|
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: 550.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPmygpGQSSFLNIE 611
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGR----GQIGFNNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 612 LISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACGQDPELV 691
Cdd:cd02940 77 LISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 692 RNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDGTPwPAVGIAKRTTYGGVSGTAIR 771
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTP-PAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119943098 772 PIALRAVTSIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGL 834
Cdd:cd02940 236 PIALRAVSQIARAPePGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
532-1007 |
3.96e-123 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 382.37 E-value: 3.96e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTfsLDKDIVTNVSPRIirgttsGPMYGPGQS--SFLN 609
Cdd:PRK08318 3 DLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKT--LGPPIVNVSSPRF------GALVKEDRRfiGFNN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 610 IELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACGQDPE 689
Cdd:PRK08318 75 IELITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 690 LVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDG-TPWPAVGiaKRTTYGGVSGT 768
Cdd:PRK08318 155 LVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRmIPMPIVN--GKSSHGGYCGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 769 AIRPIALRAVTSIAR--ALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGlkallylksieeL 846
Cdd:PRK08318 233 AVKPIALNMVAEIARdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISG------------L 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 847 QDWdgqspatvshqkgkpvpriaelMDKKlpsfgpyleqrkkiiaenkirlkeqnvafsplkrncfipkrPIPTIKDVIG 926
Cdd:PRK08318 301 SHY----------------------MDEK-----------------------------------------GFASLEDMVG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 927 KALQYLGTFGELSNVEQVVAMIDEEMCINCGKCYMTCNDSGYQAIQFDPET--HLPTITDTCTGCTLCLSVCPIVDCIKM 1004
Cdd:PRK08318 318 LAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDEDGtrTPEVIEEECVGCNLCAHVCPVEGCITM 397
|
...
gi 119943098 1005 VSR 1007
Cdd:PRK08318 398 GEV 400
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
53-513 |
4.35e-119 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 372.98 E-value: 4.35e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 53 EKLENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPT 132
Cdd:PRK11749 17 EERAQNFDEV-APGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 133 SDLCVGGCNLYATEEgPINIGGLQQFATEvfKAMSIPQIRNPSLPPPEKmseaysaKIALFGAGPASISCASFLARLGYs 212
Cdd:PRK11749 96 ERLCEGACVRGKKGE-PVAIGRLERYITD--WAMETGWVLFKRAPKTGK-------KVAVIGAGPAGLTAAHRLARKGY- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 213 DITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNeMTLSTLKEkGYKAAFIGIGLPEPNKDA 292
Cdd:PRK11749 165 DVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRD-ITLDELRA-GYDAVFIGTGAGLPRFLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 293 IF-QGLtqdQGFYTSKDFLPLVAKGSKAgmcachSPLPSIRGVViVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIR 371
Cdd:PRK11749 243 IPgENL---GGVYSAVDFLTRVNQAVAD------YDLPVGKRVV-VIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 372 AVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTE---QDETGKWNE-DEDQMVHLKADVVISAFGSVlSDPKV 447
Cdd:PRK11749 313 ASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMElgePDASGRRRVpIEGSEFTLPADLVIKAIGQT-PNPLI 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119943098 448 KEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQYGA 513
Cdd:PRK11749 392 LSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAASA 457
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
57-506 |
8.56e-117 |
|
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: 366.00 E-value: 8.56e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 57 NNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTsdLC 136
Cdd:COG0493 3 KDFREV-YPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--PC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 137 VGGCNLyATEEGPINIGGLQQFATEvfKAMSIPQIRNPSLPPP-EKmseaysaKIALFGAGPASISCASFLARLGYsDIT 215
Cdd:COG0493 80 EGACVR-GIVDEPVAIGALERFIAD--KAFEEGWVKPPPPAPRtGK-------KVAVVGSGPAGLAAAYQLARAGH-EVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 216 IFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNeMTLSTLKEKgYKAAFIGIG------LPEPN 289
Cdd:COG0493 149 VFEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKD-ITLDELLEE-FDAVFLATGagkprdLGIPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 290 KDAifqgltqdQGFYTSKDFLPLVAKgskagMCACHSPLPsIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVN 369
Cdd:COG0493 227 EDL--------KGVHSAMDFLTAVNL-----GEAPDTILA-VGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 370 IRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRTE---QDETGKWN--EDEDQMVHLKADVVISAFGSVLS 443
Cdd:COG0493 293 MPASKEEVEEALEEGVEFLFLVAPVEIIGdENGRVTGLECVRMElgePDESGRRRpvPIEGSEFTLPADLVILAIGQTPD 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119943098 444 DPKVKEALSpIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKY 506
Cdd:COG0493 373 PSGLEEELG-LELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
535-833 |
4.54e-98 |
|
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: 311.21 E-value: 4.54e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 535 VEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDkDIVTNVSPRIIRGTTSGPmYGPGQSSFLNIELIS 614
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLH-PRPGNPLPRVARLPPEGE-SYPEQLGILNSFGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 615 EKTAAYWCQSVTELKADFPDNIVIASIMCSyNKNDWTELAKKSEDSGADALELNLSCPHGMGERGmglaCGQDPELVRNI 694
Cdd:cd02810 79 NLGLDVWLQDIAKAKKEFPGQPLIASVGGS-SKEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 695 CRWVRQAVQIPFFAKLTPNVT--DIVSIARAAKEGGANGVTATNTVSGLMGLKsdgtpwPAVGIAKRTTYGGVSGTAIRP 772
Cdd:cd02810 154 LKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDL------KTVGPGPKRGTGGLSGAPIRP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119943098 773 IALRAVTSIARALP-GFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTG 833
Cdd:cd02810 228 LALRWVARLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
58-511 |
6.42e-85 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 281.91 E-value: 6.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 58 NFDDIkhtTLG--ERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDL 135
Cdd:PRK12831 22 NFEEV---CLGynEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 136 CVGGCNLYATEEgPINIGGLQQFATEVFKAMSIPQIrnpslPPPEKMSEaysaKIALFGAGPASISCASFLARLGYsDIT 215
Cdd:PRK12831 99 CEGKCVLGIKGE-PVAIGKLERFVADWARENGIDLS-----ETEEKKGK----KVAVIGSGPAGLTCAGDLAKMGY-DVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 216 IFEKQEYVGGLSTSEIPQFRLPYD-VVNFEIELMKDLGVKI----ICGKSLSVNEMtlstLKEKGYKAAFIGI--GLPEp 288
Cdd:PRK12831 168 IFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIetnvVVGKTVTIDEL----LEEEGFDAVFIGSgaGLPK- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 289 nkdaiFQGL--TQDQGFYTSKDFLPLVAKGsKAGMCACHSPLPSIRGVVIVlGAGDTAFDCATSALRCGArRVFIVFRKG 366
Cdd:PRK12831 243 -----FMGIpgENLNGVFSANEFLTRVNLM-KAYKPEYDTPIKVGKKVAVV-GGGNVAMDAARTALRLGA-EVHIVYRRS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 367 FVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRT---EQDETGKWN--EDEDQMVHLKADVVISAFGS 440
Cdd:PRK12831 315 EEELPARVEEVHHAKEEGVIFDLLTNPVEILGdENGWVKGMKCIKMelgEPDASGRRRpvEIEGSEFVLEVDTVIMSLGT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119943098 441 VlSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQY 511
Cdd:PRK12831 395 S-PNPLISSTTKGLKINKRGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSKKW 464
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
532-853 |
2.50e-84 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 277.87 E-value: 2.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIR------GTTSGPMYGpgqs 605
Cdd:PLN02495 10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARlraganGSAKGRVIG---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 606 sFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACG 685
Cdd:PLN02495 86 -WQNIELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 686 QDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDgTPWPAVGIAKRTTYGGV 765
Cdd:PLN02495 165 QDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLD-TLRPEPCVEGYSTPGGY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 766 SGTAIRPIALRAVTSIARALPG-FP----ILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYL 840
Cdd:PLN02495 244 SSKAVRPIALAKVMAIAKMMKSeFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKK 323
|
330
....*....|...
