFHLVHLGARAlGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGEA 501
Cdd:cd04735 1 LFEPFTLKnGVTLKNRFVMAPMTTYSSNpDGTITDDELAYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 502 WRRITDFVHA-SAPgtAIgVQLGHSGRKGSTRLmwegmdepLPDGNwpLVAPSPL-PYRPDGQTPRELSRAQLTDIREQF 579
Cdd:cd04735 80 LRKLAQAIKSkGAK--AI-LQIFHAGRMANPAL--------VPGGD--VVSPSAIaAFRPGAHTPRELTHEEIEDIIDAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 580 TSAAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAV--WPGERPMTV--RVSATD 655
Cdd:cd04735 147 GEATRRAIEAGFDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVidKHADKDFILgyRFSPEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 656 WAEGGTAPEEAVAIARAFAAHGVDAVDVSTGQVvaDERPEFGRSYQTPYADRI-RHEAG-VPVIAVGAISSWDDVNSLIL 733
Cdd:cd04735 227 PEEPGIRMEDTLALVDKLADKGLDYLHISLWDF--DRKSRRGRDDNQTIMELVkERIAGrLPLIAVGSINTPDDALEALE 304
|
330 340
....*....|....*....|....*..
gi 1036854380 734 AGrADLCALARPHLYDPHWTLHAAAEQ 760
Cdd:cd04735 305 TG-ADLVAIGRGLLVDPDWVEKIKEGR 330
|
|
| mycofact_OYE_2 |
TIGR03997 |
mycofactocin system FadH/OYE family oxidoreductase 2; The yeast protein called old yellow ... |
424-764 |
1.19e-52 |
|
mycofactocin system FadH/OYE family oxidoreductase 2; The yeast protein called old yellow enzyme and FadH from Escherichia coli (2,4-dienoyl CoA reductase) are enzymes with 4Fe-4S, FMN, and FAD prosthetic groups, and interact with NADPH as well as substrate. Members of this related protein family occur in the vicinity of the putative mycofactocin biosynthesis operon in a number of Actinobacteria such as Frankia sp. and Rhodococcus sp., in Pelotomaculum thermopropionicum SI (Firmicutes), and in Geobacter uraniireducens Rf4 (Deltaproteobacteria). The function of this oxidoreductase is unknown.
Pssm-ID: 274912 [Multi-domain] Cd Length: 644 Bit Score: 194.14 E-value: 1.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 424 MFTPFRLRDLTLRNRVVVSPMDMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGEAWR 503
Cdd:TIGR03997 2 LFSPLRIGPVTLPNRIVFGAHLTNYAVNNLPSERHAAYYAERAKGGAGLIITEELSVHPSDRPYEKLIDGYRPAVIPGYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 504 RITDFVHASapGTAIGVQLGHSGRKGS---TRLmwegmdeplpdgnwPLVAPSPLPYRPDGQTPRELSRAQLTDIREQFT 580
Cdd:TIGR03997 82 RITDAVHAH--GVKIFAQLNHNGGQGDssySRL--------------PVWAPSAVPDPLFREVPKAMEESDIAEVVAGFA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 581 SAAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSATDWAEGG 660
Cdd:TIGR03997 146 RVAGHVVAGGFDGIEIQASHSSLVRQFLSPLTNRRTDEYGGSLENRARFLLEVLEAVRKAIGPDRALGVRLCGDELVPGG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 661 TAPEEAVAIARAFAAHG-VDAVDVSTGQ-------VVADERPEFGrsYQTPYADRIRHEAGVPVIAVGAISSWDDVNSLI 732
Cdd:TIGR03997 226 LTLADAVEIARLLEALGlVDYINTSIGVatytlhlVEASMHVPPG--YAAFLAAAIREAVDLPVFAVGRINDPAQAERAL 303
|
330 340 350
....*....|....*....|....*....|..
