|
Name |
Accession |
Description |
Interval |
E-value |
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
532-834 |
0e+00 |
|
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN, and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239244 Cd Length: 299 Bit Score: 551.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPlygpGQSSFLNIE 611
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGR----GQIGFNNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 612 LISEKTAAYWCHSVTELKADFPDNILIASIMCSYNKNDWMELSKMAEASGADALELNLSCPHGMGERGMGLACGQDPELV 691
Cdd:cd02940 77 LISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 692 RNICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGLMGLKADGSPwPSVGSGKRTTYGGVSGTAIR 771
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTP-PAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937883505 772 PIALRAVTAIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGL 834
Cdd:cd02940 236 PIALRAVSQIARAPePGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
532-1009 |
2.62e-127 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 393.16 E-value: 2.62e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTfsLDKDIVTNVSPRIirgttsGPLYGPGQS--SFLN 609
Cdd:PRK08318 3 DLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKT--LGPPIVNVSSPRF------GALVKEDRRfiGFNN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 610 IELISEKTAAYWCHSVTELKADFPDNILIASIMCSYNKNDWMELSKMAEASGADALELNLSCPHGMGERGMGLACGQDPE 689
Cdd:PRK08318 75 IELITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 690 LVRNICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGLMGLKADG-SPWPSVGsGKrTTYGGVSGT 768
Cdd:PRK08318 155 LVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRmIPMPIVN-GK-SSHGGYCGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 769 AIRPIALRAVTAIAR--ALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGlkallylksieeL 846
Cdd:PRK08318 233 AVKPIALNMVAEIARdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISG------------L 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 847 SDWdgqspptmshqkgkpvphiaelmgqklpsfgpylerrkkilaaskirekdqnracspLQRKHFNSqkpipaIKDVIG 926
Cdd:PRK08318 301 SHY---------------------------------------------------------MDEKGFAS------LEDMVG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 927 KSLQYLGTFGELNVMEQVVALIDEEMCINCGKCYMTCNDSGYQAIQFDP-ETHLPTVSDT-CTGCTLCLSVCPIMDCIRM 1004
Cdd:PRK08318 318 LAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDEdGTRTPEVIEEeCVGCNLCAHVCPVEGCITM 397
|
....*
gi 1937883505 1005 VSRAT 1009
Cdd:PRK08318 398 GEVKF 402
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
53-513 |
1.13e-121 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 379.91 E-value: 1.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 53 EKLENNFDDIkHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPT 132
Cdd:PRK11749 17 EERAQNFDEV-APGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 133 SDLCVGGCNLhATEEGPINIGGLQQFATEvfKAMNIPQIRSPLLPPPEHmpeaysaKIALFGAGPASISCASFLARLGYs 212
Cdd:PRK11749 96 ERLCEGACVR-GKKGEPVAIGRLERYITD--WAMETGWVLFKRAPKTGK-------KVAVIGAGPAGLTAAHRLARKGY- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 213 DITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSISTDeMTLSTLKEnGYKAAFIGIGLPEPKKDH 292
Cdd:PRK11749 165 DVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRD-ITLDELRA-GYDAVFIGTGAGLPRFLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 293 IF-QGLtqvQGFYTSKDFLPLVAKGSKPgmcachSPLPSVRgAVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFANIR 371
Cdd:PRK11749 243 IPgENL---GGVYSAVDFLTRVNQAVAD------YDLPVGK-RVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 372 AVPEEMELAKEEKCEFLPFLSPRKVIVKDGKIVGMQFVRTE---QDETGN---WVEDEEqiVRLKADVVISAFGSVLDDP 445
Cdd:PRK11749 313 ASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMElgePDASGRrrvPIEGSE--FTLPADLVIKAIGQTPNPL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937883505 446 kVIEALSPIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKYIQAQYGA 513
Cdd:PRK11749 391 -ILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAASA 457
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
57-506 |
1.36e-120 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 376.01 E-value: 1.36e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 57 NNFDDIkHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTsdLC 136
Cdd:COG0493 3 KDFREV-YPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--PC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 137 VGGCNLhATEEGPINIGGLQQFATEVFKAMNIPQIRSPlLPPPEHmpeaysaKIALFGAGPASISCASFLARLGYsDITI 216
Cdd:COG0493 80 EGACVR-GIVDEPVAIGALERFIADKAFEEGWVKPPPP-APRTGK-------KVAVVGSGPAGLAAAYQLARAGH-EVTV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 217 FEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSISTDeMTLSTLKENgYKAAFIGIGLPEPKKDHIfQG 296
Cdd:COG0493 150 FEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKD-ITLDELLEE-FDAVFLATGAGKPRDLGI-PG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 297 lTQVQGFYTSKDFLPLVAKGSKPGmcachsPLPSVRGAVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFANIRAVPEE 376
Cdd:COG0493 227 -EDLKGVHSAMDFLTAVNLGEAPD------TILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 377 MELAKEEKCEFLPFLSPRKVIV-KDGKIVGMQFVRTE---QDETGNW----VEDEEQIvrLKADVVISAFGSVLDDPKVI 448
Cdd:COG0493 300 VEEALEEGVEFLFLVAPVEIIGdENGRVTGLECVRMElgePDESGRRrpvpIEGSEFT--LPADLVILAIGQTPDPSGLE 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937883505 449 EALSpIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKY 506
Cdd:COG0493 378 EELG-LELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
535-833 |
1.25e-96 |
|
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) 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. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 307.36 E-value: 1.25e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 535 VEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDkDIVTNVSPRIIRGTTSGPlYGPGQSSFLNIELIS 614
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLH-PRPGNPLPRVARLPPEGE-SYPEQLGILNSFGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 615 EKTAAYWCHSVTELKADFPDNILIASIMCSyNKNDWMELSKMAEASGADALELNLSCPHGMGERGmglaCGQDPELVRNI 694
Cdd:cd02810 79 NLGLDVWLQDIAKAKKEFPGQPLIASVGGS-SKEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 695 CRWVRQSVRVPFFAKLTPNVT--DIVSIARAAKEGGADGVTATNTVSGLMGLKadgspwPSVGSGKRTTYGGVSGTAIRP 772
Cdd:cd02810 154 LKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDL------KTVGPGPKRGTGGLSGAPIRP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937883505 773 IALRAVTAIARALP-GFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTG 833
Cdd:cd02810 228 LALRWVARLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
58-511 |
3.80e-90 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 296.16 E-value: 3.80e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 58 NFDDIkhtTLG--ERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDL 135
Cdd:PRK12831 22 NFEEV---CLGynEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 136 CVGGCNLHATEEgPINIGGLQQFATEVFKAMNIPQIrspllPPPEHMPEaysaKIALFGAGPASISCASFLARLGYsDIT 215
Cdd:PRK12831 99 CEGKCVLGIKGE-PVAIGKLERFVADWARENGIDLS-----ETEEKKGK----KVAVIGSGPAGLTCAGDLAKMGY-DVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 216 IFEKQEYVGGLSTSEIPQFRLPYD-VVNFEIELMKDLGVKI----ICGKSISTDEMtlstLKENGYKAAFIGIGLPEPKk 290
Cdd:PRK12831 168 IFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIetnvVVGKTVTIDEL----LEEEGFDAVFIGSGAGLPK- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 291 dhiFQGL--TQVQGFYTSKDFLPLV--AKGSKPGmcachSPLPSVRGA-VIVLGAGDTAFDCATSALRCGArRVFIVFRK 365
Cdd:PRK12831 243 ---FMGIpgENLNGVFSANEFLTRVnlMKAYKPE-----YDTPIKVGKkVAVVGGGNVAMDAARTALRLGA-EVHIVYRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 366 GFANIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KDGKIVGMQFVRT---EQDETGNW--VEDEEQIVRLKADVVISAFG 439
Cdd:PRK12831 314 SEEELPARVEEVHHAKEEGVIFDLLTNPVEILGdENGWVKGMKCIKMelgEPDASGRRrpVEIEGSEFVLEVDTVIMSLG 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937883505 440 SVlDDPKVIEALSPIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKYIQAQY 511
Cdd:PRK12831 394 TS-PNPLISSTTKGLKINKRGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSKKW 464
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
532-858 |
6.62e-86 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 282.11 E-value: 6.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIR------GTTSGPLYGpgqs 605
Cdd:PLN02495 10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARlraganGSAKGRVIG---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 606 sFLNIELISEKTAAYWCHSVTELKADFPDNILIASIMCSYNKNDWMELSKMAEASGADALELNLSCPHGMGERGMGLACG 685
Cdd:PLN02495 86 -WQNIELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 686 QDPELVRNICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGLMGLKADG-SPWPSVGSgkRTTYGG 764
Cdd:PLN02495 165 QDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLDTlRPEPCVEG--YSTPGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 765 VSGTAIRPIALRAVTAIARALPG-FP----ILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLY 839
Cdd:PLN02495 243 YSSKAVRPIALAKVMAIAKMMKSeFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMK 322
|
330
....*....|....*....
