|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
1-763 |
0e+00 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 1526.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 1 MRIVCIGGGPAGLYFALLMKKQHPEHSISVIERNKPYDTFGWGVVFSDATMVSMKAWDPESAAEIEDAFNHWDDIELLFK 80
Cdd:PRK08255 1 MRIVCIGGGPAGLYFALLMKLLDPAHEVTVVERNRPYDTFGWGVVFSDATLGNLRAADPVSAAAIGDAFNHWDDIDVHFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 81 GTRQRTSGHGFVGIGRKKLLNILQRRCEALGVELVFETDSSGDIDYP-DADLIIASDGFNSKIRNRYPEVFEPDLVVRPN 159
Cdd:PRK08255 81 GRRIRSGGHGFAGIGRKRLLNILQARCEELGVKLVFETEVPDDQALAaDADLVIASDGLNSRIRTRYADTFQPDIDTRRC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 160 RYIWLGTNKLFDAFTFDFRKTDHGWFQAHIYKFDDKTSTFIVETTEEAYEKHGLGQMDQQGSIDFCQDLFSEVLEGSELM 239
Cdd:PRK08255 161 RFVWLGTHKVFDAFTFAFEETEHGWFQAHAYRFDDDTSTFIVETPEEVWRAAGLDEMSQEESIAFCEKLFADYLDGHPLM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 240 TNARHLRGSAWLNFNRLICGKWSHFNGNSHVVLMGDAAHTAHFAIGSGTKLAIDDAIELTNQFNKLGHDkdkIPAVLETY 319
Cdd:PRK08255 241 SNASHLRGSAWINFPRVVCERWVHWNRRVPVVLMGDAAHTAHFSIGSGTKLALEDAIELARCLHEHPGD---LPAALAAY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 320 EEIRRVDVARIQNAARNAMEWFEVVgQRYADtLEPEQFMYSMLTRSQRISHENLRLRDPKWLEGYERWFAKKNGIDVsgn 399
Cdd:PRK08255 318 EEERRVEVLRIQNAARNSTEWFENV-ERYAG-LEPEQFAYSLLTRSQRISHENLRLRDAAWLEGYERWFARRAGAPV--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 400 GRTLPPMFTPYSLRETHLPNRIVMSPMAMYSAKDGMLDDFHLVHLGSRALGGAGLVFGEMTCVSPDARITPGCLGLWNDE 479
Cdd:PRK08255 393 ARPPPPMFTPFRLRGLTLKNRVVVSPMAMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 480 QAAAWKRFVTFVHDNSAAKVGIQLGHAGRKGSTKVAWEGIDQPVEQGGWDLISASALPYLKTSQVPKAMDRADMDRVKAD 559
Cdd:PRK08255 473 QEAAWKRIVDFVHANSDAKIGIQLGHSGRKGSTRLGWEGIDEPLEEGNWPLISASPLPYLPGSQVPREMTRADMDRVRDD 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 560 HVRAAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLSCHDWFE 639
Cdd:PRK08255 553 FVAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 640 GGNTPEDAAIYAQMFKDAGADLIDCSSGQVWKEEKPVYGRLFQTPFSDKIRNEIGIPTIAVGAISEADHANSIIAAGRAD 719
Cdd:PRK08255 633 GGNTPDDAVEIARAFKAAGADLIDVSSGQVSKDEKPVYGRMYQTPFADRIRNEAGIATIAVGAISEADHVNSIIAAGRAD 712
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1426492325 720 LCAVARPHLADPAWVLHEAAKIGLTNIPWPKQYYSGKAQYETNL 763
Cdd:PRK08255 713 LCALARPHLADPAWTLHEAAEIGYRDVAWPKQYLAGKRQLERNL 756
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
406-740 |
0e+00 |
|
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.
Pssm-ID: 239242 [Multi-domain] Cd Length: 336 Bit Score: 523.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 406 MFTPYSLRETHLPNRIVMSPMAMYSAKDGMLDDFHLVHLGSRALGGAGLVFGEMTCVSPDARITPGCLGLWNDEQAAAWK 485
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMCQYSAEDGVATDWHLVHYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDEQIEALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 486 RFVTFVHDNSAaKVGIQLGHAGRKGSTKVAWEGIDQ--PVEQGGWDLISASALPYLKTSQVPKAMDRADMDRVKADHVRA 563
Cdd:cd02932 81 RIVDFIHSQGA-KIGIQLAHAGRKASTAPPWEGGGPllPPGGGGWQVVAPSAIPFDEGWPTPRELTREEIAEVVDAFVAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 564 AKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLSCHDWFEGGNT 643
Cdd:cd02932 160 ARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVEGGWD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 644 PEDAAIYAQMFKDAGADLIDCSSGQVWKEEKPVYGRLFQTPFSDKIRNEIGIPTIAVGAISEADHANSIIAAGRADLCAV 723
Cdd:cd02932 240 LEDSVELAKALKELGVDLIDVSSGGNSPAQKIPVGPGYQVPFAERIRQEAGIPVIAVGLITDPEQAEAILESGRADLVAL 319
|
330
....*....|....*..