gi 1036854380 733 LAGRADLCALARPHLYDPHwtLHAAAEQGYEG 764
Cdd:TIGR03997 304 AEGQADLVGMVRGQIADPD--FAAKALEGREE 333
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
425-751 |
1.93e-52 |
|
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: 185.87 E-value: 1.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 425 FTPFRLRD-LTLRNRVVVSPMD--MYSAvDGVPGDfHLVHLGAR-ALGGAGLVMTEMVCVSAEGRITPGCAG---LYTNR 497
Cdd:cd04733 2 GQPLTLPNgATLPNRLAKAAMSerLADG-RGLPTP-ELIRLYRRwAEGGIGLIITGNVMVDPRHLEEPGIIGnvvLESGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 498 QGEAWRRITDfvHASAPGTAIGVQLGHSGRKGSTRLmwegmdeplpdgNWPLVAPSPLPYRP----DGQTPRELSRAQLT 573
Cdd:cd04733 80 DLEAFREWAA--AAKANGALIWAQLNHPGRQSPAGL------------NQNPVAPSVALDPGglgkLFGKPRAMTEEEIE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 574 DIREQFTSAAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSA 653
Cdd:cd04733 146 DVIDRFAHAARLAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 654 TDWAEGGTAPEEAVAIARAFAAHGVDAVDVSTG-------QVVADERPEFGRSYQTPYADRIRHEAGVPVIAVGAISSWD 726
Cdd:cd04733 226 ADFQRGGFTEEDALEVVEALEEAGVDLVELSGGtyespamAGAKKESTIAREAYFLEFAEKIRKVTKTPLMVTGGFRTRA 305
|
330 340
....*....|....*....|....*
gi 1036854380 727 DVNSLILAGRADLCALARPHLYDPH 751
Cdd:cd04733 306 AMEQALASGAVDGIGLARPLALEPD 330
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
424-752 |
3.01e-50 |
|
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: 180.59 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 424 MFTPFRLRDLTLRNRVVVSPMDMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMVCV-----SAEGRITPgcagLYTNRQ 498
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPMTRSFSPGGVPGQDVAAYYRRRAAGGVGLIITEGTAVdhpaaSGDPNVPR----FHGEDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 499 GEAWRRITDFVHASapGTAIGVQLGHSGrkgstrLMWEGMDEPLPDGnwPLVAPSPLpYRPDGQTPRELSRAQLTDIREQ 578
Cdd:cd04747 77 LAGWKKVVDEVHAA--GGKIAPQLWHVG------AMRKLGTPPFPDV--PPLSPSGL-VGPGKPVGREMTEADIDDVIAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 579 FTSAAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSatDW-- 656
Cdd:cd04747 146 FARAAADARRLGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFS--QWkq 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 657 ----AEGGTAPEEAVAIARAFAAHGVDAVDVSTGQVvadERPEFGRSYQTpYADRIRHEAGVPVIAVGAI---------- 722
Cdd:cd04747 224 qdytARLADTPDELEALLAPLVDAGVDIFHCSTRRF---WEPEFEGSELN-LAGWTKKLTGLPTITVGSVgldgdfigaf 299
|
330 340 350
....*....|....*....|....*....|....*...
gi 1036854380 723 --------SSWDDVNSLILAGRADLCALARPHLYDPHW 752
Cdd:cd04747 300 agdegaspASLDRLLERLERGEFDLVAVGRALLSDPAW 337
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
423-652 |
2.60e-43 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 161.05 E-value: 2.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 423 PMFTPFRLRDLTLRNRVVVSPMDMYSAVDgvPGDFHLVHLGA--RALGGAGLVMTEMVCVSAEGRITPGCAGLYTNRQGE 500
Cdd:PRK10605 2 KLFSPLKVGAITAPNRVFMAPLTRLRSIE--PGDIPTPLMAEyyRQRASAGLIISEATQISAQAKGYAGAPGLHSPEQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 501 AWRRITDFVHASapGTAIGVQLGHSGRKGSTRLMwegmdeplPDGNWPlVAPSPLP--------------YRPDGQTPRE 566
Cdd:PRK10605 80 AWKKITAGVHAE--GGHIAVQLWHTGRISHASLQ--------PGGQAP-VAPSAINagtrtslrdengqaIRVETSTPRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 567 LSRAQLTDIREQFTSAAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERp 646
Cdd:PRK10605 149 LELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGADR- 227
|
....*.