gi 1937883505 840 LKSIEELSDWDGQSPPTMS 858
Cdd:PLN02495 323 KHNFSSIEDFRGASLPYFT 341
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
532-838 |
3.73e-81 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 265.78 E-value: 3.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKdIVTNVSPRIIRgttsgpLygPGQSSFLNIE 611
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEP-QPGNPRPRLFR------L--PEDSGLINRM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 612 LISEKTAAYWCHSVTELKAdfPDNILIASIMCSyNKNDWMELSKMAEASGADALELNLSCPHGmgeRGMGLACGQDPELV 691
Cdd:COG0167 72 GLNNPGVDAFLERLLPAKR--YDVPVIVNIGGN-TVEDYVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 692 RNICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGL-MGLKAdGSPWPSvgsgkrTTYGGVSGTAI 770
Cdd:COG0167 146 AELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRaIDLET-RRPVLA------NEAGGLSGPAL 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937883505 771 RPIALRAVTAIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:COG0167 219 KPIALRMVREVAQAVGGdIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYL 287
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
57-510 |
4.15e-77 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 268.92 E-value: 4.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 57 NNFDDIkHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLC 136
Cdd:PRK12778 310 NRFEEV-NLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQC 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 137 VGGCNLHATEEGPINIGGLQQFATEVFKA---MNIPQIRspllpppehmpEAYSAKIALFGAGPASISCASFLARLGYsD 213
Cdd:PRK12778 389 ESKCIHGKMGEEAVAIGYLERFVADYEREsgnISVPEVA-----------EKNGKKVAVIGSGPAGLSFAGDLAKRGY-D 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 214 ITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKI----ICGKSISTDEMtlstlKENGYKAAFI--GIGLPe 287
Cdd:PRK12778 457 VTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFetdvIVGKTITIEEL-----EEEGFKGIFIasGAGLP- 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 288 pkkdhIFQGL--TQVQGFYTSKDFLPLV--AKGSKPGmcachSPLPSVRG-AVIVLGAGDTAFDCATSALRCGARRVFIV 362
Cdd:PRK12778 531 -----NFMNIpgENSNGVMSSNEYLTRVnlMDAASPD-----SDTPIKFGkKVAVVGGGNTAMDSARTAKRLGAERVTIV 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 363 FRKGFANIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KDGKIVGMQFVRT---EQDETGNW--VEDEEQIVRLKADVVIS 436
Cdd:PRK12778 601 YRRSEEEMPARLEEVKHAKEEGIEFLTLHNPIEYLAdEKGWVKQVVLQKMelgEPDASGRRrpVAIPGSTFTVDVDLVIV 680
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937883505 437 AFGsVLDDPKVIEALSPIKFNRWGLPEVNPEtMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKYIQAQ 510
Cdd:PRK12778 681 SVG-VSPNPLVPSSIPGLELNRKGTIVVDEE-MQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
58-508 |
3.29e-67 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 233.52 E-value: 3.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 58 NFDDIkHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSdlCV 137
Cdd:PRK12810 26 DFKEF-YEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAP--CE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 138 GGCNLhATEEGPINIGGLQQFATEvfKAMNIPQIRspllppPEHmPEAYSAK-IALFGAGPASISCASFLARLGYsDITI 216
Cdd:PRK12810 103 GACTL-NINFGPVTIKNIERYIID--KAFEEGWVK------PDP-PVKRTGKkVAVVGSGPAGLAAADQLARAGH-KVTV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 217 FEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSISTDeMTLSTLKENgYKAAFIGIG--------LPEP 288
Cdd:PRK12810 172 FERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKD-ITAEELLAE-YDAVFLGTGaykprdlgIPGR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 289 KKDHIFQGL------TQVQGFYTSKDFlpLVAKGSKpgmcachsplpsvrgaVIVLGAGDTAFDCATSALRCGARRvfiV 362
Cdd:PRK12810 250 DLDGVHFAMdfliqnTRRVLGDETEPF--ISAKGKH----------------VVVIGGGDTGMDCVGTAIRQGAKS---V 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 363 FRKGFANIRAVPE-------------EMELAKEEKCEFLPFLSPRKVIVKDGKIVGMQFVRTEQDETGNW-VEDEEQIvr 428
Cdd:PRK12810 309 TQRDIMPMPPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGDFEpVEGSEFV-- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 429 LKADVVISAFGSVLDDPKVIEALSpIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKYIQ 508
Cdd:PRK12810 387 LPADLVLLAMGFTGPEAGLLAQFG-VELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLM 465
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
534-846 |
3.27e-62 |
|
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: 213.56 E-value: 3.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 534 SVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSG-----PLYGPGQSSFL 608
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPRE-GNPPPRVVE-TPGGmlnaiGLQNPGVEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 609 NIELIsektaaywchsvtelKADFPDNILIASIMCSyNKNDWMELSKMAEASGADALELNLSCPHgmgERGMGLACGQDP 688
Cdd:cd04740 79 EELLP---------------WLREFGTPVIASIAGS-TVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 689 ELVRNICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTvsgLMGLKADgspwpsVGSGKR---TTYGGV 765
Cdd:cd04740 140 EAVAEIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINT---LKGMAID------IETRKPilgNVTGGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 766 SGTAIRPIALRAVTAIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIEDYCTGLKALL---YLKS 842
Cdd:cd04740 211 SGPAIKPIALRMVYQVYKAV-EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLdeeGIKS 288
|
....
gi 1937883505 843 IEEL 846
Cdd:cd04740 289 IEEL 292
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
82-510 |
1.22e-60 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 219.60 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 82 CAD--APCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSdlCVGGCNLHATEEgPINIGGLQQFA 159
Cdd:PRK12814 97 CGDclGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDE-PVSICALKRYA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 160 TEvfKAMNIPqirSPLLPPPEhmpEAYSAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYD 239
Cdd:PRK12814 174 AD--RDMESA---ERYIPERA---PKSGKKVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGMMRYGIPRFRLPES 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 240 VVNFEIELMKDLGVKIIC----GKSISTDEMtlstlkENGYKAAFIGIGLPEPKKDHIfQGlTQVQGFYTSKDFLPLVAK 315
Cdd:PRK12814 245 VIDADIAPLRAMGAEFRFntvfGRDITLEEL------QKEFDAVLLAVGAQKASKMGI-PG-EELPGVISGIDFLRNVAL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 316 GSKPgmcachSPLPSVrgavIVLGAGDTAFDCATSALRCGARRVFIVFRKGFANIRAVPEEMELAKEEKCEFLPFLSPRK 395
Cdd:PRK12814 317 GTAL------HPGKKV----VVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 396 VIVKDGKIVgMQFVRTEQ---DETGNW----VEDEEqiVRLKADVVISAFGSVLDDPkvIEALSPIKFNRWGLPEVNPET 468
Cdd:PRK12814 387 IERSEGGLE-LTAIKMQQgepDESGRRrpvpVEGSE--FTLQADTVISAIGQQVDPP--IAEAAGIGTSRNGTVKVDPET 461
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1937883505 469 MQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKYIQAQ 510
Cdd:PRK12814 462 LQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGK 503
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
532-846 |
2.61e-60 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 208.47 E-value: 2.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSG-----PLYGPGQSS 606
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPRE-GNPTPRIAE-TPGGmlnaiGLQNPGVDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 607 FLNIELISEKtaaywchsvtelKADFPdniLIASImCSYNKNDWMEL-SKMAEASGADALELNLSCPHGMGergMGLACG 685
Cdd:PRK07259 79 FIEEELPWLE------------EFDTP---IIANV-AGSTEEEYAEVaEKLSKAPNVDAIELNISCPNVKH---GGMAFG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 686 QDPELVRNICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTvsgLMGLKADgspwpsVGSGK---RTTY 762
Cdd:PRK07259 140 TDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAID------IKTRKpilANVT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 763 GGVSGTAIRPIALRAVTAIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIEDYCTGLKALLY--- 839
Cdd:PRK07259 211 GGLSGPAIKPIALRMVYQVYQAV-DIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDkyg 288
|
....*..