gi 119943098 841 KSIEELQDWDGQS 853
Cdd:PLN02495 324 HNFSSIEDFRGAS 336
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
532-838 |
4.69e-82 |
|
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: 268.09 E-value: 4.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKdIVTNVSPRIIRgtTsgpmygPGQSSFLNIE 611
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEP-QPGNPRPRLFR--L------PEDSGLINRM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 612 LISEKTAAYWCQSVTELKAdfPDNIVIASIMCSyNKNDWTELAKKSEDSGADALELNLSCPHGmgeRGMGLACGQDPELV 691
Cdd:COG0167 72 GLNNPGVDAFLERLLPAKR--YDVPVIVNIGGN-TVEDYVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 692 RNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLmglksdgtpwpAVGIAKRT-----TYGGVS 766
Cdd:COG0167 146 AELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGR-----------AIDLETRRpvlanEAGGLS 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119943098 767 GTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:COG0167 215 GPALKPIALRMVREVAQAVGGdIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYL 287
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
57-510 |
2.99e-78 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 272.00 E-value: 2.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 57 NNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLC 136
Cdd:PRK12778 310 NRFEEV-NLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQC 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 137 VGGCNLYATEEGPINIGGLQQFATEVFKamsipQIRNPSLPppeKMSEAYSAKIALFGAGPASISCASFLARLGYsDITI 216
Cdd:PRK12778 389 ESKCIHGKMGEEAVAIGYLERFVADYER-----ESGNISVP---EVAEKNGKKVAVIGSGPAGLSFAGDLAKRGY-DVTV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 217 FEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKI----ICGKSLSVNEMtlstlKEKGYKAAFIGIGLPEPNkda 292
Cdd:PRK12778 460 FEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFetdvIVGKTITIEEL-----EEEGFKGIFIASGAGLPN--- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 293 iFQGLTQDQ--GFYTSKDFLplvakgSKAGMCACHSPL---PSIRG-VVIVLGAGDTAFDCATSALRCGARRVFIVFRKG 366
Cdd:PRK12778 532 -FMNIPGENsnGVMSSNEYL------TRVNLMDAASPDsdtPIKFGkKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRS 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 367 FVNIRAVPEEMELAKEEKCEFLPFLSPRKVI------VKGGRIVAMQFvrTEQDETGKWN--EDEDQMVHLKADVVISAF 438
Cdd:PRK12778 605 EEEMPARLEEVKHAKEEGIEFLTLHNPIEYLadekgwVKQVVLQKMEL--GEPDASGRRRpvAIPGSTFTVDVDLVIVSV 682
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119943098 439 GsVLSDPKVKEALSPIKFNRWGLPEVDPEtMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQ 510
Cdd:PRK12778 683 G-VSPNPLVPSSIPGLELNRKGTIVVDEE-MQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
58-506 |
2.22e-63 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 222.73 E-value: 2.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 58 NFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCV 137
Cdd:PRK12810 26 DFKEF-YEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAP--CE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 138 GGCNLyATEEGPINIGGLQQFATEvfKAMSIPQIRnpslppPEKMSEAYSAKIALFGAGPASISCASFLARLGYsDITIF 217
Cdd:PRK12810 103 GACTL-NINFGPVTIKNIERYIID--KAFEEGWVK------PDPPVKRTGKKVAVVGSGPAGLAAADQLARAGH-KVTVF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 218 EKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNeMTLSTLKEKgYKAAFIGIG------LPEPNKD 291
Cdd:PRK12810 173 ERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKD-ITAEELLAE-YDAVFLGTGaykprdLGIPGRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 292 AifqgltqdQGFYTSKDFLP--------------LVAKGSKagmcachsplpsirgvVIVLGAGDTAFDCATSALRCGAR 357
Cdd:PRK12810 251 L--------DGVHFAMDFLIqntrrvlgdetepfISAKGKH----------------VVVIGGGDTGMDCVGTAIRQGAK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 358 RVfIVFrkgfvNIRAVP----------------EEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEqdetgkWNE 421
Cdd:PRK12810 307 SV-TQR-----DIMPMPpsrrnknnpwpywpmkLEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTE------LGE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 422 DEDQMV-----HLKADVVISAFGSVLSDPKVKEALSpIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDG 496
Cdd:PRK12810 375 GDFEPVegsefVLPADLVLLAMGFTGPEAGLLAQFG-VELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEG 453
|
490
....*....|
gi 119943098 497 KQASWYIHKY 506
Cdd:PRK12810 454 RQAARAIDAY 463
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
534-846 |
8.18e-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: 212.41 E-value: 8.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 534 SVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSGPMY-----GPGQSSFL 608
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPRE-GNPPPRVVE-TPGGMLNaiglqNPGVEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 609 NIELIsektaaywcqsvtelKADFPDNIVIASIMCSyNKNDWTELAKKSEDSGADALELNLSCPHgmgERGMGLACGQDP 688
Cdd:cd04740 79 EELLP---------------WLREFGTPVIASIAGS-TVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 689 ELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLmglksdgtpwpAVGIAKRT-----TYG 763
Cdd:cd04740 140 EAVAEIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKGM-----------AIDIETRKpilgnVTG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 764 GVSGTAIRPIALRAVTSIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIEDYCTGLKALL---YL 840
Cdd:cd04740 209 GLSGPAIKPIALRMVYQVYKAV-EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLdeeGI 286
|
....*.
gi 119943098 841 KSIEEL 846
Cdd:cd04740 287 KSIEEL 292
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
532-846 |
3.37e-61 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 210.78 E-value: 3.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSGPM--YG---PGQSS 606
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPRE-GNPTPRIAE-TPGGMLnaIGlqnPGVDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 607 FLNIELISEKtaaywcqsvtelKADFPdniVIASImCSYNKNDWTELAKKSEDSG-ADALELNLSCPHGMGergMGLACG 685
Cdd:PRK07259 79 FIEEELPWLE------------EFDTP---IIANV-AGSTEEEYAEVAEKLSKAPnVDAIELNISCPNVKH---GGMAFG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 686 QDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTvsgLMGLKSDgtpwpavgIAKR-----T 760
Cdd:PRK07259 140 TDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAID--------IKTRkpilaN 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 761 TYGGVSGTAIRPIALRAVTSIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIEDYCTGLKALLY- 839
Cdd:PRK07259 209 VTGGLSGPAIKPIALRMVYQVYQAV-DIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDk 286
|
....*....