gi 1036854380 647 MTVRVS 652
Cdd:PRK10605 228 IGIRIS 233
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
418-655 |
5.22e-38 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 146.54 E-value: 5.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 418 AVGTPPMFTPFRLRDLTLRNRVVVSPMDMYSAVDGVPGDFHLVHLGARALGGaGLVMTEMVCVSAEGRITPGCAGLYTNR 497
Cdd:PLN02411 6 GNSNETLFSPYKMGRFDLSHRVVLAPMTRCRALNGIPNAALAEYYAQRSTPG-GFLISEGTLISPTAPGFPHVPGIYSDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 498 QGEAWRRITDFVHASapGTAIGVQLGHSGRkGSTRLMWEGMDEPLPDGNWPLVAPsplpYR---PDGQ-----TPRELSR 569
Cdd:PLN02411 85 QVEAWKKVVDAVHAK--GSIIFCQLWHVGR-ASHQVYQPGGAAPISSTNKPISER----WRilmPDGSygkypKPRALET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 570 AQLTDIREQFTSAAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERpMTV 649
Cdd:PLN02411 158 SEIPEVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGADR-VGV 236
|
....*..
gi 1036854380 650 RVS-ATD 655
Cdd:PLN02411 237 RVSpAID 243
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
423-750 |
5.07e-36 |
|
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: 140.18 E-value: 5.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 423 PMFTPFRLRDLTLRNRVVVSPMDMYSAVDGvPGdFHLVHLGARALGGAGLVMTEMVCVSAEGRITP-GCAGLYTNRQGEA 501
Cdd:cd02929 7 ILFEPIKIGPVTARNRFYQVPHCNGMGYRK-PS-AQAAMRGIKAEGGWGVVNTEQCSIHPSSDDTPrISARLWDDGDIRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 502 WRRITDFVHASapGTAIGVQLGHSGRKGSTRLMWEgmdeplpdgnwPLVAPSPLPYRPDG---QTPRELSRAQLTDIREQ 578
Cdd:cd02929 85 LAAMTDAVHKH--GALAGIELWHGGAHAPNRESRE-----------TPLGPSQLPSEFPTggpVQAREMDKDDIKRVRRW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 579 FTSAAVRAARAGFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSA-TDWA 657
Cdd:cd02929 152 YVDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVdELIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 658 EGGTAPEEAVAIARAFAAHGVDAVDVSTGQVVADE-----RPEfgrSYQTPYADRIRHEAGVPVIAVGAISSWDDVNSLI 732
Cdd:cd02929 232 PGGIESEGEGVEFVEMLDELPDLWDVNVGDWANDGedsrfYPE---GHQEPYIKFVKQVTSKPVVGVGRFTSPDKMVEVV 308
|
330
....*....|....*...
gi 1036854380 733 LAGRADLCALARPHLYDP 750
Cdd:cd02929 309 KSGILDLIGAARPSIADP 326
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
424-752 |
5.64e-36 |
|
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: 140.34 E-value: 5.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 424 MFTPFRLRDLTLRNRVVVSPMDMYSAVDGvPGDFH---LVHLGARALGGAGLVMTEMVCVSAE----GRITPGCAGLYTN 496
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPLGLADN-DGAFNqrgIDYYVERAKGGTGLIITGVTMVDNEieqfPMPSLPCPTYNPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 497 RQGEAWRRITDFVHASapGTAIGVQLGHSgrkgstrlmWEGMDEPLPDGNWPLVAPSPLPYR-PDGQTPRELSRAQLTDI 575
Cdd:cd02931 80 AFIRTAKEMTERVHAY--GTKIFLQLTAG---------FGRVCIPGFLGEDKPVAPSPIPNRwLPEITCRELTTEEVETF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 576 REQFTSAAVRAARAGFDLLELHCAH-GYLLSGFLSPLTNRRTDAYGGSPEKRLRFPLEVFDAVRAVWPGERPMTVRVSA- 653
Cdd:cd02931 149 VGKFGESAVIAKEAGFDGVEIHAVHeGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSVk 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 654 ---TDWAEG----------GTAPEEAVAIARAFAAHGVDAVDVSTGQVVA---DERPEFGRS--YQtPYADRIRHEAGVP 715
Cdd:cd02931 229 syiKDLRQGalpgeefqekGRDLEEGLKAAKILEEAGYDALDVDAGSYDAwywNHPPMYQKKgmYL-PYCKALKEVVDVP 307
|
330 340 350
....*....|....*....|....*....|....*..
