|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
1-758 |
0e+00 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 1443.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 1 MNIVCIGGGPAGLYFGLLMKLQNPKNRVVVVERNRPYDTFGWGVVFSDATLSNLRQADPVSAKTISAEFSHWDDIDVHFK 80
Cdd:PRK08255 1 MRIVCIGGGPAGLYFALLMKLLDPAHEVTVVERNRPYDTFGWGVVFSDATLGNLRAADPVSAAAIGDAFNHWDDIDVHFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 81 GVCNRSGGHGFIGIGRKKLLNILQDRCVELGVELVFETQVTDDQAIAREyqADLLIASDGINSTVRTRYENVFKPDIDPR 160
Cdd:PRK08255 81 GRRIRSGGHGFAGIGRKRLLNILQARCEELGVKLVFETEVPDDQALAAD--ADLVIASDGLNSRIRTRYADTFQPDIDTR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 161 RCRFVWLGTKKIFDAFTFLFAKNEHGWFQVHAYQFQEGLSTFIVETTEETWLKAGIDQMSQEDGIAYCEKLFAPWLDGEK 240
Cdd:PRK08255 159 RCRFVWLGTHKVFDAFTFAFEETEHGWFQAHAYRFDDDTSTFIVETPEEVWRAAGLDEMSQEESIAFCEKLFADYLDGHP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 241 LIANAAHLRGAAiWIRFPRVICGNWVHWTqptqgKDVPVVLMGDAAHTAHFSIGSGTKLALEDAIELCESLKTSGGDLRK 320
Cdd:PRK08255 239 LMSNASHLRGSA-WINFPRVVCERWVHWN-----RRVPVVLMGDAAHTAHFSIGSGTKLALEDAIELARCLHEHPGDLPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 321 GLEHYQKVRSVEVLKIQNAARNSTEWFENVCRYENLAPEQFAYSLLTRSQRISHENLRVRDAVWLENYEQWFAEQTGVTS 400
Cdd:PRK08255 313 ALAAYEEERRVEVLRIQNAARNSTEWFENVERYAGLEPEQFAYSLLTRSQRISHENLRLRDAAWLEGYERWFARRAGAPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 401 KAKVPPMLTPYHVRGITLNNRVVASPTLLYCANQGIPDDFHLVHLGSRALGGVGLVMTEMTAIAPDARVTKGCVGIWNDE 480
Cdd:PRK08255 393 ARPPPPMFTPFRLRGLTLKNRVVVSPMAMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 481 QVTAWQRVTDFIHQKTDAKIGIQLGHAGRRGSTQRGWEKENHPMDADNWPLVSASALPYLPNiSQTPVELSEAQMTTVID 560
Cdd:PRK08255 473 QEAAWKRIVDFVHANSDAKIGIQLGHSGRKGSTRLGWEGIDEPLEEGNWPLISASPLPYLPG-SQVPREMTRADMDRVRD 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 561 QFVAAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVW--SKPLSVRISSTDWV 638
Cdd:PRK08255 552 DFVAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWpaEKPMSVRISAHDWV 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 639 DGGTTVDDAVEIGRAMKQAGADMIDCSSGEVSPQQQPVYGRMYQTPMADRIRNEAGIPVIAVGAITDADQVNSIIAAGRA 718
Cdd:PRK08255 632 EGGNTPDDAVEIARAFKAAGADLIDVSSGQVSKDEKPVYGRMYQTPFADRIRNEAGIATIAVGAISEADHVNSIIAAGRA 711
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1997815582 719 DLCALSRPLLSDPAWVLHECARYGW-ETRWPAPYEYGRQQL 758
Cdd:PRK08255 712 DLCALARPHLADPAWTLHEAAEIGYrDVAWPKQYLAGKRQL 752
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
407-736 |
4.23e-177 |
|
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: 510.50 E-value: 4.23e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 407 MLTPYHVRGITLNNRVVASPTLLYCANQGIPDDFHLVHLGSRALGGVGLVMTEMTAIAPDARVTKGCVGIWNDEQVTAWQ 486
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMCQYSAEDGVATDWHLVHYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDEQIEALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 487 RVTDFIHqKTDAKIGIQLGHAGRRGSTQRGWEKENH--PMDADNWPLVSASALPYLPNiSQTPVELSEAQMTTVIDQFVA 564
Cdd:cd02932 81 RIVDFIH-SQGAKIGIQLAHAGRKASTAPPWEGGGPllPPGGGGWQVVAPSAIPFDEG-WPTPRELTREEIAEVVDAFVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 565 AAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVW--SKPLSVRISSTDWVDGGT 642
Cdd:cd02932 159 AARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWpeDKPLFVRISATDWVEGGW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 643 TVDDAVEIGRAMKQAGADMIDCSSGEVSPQQQPVYGRMYQTPMADRIRNEAGIPVIAVGAITDADQVNSIIAAGRADLCA 722
Cdd:cd02932 239 DLEDSVELAKALKELGVDLIDVSSGGNSPAQKIPVGPGYQVPFAERIRQEAGIPVIAVGLITDPEQAEAILESGRADLVA 318
|
330
....*....|....
gi 1997815582 723 LSRPLLSDPAWVLH 736
Cdd:cd02932 319 LGRELLRNPYWPLH 332
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
402-750 |
1.21e-142 |
|
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: 423.43 E-value: 1.21e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 402 AKVPPMLTPYHVRGITLNNRVVASPTLLYCANQ-GIPDDFHLVHLGSRALGGVGLVMTEMTAIAPDARVTKGCVGIWNDE 480
Cdd:COG1902 2 MKMPKLFSPLTLGGLTLKNRIVMAPMTRGRADEdGVPTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 481 QVTAWQRVTDFIHQKtDAKIGIQLGHAGRRGstqrgwekenHPMDADNWPLVSASALPYlPNISQTPVELSEAQMTTVID 560
Cdd:COG1902 82 QIAGLRRVTDAVHAA-GGKIFIQLWHAGRKA----------HPDLPGGWPPVAPSAIPA-PGGPPTPRALTTEEIERIIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 561 QFVAAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVWSK--PLSVRISSTDWV 638
Cdd:COG1902 150 DFAAAARRAKEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPdfPVGVRLSPTDFV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 639 DGGTTVDDAVEIGRAMKQAGADMIDCSSGEVSPQQQP--VYGRMYQTPMADRIRNEAGIPVIAVGAITDADQVNSIIAAG 716
Cdd:COG1902 230 EGGLTLEESVELAKALEEAGVDYLHVSSGGYEPDAMIptIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASG 309
|
330 340 350
....*....|....*....|....*....|....