gi 119943098 840 --LKSIEEL 846
Cdd:PRK07259 287 ygIKSIEEI 295
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
72-508 |
3.81e-56 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 211.34 E-value: 3.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 72 ALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCnLYATEEGPIN 151
Cdd:PRK12775 326 ALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQC-IIAKKHESVG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 152 IGGLQQFATEVFKAmsipqirNPSLPPpeKMSEAYsAKIALFGAGPASISCASFLARLGySDITIFEKQEYVGGLSTSEI 231
Cdd:PRK12775 405 IGRLERFVGDNARA-------KPVKPP--RFSKKL-GKVAICGSGPAGLAAAADLVKYG-VDVTVYEALHVVGGVLQYGI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 232 PQFRLPYDVVNFEIELMKDLGVKI----ICGKSLSVNEMtlstLKEKGYKAAFIGIGLPEPNkdaiFQGLTQDQG--FYT 305
Cdd:PRK12775 474 PSFRLPRDIIDREVQRLVDIGVKIetnkVIGKTFTVPQL----MNDKGFDAVFLGVGAGAPT----FLGIPGEFAgqVYS 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 306 SKDFLPLVAKGSKAGMCACHSPLpSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKC 385
Cdd:PRK12775 546 ANEFLTRVNLMGGDKFPFLDTPI-SLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGI 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 386 EFLPFLSPRKVI------VKGGRIVAMQFvrTEQDETGKWNE-DEDQMVHLKADVVISAFGSVlSDPKVKEALSPIKFNR 458
Cdd:PRK12775 625 DFFFLHSPVEIYvdaegsVRGMKVEEMEL--GEPDEKGRRKPmPTGEFKDLECDTVIYALGTK-ANPIITQSTPGLALNK 701
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 119943098 459 WGLPEVD----PETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQ 508
Cdd:PRK12775 702 WGNIAADdgklESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYLR 755
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
82-519 |
6.31e-56 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 205.73 E-value: 6.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 82 CAD--APCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCVGGCNLYATEEgPINIGGLQQFA 159
Cdd:PRK12814 97 CGDclGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDE-PVSICALKRYA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 160 TEvfKAMSIPQirnPSLPPPEKMSeaySAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYD 239
Cdd:PRK12814 174 AD--RDMESAE---RYIPERAPKS---GKKVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGMMRYGIPRFRLPES 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 240 VVNFEIELMKDLGVKIICGKSLSvNEMTLSTLKeKGYKAAFIGIGLPEPNKDAIfQGlTQDQGFYTSKDFLPLVAKGSKa 319
Cdd:PRK12814 245 VIDADIAPLRAMGAEFRFNTVFG-RDITLEELQ-KEFDAVLLAVGAQKASKMGI-PG-EELPGVISGIDFLRNVALGTA- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 320 gmcachsplPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVK 399
Cdd:PRK12814 320 ---------LHPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 400 GGRIVaMQFVRTEQ---DETGKWNED--EDQMVHLKADVVISAFGSVLsDPKVKEAlSPIKFNRWGLPEVDPETMQTSEA 474
Cdd:PRK12814 391 EGGLE-LTAIKMQQgepDESGRRRPVpvEGSEFTLQADTVISAIGQQV-DPPIAEA-AGIGTSRNGTVKVDPETLQTSVA 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 119943098 475 WVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQsqyGASVSAKP 519
Cdd:PRK12814 468 GVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLN---GKPVTAPV 509
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
86-506 |
5.96e-54 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 198.18 E-value: 5.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 86 PCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCVGGCNlYATEEGPINIGGLQQFATEVFKA 165
Cdd:PRK12771 48 PCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCN-RGQVDDAVGINAVERFLGDYAIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 166 msipqiRNPSLPPPEKMSeaySAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEI 245
Cdd:PRK12771 125 ------NGWKFPAPAPDT---GKRVAVIGGGPAGLSAAYHLRRMGH-AVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 246 ELMKDLGVKIICGKSLSVNeMTLSTLkEKGYKAAFIGIG------LPEPNKDAifqgltqdQGFYTSKDFLPLVAKGSKa 319
Cdd:PRK12771 195 QRILDLGVEVRLGVRVGED-ITLEQL-EGEFDAVFVAIGaqlgkrLPIPGEDA--------AGVLDAVDFLRAVGEGEP- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 320 gmcachsplPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVK 399
Cdd:PRK12771 264 ---------PFLGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 400 GGRIVAM---QFVRTEQDETGKWNEDEDQMVHLKADVVISAFGSVlSDPKVKEALSPIKFNRwGLPEVDPETMQTSEAWV 476
Cdd:PRK12771 335 ENGATGLrviTVEKMELDEDGRPSPVTGEEETLEADLVVLAIGQD-IDSAGLESVPGVEVGR-GVVQVDPNFMMTGRPGV 412
|
410 420 430
....*....|....*....|....*....|
gi 119943098 477 FAGGDVVGLANTTVESVNDGKQASWYIHKY 506
Cdd:PRK12771 413 FAGGDMVPGPRTVTTAIGHGKKAARNIDAF 442
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
72-510 |
3.09e-52 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 194.22 E-value: 3.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 72 ALREAMRCLKCAdaPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCptSDLCVGGCNLYATEEgPIN 151
Cdd:PRK13984 180 AMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVC--THKCETVCSIGHRGE-PIA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 152 IGGLQQFATEVFKAMSIPQIRNpsLPPPEKmseaySAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEI 231
Cdd:PRK13984 255 IRWLKRYIVDNVPVEKYSEILD--DEPEKK-----NKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGVMRYGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 232 PQFRLPYDVVNFEIELMKDLGVKIICGKSLsVNEMTLSTLKEKgYKAAFIGIGL--------PEPNKDAIFQGLTQdqgF 303
Cdd:PRK13984 327 PSYRLPDEALDKDIAFIEALGVKIHLNTRV-GKDIPLEELREK-HDAVFLSTGFtlgrstriPGTDHPDVIQALPL---L 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 304 YTSKDFLplvaKGSkagmcachSPLPSIRGVVIVLGAGDTAFDCATSALRC-----GARRVFIV-FRKGFVNIRAVPEEM 377
Cdd:PRK13984 402 REIRDYL----RGE--------GPKPKIPRSLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTsLERTFEEMPADMEEI 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 378 ELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQ--DETGKWNE--DEDQMVHLKADVVISAFG-----SVLSDPkVK 448
Cdd:PRK13984 470 EEGLEEGVVIYPGWGPMEVVIENDKVKGVKFKKCVEvfDEEGRFNPkfDESDQIIVEADMVVEAIGqapdySYLPEE-LK 548
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119943098 449 EALspiKFNRwGLPEVDpETMQTSEAWVFAGGDVVGlANTTVESVNDGKQASWYIHKYVQSQ 510
Cdd:PRK13984 549 SKL---EFVR-GRILTN-EYGQTSIPWLFAGGDIVH-GPDIIHGVADGYWAAEGIDMYLRKQ 604
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
533-846 |
2.03e-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: 2.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 533 ISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSG-----PMYGPGQSSF 607
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRP-GYRNPTIVE-TPCGmlnaiGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 608 LNiELISEKTaaywcqsvtelkaDFPDNIvIASIMCSyNKNDWTELAKKSEDSG--ADALELNLSCPHGMGergMGLACG 685
Cdd:TIGR01037 79 LE-ELKPVRE-------------EFPTPL-IASVYGS-SVEEFAEVAEKLEKAPpyVDAYELNLSCPHVKG---GGIAIG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 686 QDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTvsgLMGLKSD---GTPWPAvgiakrTTY 762
Cdd:TIGR01037 140 QDPELSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKIDiktGKPILA------NKT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 763 GGVSGTAIRPIALRAVTSIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFtVIEDYCTGLKALLY--- 839
Cdd:TIGR01037 211 GGLSGPAIKPIALRMVYDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKaeg 288
|
....*..