gi 1036854380 716 VIAVGAISSWDDVNSLILAGRADLCALARPHLYDPHW 752
Cdd:cd02931 308 VIMAGRMEDPELASEAINEGIADMISLGRPLLADPDV 344
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
39-394 |
1.36e-35 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 137.76 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 39 NHPHRIAVVGGGPGGLYTAALLKRLapDREITVHERNAPDDTFGFGVVLSDETLGGIEhaDADVYAALKAHFVRWDDIDI 118
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARA--GIRVTVVERAPPPRPDGRGIALSPRSLELLR--RLGLWDRLLARGAPIRGIRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 119 --------VHRGHRHTSGGHRFAALGRRRLLEILHERCRALGVGLRFGAEA------PDPAEL------ARTHDLVVAAD 178
Cdd:COG0654 77 rdgsdgrvLARFDAAETGLPAGLVVPRADLERALLEAARALGVELRFGTEVtgleqdADGVTVtladgrTLRADLVVGAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 179 GVHSATREAFRDVFRPHVTGHRCRYIWLAADFAldafrfeiaetehgvmqlhgyPYAADASTVIVEMREEVWRAAgfdel 258
Cdd:COG0654 157 GARSAVRRLLGIGFTGRDYPQRALWAGVRTELR---------------------ARLAAAGPRLGELLELSPRSA----- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 259 geeestarcakifadalggrplrsnnsawTTFRTVVNERWSHGNTVLLGDAAHTAHFSIGSGTKLAVEDALALAACLEER 338
Cdd:COG0654 211 -----------------------------FPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAA 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1036854380 339 PSLAEALAAYE---EERRPVVASTQRAAKASMEWFEDlaryvDQPPRQFAFNLLTRSRR 394
Cdd:COG0654 262 LRGRDDEAALAryeRERRPRAARVQRAADALGRLFHP-----DSPPLRLLRNAGLRLLD 315
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
42-340 |
4.91e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 83.77 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 42 HRIAVVGGGPGGLYTAALLKRLApdreITVH--ERNAPDDTFGFGVVLSDETLGGIEhaDADVYAALKAHFVRWDDIDIv 119
Cdd:PRK06847 5 KKVLIVGGGIGGLSAAIALRRAG----IAVDlvEIDPEWRVYGAGITLQGNALRALR--ELGVLDECLEAGFGFDGVDL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 120 hrghrHTSGGHRFA----------------ALGRRRLLEILHERCRALGVGLRFG------AEAPDPAEL------ARTH 171
Cdd:PRK06847 78 -----FDPDGTLLAelptprlagddlpgggGIMRPALARILADAARAAGADVRLGttvtaiEQDDDGVTVtfsdgtTGRY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 172 DLVVAADGVHSATREA-FRDVFRPHVTGHRCryiWlaadfaldafRFEI---AETEHGVMQLH-----GY-PYAADASTV 241
Cdd:PRK06847 153 DLVVGADGLYSKVRSLvFPDEPEPEYTGQGV---W----------RAVLprpAEVDRSLMYLGpttkaGVvPLSEDLMYL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 242 -IVEMREE---VWRAAGFDELgeEESTARCAKIFADALggRPLRSNNSA--WTTFRTV-VNERWSHGNTVLLGDAAH--T 312
Cdd:PRK06847 220 fVTEPRPDnprIEPDTLAALL--RELLAPFGGPVLQEL--REQITDDAQvvYRPLETLlVPAPWHRGRVVLIGDAAHatT 295
|
330 340
....*....|....*....|....*...