gi 1426492325 724 ARPHLADPAWVLHEAAK 740
Cdd:cd02932 320 GRELLRNPYWPLHAAAE 336
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
404-752 |
2.46e-141 |
|
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: 420.34 E-value: 2.46e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 404 PPMFTPYSLRETHLPNRIVMSPMAMYSA-KDGMLDDFHLVHLGSRALGGAGLVFGEMTCVSPDARITPGCLGLWNDEQAA 482
Cdd:COG1902 5 PKLFSPLTLGGLTLKNRIVMAPMTRGRAdEDGVPTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDEQIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 483 AWKRFVTFVHDNSAaKVGIQLGHAGRKGSTKVawegidqpveQGGWDLISASALPYLKTSQVPKAMDRADMDRVKADHVR 562
Cdd:COG1902 85 GLRRVTDAVHAAGG-KIFIQLWHAGRKAHPDL----------PGGWPPVAPSAIPAPGGPPTPRALTTEEIERIIEDFAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 563 AAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLSCHDWFEGGN 642
Cdd:COG1902 154 AARRAKEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 643 TPEDAAIYAQMFKDAGADLIDCSSGQVWKEEKP--VYGRLFQTPFSDKIRNEIGIPTIAVGAISEADHANSIIAAGRADL 720
Cdd:COG1902 234 TLEESVELAKALEEAGVDYLHVSSGGYEPDAMIptIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADL 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 1426492325 721 CAVARPHLADPAWVLHEAAKIG-------LTNIPWPKQY 752
Cdd:COG1902 314 VALGRPLLADPDLPNKAAAGRGdeirpciGCNQCLPTFY 352
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
406-752 |
2.93e-112 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 344.37 E-value: 2.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 406 MFTPYSLRETHLPNRIVMSPMAMYSA--KDGMLDDFHLVHLGSRALGGAGLVFGEMTCVSPDARITPGCLGLWNDEQAAA 483
Cdd:PRK13523 3 LFSPYTIKDVTLKNRIVMSPMCMYSSenKDGKVTNFHLIHYGTRAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHIEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 484 WKRFVTFVHDNsAAKVGIQLGHAGRKGSTkvawEGidqpveqggwDLISASALPYLKTSQVPKAMDRADMDRVKADHVRA 563
Cdd:PRK13523 83 LHKLVTFIHDH-GAKAAIQLAHAGRKAEL----EG----------DIVAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 564 AKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWpaDKPISVRLSCHDWFEGGNT 643
Cdd:PRK13523 148 AVRAKEAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVW--DGPLFVRISASDYHPGGLT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 644 PEDAAIYAQMFKDAGADLIDCSSGQVWKEEKPVY-GrlFQTPFSDKIRNEIGIPTIAVGAISEADHANSIIAAGRADLCA 722
Cdd:PRK13523 226 VQDYVQYAKWMKEQGVDLIDVSSGAVVPARIDVYpG--YQVPFAEHIREHANIATGAVGLITSGAQAEEILQNNRADLIF 303
|
330 340 350
....*....|....*....|....*....|
gi 1426492325 723 VARPHLADPAWVLHEAAKIGlTNIPWPKQY 752
Cdd:PRK13523 304 IGRELLRNPYFPRIAAKELG-FEIEAPKQY 332
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
407-734 |
2.11e-99 |
|
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: 310.66 E-value: 2.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 407 FTPYSLRETHLPNRIVMSPMA-MYSAKDGMLDDFHLVHLGSRALGGAGLVFGEMTCVSPDARITPGCLGLWNDEQAAAWK 485
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTeNMATEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 486 RFVTFVHDNSAaKVGIQLGHAGRKGSTKVAWEGIdqpveqggwdlISASALPYLKTSQVPKAMDRADMDRVKADHVRAAK 565
Cdd:cd02803 81 KLTEAVHAHGA-KIFAQLAHAGRQAQPNLTGGPP-----------PAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 566 YAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLSCHDWFEGGNTPE 645
Cdd:cd02803 149 RAKEAGFDGVEIHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 646 DAAIYAQMFKDAGADLIDCSSG----QVWKEEKPVYGRLFQTPFSDKIRNEIGIPTIAVGAISEADHANSIIAAGRADLC 721
Cdd:cd02803 229 EAIEIAKALEEAGVDALHVSGGsyesPPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLV 308
|
330
....*....|...
gi 1426492325 722 AVARPHLADPAWV 734
Cdd:cd02803 309 ALGRALLADPDLP 321
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
406-734 |
1.09e-62 |
|
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: 214.01 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 406 MFTPYSLRETHLPNRIVMSPMAMYSAKDGMLDDFHLVHLGSRALGGAGLVFGEMTCVSPDARITPGCLGLWNDEQAAAWK 485
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPGFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 486 RFVTFVHDNsAAKVGIQLGHAGRKGSTKVAWegidQPVeqggwdlISASALPYLKTSQVPKAMDRADMDRVKADHVRAAK 565
Cdd:cd04734 81 RLAEAVHAH-GAVIMIQLTHLGRRGDGDGSW----LPP-------LAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 566 YAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLSCHDWFEGGNTPE 645
Cdd:cd04734 149 RCQAGGLDGVELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 646 DAAIYAQMFKDAGA-DLIDCSSGQVWKEEKPV-------YGRLFQTPFSDKIRNEIGIPTIAVGAISEADHANSIIAAGR 717
Cdd:cd04734 229 EALEIAARLAAEGLiDYVNVSAGSYYTLLGLAhvvpsmgMPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAGH 308
|
330
....*....|....*..