gi 119943098 840 LKSIEEL 846
Cdd:TIGR01037 289 FTSIEEL 295
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
53-500 |
1.60e-49 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 186.77 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 53 EKLENNFDDIkHTTLGERGALREAMRCLKCAD-APCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCP 131
Cdd:PRK12809 185 SERKTHFGEI-YCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 132 TSDLCVGGCNLyATEEGPINIGGLQQFATEVFKAMS-IPQIRNPSlppPEKmseaysAKIALFGAGPASISCASFLARLG 210
Cdd:PRK12809 264 QDRLCEGACTL-KDHSGAVSIGNLERYITDTALAMGwRPDVSKVV---PRS------EKVAVIGAGPAGLGCADILARAG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 211 YSdITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSvNEMTLSTLKEKgYKAAFIGIG------ 284
Cdd:PRK12809 334 VQ-VDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIG-RDITFSDLTSE-YDAVFIGVGtygmmr 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 285 --LPEPNKDAIFQGLtqdqgfytskdflPLVAKGSKAGMCACHS---PLPSIRGV-VIVLGAGDTAFDCATSALRCGARR 358
Cdd:PRK12809 411 adLPHEDAPGVIQAL-------------PFLTAHTRQLMGLPESeeyPLTDVEGKrVVVLGGGDTTMDCLRTSIRLNAAS 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 359 VFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRTEQDETGKWNEDEDQMV-----HLKAD 432
Cdd:PRK12809 478 VTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACdEDGRLTAVGLIRTAMGEPGPDGRRRPRPVagsefELPAD 557
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119943098 433 VVISAFGSVLSDPKVKEALSpIKFNRWGL---PEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQAS 500
Cdd:PRK12809 558 VLIMAFGFQAHAMPWLQGSG-IKLDKWGLiqtGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAA 627
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
30-500 |
1.54e-45 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 174.94 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 30 STSAKKLDKKHW--KRNPDKNCFNCEKleNNFDDIKHTTLGERgALREAMRCLKCAD-APCQKSCPTNLDIKSFITSIAN 106
Cdd:PRK12769 179 PAMSKVEQMQATppRGEPDKLAIEARK--TGFDEIYLPFRADQ-AQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 107 KNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLyATEEGPINIGGLQQFATEVFKAMSIpqirNPSLPPPEKMSEay 186
Cdd:PRK12769 256 GNIDAAVELSHQTNSLPEITGRVCPQDRLCEGACTL-RDEYGAVTIGNIERYISDQALAKGW----RPDLSQVTKSDK-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 187 saKIALFGAGPASISCASFLARLGYSdITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKII----CGKSLS 262
Cdd:PRK12769 329 --RVAIIGAGPAGLACADVLARNGVA-VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFElnceVGKDIS 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 263 vnemtLSTLKEKgYKAAFIGIGLPE------PNKDAifqgltqdQGFYtskDFLPLVAKGSKAGM---CACHSPLPSIRG 333
Cdd:PRK12769 406 -----LESLLED-YDAVFVGVGTYRsmkaglPNEDA--------PGVY---DALPFLIANTKQVMgleELPEEPFINTAG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 334 V-VIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRT 411
Cdd:PRK12769 469 LnVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELnEQGHVCGIRFLRT 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 412 ---EQDETGKWNED--EDQMVHLKADVVISAFG-SVLSDPKVKEAlsPIKFNRWGLPEVDPET---MQTSEAWVFAGGDV 482
Cdd:PRK12769 549 rlgEPDAQGRRRPVpiPGSEFVMPADAVIMAFGfNPHGMPWLESH--GVTVDKWGRIIADVESqyrYQTSNPKIFAGGDA 626
|
490
....*....|....*...