gi 1997815582 717 RADLCALSRPLLSDPAWVLHecARYGWETRWPAP 750
Cdd:COG1902 310 DADLVALGRPLLADPDLPNK--AAAGRGDEIRPC 341
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
407-754 |
8.00e-116 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 353.23 E-value: 8.00e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 407 MLTPYHVRGITLNNRVVASPTLLYCANQ--GIPDDFHLVHLGSRALGGVGLVMTEMTAIAPDARVTKGCVGIWNDEQVTA 484
Cdd:PRK13523 3 LFSPYTIKDVTLKNRIVMSPMCMYSSENkdGKVTNFHLIHYGTRAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHIEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 485 WQRVTDFIHqKTDAKIGIQLGHAGRrgstqrgweKENHPMDAdnwplVSASALPYLPNiSQTPVELSEAQMTTVIDQFVA 564
Cdd:PRK13523 83 LHKLVTFIH-DHGAKAAIQLAHAGR---------KAELEGDI-----VAPSAIPFDEK-SKTPVEMTKEQIKETVLAFKQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 565 AAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVWSKPLSVRISSTDWVDGGTTV 644
Cdd:PRK13523 147 AAVRAKEAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVWDGPLFVRISASDYHPGGLTV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 645 DDAVEIGRAMKQAGADMIDCSSGEVSPQQQPVY-GrmYQTPMADRIRNEAGIPVIAVGAITDADQVNSIIAAGRADLCAL 723
Cdd:PRK13523 227 QDYVQYAKWMKEQGVDLIDVSSGAVVPARIDVYpG--YQVPFAEHIREHANIATGAVGLITSGAQAEEILQNNRADLIFI 304
|
330 340 350
....*....|....*....|....*....|.
gi 1997815582 724 SRPLLSDPAWVLHECARYGWETRWPAPYEYG 754
Cdd:PRK13523 305 GRELLRNPYFPRIAAKELGFEIEAPKQYERA 335
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
408-734 |
5.94e-107 |
|
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: 329.92 E-value: 5.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 408 LTPYHVRGITLNNRVVASP-TLLYCANQGIPDDFHLVHLGSRALGGVGLVMTEMTAIAPDARVTKGCVGIWNDEQVTAWQ 486
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPmTENMATEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 487 RVTDFIHQKtDAKIGIQLGHAGRRGstqrgwekenhPMDADNWPLVSASALPYlPNISQTPVELSEAQMTTVIDQFVAAA 566
Cdd:cd02803 81 KLTEAVHAH-GAKIFAQLAHAGRQA-----------QPNLTGGPPPAPSAIPS-PGGGEPPREMTKEEIEQIIEDFAAAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 567 KRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVWSK--PLSVRISSTDWVDGGTTV 644
Cdd:cd02803 148 RRAKEAGFDGVEIHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPdfPVGVRLSADDFVPGGLTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 645 DDAVEIGRAMKQAGADMIDCSSGEVSP----QQQPVYGRMYQTPMADRIRNEAGIPVIAVGAITDADQVNSIIAAGRADL 720
Cdd:cd02803 228 EEAIEIAKALEEAGVDALHVSGGSYESpppiIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADL 307
|
330
....*....|....
gi 1997815582 721 CALSRPLLSDPAWV 734
Cdd:cd02803 308 VALGRALLADPDLP 321
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
407-734 |
2.71e-74 |
|
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: 244.83 E-value: 2.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 407 MLTPYHVRGITLNNRVVASPTLLYCANQGIPDDFHLVHLGSRALGGVGLVMTEMTAIAPDARVTKGCVGIWNDEQVTAWQ 486
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPGFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 487 RVTDFIHQkTDAKIGIQLGHAGRRGSTQRGWEkenhpmdadnwPLVSASALPYlPNISQTPVELSEAQMTTVIDQFVAAA 566
Cdd:cd04734 81 RLAEAVHA-HGAVIMIQLTHLGRRGDGDGSWL-----------PPLAPSAVPE-PRHRAVPKAMEEEDIEEIIAAFADAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 567 KRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVWSK--PLSVRISSTDWVDGGTTV 644
Cdd:cd04734 148 RRCQAGGLDGVELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPdfIVGIRISGDEDTEGGLSP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 645 DDAVEIGRAMKQAGA-DMIDCSSGEVS--PQQQPVYGRM-----YQTPMADRIRNEAGIPVIAVGAITDADQVNSIIAAG 716
Cdd:cd04734 228 DEALEIAARLAAEGLiDYVNVSAGSYYtlLGLAHVVPSMgmppgPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAG 307
|
330
....*....|....*...
gi 1997815582 717 RADLCALSRPLLSDPAWV 734
Cdd:cd04734 308 HADMVGMTRAHIADPHLV 325
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
406-734 |
9.24e-67 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 224.64 E-value: 9.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 406 PMLTPYHVRGITLNNRVVASPTLLYCANQ--GIPDDFHLVHLGSRALGGVGLVMTEMTAIAPDARVTKGCVGIWNDEQVT 483
Cdd:pfam00724 1 KLFEPIKIGNTTLKNRIVMAPMTRLRSLDdgTKATGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 484 AWQRVTDFIHQKtDAKIGIQLGHAGRRGstqrgwekenhPMDADNWP-LVSASALPYLP---NISQTPV-ELSEAQMTTV 558
Cdd:pfam00724 81 GWRKLTEAVHKN-GSKAGVQLWHLGREA-----------PMEYRPDLeVDGPSDPFALGaqeFEIASPRyEMSKEEIKQH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 559 IDQFVAAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQV--WSKPLSVRIS-ST 635
Cdd:pfam00724 149 IQDFVDAAKRAREAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAvgQERIVGYRLSpFD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 636 DWVDGGTTVDDAVEIgRAMKQAGADMIDCSSGE----VSPQQQ-PVYGRMYQTPMADRIRNEAGIPVIAVGAITDADQVN 710
Cdd:pfam00724 229 VVGPGLDFAETAQFI-YLLAELGVRLPDGWHLAyihaIEPRPRgAGPVRTRQQHNTLFVKGVWKGPLITVGRIDDPSVAA 307
|
330 340
....*....|....*....|....