gi 1937883505 840 LKSIEEL 846
Cdd:PRK07259 289 IKSIEEI 295
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
72-510 |
2.45e-57 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 208.85 E-value: 2.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 72 ALREAVRCLKCAdaPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCptSDLCVGGCNLHATEEgPIN 151
Cdd:PRK13984 180 AMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVC--THKCETVCSIGHRGE-PIA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 152 IGGLQQFATEvfkamNIPQIRSPLLPPPEhmPEAYSAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEI 231
Cdd:PRK13984 255 IRWLKRYIVD-----NVPVEKYSEILDDE--PEKKNKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGVMRYGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 232 PQFRLPYDVVNFEIELMKDLGVKIICGKSISTDeMTLSTLKEnGYKAAFIGIGL------PEPKKDH--IFQGLTQVQGF 303
Cdd:PRK13984 327 PSYRLPDEALDKDIAFIEALGVKIHLNTRVGKD-IPLEELRE-KHDAVFLSTGFtlgrstRIPGTDHpdVIQALPLLREI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 304 ytsKDFLPlvAKGSKPgmcachsPLPSvrgAVIVLGAGDTAFDCATSALRC-----GARRVFIV-FRKGFANIRAVPEEM 377
Cdd:PRK13984 405 ---RDYLR--GEGPKP-------KIPR---SLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTsLERTFEEMPADMEEI 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 378 ELAKEEKCEFLPFLSPRKVIVKDGKIVGMQFVRTEQ--DETG--NWVEDEEQIVRLKADVVISAFGSVLDDPKVIEAL-S 452
Cdd:PRK13984 470 EEGLEEGVVIYPGWGPMEVVIENDKVKGVKFKKCVEvfDEEGrfNPKFDESDQIIVEADMVVEAIGQAPDYSYLPEELkS 549
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937883505 453 PIKFNRwGLPEVNpETMQTSEPWVFAGGDVVGMANtTVESVNDGKQASWYIHKYIQAQ 510
Cdd:PRK13984 550 KLEFVR-GRILTN-EYGQTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYLRKQ 604
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
86-510 |
2.09e-56 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 205.11 E-value: 2.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 86 PCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSdlCVGGCNlHATEEGPINIGGLQQFATEVFKA 165
Cdd:PRK12771 48 PCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCN-RGQVDDAVGINAVERFLGDYAIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 166 MNIPqirsplLPPPEhmpEAYSAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEI 245
Cdd:PRK12771 125 NGWK------FPAPA---PDTGKRVAVIGGGPAGLSAAYHLRRMGH-AVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 246 ELMKDLGVKIICGKSISTDeMTLSTLkENGYKAAFIGIG------LPEPKKD--HIFQGLtqvqgfytskDFLPLVAKGS 317
Cdd:PRK12771 195 QRILDLGVEVRLGVRVGED-ITLEQL-EGEFDAVFVAIGaqlgkrLPIPGEDaaGVLDAV----------DFLRAVGEGE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 318 KPGmcachsplpsVRGAVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFANIRAVPEEMELAKEEKCEFLPFLSPRKVI 397
Cdd:PRK12771 263 PPF----------LGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 398 VKDGKIVGM---QFVRTEQDETGNWVEDEEQIVRLKADVVISAFGSVLDDpKVIEALSPIKFNRwGLPEVNPETMQTSEP 474
Cdd:PRK12771 333 GDENGATGLrviTVEKMELDEDGRPSPVTGEEETLEADLVVLAIGQDIDS-AGLESVPGVEVGR-GVVQVDPNFMMTGRP 410
|
410 420 430
....*....|....*....|....*....|....*.
gi 1937883505 475 WVFAGGDVVGMANTTVESVNDGKQASWYIHKYIQAQ 510
Cdd:PRK12771 411 GVFAGGDMVPGPRTVTTAIGHGKKAARNIDAFLGGE 446
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
72-508 |
2.11e-55 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 209.03 E-value: 2.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 72 ALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNLHATEEgPIN 151
Cdd:PRK12775 326 ALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQCIIAKKHE-SVG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 152 IGGLQQFATEvfkamnipQIRSPLLPPPEHMPEAysAKIALFGAGPASISCASFLARLGySDITIFEKQEYVGGLSTSEI 231
Cdd:PRK12775 405 IGRLERFVGD--------NARAKPVKPPRFSKKL--GKVAICGSGPAGLAAAADLVKYG-VDVTVYEALHVVGGVLQYGI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 232 PQFRLPYDVVNFEIELMKDLGVKI----ICGKSISTDEMtlstLKENGYKAAFIGIGLPEPKkdhiFQGL-----TQVqg 302
Cdd:PRK12775 474 PSFRLPRDIIDREVQRLVDIGVKIetnkVIGKTFTVPQL----MNDKGFDAVFLGVGAGAPT----FLGIpgefaGQV-- 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 303 fYTSKDFLPLVAKGSKPGMCACHSPLpSVRGAVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFANIRAVPEEMELAKE 382
Cdd:PRK12775 544 -YSANEFLTRVNLMGGDKFPFLDTPI-SLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKE 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 383 EKCEFLPFLSPRKVIV-KDGKIVGMQFVRTE---QDETGNWVE-DEEQIVRLKADVVISAFGSVlDDPKVIEALSPIKFN 457
Cdd:PRK12775 622 EGIDFFFLHSPVEIYVdAEGSVRGMKVEEMElgePDEKGRRKPmPTGEFKDLECDTVIYALGTK-ANPIITQSTPGLALN 700
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1937883505 458 RWGLPEVN----PETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKYIQ 508
Cdd:PRK12775 701 KWGNIAADdgklESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYLR 755
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
23-500 |
1.21e-52 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 196.01 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 23 QAHATLRSTMAKKLDKKHWKRNTDKncFTCEKLENNFDDIkHTTLGERGALREAVRCLKCAD-APCQKSCPTSLDIKSFI 101
Cdd:PRK12809 157 KASSDAQPSRSAALLPVNSRKGADK--ISASERKTHFGEI-YCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYI 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 102 TSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNLHaTEEGPINIGGLQQFATEVFKAMN-IPQIrSPLLPPPE 180
Cdd:PRK12809 234 RLVQEGKIIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLK-DHSGAVSIGNLERYITDTALAMGwRPDV-SKVVPRSE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 181 hmpeaysaKIALFGAGPASISCASFLARLGYSdITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKS 260
Cdd:PRK12809 312 --------KVAVIGAGPAGLGCADILARAGVQ-VDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 261 ISTDeMTLSTLKENgYKAAFIGIG--------LPEPKKDHIFQGLT-------QVQGFYTSKDFlplvakgskpgmcach 325
Cdd:PRK12809 383 IGRD-ITFSDLTSE-YDAVFIGVGtygmmradLPHEDAPGVIQALPfltahtrQLMGLPESEEY---------------- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 326 sPLPSVRGA-VIVLGAGDTAFDCATSALRCGARRVFIVFRKGFANIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KDGKI 403
Cdd:PRK12809 445 -PLTDVEGKrVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACdEDGRL 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 404 VGMQFVRTEQDETGNWVEDEEQIV-----RLKADVVISAFGSVLDDPKVIEALSpIKFNRWGL---PEVNPETMQTSEPW 475
Cdd:PRK12809 524 TAVGLIRTAMGEPGPDGRRRPRPVagsefELPADVLIMAFGFQAHAMPWLQGSG-IKLDKWGLiqtGDVGYLPTQTHLKK 602
|
490 500
....*....|....*....|....*
gi 1937883505 476 VFAGGDVVGMANTTVESVNDGKQAS 500
Cdd:PRK12809 603 VFAGGDAVHGADLVVTAMAAGRQAA 627
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
533-846 |
2.45e-51 |
|
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.
Pssm-ID: 130109 [Multi-domain] Cd Length: 300 Bit Score: 183.01 E-value: 2.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 533 ISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSG-----PLYGPGQSSF 607
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRP-GYRNPTIVE-TPCGmlnaiGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 608 LNiELISEKTaaywchsvtelkaDFPDNIlIASIMCSyNKNDWMELSKMAEASG--ADALELNLSCPHGMGergMGLACG 685
Cdd:TIGR01037 79 LE-ELKPVRE-------------EFPTPL-IASVYGS-SVEEFAEVAEKLEKAPpyVDAYELNLSCPHVKG---GGIAIG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 686 QDPELVRNICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTvsgLMGLKADgspwpsVGSGK---RTTY 762
Cdd:TIGR01037 140 QDPELSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKID------IKTGKpilANKT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 763 GGVSGTAIRPIALRAVTAIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFtVIEDYCTGLKALLY--- 839
Cdd:TIGR01037 211 GGLSGPAIKPIALRMVYDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKaeg 288
|
....*..
gi 1937883505 840 LKSIEEL 846
Cdd:TIGR01037 289 FTSIEEL 295
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
19-500 |
9.60e-49 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 184.57 E-value: 9.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 19 NPRIQAHATLRSTMAKKLDK-KHWKRNTDKNCFTCEKLENNFDDIKHTTLGERgALREAVRCLKCAD-APCQKSCPTSLD 96
Cdd:PRK12769 167 QPWHASTAAQEMPAMSKVEQmQATPPRGEPDKLAIEARKTGFDEIYLPFRADQ-AQREASRCLKCGEhSICEWTCPLHNH 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 97 IKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNLHaTEEGPINIGGLQQFATEVFKAMNIPQIRSPLL 176
Cdd:PRK12769 246 IPQWIELVKAGNIDAAVELSHQTNSLPEITGRVCPQDRLCEGACTLR-DEYGAVTIGNIERYISDQALAKGWRPDLSQVT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 177 PPPEHmpeaysakIALFGAGPASISCASFLARLGYSdITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKII 256
Cdd:PRK12769 325 KSDKR--------VAIIGAGPAGLACADVLARNGVA-VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 257 CGKSISTDeMTLSTLKENgYKAAFIGIGLPEPKKDHIFQglTQVQGFYtskDFLPLVAKGSKPGM---CACHSPLPSVRG 333
Cdd:PRK12769 396 LNCEVGKD-ISLESLLED-YDAVFVGVGTYRSMKAGLPN--EDAPGVY---DALPFLIANTKQVMgleELPEEPFINTAG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 334 A-VIVLGAGDTAFDCATSALRCGARRVFIVFRKGFANIRAVPEEMELAKEEKCEFLPFLSPRKVIVKD-GKIVGMQFVRT 411
Cdd:PRK12769 469 LnVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEqGHVCGIRFLRT 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 412 ---EQDETGNW----VEDEEQIvrLKADVVISAFGSVLDDPKVIEALSpIKFNRWGLPEVNPET---MQTSEPWVFAGGD 481
Cdd:PRK12769 549 rlgEPDAQGRRrpvpIPGSEFV--MPADAVIMAFGFNPHGMPWLESHG-VTVDKWGRIIADVESqyrYQTSNPKIFAGGD 625
|
490
....*....|....*....
gi 1937883505 482 VVGMANTTVESVNDGKQAS 500
Cdd:PRK12769 626 AVRGADLVVTAMAEGRHAA 644
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
56-168 |
7.48e-45 |
|
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.