gi 119943098 483 VGLANTTVESVNDGKQAS 500
Cdd:PRK12769 627 VRGADLVVTAMAEGRHAA 644
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
56-168 |
8.55e-44 |
|
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: 154.23 E-value: 8.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 56 ENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDL 135
Cdd:pfam14691 2 IKNFEEV-ALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 119943098 136 CVGGCNLYATEEGPINIGGLQQFATEVFKAMSI 168
Cdd:pfam14691 81 CEGACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
75-500 |
5.73e-40 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 160.38 E-value: 5.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 75 EAMRCLKCADAPCQ------------KSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCnl 142
Cdd:PRK12779 186 EVMRDKQCDDKPCElgvlvqgkaepkGGCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVC-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 143 yATEEGPINIGGLQQFATEVFKAMSiPQIRNPSLPPPEKMSEAYSAKIALFGAGPASISCASFLARLGYSdITIFEKQEY 222
Cdd:PRK12779 264 -THTKRPIEIGQLEWYLPQHEKLVN-PNANERFAGRISPWAAAVKPPIAVVGSGPSGLINAYLLAVEGFP-VTVFEAFHD 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 223 VGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKI----ICGKSlsvneMTLSTLKEKGYKAAFIGIGLPEPNkdaiFQGLT 298
Cdd:PRK12779 341 LGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFvknfVVGKT-----ATLEDLKAAGFWKIFVGTGAGLPT----FMNVP 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 299 QDQ--GFYTSKDFLPLV--AKGSKAGMcacHSPLPSIRGV-VIVLGAGDTAFDCATSALRCGARrVFIVFRKGFVNIRAV 373
Cdd:PRK12779 412 GEHllGVMSANEFLTRVnlMRGLDDDY---ETPLPEVKGKeVFVIGGGNTAMDAARTAKRLGGN-VTIVYRRTKSEMPAR 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 374 PEEMELAKEEKCEFLPFLSPRKVI-------VKGGRIVAMQFvrTEQDETGKWN-EDEDQMVHLKADVVISAFGSVlSDP 445
Cdd:PRK12779 488 VEELHHALEEGINLAVLRAPREFIgddhthfVTHALLDVNEL--GEPDKSGRRSpKPTGEIERVPVDLVIMALGNT-ANP 564
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 119943098 446 KVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQAS 500
Cdd:PRK12779 565 IMKDAEPGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAA 619
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
534-838 |
1.90e-33 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 130.93 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 534 SVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDiVTNVSPRIIRgTTSGpmygpgqssFLN-IEL 612
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQ-PGNPTPRVFR-LPEG---------VLNrMGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 613 ISEKTAAYWCQSVTELKADFPDNI-VIASImcsyNKN---DWTELAKKSEDSgADALELNLSCPHGMGERgmglACGQDP 688
Cdd:pfam01180 72 NNPGLDAVLAELLKRRKEYPRPDLgINLSK----AGMtvdDYVEVARKIGPF-ADYIELNVSCPNTPGLR----ALQTDP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 689 ELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATN----TVSGlMGLKSDGTPwpavGIAKRTTyGG 764
Cdd:pfam01180 143 ELAAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINatntTVRG-MRIDLKTEK----PILANGT-GG 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119943098 765 VSGTAIRPIALRAVTSIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:pfam01180 217 LSGPPIKPIALKVIRELYQRTgPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
189-510 |
3.07e-33 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 132.04 E-value: 3.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGV------KIICGKSLS 262
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYLACLGY-EVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVvfhtrtKVCCGEPLH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 263 VNE--------MTLSTLKEKgYKAAFIGIGLPEPNKDAIfQGlTQDQGFYTSKDFLpLVAKGSKAGMcACHSPLPSIRG- 333
Cdd:PRK12770 99 EEEgdefveriVSLEELVKK-YDAVLIATGTWKSRKLGI-PG-EDLPGVYSALEYL-FRIRAAKLGY-LPWEKVPPVEGk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 334 VVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIvKGGRIVAMQFVRT-- 411
Cdd:PRK12770 174 KVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRII-GEGRVEGVELAKMrl 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 412 -EQDETGKWNED--EDQMVHLKADVVISAFGSVLSDPKVKEALSpIKFNRWGLPEVDpETMQTSEAWVFAGGDVV----- 483
Cdd:PRK12770 253 gEPDESGRPRPVpiPGSEFVLEADTVVFAIGEIPTPPFAKECLG-IELNRKGEIVVD-EKHMTSREGVFAAGDVVtgpsk 330
|
330 340
....*....|....*....|....*...
gi 119943098 484 -GLAnttvesVNDGKQASWYIHKYVQSQ 510
Cdd:PRK12770 331 iGKA------IKSGLRAAQSIHEWLDLK 352
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
946-1004 |
1.91e-28 |
|
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: 108.52 E-value: 1.91e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 119943098 946 AMIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKM 1004
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDDCITM 59
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
521-819 |
4.78e-22 |
|
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: 98.34 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 521 LPLFYTPIDLvdiSVEMAGLKFINPFGLA-----SATpatstsMIRRAFEAGWGFALTKTfsldkdiVT------NVSPR 589
Cdd:cd04738 30 LLLVYDDPRL---EVEVFGLTFPNPVGLAagfdkNAE------AIDALLALGFGFVEVGT-------VTprpqpgNPKPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 590 IIRGTTSGPM---YGpgqssFLN--IELISEKtaaywcqsvteLKADFPDNIVI-ASImcsyNKNDWTELAKKSED---- 659
Cdd:cd04738 94 LFRLPEDEALinrMG-----FNNdgADAVAKR-----------LKKRRPRGGPLgVNI----GKNKDTPLEDAVEDyvig 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 660 -----SGADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAV-----QIPFFAKLTPNVTD--IVSIARAAKEG 727
Cdd:cd04738 154 vrklgPYADYLVVNVSSPNTPGLRDL-----QGKEALRELLTAVKEERnklgkKVPLLVKIAPDLSDeeLEDIADVALEH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 728 GANGVTATNTVSGLMGLKSDgtpwpavgiAKRTTYGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFL 806
Cdd:cd04738 229 GVDGIIATNTTISRPGLLRS---------PLANETGGLSGAPLKERSTEVLRELYKLTGGkIPIIGVGGISSGEDAYEKI 299
|
330
....*....|...
gi 119943098 807 HSGASVLQVCSAI 819
Cdd:cd04738 300 RAGASLVQLYTGL 312
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
532-852 |
2.21e-19 |
|
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: 90.37 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGfALTkTFSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFLNIE 611
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAG-AIV-LPSLFEEQIEREAQELDRFLTYGSSFAEALSYFPEYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 612 LISEKTAAYWCQsVTELKA--DFPdniVIASIMCSYNkNDWTELAKKSEDSGADALELNLscphgmgergmgLACGQDPE 689
Cdd:cd04739 79 RYNLGPEEYLEL-IRRAKRavSIP---VIASLNGVSA-GGWVDYARQIEEAGADALELNI------------YALPTDPD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 690 LVRN--------ICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVsglmglksdgtPWPAVGIAKRTT 761
Cdd:cd04739 142 ISGAeveqryldILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRF-----------YQPDIDLETLEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 762 YGGVS-------GTAIRPIAlravtsIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGL 834
Cdd:cd04739 211 VPNLLlsspaeiRLPLRWIA------ILSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGL 284
|
330
....*....|....*...
gi 119943098 835 KALLYLKSIEELQDWDGQ 852
Cdd:cd04739 285 EAWMEEHGYESVQQLRGS 302
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
559-817 |
2.79e-19 |
|
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: 87.26 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 559 MIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRgttsgpmygpgqssflnielisektaaywcqsvteLKADFPDNIVI 638
Cdd:cd04722 17 LAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLK-----------------------------------EVAAETDLPLG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 639 ASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGmgergmglacgqdPELVRNICRWVRQAV-QIPFFAKLTPNVTDI 717
Cdd:cd04722 62 VQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL-------------AREDLELIRELREAVpDVKVVVKLSPTGELA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 718 vsiARAAKEGGANGVTATNtvsglmglksdgtpwpavgiakrttYGGVSGTAIRPIALRAVTSIARALPGFPILATGGID 797
Cdd:cd04722 129 ---AAAAEEAGVDEVGLGN-------------------------GGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGIN 180
|
250 260
....*....|....*....|
gi 119943098 798 SAESGLQFLHSGASVLQVCS 817
Cdd:cd04722 181 DPEDAAEALALGADGVIVGS 200
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
532-852 |
3.18e-19 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 90.31 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 532 DISVEMAGLKFINPFgLASATPAT-STSMIRRAFEAGWGFALTKtfSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFlni 610
Cdd:PRK07565 2 DLSTTYLGLTLRNPL-VASASPLSeSVDNVKRLEDAGAGAVVLK--SLFEEQIRHEAAELDRHLTHGTESFAEALDY--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 611 elISEKTAAYW-----CQSVTELKA--DFPdniVIASIMCSYNkNDWTELAKKSEDSGADALELNLSCPHGmgerGMGLA 683
Cdd:PRK07565 76 --FPEPAKFYVgpeeyLELIRRAKEavDIP---VIASLNGSSA-GGWVDYARQIEQAGADALELNIYYLPT----DPDIS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 684 CGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVsglmglksdgtPWPAVGIAKRTTYG 763
Cdd:PRK07565 146 GAEVEQRYLDILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRF-----------YQPDIDLETLEVVP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 764 GV--SGTAIRPIALRAVtSIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLK 841
Cdd:PRK07565 215 GLvlSTPAELRLPLRWI-AILSGRVGADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERH 293
|
330
....*....|.