gi 1997815582 711 SIIAAGRADLCALSRPLLSDPAWV 734
Cdd:pfam00724 308 EIVSKGRADLVAMGRPFLADPDLP 331
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
406-731 |
2.08e-59 |
|
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: 204.63 E-value: 2.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 406 PMLTPYHVRGITLNNRVVASP-TLLYCANQGIPDDFHLVHLGSRAlgGVGLVMTEMTAIAPDARVTKGCVGIWNDEQVTA 484
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIVMAPlTRSRADPDGVPTDLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIYTDEQVEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 485 WQRVTDFIHQKtDAKIGIQLGHAGRRGSTqrgwekENHPmdaDNWPLVSASALP-----YLPNISQ---TPVELSEAQMT 556
Cdd:cd02933 79 WKKVTDAVHAK-GGKIFLQLWHVGRVSHP------SLLP---GGAPPVAPSAIAaegkvFTPAGKVpypTPRALTTEEIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 557 TVIDQFVAAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVW-SKPLSVRIS-- 633
Cdd:cd02933 149 GIVADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIgADRVGIRLSpf 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 634 STDWvdgGTTVDDAVEIGRAM-KQAGA------DMIDCSSGEVSPQQQPVygrmyqtpMADRIRNEAGIPVIAVGAItDA 706
Cdd:cd02933 229 GTFN---DMGDSDPEATFSYLaKELNKrglaylHLVEPRVAGNPEDQPPD--------FLDFLRKAFKGPLIAAGGY-DA 296
|
330 340
....*....|....*....|....*
gi 1997815582 707 DQVNSIIAAGRADLCALSRPLLSDP 731
Cdd:cd02933 297 ESAEAALADGKADLVAFGRPFIANP 321
|
|
| mycofact_OYE_2 |
TIGR03997 |
mycofactocin system FadH/OYE family oxidoreductase 2; The yeast protein called old yellow ... |
407-732 |
3.87e-59 |
|
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: 212.24 E-value: 3.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 407 MLTPYHVRGITLNNRVVASPTLLYCANQGIPDDFHLVHLGSRALGGVGLVMTEMTAIAPDARVTKGCVGIWNDEQVTAWQ 486
Cdd:TIGR03997 2 LFSPLRIGPVTLPNRIVFGAHLTNYAVNNLPSERHAAYYAERAKGGAGLIITEELSVHPSDRPYEKLIDGYRPAVIPGYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 487 RVTDFIHQKtDAKIGIQLGHAGRRGSTqrgwekeNHPMdadnWPLVSASALPYlPNISQTPVELSEAQMTTVIDQFVAAA 566
Cdd:TIGR03997 82 RITDAVHAH-GVKIFAQLNHNGGQGDS-------SYSR----LPVWAPSAVPD-PLFREVPKAMEESDIAEVVAGFARVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 567 KRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVWSKP--LSVRISSTDWVDGGTTV 644
Cdd:TIGR03997 149 GHVVAGGFDGIEIQASHSSLVRQFLSPLTNRRTDEYGGSLENRARFLLEVLEAVRKAIGPDraLGVRLCGDELVPGGLTL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 645 DDAVEIGRAMKQAGA-DMIDCSSGEVSPQQQPVYGRM-----YQTPMADRIRNEAGIPVIAVGAITDADQVNSIIAAGRA 718
Cdd:TIGR03997 229 ADAVEIARLLEALGLvDYINTSIGVATYTLHLVEASMhvppgYAAFLAAAIREAVDLPVFAVGRINDPAQAERALAEGQA 308
|
330
....*....|....
gi 1997815582 719 DLCALSRPLLSDPA 732
Cdd:TIGR03997 309 DLVGMVRGQIADPD 322
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
407-734 |
3.71e-58 |
|
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.
Pssm-ID: 239240 [Multi-domain] Cd Length: 353 Bit Score: 201.75 E-value: 3.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 407 MLTPYHVRGITLNNRVVASP--TLLycanQGIPDDFHLVHL--GSRALGGVGLVMTemTAIAPDA--RVTKGCVGIWNDE 480
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSmhTGL----EELDDGIDRLAAfyAERARGGVGLIVT--GGFAPNEagKLGPGGPVLNSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 481 QVTAWQRVTDFIHQKtDAKIGIQLGHAGRRGStqrgwekenHPMdadnwpLVSASALPyLPNISQTPVELSEAQMTTVID 560
Cdd:cd02930 75 QAAGHRLITDAVHAE-GGKIALQILHAGRYAY---------HPL------CVAPSAIR-APINPFTPRELSEEEIEQTIE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 561 QFVAAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVWSK--PLSVRISSTDWV 638
Cdd:cd02930 138 DFARCAALAREAGYDGVEIMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEdfIIIYRLSMLDLV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 639 DGGTTVDDAVEIGRAMKQAGADMIDCSSG----EVSPQQQPVyGRMYQTPMADRIRNEAGIPVIAVGAITDADQVNSIIA 714
Cdd:cd02930 218 EGGSTWEEVVALAKALEAAGADILNTGIGwheaRVPTIATSV-PRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLA 296
|
330 340
....*....|....*....|
gi 1997815582 715 AGRADLCALSRPLLSDPAWV 734
Cdd:cd02930 297 DGDADMVSMARPFLADPDFV 316
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
415-731 |
3.92e-56 |
|
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: 195.50 E-value: 3.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 415 GITLNNRVVASP---TLlyCANQGIPDDfHLVHLGSR-ALGGVGLVMTEMTAIAPDARVTKGCVG---IWNDEQVTAWQR 487
Cdd:cd04733 10 GATLPNRLAKAAmseRL--ADGRGLPTP-ELIRLYRRwAEGGIGLIITGNVMVDPRHLEEPGIIGnvvLESGEDLEAFRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 488 VTDfIHQKTDAKIGIQLGHAGR---RGSTQRGWekenhpmdadnwplvSASALPYLPNISQ---TPVELSEAQMTTVIDQ 561
Cdd:cd04733 87 WAA-AAKANGALIWAQLNHPGRqspAGLNQNPV---------------APSVALDPGGLGKlfgKPRAMTEEEIEDVIDR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 562 FVAAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVWSK--PLSVRISSTDWVD 639
Cdd:cd04733 151 FAHAARLAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPgfPVGIKLNSADFQR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 640 GGTTVDDAVEIGRAMKQAGADMIDCSSGEvspqqqpvygrmYQTPM-------------------ADRIRNEAGIPVIAV 700
Cdd:cd04733 231 GGFTEEDALEVVEALEEAGVDLVELSGGT------------YESPAmagakkestiareayflefAEKIRKVTKTPLMVT 298
|
330 340 350
....*....|....*....|....*....|.