gi 1426492325 718 ADLCAVARPHLADPAWV 734
Cdd:cd04734 309 ADMVGMTRAHIADPHLV 325
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
405-734 |
2.13e-61 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 210.38 E-value: 2.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 405 PMFTPYSLRETHLPNRIVMSPMAMYSA--KDGMLDDFHLVHLGSRALGGAGLVFGEMTCVSPDARITPGCLGLWNDEQAA 482
Cdd:pfam00724 1 KLFEPIKIGNTTLKNRIVMAPMTRLRSldDGTKATGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 483 AWKRFVTFVHDNsAAKVGIQLGHAGRKGSTkvawEGIDQPVEQGGWDLISASALPYLKTSQVpKAMDRADMDRVKADHVR 562
Cdd:pfam00724 81 GWRKLTEAVHKN-GSKAGVQLWHLGREAPM----EYRPDLEVDGPSDPFALGAQEFEIASPR-YEMSKEEIKQHIQDFVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 563 AAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLSCHDWFEGGN 642
Cdd:pfam00724 155 AAKRAREAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 643 TPEDAAIYAQMFKDAGADLIDCSSGQ-VWKEEKPVYG----RLFQTPFSDKIRNEIGIPTIAVGAISEADHANSIIAAGR 717
Cdd:pfam00724 235 DFAETAQFIYLLAELGVRLPDGWHLAyIHAIEPRPRGagpvRTRQQHNTLFVKGVWKGPLITVGRIDDPSVAAEIVSKGR 314
|
330
....*....|....*..
gi 1426492325 718 ADLCAVARPHLADPAWV 734
Cdd:pfam00724 315 ADLVAMGRPFLADPDLP 331
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
406-734 |
5.57e-56 |
|
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: 195.97 E-value: 5.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 406 MFTPYSLRETHLPNRIVMSpmAMYSAKDGMLDDFHLVHL--GSRALGGAGL-VFGEmtcVSPDA--RITPGCLGLWNDEQ 480
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMG--SMHTGLEELDDGIDRLAAfyAERARGGVGLiVTGG---FAPNEagKLGPGGPVLNSPRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 481 AAAWKRFVTFVHDnSAAKVGIQLGHAGRKGSTKvawegidqpveqggwDLISASALPYLKTSQVPKAMDRADMDRVKADH 560
Cdd:cd02930 76 AAGHRLITDAVHA-EGGKIALQILHAGRYAYHP---------------LCVAPSAIRAPINPFTPRELSEEEIEQTIEDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 561 VRAAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLSCHDWFEG 640
Cdd:cd02930 140 ARCAALAREAGYDGVEIMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 641 GNTPEDAAIYAQMFKDAGADLIDCSSGqvWKEEK------PVYGRLFqTPFSDKIRNEIGIPTIAVGAISEADHANSIIA 714
Cdd:cd02930 220 GSTWEEVVALAKALEAAGADILNTGIG--WHEARvptiatSVPRGAF-AWATAKLKRAVDIPVIASNRINTPEVAERLLA 296
|
330 340
....*....|....*....|
gi 1426492325 715 AGRADLCAVARPHLADPAWV 734
Cdd:cd02930 297 DGDADMVSMARPFLADPDFV 316
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
405-731 |
6.68e-55 |
|
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: 192.30 E-value: 6.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 405 PMFTPYSLRETHLPNRIVMSPMA-MYSAKDGMLDDFHLVHLGSRAlgGAGLVFGEMTCVSPDARITPGCLGLWNDEQAAA 483
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIVMAPLTrSRADPDGVPTDLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIYTDEQVEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 484 WKRFVTFVHDNsAAKVGIQLGHAGRKGSTKVawegidQPveqGGWDLISASALPY---------LKTSQVPKAMDRADMD 554
Cdd:cd02933 79 WKKVTDAVHAK-GGKIFLQLWHVGRVSHPSL------LP---GGAPPVAPSAIAAegkvftpagKVPYPTPRALTTEEIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 555 RVKADHVRAAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKpISVRLSC 634
Cdd:cd02933 149 GIVADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADR-VGIRLSP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 635 HDWFEGGNTPEDAAIYAQMFKDAGA------DLIDCSSGQVWKEEKPVygrlfqtpFSDKIRNEIGIPTIAVGAISeADH 708
Cdd:cd02933 228 FGTFNDMGDSDPEATFSYLAKELNKrglaylHLVEPRVAGNPEDQPPD--------FLDFLRKAFKGPLIAAGGYD-AES 298
|
330 340
....*....|....*....|...