Pssm-ID: 434132 [Multi-domain] Cd Length: 113 Bit Score: 157.32 E-value: 7.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 56 ENNFDDIkHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDL 135
Cdd:pfam14691 2 IKNFEEV-ALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 1937883505 136 CVGGCNLHATEEGPINIGGLQQFATEVFKAMNI 168
Cdd:pfam14691 81 CEGACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
75-500 |
6.99e-41 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 163.46 E-value: 6.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 75 EAVRCLKCADAPCQ------------KSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNl 142
Cdd:PRK12779 186 EVMRDKQCDDKPCElgvlvqgkaepkGGCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCT- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 143 HatEEGPINIGGLQQFATEVFKAMNiPQIRSPLLPPPEHMPEAYSAKIALFGAGPASISCASFLARLGYSdITIFEKQEY 222
Cdd:PRK12779 265 H--TKRPIEIGQLEWYLPQHEKLVN-PNANERFAGRISPWAAAVKPPIAVVGSGPSGLINAYLLAVEGFP-VTVFEAFHD 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 223 VGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKI----ICGKSistdeMTLSTLKENGYKAAFIGIGLPEPKkdhiFQGL- 297
Cdd:PRK12779 341 LGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFvknfVVGKT-----ATLEDLKAAGFWKIFVGTGAGLPT----FMNVp 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 298 -TQVQGFYTSKDFLPLV--AKGSKPGMcacHSPLPSVRGA-VIVLGAGDTAFDCATSALRCGARrVFIVFRKGFANIRAV 373
Cdd:PRK12779 412 gEHLLGVMSANEFLTRVnlMRGLDDDY---ETPLPEVKGKeVFVIGGGNTAMDAARTAKRLGGN-VTIVYRRTKSEMPAR 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 374 PEEMELAKEEKCEFLPFLSPRKVIvKDGKivgMQFVRT---------EQDETGNWV-EDEEQIVRLKADVVISAFGSVlD 443
Cdd:PRK12779 488 VEELHHALEEGINLAVLRAPREFI-GDDH---THFVTHalldvnelgEPDKSGRRSpKPTGEIERVPVDLVIMALGNT-A 562
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937883505 444 DPKVIEALSPIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQAS 500
Cdd:PRK12779 563 NPIMKDAEPGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAA 619
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
534-838 |
9.24e-35 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 134.78 E-value: 9.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 534 SVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDiVTNVSPRIIRgTTSGPLYGPGqssFLNIELi 613
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQ-PGNPTPRVFR-LPEGVLNRMG---LNNPGL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 614 sEKTAAYWCHSVTELKADFPdniliaSIMCSYNKNDWMELSKMAEASG--ADALELNLSCPHGMGERgmglACGQDPELV 691
Cdd:pfam01180 77 -DAVLAELLKRRKEYPRPDL------GINLSKAGMTVDDYVEVARKIGpfADYIELNVSCPNTPGLR----ALQTDPELA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 692 RNICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATN-TVSGLMGLKADGSPWPSVGSGKrttYGGVSGTAI 770
Cdd:pfam01180 146 AILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINaTNTTVRGMRIDLKTEKPILANG---TGGLSGPPI 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937883505 771 RPIALRAVTAIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:pfam01180 223 KPIALKVIRELYQRTgPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
189-510 |
1.64e-34 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 135.89 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGV------KIICGKSIS 262
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYLACLGY-EVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVvfhtrtKVCCGEPLH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 263 TDE--------MTLSTLKENgYKAAFIGIGLPEPKKDHIfQGlTQVQGFYTSKDFL---PLVAKGSKPgmcacHSPLPSV 331
Cdd:PRK12770 99 EEEgdefveriVSLEELVKK-YDAVLIATGTWKSRKLGI-PG-EDLPGVYSALEYLfriRAAKLGYLP-----WEKVPPV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 332 RGA-VIVLGAGDTAFDCATSALRCGARRVFIVFRKGFANIRAVPEEMELAKEEKCEFLPFLSPRKVIvKDGKIVGMQFVR 410
Cdd:PRK12770 171 EGKkVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRII-GEGRVEGVELAK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 411 T---EQDETGNW----VEDEEQIvrLKADVVISAFGSVLDDPKVIEALSpIKFNRWGLPEVNpETMQTSEPWVFAGGDVV 483
Cdd:PRK12770 250 MrlgEPDESGRPrpvpIPGSEFV--LEADTVVFAIGEIPTPPFAKECLG-IELNRKGEIVVD-EKHMTSREGVFAAGDVV 325
|
330 340
....*....|....*....|....*..
gi 1937883505 484 GMANTTVESVNDGKQASWYIHKYIQAQ 510
Cdd:PRK12770 326 TGPSKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
946-1004 |
6.42e-29 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 434137 [Multi-domain] Cd Length: 59 Bit Score: 109.68 E-value: 6.42e-29
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937883505 946 ALIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTVSDTCTGCTLCLSVCPIMDCIRM 1004
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDDCITM 59
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
662-819 |
5.11e-23 |
|
Dihydroorotate dehydrogenase (DHOD) class 2. 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, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.
Pssm-ID: 240089 Cd Length: 327 Bit Score: 101.42 E-value: 5.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 662 ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQ-----SVRVPFFAKLTPNVTD--IVSIARAAKEGGADGVTA 734
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDL-----QGKEALRELLTAVKEernklGKKVPLLVKIAPDLSDeeLEDIADVALEHGVDGIIA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 735 TNTVSGLMGLKadGSPWpsvgsgkRTTYGGVSGTAIRPIALRAVTAIARALPG-FPILATGGIDSAESGLQFLHSGASVL 813
Cdd:cd04738 236 TNTTISRPGLL--RSPL-------ANETGGLSGAPLKERSTEVLRELYKLTGGkIPIIGVGGISSGEDAYEKIRAGASLV 306
|
....*.
gi 1937883505 814 QVCSAI 819
Cdd:cd04738 307 QLYTGL 312
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
559-817 |
1.70e-20 |
|
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: 90.72 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 559 MIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRgttsgplygpgqssflnielisektaaywchsvteLKADFPDNILI 638
Cdd:cd04722 17 LAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLK-----------------------------------EVAAETDLPLG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 639 ASIMCSYNKNDWMELSKMAEASGADALELNLSCPHGmgergmglacgqdPELVRNICRWVRQSVR-VPFFAKLTPNVTDi 717
Cdd:cd04722 62 VQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL-------------AREDLELIRELREAVPdVKVVVKLSPTGEL- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 718 vsIARAAKEGGADGVTATNtvsglmglkadgspwpsvgSGKRTTYGGVSGTAIRpialraVTAIARALPGFPILATGGID 797
Cdd:cd04722 128 --AAAAAEEAGVDEVGLGN-------------------GGGGGGGRDAVPIADL------LLILAKRGSKVPVIAGGGIN 180
|
250 260
....*....|....*....|
gi 1937883505 798 SAESGLQFLHSGASVLQVCS 817
Cdd:cd04722 181 DPEDAAEALALGADGVIVGS 200
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
534-838 |
1.25e-18 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 88.68 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 534 SVEMAGLRFPNPFGLA-----SATpatstpMIRrAFEA-GWGFALTKTfsldkdiVT------NVSPRIIRgttsgpLyg 601
Cdd:PRK05286 50 PVTVMGLTFPNPVGLAagfdkNGE------AID-ALGAlGFGFVEVGT-------VTprpqpgNPKPRLFR------L-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 602 PGQSSFLN--------IELISEKtaaywchsvteLKADFPDNILIASImcsyNKN----------DWMELSKMAeASGAD 663
Cdd:PRK05286 108 PEDEALINrmgfnndgADALAER-----------LKKAYRGIPLGINI----GKNkdtpledavdDYLICLEKL-YPYAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 664 ALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQ-----SVRVPFFAKLTPNVTD--IVSIARAAKEGGADGVTATN 736
Cdd:PRK05286 172 YFTVNISSPNTPGLRDL-----QYGEALDELLAALKEaqaelHGYVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIATN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 737 TV---SGLMGLKADGSPwpsvgsgkrttyGGVSGTAIRPIALRAVTAIARALPG-FPILATGGIDSAESGLQFLHSGASV 812
Cdd:PRK05286 247 TTlsrDGLKGLPNADEA------------GGLSGRPLFERSTEVIRRLYKELGGrLPIIGVGGIDSAEDAYEKIRAGASL 314
|
330 340
....*....|....*....|....*.