gi 119943098 842 SIEELQDWDGQ 852
Cdd:PRK07565 294 GYESLQQFRGS 304
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
535-838 |
1.17e-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: 84.68 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 535 VEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKdivtnvspriiRGTTSGPMYGPGQSSFLNIELIS 614
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAG-----------RPGNPEPRYYAFPLGSINSLGLP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 615 EKTAAYWCQSVTElkadfpdnivIASIMCSYNK----------NDWTELAKK---SEDSGADALELNLSCPH--GMGERG 679
Cdd:cd04741 70 NLGLDYYLEYIRT----------ISDGLPGSAKpffisvtgsaEDIAAMYKKiaaHQKQFPLAMELNLSCPNvpGKPPPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 680 MglacgqDPELVRNICRWVRQAVQIPFFAKLTPnVTDIVSIARAAK-----EGGANGVTATNTV-SGLMgLKSDGTpwpA 753
Cdd:cd04741 140 Y------DFDATLEYLTAVKAAYSIPVGVKTPP-YTDPAQFDTLAEalnafACPISFITATNTLgNGLV-LDPERE---T 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 754 VGIAKRTTYGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCT 832
Cdd:cd04741 209 VVLKPKTGFGGLAGAYLHPLALGNVRTFRRLLPSeIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEK 288
|
....*.
gi 119943098 833 GLKALL 838
Cdd:cd04741 289 ELEDIW 294
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
662-838 |
3.60e-17 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 84.06 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 662 ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAVQ-----IPFFAKLTPNVTD--IVSIARAAKEGGANGVTA 734
Cdd:PRK05286 170 ADYFTVNISSPNTPGLRDL-----QYGEALDELLAALKEAQAelhgyVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 735 TNTV---SGLMGLKsdgtpwpavgIAKRTtyGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLHSGA 810
Cdd:PRK05286 245 TNTTlsrDGLKGLP----------NADEA--GGLSGRPLFERSTEVIRRLYKELGGrLPIIGVGGIDSAEDAYEKIRAGA 312
|
170 180
....*....|....*....|....*...
gi 119943098 811 SVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:PRK05286 313 SLVQIYSGLIYEGPGLVKEIVRGLARLL 340
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
515-818 |
1.68e-15 |
|
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: 79.06 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 515 VSAKPELPLFYTPIDLVD-ISVEMAGLKFINPFGLAsATPATSTSMIRRAFEAGWGFALTKTFSlDKDIVTNVSPRIIRG 593
Cdd:TIGR01036 27 GTGTPFLALLRSLFGASDpLEVTVLGLKFPNPLGLA-AGFDKDGEAIDALGAMGFGFLEIGTVT-PKPQPGNPRPRLFRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 594 ttsgpmygPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIAsimcsynKNDWTELAKKSED---------SGADA 664
Cdd:TIGR01036 105 --------IEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIG-------KNKDTPSEDAKEDyaaclrklgPLADY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 665 LELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAVQI-------PFFAKLTPNVT--DIVSIARAAKEGGANGVTAT 735
Cdd:TIGR01036 170 LVVNVSSPNTPGLRDL-----QYKAELRDLLTAVKQEQDGlrrvhrvPVLVKIAPDLTesDLEDIADSLVELGIDGVIAT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 736 NTV---SGLMGLKSDGTPwpavgiakrttyGGVSGtaiRPIALRAVTSIAR---ALPG-FPILATGGIDSAESGLQFLHS 808
Cdd:TIGR01036 245 NTTvsrSLVQGPKNSDET------------GGLSG---KPLQDKSTEIIRRlyaELQGrLPIIGVGGISSAQDALEKIRA 309
|
330
....*....|
gi 119943098 809 GASVLQVCSA 818
Cdd:TIGR01036 310 GASLLQIYSG 319
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
948-1008 |
4.30e-13 |
|
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: 65.46 E-value: 4.30e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119943098 948 IDEEMCINCGKCYMTCNDsgyQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMVSRT 1008
Cdd:COG1144 27 VDEDKCIGCGLCWIVCPD---GAIRVDDGKYYGIDYDYCKGCGICAEVCP-VKAIEMVPEE 83
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
620-852 |
1.27e-12 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 69.98 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 620 YWCQSVTELKADFPDNIVIASIMcSYNKNDWTELAKKSEDSG-ADALELNLSCPHGMGERGMGLacgqDPELVRNICRWV 698
Cdd:PRK02506 78 YYLDYVLELQKKGPNKPHFLSVV-GLSPEETHTILKKIQASDfNGLVELNLSCPNVPGKPQIAY----DFETTEQILEEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 699 RQAVQIPFFAKLTPNVtDIVSIARAA---KEGGANGVTATNTV-SGLMGLKSDGTpwpaVGIAKRTTYGGVSGTAIRPIA 774
Cdd:PRK02506 153 FTYFTKPLGVKLPPYF-DIVHFDQAAaifNKFPLAFVNCINSIgNGLVIDPEDET----VVIKPKNGFGGIGGDYIKPTA 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119943098 775 LRAVTSIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQ 852
Cdd:PRK02506 228 LANVRAFYQRLnPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGK 306
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
945-1009 |
1.44e-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: 60.90 E-value: 1.44e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119943098 945 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMVSRTT 1009
Cdd:COG1149 5 IPVIDEEKCIGCGLCVEVCP---EGAIKLDDGGAPVVDPDLCTGCGACVGVCP-TGAITLEEREA 65
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
189-482 |
9.75e-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: 63.88 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 189 KIALFGAGPASISCASFLARLGYsDITIFEKQE---YVGGLSTSEIPQFRLPYDVVNFEIELMKDL---------GVKII 256
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGG-KVTLIEDEGtcpYGGCVLSKALLGAAEAPEIASLWADLYKRKeevvkklnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 257 CGKS-LSVN----EMTLSTLKEKG-----YKAAFIGIGlPEPNKDAIfQGLTQDQGF----YTSKDFLPLVAKGSKagmc 322
Cdd:pfam07992 81 LGTEvVSIDpgakKVVLEELVDGDgetitYDRLVIATG-ARPRLPPI-PGVELNVGFlvrtLDSAEALRLKLLPKR---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 323 achsplpsirgvVIVLGAGDTAFDCATSALRCGARrVFIVFRKGFVNiRAVPEEMELAKEEKceflpfLSPRKVIVKGGR 402
Cdd:pfam07992 155 ------------VVVVGGGYIGVELAAALAKLGKE-VTLIEALDRLL-RAFDEEISAALEKA------LEKNGVEVRLGT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 403 IVamqfVRTEQDETGKWNEDEDQMVhLKADVVISAFGSVLSDPKVKEAlsPIKFNRWGLPEVDpETMQTSEAWVFAGGDV 482
Cdd:pfam07992 215 SV----KEIIGDGDGVEVILKDGTE-IDADLVVVAIGRRPNTELLEAA--GLELDERGGIVVD-EYLRTSVPGIYAAGDC 286
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
945-1005 |
2.34e-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: 60.20 E-value: 2.34e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119943098 945 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 1005
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACP---VDAIVGAAKAMHTVIADECTGCDLCVEPCP-TDCIEMI 163
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
945-1005 |
1.41e-09 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 58.80 E-value: 1.41e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119943098 945 VAMIDEEMCINCGKCYMTCNdsgYQAIqFDPETHLPT-ITDTCTGCTLCLSVCPiVDCIKMV 1005
Cdd:PRK05113 108 VAFIDEDNCIGCTKCIQACP---VDAI-VGATKAMHTvISDLCTGCDLCVAPCP-TDCIEMI 164
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
945-1017 |
1.95e-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: 59.62 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 945 VAMI-----DEEMCINCGKCYmtcndsgyQAIQFD----PETHLPT-ITDTCTGCTLCLSVCPiVDCIKMVsrttPYEPK 1014
Cdd:COG2878 126 AAVIggpkgCEYGCIGCGDCI--------KACPFDaivgAAKGMHTvDEDKCTGCGLCVEACP-VDCIEMV----PVSPT 192
|
...