gi 1426492325 709 ANSIIAAGRADLCAVARPHLADP 731
Cdd:cd02933 299 AEAALADGKADLVAFGRPFIANP 321
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
406-735 |
3.43e-44 |
|
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: 163.26 E-value: 3.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 406 MFTPYSLRETHLPNRIVMSPMAMYSAKDGMLDDFHLVHLGSRALGGAGLVFGEMTCV-----SPDARITPgclgLWNDEQ 480
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPMTRSFSPGGVPGQDVAAYYRRRAAGGVGLIITEGTAVdhpaaSGDPNVPR----FHGEDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 481 AAAWKRFVTFVHDNsAAKVGIQLGHAGrkgSTKVAWEGIDQPVEqggwdLISASALpYLKTSQVPKAMDRADMDRVKADH 560
Cdd:cd04747 77 LAGWKKVVDEVHAA-GGKIAPQLWHVG---AMRKLGTPPFPDVP-----PLSPSGL-VGPGKPVGREMTEADIDDVIAAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 561 VRAAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLSchDWFEG 640
Cdd:cd04747 147 ARAAADARRLGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFS--QWKQQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 641 ------GNTPEDAAIYAQMFKDAGADLIDCSSGQVWKEEkpvygrlfqtpFSDKIRN-------EIGIPTIAVG------ 701
Cdd:cd04747 225 dytarlADTPDELEALLAPLVDAGVDIFHCSTRRFWEPE-----------FEGSELNlagwtkkLTGLPTITVGsvgldg 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1426492325 702 ------AISEADHANSI------IAAGRADLCAVARPHLADPAWVL 735
Cdd:cd04747 294 dfigafAGDEGASPASLdrllerLERGEFDLVAVGRALLSDPAWVA 339
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
417-731 |
1.62e-43 |
|
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: 160.83 E-value: 1.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 417 LPNRIVMSPMA--MYSaKDGMLDDfHLVHLGSR-ALGGAGLVF-GE-MtcVSPDARITPGCLG---LWNDEQAAAWKRFV 488
Cdd:cd04733 13 LPNRLAKAAMSerLAD-GRGLPTP-ELIRLYRRwAEGGIGLIItGNvM--VDPRHLEEPGIIGnvvLESGEDLEAFREWA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 489 tfvhdnSAAKVG-----IQLGHAGRKgstkvAWEGIDQPVeqggwdlISASALPYLKTSQV----PKAMDRADMDRVKAD 559
Cdd:cd04733 89 ------AAAKANgaliwAQLNHPGRQ-----SPAGLNQNP-------VAPSVALDPGGLGKlfgkPRAMTEEEIEDVIDR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 560 HVRAAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLSCHDWFE 639
Cdd:cd04733 151 FAHAARLAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 640 GGNTPEDAAIYAQMFKDAGADLIDCSSGQVwkeEKPVygrlFQTP--------------FSDKIRNEIGIPTIAVGAISE 705
Cdd:cd04733 231 GGFTEEDALEVVEALEEAGVDLVELSGGTY---ESPA----MAGAkkestiareayfleFAEKIRKVTKTPLMVTGGFRT 303
|
330 340
....*....|....*....|....*.
gi 1426492325 706 ADHANSIIAAGRADLCAVARPHLADP 731
Cdd:cd04733 304 RAAMEQALASGAVDGIGLARPLALEP 329
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
406-734 |
6.50e-43 |
|
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: 159.30 E-value: 6.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 406 MFTPYSLRE-THLPNRIVMSPMAMYSA-KDGMLDDFHLVHLGSRAlGGAGLVFGEMTCVSPDARITPGCLGLWNDEQAAA 483
Cdd:cd04735 1 LFEPFTLKNgVTLKNRFVMAPMTTYSSnPDGTITDDELAYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 484 WKRFVTFVHDNSAaKVGIQLGHAGRKGSTKVawegidqpvEQGGwDLISASAL-PYLKTSQVPKAMDRADMDRVKADHVR 562
Cdd:cd04735 80 LRKLAQAIKSKGA-KAILQIFHAGRMANPAL---------VPGG-DVVSPSAIaAFRPGAHTPRELTHEEIEDIIDAFGE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 563 AAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREV--WPADKP--ISVRLSCHDWF 638
Cdd:cd04735 149 ATRRAIEAGFDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVidKHADKDfiLGYRFSPEEPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 639 EGGNTPEDAAIYAQMFKDAGADLIDCSSGQVWKeeKPVYGRLFQTPFSDKIRNEIG--IPTIAVGAISEADHANSIIAAG 716
Cdd:cd04735 229 EPGIRMEDTLALVDKLADKGLDYLHISLWDFDR--KSRRGRDDNQTIMELVKERIAgrLPLIAVGSINTPDDALEALETG 306
|
330
....*....|....*...
gi 1426492325 717 rADLCAVARPHLADPAWV 734
Cdd:cd04735 307 -ADLVAIGRGLLVDPDWV 323
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
405-758 |
1.05e-42 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 159.12 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 405 PMFTPYSLRETHLPNRIVMSPMA-MYSAKDG-----MLDDFHlvhlgsRALGGAGLVFGEMTCVSPDARITPGCLGLWND 478
Cdd:PRK10605 2 KLFSPLKVGAITAPNRVFMAPLTrLRSIEPGdiptpLMAEYY------RQRASAGLIISEATQISAQAKGYAGAPGLHSP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 479 EQAAAWKRFVTFVHDNSAaKVGIQLGHAGRKGSTKVawegidQPveqGGWDLISASALPY-LKTS-------------QV 544
Cdd:PRK10605 76 EQIAAWKKITAGVHAEGG-HIAVQLWHTGRISHASL------QP---GGQAPVAPSAINAgTRTSlrdengqairvetST 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 545 PKAMDRADMDRVKADHVRAAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPA 624
Cdd:PRK10605 146 PRALELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 625 DKpISVRLSCHDWFEG---GNTPEDAAIY--AQMFKDAGADLidCSSGQVWKEEKPvygrlFQTPFSDKIRNEIGIPTIA 699
Cdd:PRK10605 226 DR-IGIRISPLGTFNNvdnGPNEEADALYliEQLGKRGIAYL--HMSEPDWAGGEP-----YSDAFREKVRARFHGVIIG 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426492325 700 VGAISeADHANSIIAAGRADLCAVARPHLADPAWV--LHEAAKIgltNIPWPKQYYSGKAQ 758