gi 1036854380 313 AHfsIGSGTKLAVEDALALAACLEERPS 340
Cdd:PRK06847 296 PH--LAQGAGMAIEDAIVLAEELARHDS 321
|
|
| PRK07236 |
PRK07236 |
hypothetical protein; Provisional |
43-340 |
4.04e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235980 [Multi-domain] Cd Length: 386 Bit Score: 65.71 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 43 RIAVVGGGPGGLYTAALLKRLAPDreITVHERNAPD-DTFGFGVVLSDETLGGIEHADADVYAAL--KAHFVRWDDID-- 117
Cdd:PRK07236 8 RAVVIGGSLGGLFAALLLRRAGWD--VDVFERSPTElDGRGAGIVLQPELLRALAEAGVALPADIgvPSRERIYLDRDgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 118 IVHR---GHRHTSGGHRFAALGRRRLLEILH--ERCRAL-----GVGLRF--GAEApdpaelarTHDLVVAADGVHSATR 185
Cdd:PRK07236 86 VVQRrpmPQTQTSWNVLYRALRAAFPAERYHlgETLVGFeqdgdRVTARFadGRRE--------TADLLVGADGGRSTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 186 EAFRDVFRPHVTGhrcrYI-W-----------LAADFALDAFRFEIAETEHGVmqlhGYPYA-ADASTVIVEMREE-VW- 250
Cdd:PRK07236 158 AQLLPDVRPTYAG----YVaWrglvdeaalppEARAALRDRFTFQLGPGSHIL----GYPVPgEDGSTEPGKRRYNwVWy 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 251 -RAAGFDELgEEESTARCAKIFADALGGRPLRSNNSAWT----------TFRTVVN---------------ERWSHGNTV 304
Cdd:PRK07236 230 rNAPAGEEL-DELLTDRDGTRRPFSVPPGALRDDVLAELrddaaellapVFAELVEataqpfvqaifdlevPRMAFGRVA 308
|
330 340 350
....*....|....*....|....*....|....*.
gi 1036854380 305 LLGDAAHTAHFSIGSGTKLAVEDALALAACLEERPS 340
Cdd:PRK07236 309 LLGDAAFVARPHTAAGVAKAAADAVALAEALAAAAG 344
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
44-332 |
6.13e-09 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 58.49 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 44 IAVVGGGPGGLYTAALLKRLAPDreITVHERNAPDDTFGFGVVLSDETLGGIEhaDADVYAALKAHFVRWDDIDIVHRGH 123
Cdd:pfam01494 4 VLIVGGGPAGLMLALLLARAGVR--VVLVERHATTSVLPRAHGLNQRTMELLR--QAGLEDRILAEGVPHEGMGLAFYNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 124 RHT------SGGHRFAALGRRRLLEILHERCRALGVGLRFGAEA----------------PDPAELARTH-DLVVAADGV 180
Cdd:pfam01494 80 RRRadldflTSPPRVTVYPQTELEPILVEHAEARGAQVRFGTEVlsleqdgdgvtavvrdRRDGEEYTVRaKYLVGCDGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 181 HSATREAF---RDVFRP---HVTGHRCRYIWLAADFALDAFRFEIAETEH-GVMQLHGYPYAADASTVIVEMREEVwrAA 253
Cdd:pfam01494 160 RSPVRKTLgieFEGFEGvpfGSLDVLFDAPDLSDPVERAFVHYLIYAPHSrGFMVGPWRSAGRERYYVQVPWDEEV--EE 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036854380 254 GFDELGEEESTARCAKIFADALGGRPLRSnNSAWTTfRTVVNERWSHGNTVLLGDAAHTAHFSIGSGTKLAVEDALALA 332
Cdd:pfam01494 238 RPEEFTDEELKQRLRSIVGIDLALVEILW-KSIWGV-ASRVATRYRKGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLA 314
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
43-339 |
9.87e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 51.61 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 43 RIAVVGGGPGGLYTAALLKRLapDREITVHERNAPDDTFGFGVVLSDETLGGIEHADadVYAALK------AHFVRWDDI 116
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQ--GHEVKVFEKNESVKEVGAGIGIGDNVIKKLGNHD--LAKGIKnagqilSTMNLLDDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 117 DIVHRGHRHTSGGHRFAaLGRRRLLEILHERCRALGVGLRFGAEAPDPAELART----------HDLVVAADGVHSATRE 186
Cdd:PRK06753 78 GTLLNKVKLKSNTLNVT-LHRQTLIDIIKSYVKEDAIFTGKEVTKIENETDKVTihfadgeseaFDLCIGADGIHSKVRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 187 AF--RDVFRphVTGHRC-RYIWLAADFAL--DAFRFEIAETEHGVMQL---HGYPYAadasTVIVEMREEVWRA------ 252
Cdd:PRK06753 157 SVnaDSKVR--YQGYTCfRGLIDDIDLKLpdCAKEYWGTKGRFGIVPLlnnQAYWFI----TINAKERDPKYSSfgkphl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 253 -AGFDELGEEestarCAKIFADALGGRPLRSNNSAWTTFRTVVNerwshGNTVLLGDAAHTAHFSIGSGTKLAVEDALAL 331
Cdd:PRK06753 231 qAYFNHYPNE-----VREILDKQSETGILHHDIYDLKPLKSFVY-----GRIVLLGDAAHATTPNMGQGAGQAMEDAIVL 300
|
....*...