gi 119943098 1015 RGV 1017
Cdd:COG2878 193 VVV 195
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
940-1007 |
2.07e-09 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 59.35 E-value: 2.07e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119943098 940 NVEQVVAMIDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTI-TDTCTGCTLCLSVCPiVDCIKMVSR 1007
Cdd:COG1145 171 AIKKAKAVIDAEKCIGCGLCVKVC---PTGAIRLKDGKPQIVVdPDKCIGCGACVKVCP-VGAISLEPK 235
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
945-1008 |
2.32e-09 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 59.42 E-value: 2.32e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119943098 945 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMVSRT 1008
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACP---VDAIVGAPKQMHTVLADLCTGCDLCVPPCP-VDCIDMVPVT 138
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
931-1005 |
2.01e-08 |
|
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: 53.55 E-value: 2.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119943098 931 YLGTFGELSNVEQVVAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 1005
Cdd:cd10549 58 ELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCP---VDAITLEDELEIVIDKEKCIGCGICAEVCP-VNAIKLV 128
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
945-1007 |
2.98e-08 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 51.58 E-value: 2.98e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119943098 945 VAM---IDEEMCINCGKCYMTCNdsgyqAIQFDPETHLPTI-TDTCTGCTLCLSVCPiVDCIKMVSR 1007
Cdd:COG4231 13 TAMryvIDEDKCTGCGACVKVCP-----ADAIEEGDGKAVIdPDLCIGCGSCVQVCP-VDAIKLEKR 73
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
948-1007 |
3.09e-08 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 51.25 E-value: 3.09e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119943098 948 IDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTIT--DTCTGCTLCLSVCPiVDCIKMVSR 1007
Cdd:COG1146 5 IDTDKCIGCGACVEVC---PVDVLELDEEGKKALVInpEECIGCGACELVCP-VGAITVEDD 62
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
651-810 |
5.55e-08 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 55.79 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 651 TELAKKSEDSGADALELNLSCPHGMGERGMGLAC-GQDPELVRNICRWVRQAVQIPFFAKLT----PNVTDIVSIARAAK 725
Cdd:pfam01207 69 AEAAKLVEDRGADGIDINMGCPSKKVTRGGGGAAlLRNPDLVAQIVKAVVKAVGIPVTVKIRigwdDSHENAVEIAKIVE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 726 EGGANGVTatntvsglmglksdgtpwpavgIAKRTTYGGVSGTAirpiALRAVTSIARALPgFPILATGGIDSAESGLQF 805
Cdd:pfam01207 149 DAGAQALT----------------------VHGRTRAQNYEGTA----DWDAIKQVKQAVS-IPVIANGDITDPEDAQRC 201
|
....*.
gi 119943098 806 L-HSGA 810
Cdd:pfam01207 202 LaYTGA 207
|
|
| 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 119943098 194 GAGPASISCASFLARLGYsDITIFEKQEYVGGLSTS-EIPQFRLPY 238
Cdd:pfam13450 3 GAGLAGLVAAALLAKRGF-RVLVLEKRDRLGGNAYSyRVPGYVFDY 47
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
950-1004 |
2.34e-07 |
|
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: 48.59 E-value: 2.34e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 119943098 950 EEMCINCGKCYMTCNdsgYQAIQFDPETHLPTIT---DTCTGCTLCLSVCPiVDCIKM 1004
Cdd:COG1143 1 EDKCIGCGLCVRVCP---VDAITIEDGEPGKVYVidpDKCIGCGLCVEVCP-TGAISM 54
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
654-810 |
2.53e-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: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 654 AKKSEDSGADALELNLSCP-----HGmgerGMGLACGQDPELVRNICRWVRQAVQIPFFAK---LTPNVTDIVSIARAAK 725
Cdd:cd02801 73 AKIVEELGADGIDLNMGCPspkvtKG----GAGAALLKDPELVAEIVRAVREAVPIPVTVKirlGWDDEEETLELAKALE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 726 EGGANGVtatnTVSGlmglksdgtpwpavgiakRTTYGGVSGTA----IRPIalravtsiaRALPGFPILATGGIDSAES 801
Cdd:cd02801 149 DAGASAL----TVHG------------------RTREQRYSGPAdwdyIAEI---------KEAVSIPVIANGDIFSLED 197
|
170
....*....|
gi 119943098 802 GLQFL-HSGA 810
Cdd:cd02801 198 ALRCLeQTGV 207
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
947-1005 |
3.02e-07 |
|
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: 50.27 E-value: 3.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 119943098 947 MIDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 1005
Cdd:cd10550 76 VVDEDKCIGCGMCVEAC---PFGAIRVDPETGKAIKCDLCGGDPACVKVCP-TGALEFV 130
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
926-1004 |
4.53e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 53.71 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 926 GKALQYLGTfGELSnVEQVVAMIDEEMCINCGKCYMTCNdsgYQAIQFDpETHLPTITDT-CTGCTLCLSVCPiVDCIKM 1004
Cdd:COG1148 473 ARAIQLLSK-GELG-VEPSVAEVDPEKCTGCGRCVEVCP---YGAISID-EKGVAEVNPAlCKGCGTCAAACP-SGAISL 545
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
944-1010 |
1.27e-06 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 47.03 E-value: 1.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119943098 944 VVAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLpTITDTCTGCTLCLSVCPiVDCIKMVSRTTP 1010
Cdd:COG2768 4 GKPYVDEEKCIGCGACVKVCP---VGAISIEDGKAV-IDPEKCIGCGACIEVCP-VGAIKIEWEEDE 65
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
953-997 |
1.33e-06 |
|
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: 45.98 E-value: 1.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 119943098 953 CINCGKCYMTCNdsgYQAIQFDPETHLPTIT------DTCTGCTLCLSVCP 997
Cdd:pfam12838 1 CIGCGACVAACP---VGAITLDEVGEKKGTKtvvidpERCVGCGACVAVCP 48
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