Cdd:PRK10605 298 AGAYT-AEKAETLIGKGLIDAVAFGRDYIANPDLVarLQRKAEL---NPQRPESFYGGGAE 354
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-342 |
2.74e-38 |
|
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: 145.47 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 1 MRIVCIGGGPAGLYFALLMKKQHpeHSISVIERNKPYDTFGWGVVFSDATMVSMKAWDpeSAAEIEDAFNHWDDIELLFK 80
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAG--IRVTVVERAPPPRPDGRGIALSPRSLELLRRLG--LWDRLLARGAPIRGIRVRDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 81 GTRQRT-------SGHGF-VGIGRKKLLNILQRRCEALGVELVFET-------DSSG-DIDYPD-----ADLIIASDGFN 139
Cdd:COG0654 80 SDGRVLarfdaaeTGLPAgLVVPRADLERALLEAARALGVELRFGTevtgleqDADGvTVTLADgrtlrADLVVGADGAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 140 SKIRNRYPevFEPDLVVRPNRYIWLGtnklfdaFTFDFRKtdhgWFQAHiykFDDktstfivetteeayekhgLGQMdqq 219
Cdd:COG0654 160 SAVRRLLG--IGFTGRDYPQRALWAG-------VRTELRA----RLAAA---GPR------------------LGEL--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 220 gsidfcqdlfsevlegselmtnaRHLRGSAWLNFNRLICGKWSHfngnSHVVLMGDAAHTAHFAIGSGTKLAIDDAIELT 299
Cdd:COG0654 203 -----------------------LELSPRSAFPLRRRRAERWRR----GRVVLLGDAAHTMHPLGGQGANLALRDAAALA 255
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1426492325 300 NQFNKLGHDKDkIPAVLETYEEIRRVDVARIQNAARNAMEWFE 342
Cdd:COG0654 256 WKLAAALRGRD-DEAALARYERERRPRAARVQRAADALGRLFH 297
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
405-731 |
2.26e-29 |
|
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: 120.54 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 405 PMFTPYSLRETHLPNRIVMSP--MAMYSAKDGMLddfhLVHLGSRALGGAGLVFGEMTCVSPDARITP-GCLGLWNDEQA 481
Cdd:cd02929 7 ILFEPIKIGPVTARNRFYQVPhcNGMGYRKPSAQ----AAMRGIKAEGGWGVVNTEQCSIHPSSDDTPrISARLWDDGDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 482 AAWKRFVTFVHDNSAAkVGIQLGHAGRKGSTKVAWEgidQPVEQGGWdlisASALPYLKTSQvPKAMDRADMDRVKADHV 561
Cdd:cd02929 83 RNLAAMTDAVHKHGAL-AGIELWHGGAHAPNRESRE---TPLGPSQL----PSEFPTGGPVQ-AREMDKDDIKRVRRWYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 562 RAAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLSCHDWF--E 639
Cdd:cd02929 154 DAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDELIgpG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 640 GGNTPEDAAIYAQMFKDAgADLIDCSSGQV--WKEEKPVYGRLFQTPFSDKIRNEIGIPTIAVGAISEADHANSIIAAGR 717
Cdd:cd02929 234 GIESEGEGVEFVEMLDEL-PDLWDVNVGDWanDGEDSRFYPEGHQEPYIKFVKQVTSKPVVGVGRFTSPDKMVEVVKSGI 312
|
330
....*....|....
gi 1426492325 718 ADLCAVARPHLADP 731
Cdd:cd02929 313 LDLIGAARPSIADP 326
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
404-633 |
9.04e-28 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 116.11 E-value: 9.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 404 PPMFTPYSLRETHLPNRIVMSPMAMYSAKDGMLDDFHLVHLGSRALGGaGLVFGEMTCVSPDARITPGCLGLWNDEQAAA 483
Cdd:PLN02411 10 ETLFSPYKMGRFDLSHRVVLAPMTRCRALNGIPNAALAEYYAQRSTPG-GFLISEGTLISPTAPGFPHVPGIYSDEQVEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 484 WKRFVTFVHdnsaAKVGI---QLGHAGRkgstkvAWEGIDQPveqGGWDLISASALP-------------YLKTSQvPKA 547
Cdd:PLN02411 89 WKKVVDAVH----AKGSIifcQLWHVGR------ASHQVYQP---GGAAPISSTNKPiserwrilmpdgsYGKYPK-PRA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 548 MDRADMDRVKADHVRAAKYAAEAGADWLELHCAHGYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKp 627
Cdd:PLN02411 155 LETSEIPEVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGADR- 233
|
....*.
gi 1426492325 628 ISVRLS 633
Cdd:PLN02411 234 VGVRVS 239
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
406-734 |
9.24e-25 |
|
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: 107.21 E-value: 9.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 406 MFTPYSLRETHLPNRIVMSPMAMY--SAKDGMLDDFHLVHLGSRALGGAGLVFGEMTCVSPDARITPG----CLGLWNDE 479
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPLglADNDGAFNQRGIDYYVERAKGGTGLIITGVTMVDNEIEQFPMpslpCPTYNPTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 480 QAAAWKRFVTFVHDNSAaKVGIQLGhAGRKGSTKVAWEGIDQPveqggwdlISASALPY-LKTSQVPKAMDRADMDRVKA 558
Cdd:cd02931 81 FIRTAKEMTERVHAYGT-KIFLQLT-AGFGRVCIPGFLGEDKP--------VAPSPIPNrWLPEITCRELTTEEVETFVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 559 DHVRAAKYAAEAGADWLELHCAH-GYLLSSFLSPLTNIRTDEYGGSHENRARYPLEVFKAIREVWPADKPISVRLS---- 633
Cdd:cd02931 151 KFGESAVIAKEAGFDGVEIHAVHeGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSvksy 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 634 CHDWFEG----------GNTPEDAAIYAQMFKDAGADLIDCSSGQV---WKEEKPVYGR--LFQtPFSDKIRNEIGIPTI 698
Cdd:cd02931 231 IKDLRQGalpgeefqekGRDLEEGLKAAKILEEAGYDALDVDAGSYdawYWNHPPMYQKkgMYL-PYCKALKEVVDVPVI 309
|
330 340 350
....*....|....*....|....*....|....*.