gi 1997815582 701 GAITDADQVNSIIAAGRADLCALSRPLLSDP 731
Cdd:cd04733 299 GGFRTRAAMEQALASGAVDGIGLARPLALEP 329
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
407-734 |
8.42e-54 |
|
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: 189.73 E-value: 8.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 407 MLTPYHVR-GITLNNRVVASPTLLYCANQG--IPDDfHLVHLGSRAlGGVGLVMTEMTAIAPDARVTKGCVGIWNDEQVT 483
Cdd:cd04735 1 LFEPFTLKnGVTLKNRFVMAPMTTYSSNPDgtITDD-ELAYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 484 AWQRVTDFIHQKtDAKIGIQLGHAGRRGstqrgwekenHPMDADNWPLVSASALPYLPNISQTPVELSEAQMTTVIDQFV 563
Cdd:cd04735 79 GLRKLAQAIKSK-GAKAILQIFHAGRMA----------NPALVPGGDVVSPSAIAAFRPGAHTPRELTHEEIEDIIDAFG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 564 AAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVWSKP------LSVRISSTDW 637
Cdd:cd04735 148 EATRRAIEAGFDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDKHadkdfiLGYRFSPEEP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 638 VDGGTTVDDAVEIGRAMKQAGADMIDCSSG-------EVSPQQQPVYGRMYQTpMADRirneagIPVIAVGAITDADQVN 710
Cdd:cd04735 228 EEPGIRMEDTLALVDKLADKGLDYLHISLWdfdrksrRGRDDNQTIMELVKER-IAGR------LPLIAVGSINTPDDAL 300
|
330 340
....*....|....*....|....
gi 1997815582 711 SIIAAGrADLCALSRPLLSDPAWV 734
Cdd:cd04735 301 EALETG-ADLVAIGRGLLVDPDWV 323
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
407-735 |
6.86e-48 |
|
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: 173.66 E-value: 6.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 407 MLTPYHVRGITLNNRVVASPTLLYCANQGIPDDFHLVHLGSRALGGVGLVMTEMTAIAPDARVTKGCV-GIWNDEQVTAW 485
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPMTRSFSPGGVPGQDVAAYYRRRAAGGVGLIITEGTAVDHPAASGDPNVpRFHGEDALAGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 486 QRVTDFIHqKTDAKIGIQLGHAGrrgstqrGWEKENHPMDADNwPLVSASALpylpNISQTPV--ELSEAQMTTVIDQFV 563
Cdd:cd04747 81 KKVVDEVH-AAGGKIAPQLWHVG-------AMRKLGTPPFPDV-PPLSPSGL----VGPGKPVgrEMTEADIDDVIAAFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 564 AAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVR-QVW-SKPLSVRISSTDWVDGG 641
Cdd:cd04747 148 RAAADARRLGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRaAVGpDFPIILRFSQWKQQDYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 642 T----TVDDAVEIGRAMKQAGADMIDCSSgevspqqqpvygRMYQTP--------MADRIRNEAGIPVIAVGAI------ 703
Cdd:cd04747 228 ArladTPDELEALLAPLVDAGVDIFHCST------------RRFWEPefegselnLAGWTKKLTGLPTITVGSVgldgdf 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1997815582 704 ------------TDADQVNSIIAAGRADLCALSRPLLSDPAWVL 735
Cdd:cd04747 296 igafagdegaspASLDRLLERLERGEFDLVAVGRALLSDPAWVA 339
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
406-731 |
4.12e-42 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 157.20 E-value: 4.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 406 PMLTPYHVRGITLNNRVVASP-TLLYCANQG-IPDDFHLVHLGSRAlgGVGLVMTEMTAIAPDARVTKGCVGIWNDEQVT 483
Cdd:PRK10605 2 KLFSPLKVGAITAPNRVFMAPlTRLRSIEPGdIPTPLMAEYYRQRA--SAGLIISEATQISAQAKGYAGAPGLHSPEQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 484 AWQRVTDFIHQKtDAKIGIQLGHAGR--RGSTQRGWEkenhpmdadnwPLVSASALPYLPNIS-------------QTPV 548
Cdd:PRK10605 80 AWKKITAGVHAE-GGHIAVQLWHTGRisHASLQPGGQ-----------APVAPSAINAGTRTSlrdengqairvetSTPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 549 ELSEAQMTTVIDQFVAAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVWSKP- 627
Cdd:PRK10605 148 ALELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGADr 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 628 LSVRIS---STDWVDGGTTVD-DAVEIGRAMKQAGADMIDCSsgevspqqQPVY--GRMYQTPMADRIRNEAGIPVIAVG 701
Cdd:PRK10605 228 IGIRISplgTFNNVDNGPNEEaDALYLIEQLGKRGIAYLHMS--------EPDWagGEPYSDAFREKVRARFHGVIIGAG 299
|
330 340 350
....*....|....*....|....*....|
gi 1997815582 702 AITdADQVNSIIAAGRADLCALSRPLLSDP 731
Cdd:PRK10605 300 AYT-AEKAETLIGKGLIDAVAFGRDYIANP 328
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-349 |
3.50e-39 |
|
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: 147.78 E-value: 3.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 1 MNIVCIGGGPAGLYFGLLMKLQNpkNRVVVVERNRPYDTFGWGVVFSDATLSNLRQADpvSAKTISAEFSHWDDIDVHFK 80
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAG--IRVTVVERAPPPRPDGRGIALSPRSLELLRRLG--LWDRLLARGAPIRGIRVRDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 81 GV--------CNRSGGHGFIGIGRKKLLNILQDRCVELGVELVFETQVT-----DDQAIAR-----EYQADLLIASDGIN 142
Cdd:COG0654 80 SDgrvlarfdAAETGLPAGLVVPRADLERALLEAARALGVELRFGTEVTgleqdADGVTVTladgrTLRADLVVGADGAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 143 STVRTRYEnvFKPDIDPRRCRFVWLGTKkifdaftflfaknehgwfqvhayqfqeglstfivetteetwlkagidqmsqe 222
Cdd:COG0654 160 SAVRRLLG--IGFTGRDYPQRALWAGVR---------------------------------------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 223 dgiAYCEKLFAPWLDgekLIANAAHLRGAAIWiRFPRVICGNWVHWtqptqgkdvPVVLMGDAAHTAHFSIGSGTKLALE 302
Cdd:COG0654 186 ---TELRARLAAAGP---RLGELLELSPRSAF-PLRRRRAERWRRG---------RVVLLGDAAHTMHPLGGQGANLALR 249
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1997815582 303 DAIELCESLKT--SGGDLRKGLEHYQKVRSVEVLKIQNAARNSTEWFEN 349
Cdd:COG0654 250 DAAALAWKLAAalRGRDDEAALARYERERRPRAARVQRAADALGRLFHP 298
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
407-734 |
3.36e-38 |
|
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent reduction of carbon-carbon double bonds of several molecules, including nonactivated 2-enoates, alpha,beta-unsaturated aldehydes, cyclic ketones, and methylketones. ERs are similar to 2,4-dienoyl-CoA reductase from E. coli and to the old yellow enzyme from Saccharomyces cerevisiae.