gi 1036854380 332 AACLEERP 339
Cdd:PRK06753 301 ANCLNAYD 308
|
|
| Ubi-OHases |
TIGR01988 |
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ... |
44-408 |
4.98e-05 |
|
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273913 [Multi-domain] Cd Length: 385 Bit Score: 46.43 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 44 IAVVGGGPGGLYTAALLKRLAPDreITVHERNAP----DDTFGFGVV-LSD------ETLGGIEHADADVYAALKAHFVr 112
Cdd:TIGR01988 2 IVIVGGGMVGLALALALARSGLK--VALIEATPLpapaDPGFDNRVSaLSAasirllEKLGVWDKIEPARAQPIRDIHV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 113 WDDidiVHRGHRHTSGGHRFA-ALG----RRRLLEILHERCRAL-GVGLRFGAEA------PDPAELAR------THDLV 174
Cdd:TIGR01988 79 SDG---GSFGALRFDADEIGLeALGyvveNRVLQQALWERLQELpNVTLLCPARVvelprhSDHVELTLddgqqlRARLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 175 VAADGVHSATREAFRdvfrPHVTGHRCRYIWLAADFALD------AF-RFeiaeTEHGVMQLhgYPYAADASTVIVEMRE 247
Cdd:TIGR01988 156 VGADGANSKVRQLAG----IPTTGWDYGQSAVVANVKHErphqgtAWeRF----TPTGPLAL--LPLPDNRSSLVWTLPP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 248 EvwRAAGFDELGEEESTARCAKIFADALGGRPLRSNNSAWTTFRTVVNERWSHGnTVLLGDAAHTAHFSIGSGTKLAVED 327
Cdd:TIGR01988 226 E--EAERLLALSDEEFLAELQRAFGSRLGAITLVGERHAFPLSLTHAKRYVAPR-LALIGDAAHTIHPLAGQGLNLGLRD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 328 ALALAACLEERPSLAEALaayeeerrpvvastqrAAKASMEWFEDlARYVDQPPRQFAFNLLTRSRRVTHDNLR-LRDAG 406
Cdd:TIGR01988 303 VAALAEVLEDARRRGEDI----------------GSLRVLQRYER-RRRFDNAAMLGATDGLNRLFSNDFPPLRlLRNLG 365
|
..
gi 1036854380 407 FT 408
Cdd:TIGR01988 366 LR 367
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
296-377 |
9.27e-05 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 45.67 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 296 ERWSHGNTVLLGDAAHTAHFSIGSGTKLAVEDALALAACLE----ERPSLAEALAAYEEERRPVVASTQRAAKASMEWFE 371
Cdd:PRK07045 280 DRYHKRNVVLLGDAAHSIHPITGQGMNLAIEDAGELGACLDlhlsGQIALADALERFERIRRPVNEAVISYGHALATTYH 359
|
....*.