gi 1426492325 699 AVGAISEADHANSIIAAGRADLCAVARPHLADPAWV 734
Cdd:cd02931 310 MAGRMEDPELASEAINEGIADMISLGRPLLADPDVV 345
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
2-340 |
1.04e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 70.29 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 2 RIVCIGGGPAGLYFALLMKKQhpEHSISVIERNKPYDTFGWGVVFSDATMVSMKA---WDP-ESAAEIEDAFNHWD-DIE 76
Cdd:PRK06847 6 KVLIVGGGIGGLSAAIALRRA--GIAVDLVEIDPEWRVYGAGITLQGNALRALRElgvLDEcLEAGFGFDGVDLFDpDGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 77 LLFKGTRQRTSGHGF---VGIGRKKLLNILQRRCEALGVELVF--------ETDSSGDIDYPD-----ADLIIASDGFNS 140
Cdd:PRK06847 84 LLAELPTPRLAGDDLpggGGIMRPALARILADAARAAGADVRLgttvtaieQDDDGVTVTFSDgttgrYDLVVGADGLYS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 141 KIRNR-YPEVFEPD---------LVVRP----NRYIWLGTNklfdaftfdfrktdhgwFQA--------HIYkfddktsT 198
Cdd:PRK06847 164 KVRSLvFPDEPEPEytgqgvwraVLPRPaevdRSLMYLGPT-----------------TKAgvvplsedLMY-------L 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 199 FIVETTEE--AYEKHGLGQMdqqgsidfcqdlFSEVLE--GSELMTNAR-HLRGSAWLNFNR----LICGKWshFNGnsH 269
Cdd:PRK06847 220 FVTEPRPDnpRIEPDTLAAL------------LRELLApfGGPVLQELReQITDDAQVVYRPletlLVPAPW--HRG--R 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426492325 270 VVLMGDAAH--TAHFAIGSGtkLAIDDAIELTNQFNKlghdKDKIPAVLETYEEiRRVDVAR-IQNAARNAMEW 340
Cdd:PRK06847 284 VVLIGDAAHatTPHLAQGAG--MAIEDAIVLAEELAR----HDSLEAALQAYYA-RRWERCRmVVEASARIGRI 350
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
1-335 |
9.73e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 58.16 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 1 MRIVCIGGGPAGLYFALLMKKQhpEHSISVIERNKPYDTFGWGVVFSDATMVSMKAWDpeSAAEIEDAFNHWDDIELL-F 79
Cdd:PRK06753 1 MKIAIIGAGIGGLTAAALLQEQ--GHEVKVFEKNESVKEVGAGIGIGDNVIKKLGNHD--LAKGIKNAGQILSTMNLLdD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 80 KGT----RQRTSGHGFVGIGRKKLLNILQRRCEALGVELVFE------TDSSGDIDYPDA-----DLIIASDGFNSKIRN 144
Cdd:PRK06753 77 KGTllnkVKLKSNTLNVTLHRQTLIDIIKSYVKEDAIFTGKEvtkienETDKVTIHFADGeseafDLCIGADGIHSKVRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 145 rypEVFePDLVVRPNRY-IWLG---TNKLFDAFTFDFRKTDHGWF------QAHIYKF--------DDKTSTFiveTTE- 205
Cdd:PRK06753 157 ---SVN-ADSKVRYQGYtCFRGlidDIDLKLPDCAKEYWGTKGRFgivpllNNQAYWFitinakerDPKYSSF---GKPh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 206 -EAYEKHGLGQ----MDQQGSID-FCQDLFSevlegselMTNARHLrgsawlnfnrlicgkwshFNGNshVVLMGDAAHT 279
Cdd:PRK06753 230 lQAYFNHYPNEvreiLDKQSETGiLHHDIYD--------LKPLKSF------------------VYGR--IVLLGDAAHA 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1426492325 280 AHFAIGSGTKLAIDDAIELTNQFNKLGHDKdkipaVLETYEEIRRVDVARIQNAAR 335
Cdd:PRK06753 282 TTPNMGQGAGQAMEDAIVLANCLNAYDFEK-----ALQRYDKIRVKHTAKVIKRSR 332
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
4-337 |
3.24e-07 |
|