Pssm-ID: 239241 [Multi-domain] Cd Length: 382 Bit Score: 146.50 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 407 MLTPYHVRGITLNNRVVASP--TLLYCANQGIPDDFHLVHLGSRALGGVGLVMTEMTAIAPDARVTKG----CVGIWNDE 480
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPmgPLGLADNDGAFNQRGIDYYVERAKGGTGLIITGVTMVDNEIEQFPMpslpCPTYNPTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 481 QVTAWQRVTDFIHqKTDAKIGIQLGhagrrgstqRGWEKENHPMDADNWPLVSASALPYLPNISQTPVELSEAQMTTVID 560
Cdd:cd02931 81 FIRTAKEMTERVH-AYGTKIFLQLT---------AGFGRVCIPGFLGEDKPVAPSPIPNRWLPEITCRELTTEEVETFVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 561 QFVAAAKRAETAGFDWLELQAGH-GYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAVRQVWSK--PLSVRISS--- 634
Cdd:cd02931 151 KFGESAVIAKEAGFDGVEIHAVHeGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEdfPVSLRYSVksy 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 635 -TDWVDGGTTVDDAVEIGRAMKQ----------AGADMIDCSSGEVSP---QQQPVYGR--MYQtPMADRIRNEAGIPVI 698
Cdd:cd02931 231 iKDLRQGALPGEEFQEKGRDLEEglkaakileeAGYDALDVDAGSYDAwywNHPPMYQKkgMYL-PYCKALKEVVDVPVI 309
|
330 340 350
....*....|....*....|....*....|....*.
gi 1997815582 699 AVGAITDADQVNSIIAAGRADLCALSRPLLSDPAWV 734
Cdd:cd02931 310 MAGRMEDPELASEAINEGIADMISLGRPLLADPDVV 345
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
405-735 |
5.04e-32 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 128.82 E-value: 5.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 405 PPMLTPYHVRGITLNNRVVASPTLLYCANQGIPDDFHLVHLGSRALGGvGLVMTEMTAIAPDARVTKGCVGIWNDEQVTA 484
Cdd:PLN02411 10 ETLFSPYKMGRFDLSHRVVLAPMTRCRALNGIPNAALAEYYAQRSTPG-GFLISEGTLISPTAPGFPHVPGIYSDEQVEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 485 WQRVTDFIHQKtDAKIGIQLGHAGRrGSTQRGWEKENHPMDADNWPlVSASALPYLPNISQ----TPVELSEAQMTTVID 560
Cdd:PLN02411 89 WKKVVDAVHAK-GSIIFCQLWHVGR-ASHQVYQPGGAAPISSTNKP-ISERWRILMPDGSYgkypKPRALETSEIPEVVE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 561 QFVAAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNYGGTLENRLRFPLAVISAV-RQVWSKPLSVRIS-STDWV 638
Cdd:PLN02411 166 HYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVvSAIGADRVGVRVSpAIDHL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 639 DGgtTVDDAVEIGRAMkqagADMIDCSSGEVSPQ------QQPVYGRMYQTP------------MADRIRNEAGIPVIAV 700
Cdd:PLN02411 246 DA--TDSDPLNLGLAV----VERLNKLQLQNGSKlaylhvTQPRYTAYGQTEsgrhgseeeeaqLMRTLRRAYQGTFMCS 319
|
330 340 350
....*....|....*....|....*....|....*
gi 1997815582 701 GAITDADQVNSiIAAGRADLCALSRPLLSDPAWVL 735
Cdd:PLN02411 320 GGFTRELGMQA-VQQGDADLVSYGRLFISNPDLVL 353
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
444-731 |
1.56e-31 |
|
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: 126.70 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 444 HLGSRALGGVGLVMTEMTAIAPDARVTKGCVG-IWNDEQVTAWQRVTDFIHqKTDAKIGIQLGHAGRRGSTQRGWEKENH 522
Cdd:cd02929 43 MRGIKAEGGWGVVNTEQCSIHPSSDDTPRISArLWDDGDIRNLAAMTDAVH-KHGALAGIELWHGGAHAPNRESRETPLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 523 PMDAdnwplvsASALPYLPniSQTPVELSEAQMTTVIDQFVAAAKRAETAGFDWLELQAGHGYLLSSFISPLTNQRTDNY 602
Cdd:cd02929 122 PSQL-------PSEFPTGG--PVQAREMDKDDIKRVRRWYVDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 603 GGTLENRLRFPLAVISAVRQ-VWSK-PLSVRISstdwVD------GGTTVDDAVEIGRaMKQAGADMIDCSSGEVSPQQQ 674
Cdd:cd02929 193 GGSLENRARFWRETLEDTKDaVGDDcAVATRFS----VDeligpgGIESEGEGVEFVE-MLDELPDLWDVNVGDWANDGE 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1997815582 675 P--VYGRMYQTPMADRIRNEAGIPVIAVGAITDADQVNSIIAAGRADLCALSRPLLSDP 731
Cdd:cd02929 268 DsrFYPEGHQEPYIKFVKQVTSKPVVGVGRFTSPDKMVEVVKSGILDLIGAARPSIADP 326
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
2-346 |
8.45e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 67.59 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 2 NIVCIGGGPAGLYFGLLMKLQNPKnrVVVVERNRPYDTFGWGVVFSDATLSNLRQ---ADPVSAktisaEFSHWDDIDVH 78
Cdd:PRK06847 6 KVLIVGGGIGGLSAAIALRRAGIA--VDLVEIDPEWRVYGAGITLQGNALRALRElgvLDECLE-----AGFGFDGVDLF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 79 -------FKGVCNRSGGHGF---IGIGRKKLLNILQDRCVELGVELVFETQVT----DDQAIA------REYQADLLIAS 138
Cdd:PRK06847 79 dpdgtllAELPTPRLAGDDLpggGGIMRPALARILADAARAAGADVRLGTTVTaieqDDDGVTvtfsdgTTGRYDLVVGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 139 DGINSTVRTRyenVFKPDIDPR-----------------RCRFVWLGTKKIF------DAFTFLF---AKNEHGWFQVHA 192
Cdd:PRK06847 159 DGLYSKVRSL---VFPDEPEPEytgqgvwravlprpaevDRSLMYLGPTTKAgvvplsEDLMYLFvtePRPDNPRIEPDT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 193 Y--QFQEGLSTFIVETteetwLKAGIDQMSQEDGIAY--CEKLF--APWLDGEklianaahlrgaaiwirfprvicgnwv 266
Cdd:PRK06847 236 LaaLLRELLAPFGGPV-----LQELREQITDDAQVVYrpLETLLvpAPWHRGR--------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 267 hwtqptqgkdvpVVLMGDAAH--TAHfsIGSGTKLALEDAIELCESLkTSGGDLRKGLEHYQKVRSVEVLKIQNAARNST 344
Cdd:PRK06847 284 ------------VVLIGDAAHatTPH--LAQGAGMAIEDAIVLAEEL-ARHDSLEAALQAYYARRWERCRMVVEASARIG 348
|
..