gi 1937883505 813 LQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:PRK05286 315 VQIYSGLIYEGPGLVKEIVRGLARLL 340
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
535-818 |
3.27e-18 |
|
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273408 Cd Length: 335 Bit Score: 87.15 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 535 VEMAGLRFPNPFGLASATPATSTpMIRRAFEAGWGFALTKTFSlDKDIVTNVSPRIIRGttsgplygPGQSSFLNIELIS 614
Cdd:TIGR01036 48 VTVLGLKFPNPLGLAAGFDKDGE-AIDALGAMGFGFLEIGTVT-PKPQPGNPRPRLFRL--------IEDEALINRMGFN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 615 EKTAAYWCHSVTELKADFPDNILIAS---IMCSYNKNDWMELSKMAEASgADALELNLSCPHGMGERGMglacgQDPELV 691
Cdd:TIGR01036 118 NHGADVLVERLKRARYKGPIGINIGKnkdTPSEDAKEDYAACLRKLGPL-ADYLVVNVSSPNTPGLRDL-----QYKAEL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 692 RNICRWVRQSV-------RVPFFAKLTPNVT--DIVSIARAAKEGGADGVTATNTV---SGLMGLKADGSPwpsvgsgkr 759
Cdd:TIGR01036 192 RDLLTAVKQEQdglrrvhRVPVLVKIAPDLTesDLEDIADSLVELGIDGVIATNTTvsrSLVQGPKNSDET--------- 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937883505 760 ttyGGVSGtaiRPIALRAVTAIAR---ALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSA 818
Cdd:TIGR01036 263 ---GGLSG---KPLQDKSTEIIRRlyaELQGrLPIIGVGGISSAQDALEKIRAGASLLQIYSG 319
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
532-869 |
1.14e-17 |
|
Dihydroorotate dehydrogenase (DHOD) like proteins. 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. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.
Pssm-ID: 240090 Cd Length: 325 Bit Score: 85.36 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGfALTkTFSLDKDIVTNVSPRIIRGTTSGPLYGPGQSSFLNIE 611
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAG-AIV-LPSLFEEQIEREAQELDRFLTYGSSFAEALSYFPEYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 612 LISEKTAAYWCHsVTELKA--DFPdniLIASIMCSYNkNDWMELSKMAEASGADALELNLscphgmgergmgLACGQDPE 689
Cdd:cd04739 79 RYNLGPEEYLEL-IRRAKRavSIP---VIASLNGVSA-GGWVDYARQIEEAGADALELNI------------YALPTDPD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 690 LVRN--------ICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTvsglmglkadgSPWPSVGSGKRTT 761
Cdd:cd04739 142 ISGAeveqryldILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNR-----------FYQPDIDLETLEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 762 YGGV--SGTAIRPIALRAVtAIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLY 839
Cdd:cd04739 211 VPNLllSSPAEIRLPLRWI-AILSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWME 289
|
330 340 350
....*....|....*....|....*....|
gi 1937883505 840 LKSIEELSDWDGQspptMSHqkgKPVPHIA 869
Cdd:cd04739 290 EHGYESVQQLRGS----MSQ---KNVPDPA 312
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
535-838 |
8.39e-17 |
|
Dihydroorotate dehydrogenase (DHOD) class 1A 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: 240092 Cd Length: 294 Bit Score: 81.99 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 535 VEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKdivtnvspriiRGTTSGPLYGPGQSSFLNIELIS 614
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAG-----------RPGNPEPRYYAFPLGSINSLGLP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 615 EKTAAYWCHSVTElkadfpdnilIASIMCSYNKNDWMELSKMAE-------------ASGADALELNLSCPH--GMGERG 679
Cdd:cd04741 70 NLGLDYYLEYIRT----------ISDGLPGSAKPFFISVTGSAEdiaamykkiaahqKQFPLAMELNLSCPNvpGKPPPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 680 MglacgqDPELVRNICRWVRQSVRVPFFAKLTPnVTDIVSIARAAK--EGGADG---VTATNTV-SGLMglkADGSPWPS 753
Cdd:cd04741 140 Y------DFDATLEYLTAVKAAYSIPVGVKTPP-YTDPAQFDTLAEalNAFACPisfITATNTLgNGLV---LDPERETV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 754 VGSGKrTTYGGVSGTAIRPIALRAVTAIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCT 832
Cdd:cd04741 210 VLKPK-TGFGGLAGAYLHPLALGNVRTFRRLLPSeIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEK 288
|
....*.
gi 1937883505 833 GLKALL 838
Cdd:cd04741 289 ELEDIW 294
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
532-860 |
3.12e-16 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 81.07 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 532 DISVEMAGLRFPNPFgLASATPAT-STPMIRRAFEAGWGFALTKtfSLDKDIVTNVSPRIIRGTTSGPLYGPGQSSFLNI 610
Cdd:PRK07565 2 DLSTTYLGLTLRNPL-VASASPLSeSVDNVKRLEDAGAGAVVLK--SLFEEQIRHEAAELDRHLTHGTESFAEALDYFPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 611 ELISE-KTAAYWCHsVTELKA--DFPdniLIASIMCSYNkNDWMELSKMAEASGADALELNLSCPHGmgerGMGLACGQD 687
Cdd:PRK07565 79 PAKFYvGPEEYLEL-IRRAKEavDIP---VIASLNGSSA-GGWVDYARQIEQAGADALELNIYYLPT----DPDISGAEV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 688 PELVRNICRWVRQSVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTvsglmglkadgSPWPSVGSGKRTTYGGV-- 765
Cdd:PRK07565 150 EQRYLDILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNR-----------FYQPDIDLETLEVVPGLvl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 766 SGTAIRPIALRAVtAIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEE 845
Cdd:PRK07565 219 STPAELRLPLRWI-AILSGRVGADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYES 297
|
330
....*....|....*
gi 1937883505 846 LSDWDGQspptMSHQ 860
Cdd:PRK07565 298 LQQFRGS----MSQK 308
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
620-852 |
4.64e-12 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 68.06 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 620 YWCHSVTELKADFPDNILIASIM-CSYNKNDWMeLSKMAEASGADALELNLSCPHGMGERGMGLacgqDPELVRNICRWV 698
Cdd:PRK02506 78 YYLDYVLELQKKGPNKPHFLSVVgLSPEETHTI-LKKIQASDFNGLVELNLSCPNVPGKPQIAY----DFETTEQILEEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 699 RQSVRVPFFAKLTPNVtDIVSIARAA---KEGGADGVTATNTV-SGLMGLKADGSPW--PSVGsgkrttYGGVSGTAIRP 772
Cdd:PRK02506 153 FTYFTKPLGVKLPPYF-DIVHFDQAAaifNKFPLAFVNCINSIgNGLVIDPEDETVVikPKNG------FGGIGGDYIKP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 773 IALRAVTAIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELSDWDG 851
Cdd:PRK02506 226 TALANVRAFYQRLnPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRG 305
|
.
gi 1937883505 852 Q 852
Cdd:PRK02506 306 K 306
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
189-482 |
2.72e-11 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 65.80 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 189 KIALFGAGPASISCASFLARLGYsDITIFEKQE---YVGGLSTSEIPQFRLPYDVVNFEIELMKDL---------GVKII 256
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGG-KVTLIEDEGtcpYGGCVLSKALLGAAEAPEIASLWADLYKRKeevvkklnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 257 CGK---SISTDEMTLSTLKENG-------YKAAFIGIG-------LPEPKKDHIFQGLTqvqgfYTSKDFLPLVAKGSKp 319
Cdd:pfam07992 81 LGTevvSIDPGAKKVVLEELVDgdgetitYDRLVIATGarprlppIPGVELNVGFLVRT-----LDSAEALRLKLLPKR- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 320 gmcachsplpsvrgaVIVLGAGDTAFDCATSALRCGARrVFIVFRKGFANiRAVPEEMELAKEEKceflpfLSPRKVIVK 399
Cdd:pfam07992 155 ---------------VVVVGGGYIGVELAAALAKLGKE-VTLIEALDRLL-RAFDEEISAALEKA------LEKNGVEVR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 400 DGKIVgmqfVRTEQDETGNWVEDEEQiVRLKADVVISAFGsVLDDPKVIEALsPIKFNRWGLPEVNpETMQTSEPWVFAG 479
Cdd:pfam07992 212 LGTSV----KEIIGDGDGVEVILKDG-TEIDADLVVVAIG-RRPNTELLEAA-GLELDERGGIVVD-EYLRTSVPGIYAA 283
|
...