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: 53.10 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 4 VCI-GGGPAGLYFALLMKKQHPEHsiSVIER-NKPYDTFGwGVVFSDATMVSMKawDPESAAEIEDAFNHWDDIELLFKG 81
Cdd:pfam01494 4 VLIvGGGPAGLMLALLLARAGVRV--VLVERhATTSVLPR-AHGLNQRTMELLR--QAGLEDRILAEGVPHEGMGLAFYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 82 TRQRT-----SGHGFV-GIGRKKLLNILQRRCEALGVELVFETD------------------SSGDIDYPDADLIIASDG 137
Cdd:pfam01494 79 TRRRAdldflTSPPRVtVYPQTELEPILVEHAEARGAQVRFGTEvlsleqdgdgvtavvrdrRDGEEYTVRAKYLVGCDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 138 FNSKIRNRYPEVFEPDLVVRPNryiWLGTnkLFDAFTFDFRKTDHgWFQAHIYKFDDKTSTFIV---ETTEEAYEKHGLG 214
Cdd:pfam01494 159 GRSPVRKTLGIEFEGFEGVPFG---SLDV--LFDAPDLSDPVERA-FVHYLIYAPHSRGFMVGPwrsAGRERYYVQVPWD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 215 QMDQQGSIDFCQDLFSEVLE---GSELMTnARHLRGSAWlNFNRLICGKWSHfnGNshVVLMGDAAHTAHFAIGSGTKLA 291
Cdd:pfam01494 233 EEVEERPEEFTDEELKQRLRsivGIDLAL-VEILWKSIW-GVASRVATRYRK--GR--VFLAGDAAHIHPPTGGQGLNTA 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1426492325 292 IDDAielTNQFNKL-----GHDKdkiPAVLETYEEIRRvdvARIQNAARNA 337
Cdd:pfam01494 307 IQDA---FNLAWKLaavlrGQAG---ESLLDTYSAERL---PVAWAVVDFA 348
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
8-145 |
1.62e-06 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 50.35 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 8 GGPAGLYFALLMKKQhpEHSISVIERNK-PYDTFGWGVVFSDAtmvsMKAWDPesaAEIEDAFNHW-DDIELLFKGTRQR 85
Cdd:COG0644 1 AGPAGSAAARRLARA--GLSVLLLEKGSfPGDKICGGGLLPRA----LEELEP---LGLDEPLERPvRGARFYSPGGKSV 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1426492325 86 T----SGHGFVgIGRKKLLNILQRRCEALGVELVFET--------DSSGDIDYPD-----ADLIIASDGFNSKIRNR 145
Cdd:COG0644 72 ElppgRGGGYV-VDRARFDRWLAEQAEEAGAEVRTGTrvtdvlrdDGRVVVRTGDgeeirADYVVDADGARSLLARK 147
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
250-335 |
1.10e-04 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 45.41 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 250 WLNFNRLICGKWSHfngnSHVVLMGDAAH--TAHFAIGSGtkLAIDDAIELTNQFNKLGHDkdkIPAVLETYEEIRRVDV 327
Cdd:PRK08163 272 WATADREPVAKWST----GRVTLLGDAAHpmTQYMAQGAC--MALEDAVTLGKALEGCDGD---AEAAFALYESVRIPRT 342
|
....*...
gi 1426492325 328 ARIQNAAR 335
Cdd:PRK08163 343 ARVVLSAR 350
|
|
| PRK07333 |
PRK07333 |
ubiquinone biosynthesis hydroxylase; |
3-145 |
1.24e-04 |
|
ubiquinone biosynthesis hydroxylase;
Pssm-ID: 180935 [Multi-domain] Cd Length: 403 Bit Score: 45.36 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 3 IVCIGGGPAGLYFALLMKKQHPEHSISVIErnkPYDTFGWGvvfSDATMVSMKAwdpeSAAEIEDAFNHWDDIE------ 76
Cdd:PRK07333 4 VVIAGGGYVGLALAVALKQAAPHLPVTVVD---AAPAGAWS---RDPRASAIAA----AARRMLEALGVWDEIApeaqpi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 77 ------------------LLFKGtrQRTSGHGFVG-IGRKKLLNILQRRCEALGVELV-------FETDSSG------DI 124
Cdd:PRK07333 74 tdmvitdsrtsdpvrpvfLTFEG--EVEPGEPFAHmVENRVLINALRKRAEALGIDLReatsvtdFETRDEGvtvtlsDG 151
|
170 180
....*....|....*....|.