gi 1036854380 372 DLARYV 377
Cdd:PRK07045 360 DRAALV 365
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
152-363 |
4.89e-04 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 43.19 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 152 GVGLRFGAEAPdpaelaRTHDLVVAADGVHSATReafRDVFRPH---------------VTGHRCRYIWLAADFALDAF- 215
Cdd:PRK07588 134 GVRVTFERGTP------RDFDLVIGADGLHSHVR---RLVFGPErdfehylgckvaacvVDGYRPRDERTYVLYNEVGRq 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 216 --RFEIAETEhgVMQLHGYPYAADASTVIVEMREEVWRAAgFDELGEEestarCAKIFAdalggrplRSNNSAWTTFRTV 293
Cdd:PRK07588 205 vaRVALRGDR--TLFLFIFRAEHDNPPLTPAEEKQLLRDQ-FGDVGWE-----TPDILA--------ALDDVEDLYFDVV 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1036854380 294 VN---ERWSHGNTVLLGDAAHTAHFSIGSGTKLAVEDALALAACLEERPSLAEALAAYEEER-RPVVASTQRAA 363
Cdd:PRK07588 269 SQirmDRWSRGRVALVGDAAACPSLLGGEGSGLAITEAYVLAGELARAGGDHRRAFDAYEKRlRPFIAGKQAAA 342
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
49-337 |
6.05e-04 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 42.65 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 49 GGPGGLYTAALLKRlaPDREITVHERnapdDTFGFGVVLSDETLGGI--EHADADVYAALKAHfVRWDDIDIVHRGHRHT 126
Cdd:COG0644 1 AGPAGSAAARRLAR--AGLSVLLLEK----GSFPGDKICGGGLLPRAleELEPLGLDEPLERP-VRGARFYSPGGKSVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 127 SGGHRFAALGRRRLL-EILHERCRALGVGLRFGAEAPDPA--------ELARTH----DLVVAADGVHSATREAFRDVFR 193
Cdd:COG0644 74 PPGRGGGYVVDRARFdRWLAEQAEEAGAEVRTGTRVTDVLrddgrvvvRTGDGEeiraDYVVDADGARSLLARKLGLKRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 194 PHVTGHRCRYI--WLAADFALDAFRFEIAETEHGVMQlHGYP--YAADASTVIVemreevwraagfdelgeeestarcak 269
Cdd:COG0644 154 SDEPQDYALAIkeHWELPPLEGVDPGAVEFFFGEGAP-GGYGwvFPLGDGRVSV-------------------------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036854380 270 ifadalgGRPLRSNnsawttfrtvvNERWSHGNTVLLGDAAHTAHFSIGSGTKLAVEDALALAACLEE 337
Cdd:COG0644 207 -------GIPLGGP-----------RPRLVGDGVLLVGDAAGFVDPLTGEGIHLAMKSGRLAAEAIAE 256
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
39-113 |
6.96e-04 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 43.02 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 39 NHPHRIAVVGGGPGGLYTA-ALLKRLAPDREITVHERNAPddtFGFGVVLSDETLggiEH------ADADVYAALKAHFV 111
Cdd:COG4529 3 GARKRIAIIGGGASGTALAiHLLRRAPEPLRITLFEPRPE---LGRGVAYSTDSP---EHllnvpaGRMSAFPDDPDHFL 76
|
..
gi 1036854380 112 RW 113
Cdd:COG4529 77 RW 78
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
297-362 |
3.29e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 40.65 E-value: 3.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036854380 297 RWSHGNTVLLGDAAHtAHFSIGS-GTKLAVEDALALAACLEERPSLAEALAAYEEERRPVVASTQRA 362
Cdd:PRK07538 293 RWTRGRVTLLGDAAH-PMYPVGSnGASQAILDARALADALAAHGDPEAALAAYEAERRPATAQIVLA 358
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
573-744 |
4.72e-03 |
|
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: 39.11 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 573 TDIREQFTSAAVRAARAGFDLLELHCAHGYllsgflspltnrrtdayggspekRLRFPLEVFDAVRAVWPGeRPMTVRVS 652
Cdd:cd04722 67 NDAAAAVDIAAAAARAAGADGVEIHGAVGY-----------------------LAREDLELIRELREAVPD-VKVVVKLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 653 ATDwaeggtapeeaVAIARAFAAHGVDAVDVSTGQVVADERPEFGRSYQTpyADRIRHEAGVPVIAVGAISSWDDVNSLI 732
Cdd:cd04722 123 PTG-----------ELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLL--LILAKRGSKVPVIAGGGINDPEDAAEAL 189
|
170
....*....|..
gi 1036854380 733 LAGrADLCALAR 744
Cdd:cd04722 190 ALG-ADGVIVGS 200
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
17-76 |
8.58e-03 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 39.35 E-value: 8.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036854380 17 ADVRLRRGARPAPTHPQPSDslnhpHRIAVVGGGPGGLYTAALLKRLApdREITVHERNA 76
Cdd:COG0493 102 ADKAFEEGWVKPPPPAPRTG-----KKVAVVGSGPAGLAAAYQLARAG--HEVTVFEALD 154
|
|
| |