gi 1937883505 480 GDV 482
Cdd:pfam07992 284 GDC 286
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
948-1008 |
2.91e-11 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 60.45 E-value: 2.91e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937883505 948 IDEEMCINCGKCYMTCNDsgyQAIQFDPETHLPTVSDTCTGCTLCLSVCPImDCIRMVSRA 1008
Cdd:COG1144 27 VDEDKCIGCGLCWIVCPD---GAIRVDDGKYYGIDYDYCKGCGICAEVCPV-KAIEMVPEE 83
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
945-1007 |
8.20e-11 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 58.59 E-value: 8.20e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937883505 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVSDTCTGCTLCLSVCPiMDCIRMVSR 1007
Cdd:COG1149 5 IPVIDEEKCIGCGLCVEVCP---EGAIKLDDGGAPVVDPDLCTGCGACVGVCP-TGAITLEER 63
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
945-1005 |
7.80e-10 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 58.66 E-value: 7.80e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937883505 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVSDTCTGCTLCLSVCPImDCIRMV 1005
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACP---VDAIVGAAKAMHTVIADECTGCDLCVEPCPT-DCIEMI 163
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
916-1008 |
3.51e-09 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 58.58 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 916 KPIPAIKDVIGKSLQYLGTFGELNVMEQVVALIDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTVS-DTCTGCTLCLS 994
Cdd:COG1145 147 LGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVC---PTGAIRLKDGKPQIVVDpDKCIGCGACVK 223
|
90
....*....|....
gi 1937883505 995 VCPiMDCIRMVSRA 1008
Cdd:COG1145 224 VCP-VGAISLEPKE 236
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
945-1009 |
4.03e-09 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 57.26 E-value: 4.03e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937883505 945 VALIDEEMCINCGKCYMTCNdsgYQAIqFDPETHLPTV-SDTCTGCTLCLSVCPImDCIRMVSRAT 1009
Cdd:PRK05113 108 VAFIDEDNCIGCTKCIQACP---VDAI-VGATKAMHTViSDLCTGCDLCVAPCPT-DCIEMIPVAE 168
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
476-818 |
7.67e-09 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 58.98 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 476 VFAGGDVVGMANTTVESVNDGKQASWYIHKY------------IQAQYGALVP--SQPTLPLfytpvdlvdISVEMAGLR 541
Cdd:PLN02826 12 AIAGGAYVSTVDEATFCGWLFNATKLVNPLFrlldpetahslaISAAARGLVPreKRPDPSV---------LGVEVWGRT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 542 FPNPFGLASATPATStpmirRAFEA----GWGFALTKTfsldkdiVT------NVSPRIIRGTTSGPLYGPGQSSFLNIE 611
Cdd:PLN02826 83 FSNPIGLAAGFDKNA-----EAVEGllglGFGFVEIGS-------VTplpqpgNPKPRVFRLREEGAIINRYGFNSEGIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 612 LISEKTAAY-----------WCHSVTELKADFPDNILIASIMCSYNKN------DWM----ELSKMAeasgaDALELNLS 670
Cdd:PLN02826 151 AVAKRLGAQhgkrkldetssSSFSSDDVKAGGKAGPGILGVNLGKNKTsedaaaDYVqgvrALSQYA-----DYLVINVS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 671 CPHGMGERGMglacgQDPELVRNICRWVR---------QSVRVPFFAKLTPNVT--DIVSIARAAKEGGADGVTATNTVS 739
Cdd:PLN02826 226 SPNTPGLRKL-----QGRKQLKDLLKKVLaardemqwgEEGPPPLLVKIAPDLSkeDLEDIAAVALALGIDGLIISNTTI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 740 GlmglkadgSPWPSVGSGKRTTYGGVSGTAIRPIALRAVTAIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSA 818
Cdd:PLN02826 301 S--------RPDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGkIPLVGCGGVSSGEDAYKKIRAGASLVQLYTA 372
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
945-1011 |
9.87e-09 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 57.31 E-value: 9.87e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937883505 945 VALI-----DEEMCINCGKCYmtcndsgyQAIQFD----PETHLPTV-SDTCTGCTLCLSVCPiMDCIRMVSRATPY 1011
Cdd:COG2878 126 AAVIggpkgCEYGCIGCGDCI--------KACPFDaivgAAKGMHTVdEDKCTGCGLCVEACP-VDCIEMVPVSPTV 193
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
945-1005 |
1.37e-08 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 57.11 E-value: 1.37e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937883505 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVSDTCTGCTLCLSVCPImDCIRMV 1005
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACP---VDAIVGAPKQMHTVLADLCTGCDLCVPPCPV-DCIDMV 135
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
194-238 |
1.05e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 49.84 E-value: 1.05e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1937883505 194 GAGPASISCASFLARLGYsDITIFEKQEYVGGLSTS-EIPQFRLPY 238
Cdd:pfam13450 3 GAGLAGLVAAALLAKRGF-RVLVLEKRDRLGGNAYSyRVPGYVFDY 47
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
948-1008 |
1.47e-07 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 49.32 E-value: 1.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937883505 948 IDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTV--SDTCTGCTLCLSVCPiMDCIRMVSRA 1008
Cdd:COG1146 5 IDTDKCIGCGACVEVC---PVDVLELDEEGKKALVinPEECIGCGACELVCP-VGAITVEDDE 63
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
931-1005 |
1.54e-07 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 51.24 E-value: 1.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937883505 931 YLGTFGELNVMEQVVALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVSDTCTGCTLCLSVCPiMDCIRMV 1005
Cdd:cd10549 58 ELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCP---VDAITLEDELEIVIDKEKCIGCGICAEVCP-VNAIKLV 128
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
655-810 |
2.31e-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: 52.88 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 655 KMAEASGADALELNLSCP-----HGmgerGMGLACGQDPELVRNICRWVRQSVRVPFFAK---LTPNVTDIVSIARAAKE 726
Cdd:cd02801 74 KIVEELGADGIDLNMGCPspkvtKG----GAGAALLKDPELVAEIVRAVREAVPIPVTVKirlGWDDEEETLELAKALED 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 727 GGADGVtatnTVSGlmglkadgspwpsvgsgkRTT---YggvsgtaiRPIALRAVTAIARALPGFPILATGGIDSAESGL 803
Cdd:cd02801 150 AGASAL----TVHG------------------RTReqrY--------SGPADWDYIAEIKEAVSIPVIANGDIFSLEDAL 199
|
....*...
gi 1937883505 804 QFL-HSGA 810
Cdd:cd02801 200 RCLeQTGV 207
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
649-810 |
4.88e-07 |
|
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: 52.71 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 649 DWM-ELSKMAEASGADALELNLSCPHGMGERGMGLAC-GQDPELVRNICRWVRQSVRVPFFAKLT----PNVTDIVSIAR 722
Cdd:pfam01207 66 ALLaEAAKLVEDRGADGIDINMGCPSKKVTRGGGGAAlLRNPDLVAQIVKAVVKAVGIPVTVKIRigwdDSHENAVEIAK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 723 AAKEGGADGVtatnTVSGlmglkadgspwpsvgsgkRTTYGGVSGTAirpiALRAVTAIARALPgFPILATGGIDSAESG 802
Cdd:pfam01207 146 IVEDAGAQAL----TVHG------------------RTRAQNYEGTA----DWDAIKQVKQAVS-IPVIANGDITDPEDA 198
|
....*....
gi 1937883505 803 LQFL-HSGA 810
Cdd:pfam01207 199 QRCLaYTGA 207
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
948-997 |
8.18e-07 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 46.86 E-value: 8.18e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1937883505 948 IDEEMCINCGKCYMTC--NDSGYQAIQFDPET-HLPTVSDTCTGCTLCLSVCP 997
Cdd:pfam13237 4 IDPDKCIGCGRCTAACpaGLTRVGAIVERLEGeAVRIGVWKCIGCGACVEACP 56
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
953-997 |
9.27e-07 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 46.75 E-value: 9.27e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1937883505 953 CINCGKCYMTCNdsgYQAIQFDPETHLPTV------SDTCTGCTLCLSVCP 997
Cdd:pfam12838 1 CIGCGACVAACP---VGAITLDEVGEKKGTktvvidPERCVGCGACVAVCP 48
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
335-510 |
1.08e-06 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 51.66 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 335 VIVLGAGDTAFDcatSALRCG--ARRVFIVFRKGfaNIRAVPEEMELAKE-EKCEFLPflspRKVIVK---DGKIVGMQF 408
Cdd:COG0492 144 VVVVGGGDSALE---EALYLTkfASKVTLIHRRD--ELRASKILVERLRAnPKIEVLW----NTEVTEiegDGRVEGVTL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 409 VRTEQDETgnwvedeeqiVRLKADVVISAFGSvldDPKV--IEALSpIKFNRWGLPEVNpETMQTSEPWVFAGGDVVGM- 485
Cdd:COG0492 215 KNVKTGEE----------KELEVDGVFVAIGL---KPNTelLKGLG-LELDEDGYIVVD-EDMETSVPGVFAAGDVRDYk 279
|
170 180
....*....|....*....|....*...