gi 1426492325 125 DYPDADLIIASDGFNSKIRNR 145
Cdd:PRK07333 152 SVLEARLLVAADGARSKLREL 172
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
269-324 |
2.91e-04 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 44.13 E-value: 2.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1426492325 269 HVVLMGDAAHTAHFAIGSGTKLAIDDAIELTNQFNKLGHDKDKIPAVLETYEEIRR 324
Cdd:PRK07045 286 NVVLLGDAAHSIHPITGQGMNLAIEDAGELGACLDLHLSGQIALADALERFERIRR 341
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
1-48 |
5.97e-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: 5.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1426492325 1 MRIVCIGGGPAGLYFAL-LMKKQHPEHSISVIERNKPydtFGWGVVFSD 48
Cdd:COG4529 6 KRIAIIGGGASGTALAIhLLRRAPEPLRITLFEPRPE---LGRGVAYST 51
|
|
| PRK08849 |
PRK08849 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional |
267-326 |
1.57e-03 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
Pssm-ID: 181564 [Multi-domain] Cd Length: 384 Bit Score: 41.68 E-value: 1.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 267 NSHVVLMGDAAHTAHFAIGSGTKLAIDDAIELTNQFNKLGHDKDkipAVLETYEEIRRVD 326
Cdd:PRK08849 278 KNNCVLLGDAAHTINPLAGQGVNLGFKDVDVLLAETEKQGVLND---ASFARYERRRRPD 334
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
261-337 |
1.70e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 41.42 E-value: 1.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1426492325 261 WSHfngnSHVVLMGDAAHtAHFAIGS-GTKLAIDDAIELTNQFNKLGHdkdkIPAVLETYEEIRRVDVARIQNAARNA 337
Cdd:PRK07538 294 WTR----GRVTLLGDAAH-PMYPVGSnGASQAILDARALADALAAHGD----PEAALAAYEAERRPATAQIVLANRLN 362
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
616-723 |
1.85e-03 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 40.19 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 616 KAIREVWPADKPISVrlSCHdwfeggnTPEDAAIYAQmfkdAGADLIdcssgqvwkeekpVYGRLFQTP----------- 684
Cdd:cd00564 86 AEARALLGPDLIIGV--STH-------SLEEALRAEE----LGADYV-------------GFGPVFPTPtkpgagpplgl 139
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1426492325 685 -FSDKIRNEIGIPTIAVGAISEaDHANSIIAAGrADLCAV 723
Cdd:cd00564 140 eLLREIAELVEIPVVAIGGITP-ENAAEVLAAG-ADGVAV 177
|
|
| PRK06475 |
PRK06475 |
FAD-binding protein; |
2-324 |
2.25e-03 |
|
FAD-binding protein;
Pssm-ID: 180582 [Multi-domain] Cd Length: 400 Bit Score: 40.96 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 2 RIVCIGGGPAGLYFALLMKkqHPEHSISVIERNKPYDTFGWGVVFSDATMVSMKAWDPES----AAEIEDAFNHWDDIEL 77
Cdd:PRK06475 4 SPLIAGAGVAGLSAALELA--ARGWAVTIIEKAQELSEVGAGLQLAPNAMRHLERLGVADrlsgTGVTPKALYLMDGRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 78 -------LFKGTRQRTSgHGFVGIGRKKLLNILQRRCE-------ALGVELVFETDSSGDID----------YPDADLII 133
Cdd:PRK06475 82 rpllamqLGDLARKRWH-HPYIVCHRADLQSALLDACRnnpgieiKLGAEMTSQRQTGNSITatiirtnsveTVSAAYLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 134 ASDGFNSKIRNRYPevFEPdlvVRPNRYIWLGTNKLFDAFTFDFR------KTDHGWF--QAHIYKFDDKTS---TFIVE 202
Cdd:PRK06475 161 ACDGVWSMLRAKAG--FSK---ARFSGHIAWRTTLAADALPASFLsampehKAVSAWLgnKAHFIAYPVKGGkffNFVAI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 203 TTEEAYEKhglgQMDQQGSIDFCQDLFSEVleGSELMTNARHLRG-SAWLNFNRlicgKWSHFNGNSHVVLMGDAAHTAH 281
Cdd:PRK06475 236 TGGENPGE----VWSKTGDKAHLKSIYADW--NKPVLQILAAIDEwTYWPLFEM----ADAQFVGPDRTIFLGDASHAVT 305
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1426492325 282 FAIGSGTKLAIDDAIELTNQFnklghDKDKIPAVLETYEEIRR 324
Cdd:PRK06475 306 PFAAQGAAMAIEDAAALAEAL-----DSDDQSAGLKRFDSVRK 343
|
|
| carotene-cycl |
TIGR01790 |
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ... |
3-115 |
3.23e-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: 40.49 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 3 IVCIGGGPAGLYFALLMkkQHPEHSISVIErnkPYDTFGWGVVFSdatmvsmkAWDPE-SAAEIEDAFNH-WDDIELLFK 80
Cdd:TIGR01790 2 LAVIGGGPAGLAIALEL--ARPGLRVQLIE---PHPPIPGNHTYG--------VWDDDlSDLGLADCVEHvWPDVYEYRF 68
|
90 100 110
....*....|....*....|....*....|....*
gi 1426492325 81 GTRQRTSGHGFVGIGRKKLLNILQRRCEALGVELV 115
Cdd:TIGR01790 69 PKQPRKLGTAYGSVDSTRLHEELLQKCPEGGVLWL 103
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
573-725 |
6.74e-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: 38.72 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 573 DWLELHCAHGYllssflspltnirtdeyggshenRARYPLEVFKAIREVWPaDKPISVRLSchdwfeggNTPEDAAIYAq 652
Cdd:cd04722 86 DGVEIHGAVGY-----------------------LAREDLELIRELREAVP-DVKVVVKLS--------PTGELAAAAA- 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1426492325 653 mfKDAGADLIDCSSGQvwkeekPVYGRLFQTPFSD----KIRNEIGIPTIAVGAISEADHANSIIAAGrADLCAVAR 725
Cdd:cd04722 133 --EEAGVDEVGLGNGG------GGGGGRDAVPIADllliLAKRGSKVPVIAGGGINDPEDAAEALALG-ADGVIVGS 200
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
613-740 |
6.83e-03 |
|
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: 39.01 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426492325 613 EVFKAIREVwpADKPISV--RLschdwfeGGNTPEDAAIYAQMFKDAGADLIdcssgqvwkeekPVYGR---LFQTPFSD 687
Cdd:cd02801 113 EIVRAVREA--VPIPVTVkiRL-------GWDDEEETLELAKALEDAGASAL------------TVHGRtreQRYSGPAD 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1426492325 688 -----KIRNEIGIPTIAVGAISEADHANSIIAAGRADLCAVARPHLADPaWVLHEAAK 740
Cdd:cd02801 172 wdyiaEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMIGRGALGNP-WLFREIKE 228
|
|
| |