gi 1997815582 345 EW 346
Cdd:PRK06847 349 RI 350
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
8-148 |
3.13e-11 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 64.60 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 8 GGPAGLYFGLLmkLQNPKNRVVVVERNR-PYDTFGWGVVFSDA--TLSNLRQADPVSAKTISAEFSHWDDIDVHFkgvcN 84
Cdd:COG0644 1 AGPAGSAAARR--LARAGLSVLLLEKGSfPGDKICGGGLLPRAleELEPLGLDEPLERPVRGARFYSPGGKSVEL----P 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1997815582 85 RSGGHGFIgIGRKKLLNILQDRCVELGVELVFETQVTD-----DQAI-----AREYQADLLIASDGINSTVRTR 148
Cdd:COG0644 75 PGRGGGYV-VDRARFDRWLAEQAEEAGAEVRTGTRVTDvlrddGRVVvrtgdGEEIRADYVVDADGARSLLARK 147
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
1-341 |
1.28e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 57.78 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 1 MNIVCIGGGPAGLYFGLLmkLQNPKNRVVVVERNRPYDTFGWGVVFSDATLSNLRQADpvSAKTI------SAEFSHWDD 74
Cdd:PRK06753 1 MKIAIIGAGIGGLTAAAL--LQEQGHEVKVFEKNESVKEVGAGIGIGDNVIKKLGNHD--LAKGIknagqiLSTMNLLDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 75 IDVHFKGVcNRSGGHGFIGIGRKKLLNIL----QDRCVELGVELVF----ETQVTDDQAIAREYQADLLIASDGINSTVR 146
Cdd:PRK06753 77 KGTLLNKV-KLKSNTLNVTLHRQTLIDIIksyvKEDAIFTGKEVTKieneTDKVTIHFADGESEAFDLCIGADGIHSKVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 147 --------TRYE--NVFK---PDI---DPRRCRFVWlGTKKIFDAFTFLfaKNEHGWF-QVHAyqfqeglstfivettee 209
Cdd:PRK06753 156 qsvnadskVRYQgyTCFRgliDDIdlkLPDCAKEYW-GTKGRFGIVPLL--NNQAYWFiTINA----------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 210 twlKAGiDQMSQEDGIAYCEKLFAPWLDGEKLIANAAHLRGaaiwirfprVICGNWVHWTQPTQGKDVPVVLMGDAAHTA 289
Cdd:PRK06753 216 ---KER-DPKYSSFGKPHLQAYFNHYPNEVREILDKQSETG---------ILHHDIYDLKPLKSFVYGRIVLLGDAAHAT 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1997815582 290 HFSIGSGTKLALEDAIELCESLKTSggDLRKGLEHYQKVRSVEVLKIQNAAR 341
Cdd:PRK06753 283 TPNMGQGAGQAMEDAIVLANCLNAY--DFEKALQRYDKIRVKHTAKVIKRSR 332
|
|
| PRK06475 |
PRK06475 |
FAD-binding protein; |
2-330 |
1.41e-08 |
|
FAD-binding protein;
Pssm-ID: 180582 [Multi-domain] Cd Length: 400 Bit Score: 57.53 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 2 NIVCIGGGPAGLYFGLlmKLQNPKNRVVVVERNRPYDTFGWGV-VFSDAT--LSNLRQADPVSAKTISAEFSHWDD---- 74
Cdd:PRK06475 4 SPLIAGAGVAGLSAAL--ELAARGWAVTIIEKAQELSEVGAGLqLAPNAMrhLERLGVADRLSGTGVTPKALYLMDgrka 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 75 ---IDVHFKGVCNRSGGHGFIGIGRKKLLNILQDRCVE-------LGVELVFETQVTDDQAI-------AREYQADLLIA 137
Cdd:PRK06475 82 rplLAMQLGDLARKRWHHPYIVCHRADLQSALLDACRNnpgieikLGAEMTSQRQTGNSITAtiirtnsVETVSAAYLIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 138 SDGINSTVRTRyenvfKPDIDPRRCRFVWLGTKKIFDAF--TFLFAKNEH----GWF--QVH--AYQFQEG-LSTFIV-- 204
Cdd:PRK06475 162 CDGVWSMLRAK-----AGFSKARFSGHIAWRTTLAADALpaSFLSAMPEHkavsAWLgnKAHfiAYPVKGGkFFNFVAit 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 205 --ETTEETWLKAGiDQmsqedgiAYCEKLFAPWldGEKLIANAAHLRgaaiwirfprvicgNWVHWT--QPTQGKDVPV- 279
Cdd:PRK06475 237 ggENPGEVWSKTG-DK-------AHLKSIYADW--NKPVLQILAAID--------------EWTYWPlfEMADAQFVGPd 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1997815582 280 --VLMGDAAHTAHFSIGSGTKLALEDAIELCESLktSGGDLRKGLEHYQKVRS 330
Cdd:PRK06475 293 rtIFLGDASHAVTPFAAQGAAMAIEDAAALAEAL--DSDDQSAGLKRFDSVRK 343
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
560-737 |
2.15e-07 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 52.50 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 560 DQFVAAAKRAETAGFDWLELQAG-------HGyllssfispltnqrtdNYGGTLENRLRFPLAVISAVRQVWSKPLSV-- 630
Cdd:cd02801 67 ETLAEAAKIVEELGADGIDLNMGcpspkvtKG----------------GAGAALLKDPELVAEIVRAVREAVPIPVTVki 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 631 RIsstdwvdGGTTVDDAVEIGRAMKQAGADMIdcssgevspqqqPVYGR---MYQTPMAD-----RIRNEAGIPVIAVGA 702
Cdd:cd02801 131 RL-------GWDDEEETLELAKALEDAGASAL------------TVHGRtreQRYSGPADwdyiaEIKEAVSIPVIANGD 191