gi 1937883505 486 ---ANTtveSVNDGKQASWYIHKYIQAQ 510
Cdd:COG0492 280 yrqAAT---AAGEGAIAALSAARYLEPL 304
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
950-1004 |
1.12e-06 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 46.66 E-value: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937883505 950 EEMCINCGKCYMTCNdsgYQAIQFDPETHLPTV---SDTCTGCTLCLSVCPiMDCIRM 1004
Cdd:COG1143 1 EDKCIGCGLCVRVCP---VDAITIEDGEPGKVYvidPDKCIGCGLCVEVCP-TGAISM 54
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
649-810 |
1.58e-06 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 51.25 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 649 DWM-ELSKMAEASGADALELNLSCP------HGMGergmglAC-GQDPELVRNICRWVRQSVRVPFFAK----LTPNVTD 716
Cdd:COG0042 74 EELaEAARIAEELGADEIDINMGCPvkkvtkGGAG------AAlLRDPELVAEIVKAVVEAVDVPVTVKirlgWDDDDEN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 717 IVSIARAAKEGGADGVtatnTVSGlmglkadgspwpsvgsgkRTT---YggvSGTAIRPialrAVTAIARALPgFPILAT 793
Cdd:COG0042 148 ALEFARIAEDAGAAAL----TVHG------------------RTReqrY---KGPADWD----AIARVKEAVS-IPVIGN 197
|
170
....*....|....*...
gi 1937883505 794 GGIDSAESGLQFL-HSGA 810
Cdd:COG0042 198 GDIFSPEDAKRMLeETGC 215
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
948-1008 |
1.78e-06 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 46.57 E-value: 1.78e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937883505 948 IDEEMCINCGKCYMTCN----DSGYQAIQFDPethlptvsDTCTGCTLCLSVCPImDCIRMVSRA 1008
Cdd:COG4231 19 IDEDKCTGCGACVKVCPadaiEEGDGKAVIDP--------DLCIGCGSCVQVCPV-DAIKLEKRV 74
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
947-1005 |
2.04e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 47.96 E-value: 2.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937883505 947 LIDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTVSDTCTGCTLCLSVCPiMDCIRMV 1005
Cdd:cd10550 76 VVDEDKCIGCGMCVEAC---PFGAIRVDPETGKAIKCDLCGGDPACVKVCP-TGALEFV 130
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
945-1005 |
2.59e-06 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 47.77 E-value: 2.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHlptVSDTCTGC---------TLCLSVCPImDCIRMV 1005
Cdd:cd04410 74 IVLIDEDKCIGCGSCVEACP---YGAIVFDPEPG---KAVKCDLCgdrldeglePACVKACPT-GALTFG 136
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
940-997 |
3.81e-06 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 45.43 E-value: 3.81e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937883505 940 VMEQVVALIDEEMCINCGKCYMTCNDsgyQAIQFDpETHLPTVSDTCTGCTLCLSVCP 997
Cdd:COG2221 4 IIGTWPPKIDEEKCIGCGLCVAVCPT---GAISLD-DGKLVIDEEKCIGCGACIRVCP 57
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
945-1005 |
7.45e-06 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 46.45 E-value: 7.45e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937883505 945 VALIDEEMCINCGKCYMTCNdsgYQAIqFDPETHLPTV-SDTCTGCTLCLSVCPImDCIRMV 1005
Cdd:PRK08764 79 VAWIVEADCIGCTKCIQACP---VDAI-VGGAKHMHTViAPLCTGCELCVPACPV-DCIELH 135
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
944-1004 |
8.09e-06 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 44.72 E-value: 8.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937883505 944 VVALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLpTVSDTCTGCTLCLSVCPiMDCIRM 1004
Cdd:COG2768 4 GKPYVDEEKCIGCGACVKVCP---VGAISIEDGKAV-IDPEKCIGCGACIEVCP-VGAIKI 59
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
945-997 |
9.09e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 46.86 E-value: 9.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 945 VALIDEEMCIN------CGKCYMTCNDSGYqAIQFDPETHLPTV-SDTCTGCTLCLSVCP 997
Cdd:cd16373 85 VAVIDKDRCLAwqggtdCGVCVEACPTEAI-AIVLEDDVLRPVVdEDKCVGCGLCEYVCP 143
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
926-997 |
1.13e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 49.09 E-value: 1.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937883505 926 GKSLQYLGtfGELNVMEQVVALIDEEMCINCGKCYMTCNdsgYQAIQFDpETHLPTVSDT-CTGCTLCLSVCP 997
Cdd:COG1148 473 ARAIQLLS--KGELGVEPSVAEVDPEKCTGCGRCVEVCP---YGAISID-EKGVAEVNPAlCKGCGTCAAACP 539
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
949-1005 |
1.21e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 45.73 E-value: 1.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937883505 949 DEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVsdtCTGCTLCLSVCPiMDCIRMV 1005
Cdd:cd16370 81 DKEKCIGCGNCVKACI---VGAIFWDEETNKPII---CIHCGYCARYCP-HDVLAME 130
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
194-252 |
1.39e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 48.69 E-value: 1.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937883505 194 GAGPASISCASFLARLGYsDITIFEKQEYVGG-LSTSEIPQFRL---PYDVVNFEI--ELMKDLG 252
Cdd:COG1233 10 GAGIGGLAAAALLARAGY-RVTVLEKNDTPGGrARTFERPGFRFdvgPSVLTMPGVleRLFRELG 73
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
194-503 |
1.90e-05 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 48.54 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 194 GAGPASISCASFLARLGYSdITIFEKqEYVGG-------------LSTSEI-------PQFRLPYDVVNFEI-------- 245
Cdd:COG1249 10 GAGPGGYVAAIRAAQLGLK-VALVEK-GRLGGtclnvgcipskalLHAAEVahearhaAEFGISAGAPSVDWaalmarkd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 246 -----------ELMKDLGVKIICG-------KSIS-TDEMTLSTlkengyKAAFIGIG-----LPEPKKDHIfqgltqvq 301
Cdd:COG1249 88 kvvdrlrggveELLKKNGVDVIRGrarfvdpHTVEvTGGETLTA------DHIVIATGsrprvPPIPGLDEV-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 302 GFYTSKDFLPLvakgskpgmcachSPLPSvRgaVIVLGAGDTAFDCATSALRCGARrVFIVFRKGfaniRAVP-EEMELA 380
Cdd:COG1249 154 RVLTSDEALEL-------------EELPK-S--LVVIGGGYIGLEFAQIFARLGSE-VTLVERGD----RLLPgEDPEIS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 381 KEekceflpfLspRKVIVKDG-KIV-GMQFVRTEQDETGNWV--EDEEQIVRLKADVVISAFGSVlddPKV----IEALS 452
Cdd:COG1249 213 EA--------L--EKALEKEGiDILtGAKVTSVEKTGDGVTVtlEDGGGEEAVEADKVLVATGRR---PNTdglgLEAAG 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1937883505 453 pIKFNRWGLPEVNpETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYI 503
Cdd:COG1249 280 -VELDERGGIKVD-EYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENI 328
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
190-484 |
2.97e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 47.86 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 190 IALFGAGPASISCASFLARLGYSdITIFEKQEYvGG-------------LSTSEI-------PQFRLPYDV--VNF---- 243
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKK-VALIEKGPL-GGtclnvgcipskalIAAAEAfheakhaEEFGIHADGpkIDFkkvm 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 244 --------------EIELMKDLGVKIICGKSISTDEMTLStLKENGYKAAFIGI----------GLPEPKKDHIfqgltq 299
Cdd:PRK06292 84 arvrrerdrfvggvVEGLEKKPKIDKIKGTARFVDPNTVE-VNGERIEAKNIVIatgsrvppipGVWLILGDRL------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 300 vqgfYTSKDFLPLvakgskpgmcachSPLPSvrgAVIVLGAG----DTAFdcATSALrcGARRVFIVFRKGFANIravpE 375
Cdd:PRK06292 157 ----LTSDDAFEL-------------DKLPK---SLAVIGGGviglELGQ--ALSRL--GVKVTVFERGDRILPL----E 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 376 EMELAKEekceFLPFLSPRKVIVKDGKIVGmqfVRTEQDETGNWVEDEEQIVRLKADVVISAFG--SVLDDPKvIEALSp 453
Cdd:PRK06292 209 DPEVSKQ----AQKILSKEFKIKLGAKVTS---VEKSGDEKVEELEKGGKTETIEADYVLVATGrrPNTDGLG-LENTG- 279
|
330 340 350
....*....|....*....|....*....|.