|
170 180 190
....*....|....*....|....*....|....*
gi 1997815582 703 ITDADQVNSIIAAGRADLCALSRPLLSDPaWVLHE 737
Cdd:cd02801 192 IFSLEDALRCLEQTGVDGVMIGRGALGNP-WLFRE 225
|
|
| PRK07236 |
PRK07236 |
hypothetical protein; Provisional |
1-329 |
8.40e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235980 [Multi-domain] Cd Length: 386 Bit Score: 51.85 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 1 MNIVCIGGGPAGLYFGLLmkLQNPKNRVVVVERN-RPYDTFGWGVVFSDATLSNLRQADPVSAKTISaefshwddIDVHF 79
Cdd:PRK07236 7 PRAVVIGGSLGGLFAALL--LRRAGWDVDVFERSpTELDGRGAGIVLQPELLRALAEAGVALPADIG--------VPSRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 80 KGVCNRSGGH--------GFIGIGR--KKLLNILQDRCVELGVELVFETQVtDDQAIA-----REYQADLLIASDGINST 144
Cdd:PRK07236 77 RIYLDRDGRVvqrrpmpqTQTSWNVlyRALRAAFPAERYHLGETLVGFEQD-GDRVTArfadgRRETADLLVGADGGRST 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 145 VRTRyenvFKPDIDPRRCRFV-WLGT-----------KKIFDAFTFLFAKNEHG----------------------WFQV 190
Cdd:PRK07236 156 VRAQ----LLPDVRPTYAGYVaWRGLvdeaalppearAALRDRFTFQLGPGSHIlgypvpgedgstepgkrrynwvWYRN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 191 HAYqfQEGLSTFIVETTEETW------------LKAGIDQMSQEdgiaycekLFAPWLdgEKLIANAAHlrgaaiwirfP 258
Cdd:PRK07236 232 APA--GEELDELLTDRDGTRRpfsvppgalrddVLAELRDDAAE--------LLAPVF--AELVEATAQ----------P 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1997815582 259 RVicgnwvhwtQPTQGKDVP------VVLMGDAAHTAHFSIGSGTKLALEDAIELCESLKTSGGDLRKGLEHYQKVR 329
Cdd:PRK07236 290 FV---------QAIFDLEVPrmafgrVALLGDAAFVARPHTAAGVAKAAADAVALAEALAAAAGDIDAALAAWEAER 357
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
278-341 |
4.34e-06 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 49.65 E-value: 4.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1997815582 278 PVVLMGDAAHTAHFSIGSGTKLALEDAIELCESLKTSGGDLRKGLEHYQKVRSVEVLKIQNAAR 341
Cdd:PRK08163 287 RVTLLGDAAHPMTQYMAQGACMALEDAVTLGKALEGCDGDAEAAFALYESVRIPRTARVVLSAR 350
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
559-716 |
2.60e-05 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 46.77 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 559 IDQFVAAAKRAETAGFDWLELQaghgylLSSfisPLTNQRTDNYGGTLENRLRfplaVISAVRQVWSKPLSVRISSTdwv 638
Cdd:cd04740 101 VEEFVEVAEKLADAGADAIELN------ISC---PNVKGGGMAFGTDPEAVAE----IVKAVKKATDVPVIVKLTPN--- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 639 dggttVDDAVEIGRAMKQAGADM-----------IDCSS---------GEVS-PQQQPVYGRM-YQtpmadrIRNEAGIP 696
Cdd:cd04740 165 -----VTDIVEIARAAEEAGADGltlintlkgmaIDIETrkpilgnvtGGLSgPAIKPIALRMvYQ------VYKAVEIP 233
|
170 180
....*....|....*....|
gi 1997815582 697 VIAVGAITDADQVNSIIAAG 716
Cdd:cd04740 234 IIGVGGIASGEDALEFLMAG 253
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
4-308 |
4.81e-05 |
|
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: 46.16 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 4 VCI-GGGPAGLYFGLLMKLQNPknRVVVVERNRPYDTFGWGVVFSDATLSNLRQA---DPVSAKTISAE-FSHWDDIDVH 78
Cdd:pfam01494 4 VLIvGGGPAGLMLALLLARAGV--RVVLVERHATTSVLPRAHGLNQRTMELLRQAgleDRILAEGVPHEgMGLAFYNTRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 79 FKGVCNRSGGHGFIGIGRKKLLNILQDRCVELGVELVFETQVT----DDQAIA-----------REYQADLLIASDGINS 143
Cdd:pfam01494 82 RADLDFLTSPPRVTVYPQTELEPILVEHAEARGAQVRFGTEVLsleqDGDGVTavvrdrrdgeeYTVRAKYLVGCDGGRS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 144 TVRtryENVFKPDIDPRRCRFVWLGTkkIFDAFTF-LFAKNEHGWFQVHAYQF---------QEGLSTFIV--------- 204
Cdd:pfam01494 162 PVR---KTLGIEFEGFEGVPFGSLDV--LFDAPDLsDPVERAFVHYLIYAPHSrgfmvgpwrSAGRERYYVqvpwdeeve 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 205 -ETTEETW--LKAGIDQMSQEDGIayceklfapwlDGEKLIANAAHLRG--AAIWiRFPRVICgnwvhwtqptqgkdvpv 279
Cdd:pfam01494 237 eRPEEFTDeeLKQRLRSIVGIDLA-----------LVEILWKSIWGVASrvATRY-RKGRVFL----------------- 287
|
330 340
....*....|....*....|....*....
gi 1997815582 280 vlMGDAAHTAHFSIGSGTKLALEDAIELC 308
Cdd:pfam01494 288 --AGDAAHIHPPTGGQGLNTAIQDAFNLA 314
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
560-761 |
9.98e-05 |
|
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: 45.01 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 560 DQFVAAAKRAETAGFDWLELQAGhgyllssfiSPLTNQRTDNYGGTLenrLRFP---LAVISAVRQVWSKPLSVRISsTD 636
Cdd:pfam01207 66 ALLAEAAKLVEDRGADGIDINMG---------CPSKKVTRGGGGAAL---LRNPdlvAQIVKAVVKAVGIPVTVKIR-IG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 637 WVDggtTVDDAVEIGRAMKQAGADMIdcssgevspqqqPVYGR----MYQTPmAD-----RIRNEAGIPVIAVGAITDAD 707
Cdd:pfam01207 133 WDD---SHENAVEIAKIVEDAGAQAL------------TVHGRtraqNYEGT-ADwdaikQVKQAVSIPVIANGDITDPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1997815582 708 QVNSIIAAGRADLCALSRPLLSDPaWVLHECARYGWETRWPAPYEYGRQQLVQS 761
Cdd:pfam01207 197 DAQRCLAYTGADGVMIGRGALGNP-WLFAEQHTVKTGEFGPSPPLAEEAEKVLR 249
|
|
| PRK08850 |
PRK08850 |
2-octaprenyl-6-methoxyphenol hydroxylase; Validated |
279-348 |
1.67e-04 |
|
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
Pssm-ID: 236341 [Multi-domain] Cd Length: 405 Bit Score: 44.76 E-value: 1.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1997815582 279 VVLMGDAAHTAHFSIGSGTKLALEDAIELCESLKT---SGGD--LRKGLEHYQKVRSVEVLKIQNAARNSTEWFE 348
Cdd:PRK08850 284 VALVGDAAHTIHPLAGQGVNLGLLDAASLAQEILAlwqQGRDigLKRNLRGYERWRKAEAAKMIAAMQGFRDLFS 358
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
279-329 |
3.09e-04 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 43.74 E-value: 3.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1997815582 279 VVLMGDAAHTAHFSIGSGTKLALEDAIELCESLKTSGGD---LRKGLEHYQKVR 329
Cdd:PRK07045 287 VVLLGDAAHSIHPITGQGMNLAIEDAGELGACLDLHLSGqiaLADALERFERIR 340
|
|
| PRK07608 |
PRK07608 |
UbiH/UbiF family hydroxylase; |
279-339 |
1.13e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181057 [Multi-domain] Cd Length: 388 Bit Score: 41.86 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997815582 279 VVLMGDAAHTAHFSIGSGTKLALEDAIELCESLKTSG-----GDLRKgLEHYQKVRSVEVLKIQNA 339
Cdd:PRK07608 282 VALVGDAAHLIHPLAGQGMNLGLRDVAALADVLAGREpfrdlGDLRL-LRRYERARREDILALQVA 346
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
559-721 |
1.28e-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: 40.65 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 559 IDQFVAAAKRAETAGFDWLELQAGHGYllssfispltnqrtdnyggtlenRLRFPLAVISAVRQVW-SKPLSVRISstdw 637
Cdd:cd04722 70 AAAVDIAAAAARAAGADGVEIHGAVGY-----------------------LAREDLELIRELREAVpDVKVVVKLS---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 638 vdgGTTVDDAveigRAMKQAGADMIDCSSGEVSPQQQPVYGRmyQTPMADRIRNEAGIPVIAVGAITDADQVNSIIAAGr 717
Cdd:cd04722 123 ---PTGELAA----AAAEEAGVDEVGLGNGGGGGGGRDAVPI--ADLLLILAKRGSKVPVIAGGGINDPEDAAEALALG- 192
|
....
gi 1997815582 718 ADLC 721
Cdd:cd04722 193 ADGV 196
|
|
| PRK07333 |
PRK07333 |
ubiquinone biosynthesis hydroxylase; |
97-148 |
3.41e-03 |
|
ubiquinone biosynthesis hydroxylase;
Pssm-ID: 180935 [Multi-domain] Cd Length: 403 Bit Score: 40.35 E-value: 3.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997815582 97 KKLLNILQDRCVELGVELVFETQVTD----DQAIA------REYQADLLIASDGINSTVRTR 148
Cdd:PRK07333 111 RVLINALRKRAEALGIDLREATSVTDfetrDEGVTvtlsdgSVLEARLLVAADGARSKLREL 172
|
|
| carotene-cycl |
TIGR01790 |
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ... |
2-115 |
5.89e-03 |
|
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases (which form beta and delta carotene, respectively) from bacteria and plants as well as the plant capsanthin/capsorubin and neoxanthin cyclases which appear to have evolved from the plant lycopene cyclases. The plant lycopene epsilon cyclases also transform neurosporene to alpha zeacarotene.
Pssm-ID: 130850 [Multi-domain] Cd Length: 388 Bit Score: 39.72 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997815582 2 NIVCIGGGPAGLYFGLlmKLQNPKNRVVVVERNRPY---DTFG-WGVVFSDATLSNLRQAdpvsaktisaefsHWDDIDV 77
Cdd:TIGR01790 1 DLAVIGGGPAGLAIAL--ELARPGLRVQLIEPHPPIpgnHTYGvWDDDLSDLGLADCVEH-------------VWPDVYE 65
|
90 100 110
....*....|....*....|....*....|....*...
gi 1997815582 78 HFKGVCNRSGGHGFIGIGRKKLLNILQDRCVELGVELV 115
Cdd:TIGR01790 66 YRFPKQPRKLGTAYGSVDSTRLHEELLQKCPEGGVLWL 103
|
|
| Pterin_binding |
cd00423 |
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ... |
639-697 |
8.61e-03 |
|
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). DHPS, a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.
Pssm-ID: 238242 [Multi-domain] Cd Length: 258 Bit Score: 38.79 E-value: 8.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997815582 639 DGGT--TVDDAVEIGRAMKQAGADMIDCSSGEVSPQQQPVYG-----RMyqTPMADRIRNEAGIPV 697
Cdd:cd00423 16 DGGKflSLDKALEHARRMVEEGADIIDIGGESTRPGAEPVSVeeeleRV--IPVLRALAGEPDVPI 79
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
279-327 |
8.90e-03 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 39.33 E-value: 8.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1997815582 279 VVLMGDAAHTAHFSIGSGTKLALEDAIELCESLKTSGGDLRKGLEHYQK 327
Cdd:PRK07588 281 VALVGDAAACPSLLGGEGSGLAITEAYVLAGELARAGGDHRRAFDAYEK 329
|
|
| |