gi 1937883505 454 IKFNRWGLPEVNPeTMQTSEPWVFAGGDVVG 484
Cdd:PRK06292 280 IELDERGRPVVDE-HTQTSVPGIYAAGDVNG 309
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
948-1016 |
7.35e-05 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 43.54 E-value: 7.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937883505 948 IDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVS----DTCTGCTLCLSVCPImDCIRMVSRATPYEPKRG 1016
Cdd:cd10549 3 YDPEKCIGCGICVKACP---TDAIELGPNGAIARGPeideDKCVFCGACVEVCPT-GAIELTPEGKEYVPKEK 71
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
948-1011 |
1.24e-04 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 42.77 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937883505 948 IDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTVS--------DTCTGCTLCLSVCPImDCIRMVSRATPY 1011
Cdd:cd10549 37 IDEDKCVFCGACVEVC---PTGAIELTPEGKEYVPKekeaeideEKCIGCGLCVKVCPV-DAITLEDELEIV 104
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
952-1002 |
1.56e-04 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 40.23 E-value: 1.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1937883505 952 MCINCGKCYMTCNDSGYQAIQFDPETHLPTVSDTCTGCTLCLSVCPiMDCI 1002
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQTIRGDIAGLACIGCGACVDACP-RGAI 50
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
948-997 |
3.76e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 44.25 E-value: 3.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1937883505 948 IDEEMCINCGKCYMTCndsGYQAIQFDpETHLPTVSDTCTGCTLCLSVCP 997
Cdd:COG4624 88 RDKEKCKNCYPCVRAC---PVKAIKVD-DGKAEIDEEKCISCGQCVAVCP 133
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
189-230 |
5.15e-04 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 43.67 E-value: 5.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1937883505 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSE 230
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTV 43
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
947-1010 |
6.23e-04 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 41.86 E-value: 6.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937883505 947 LIDEEMCINCGKCYMTCNdsgYQAIQFDPETHlptVSDTCTGC---------TLCLSVCPiMDCIRMVSRATP 1010
Cdd:COG0437 86 LVDYDKCIGCRYCVAACP---YGAPRFNPETG---VVEKCTFCadrldegllPACVEACP-TGALVFGDLDDP 151
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
621-733 |
6.41e-04 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 43.04 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 621 WCHSVTELKADFPDNILIASIMCSYNKNDWM-ELSKMAEASGADALELNLSCPHGMGERGM-GLACGQDPELVRNICRWV 698
Cdd:PRK10415 49 WESDKSRLRMVHIDEPGIRTVQIAGSDPKEMaDAARINVESGAQIIDINMGCPAKKVNRKLaGSALLQYPDLVKSILTEV 128
|
90 100 110
....*....|....*....|....*....|....*....
gi 1937883505 699 RQSVRVPFFAKL----TPNVTDIVSIARAAKEGGADGVT 733
Cdd:PRK10415 129 VNAVDVPVTLKIrtgwAPEHRNCVEIAQLAEDCGIQALT 167
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
949-1005 |
6.87e-04 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 40.01 E-value: 6.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937883505 949 DEEMCINCGKCYMTCNDSgyqAIQFDPETHLPTVSDTCTGCTLCLSVCPiMDCIRMV 1005
Cdd:PRK09624 49 NRDKCVRCYLCYIYCPEP---AIYLDEEGYPVFDYDYCKGCGICANECP-TKAIEMV 101
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
189-252 |
7.47e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 43.34 E-value: 7.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937883505 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSeipqfrlpYDVVNFEIE---------------LMKDLG 252
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGH-EVTVFEADDQLGGLAAS--------FEFGGLPIErfyhhifksdealleLLDELG 70
|
|
| napG |
PRK09476 |
quinol dehydrogenase periplasmic component; Provisional |
947-996 |
9.83e-04 |
|
quinol dehydrogenase periplasmic component; Provisional
Pssm-ID: 236534 [Multi-domain] Cd Length: 254 Bit Score: 41.92 E-value: 9.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937883505 947 LIDEEMCIN-----CGKCYMTCN--DsgyQAI----QFDPETH-----LPTV-SDTCTGCTLCLSVC 996
Cdd:PRK09476 133 LVDQENCLNfqglrCDVCYRVCPliD---KAItlelERNERTGkhaffLPTVhSDACTGCGKCEKAC 196
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
945-998 |
1.39e-03 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 41.60 E-value: 1.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1937883505 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPeTHLPTVSDTCTGCTLCLSVCPI 998
Cdd:cd03110 58 KAFIDQEKCIRCGNCERVCK---FGAILEFF-QKLIVDESLCEGCGACVIICPR 107
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
961-1007 |
1.59e-03 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 39.92 E-value: 1.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1937883505 961 MTCNDS-GYQAIQFDPETH---LPTV-SDTCTGCTLCLSVCPImDCIRMVSR 1007
Cdd:cd10564 89 RSCQDAcPTQAIRFRPRLGgiaLPELdADACTGCGACVSVCPV-GAITLTPL 139
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
945-997 |
1.93e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 1.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 945 VALIDEEMCiNCGKCYMTC------NDSGYQAIQFDPETHLPTVS-DTCTGCTLCLSVCP 997
Cdd:COG1245 4 IAVVDRDRC-QPKKCNYECikycpvNRTGKEAIEIDEDDGKPVISeELCIGCGICVKKCP 62
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
951-997 |
2.02e-03 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 39.35 E-value: 2.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1937883505 951 EMCINCGKCYMTCNDSgyqAIQFDPETHLPTVSDTCTGCTLCLSVCP 997
Cdd:PRK09625 59 EICINCFNCWVYCPDA---AILSRDKKLKGVDYSHCKGCGVCVEVCP 102
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
951-1024 |
2.09e-03 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 41.60 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 951 EMCINCGKCYMTC---------NDS-------------GYQAIQFDPETHLptVSDTCTGCTLCLSVCPIM-DCIRMVSR 1007
Cdd:COG0247 78 DACVGCGFCRAMCpsykatgdeKDSprgrinllrevleGELPLDLSEEVYE--VLDLCLTCKACETACPSGvDIADLIAE 155
|
90
....*....|....*...
gi 1937883505 1008 ATP-YEPKRGLPLAVKPV 1024
Cdd:COG0247 156 ARAqLVERGGRPLRDRLL 173
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
179-231 |
3.02e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 41.32 E-value: 3.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1937883505 179 PEHMPEaysaKIALFGAGPASISCASFLARLGySDITIFEKQEYVGGLSTSEI 231
Cdd:PRK06292 165 LDKLPK----SLAVIGGGVIGLELGQALSRLG-VKVTVFERGDRILPLEDPEV 212
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
428-487 |
3.03e-03 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 40.95 E-value: 3.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937883505 428 RLKADVVISAFGSVlddPKV-IEALSPIKFNRWGLPEVNpETMQTSEPWVFAGGDVVGMAN 487
Cdd:COG0446 206 EIPADLVVVAPGVR---PNTeLAKDAGLALGERGWIKVD-ETLQTSDPDVYAAGDCAEVPH 262
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
189-227 |
3.86e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 41.03 E-value: 3.86e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1937883505 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLS 227
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGIS 43
|
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
945-997 |
3.98e-03 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 38.00 E-value: 3.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1937883505 945 VALIDEEMCINCGKCYMTCNDSgyqAIQFDPETHLPTVSDTCTGCTLCLSVCP 997
Cdd:PRK09623 45 MPVVDESKCVKCYICWKFCPEP---AIYIKEDGYVAIDYDYCKGCGICANECP 94
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
981-1005 |
4.26e-03 |
|
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).
Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 40.23 E-value: 4.26e-03
10 20
....*....|....*....|....*
gi 1937883505 981 TVSDTCTGCTLCLSVCPiMDCIRMV 1005
Cdd:NF038196 182 HVTDKCIGCGICAKVCP-VNNIEME 205
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
948-1008 |
4.79e-03 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 40.05 E-value: 4.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937883505 948 IDEEMCINCGKCYMTCndsgyqaiqfdpETHLP-----TVSDTCTGCTLCLSVCPImDCIRMVSRA 1008
Cdd:COG0348 207 YDRGDCIDCGLCVKVC------------PMGIDirkgeINQSECINCGRCIDACPK-DAIRFSSRG 259
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
945-1005 |
5.37e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 5.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937883505 945 VALIDEEMCiNCGKCYMTC------NDSGYQAIQFDPETHLPTVS-DTCTGCTLCLSVCPiMDCIRMV 1005
Cdd:PRK13409 4 IAVVDYDRC-QPKKCNYECikycpvVRTGEETIEIDEDDGKPVISeELCIGCGICVKKCP-FDAISIV 69
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
649-732 |
8.15e-03 |
|
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: 39.48 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937883505 649 DWMELSKMAEASGADALelNLSCphGMGERGMGLACGQDPELVRNI--CRWVRQSVRVPFFAklTPNVTDIVSIARAAKE 726
Cdd:cd02803 229 EAIEIAKALEEAGVDAL--HVSG--GSYESPPPIIPPPYVPEGYFLelAEKIKKAVKIPVIA--VGGIRDPEVAEEILAE 302
|
....*.
gi 1937883505 727 GGADGV 732
Cdd:cd02803 303 GKADLV 308
|
|
| |