943-1003 |
1.69e-06 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 46.58 E-value: 1.69e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119943098 943 QVVAMIDEEMCINCGKCYMTCNDsgyQAIQFDpETHLPTITDTCTGCTLCLSVCPiVDCIK 1003
Cdd:COG2221 7 TWPPKIDEEKCIGCGLCVAVCPT---GAISLD-DGKLVIDEEKCIGCGACIRVCP-TGAIK 62
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
948-997 |
2.02e-06 |
|
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: 45.70 E-value: 2.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 119943098 948 IDEEMCINCGKCYMTC--NDSGYQAIQFDPET-HLPTITDTCTGCTLCLSVCP 997
Cdd:pfam13237 4 IDPDKCIGCGRCTAACpaGLTRVGAIVERLEGeAVRIGVWKCIGCGACVEACP 56
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
533-818 |
2.57e-06 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 50.89 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 533 ISVEMAGLKFINPFGLASATPATStsmirRAFEA----GWGFALTKTfsldkdiVT------NVSPRIIRGTTSGPMYGP 602
Cdd:PLN02826 74 LGVEVWGRTFSNPIGLAAGFDKNA-----EAVEGllglGFGFVEIGS-------VTplpqpgNPKPRVFRLREEGAIINR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 603 GQSSFLNIELISEKTAAY-----------WCQSVTELKADFPDNIVIASIMCSYNKNdwtelakkSEDSG---------- 661
Cdd:PLN02826 142 YGFNSEGIVAVAKRLGAQhgkrkldetssSSFSSDDVKAGGKAGPGILGVNLGKNKT--------SEDAAadyvqgvral 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 662 ---ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVR---------QAVQIPFFAKLTPNVT--DIVSIARAAKEG 727
Cdd:PLN02826 214 sqyADYLVINVSSPNTPGLRKL-----QGRKQLKDLLKKVLaardemqwgEEGPPPLLVKIAPDLSkeDLEDIAAVALAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 728 GANGVTATNTvsglmglkSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFL 806
Cdd:PLN02826 289 GIDGLIISNT--------TISRPDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGkIPLVGCGGVSSGEDAYKKI 360
|
330
....*....|..
gi 119943098 807 HSGASVLQVCSA 818
Cdd:PLN02826 361 RAGASLVQLYTA 372
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
945-1005 |
3.55e-06 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 47.61 E-value: 3.55e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119943098 945 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 1005
Cdd:PRK08764 79 VAWIVEADCIGCTKCIQACP---VDAIVGGAKHMHTVIAPLCTGCELCVPACP-VDCIELH 135
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
652-810 |
4.06e-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: 50.09 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 652 ELAKKSEDSGADALELNLSCP------HGMGergmglAC-GQDPELVRNICRWVRQAVQIPFFAK----LTPNVTDIVSI 720
Cdd:COG0042 78 EAARIAEELGADEIDINMGCPvkkvtkGGAG------AAlLRDPELVAEIVKAVVEAVDVPVTVKirlgWDDDDENALEF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 721 ARAAKEGGANGVtatnTVSGlmglksdgtpwpavgiakRTT---YggvSGTA----IRpiALRAVTSIaralpgfPILAT 793
Cdd:COG0042 152 ARIAEDAGAAAL----TVHG------------------RTReqrY---KGPAdwdaIA--RVKEAVSI-------PVIGN 197
|
170
....*....|....*...
gi 119943098 794 GGIDSAESGLQFL-HSGA 810
Cdd:COG0042 198 GDIFSPEDAKRMLeETGC 215
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
945-1005 |
4.94e-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: 47.00 E-value: 4.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 945 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTItdtCTGC---------TLCLSVCPiVDCIKMV 1005
Cdd:cd04410 74 IVLIDEDKCIGCGSCVEACP---YGAIVFDPEPGKAVK---CDLCgdrldeglePACVKACP-TGALTFG 136
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
947-1011 |
1.17e-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: 45.85 E-value: 1.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119943098 947 MIDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTIT--------DTCTGCTLCLSVCPiVDCIKMVSRTTPY 1011
Cdd:cd10549 36 EIDEDKCVFCGACVEVC---PTGAIELTPEGKEYVPKekeaeideEKCIGCGLCVKVCP-VDAITLEDELEIV 104
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
948-1016 |
1.25e-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: 45.85 E-value: 1.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119943098 948 IDEEMCINCGKCYMTCNdsgYQAIQFDP----ETHLPTITDTCTGCTLCLSVCPiVDCIKMVSRTTPYEPKRG 1016
Cdd:cd10549 3 YDPEKCIGCGICVKACP---TDAIELGPngaiARGPEIDEDKCVFCGACVEVCP-TGAIELTPEGKEYVPKEK 71
|
|
| 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 119943098 194 GAGPASISCASFLARLGYsDITIFEKQEYVGG-LSTSEIPQFRL---PYDVVNFEI--ELMKDLG 252
Cdd:COG1233 10 GAGIGGLAAAALLARAGY-RVTVLEKNDTPGGrARTFERPGFRFdvgPSVLTMPGVleRLFRELG 73
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
945-997 |
2.77e-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: 319895 [Multi-domain] Cd Length: 154 Bit Score: 45.32 E-value: 2.77e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 945 VAMIDEEMCIN------CGKCYMTCNDSGYqAIQFDPETHLPTI-TDTCTGCTLCLSVCP 997
Cdd:cd16373 85 VAVIDKDRCLAwqggtdCGVCVEACPTEAI-AIVLEDDVLRPVVdEDKCVGCGLCEYVCP 143
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
648-852 |
3.34e-05 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 47.27 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 648 NDWTELAKKSEDSGADALELNLSCPHGMGERGM-GLACGQDPELVRNICRWVRQAVQIPFFAKL----TPNVTDIVSIAR 722
Cdd:PRK10415 77 KEMADAARINVESGAQIIDINMGCPAKKVNRKLaGSALLQYPDLVKSILTEVVNAVDVPVTLKIrtgwAPEHRNCVEIAQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 723 AAKEGGANGVTatntvsglmglksdgtpwpavgIAKRTTYGGVSGTA----IRpiALRAVTSIaralpgfPILATGGIDS 798
Cdd:PRK10415 157 LAEDCGIQALT----------------------IHGRTRACLFNGEAeydsIR--AVKQKVSI-------PVIANGDITD 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119943098 799 AESGLQFL-HSGASVLQVCSAIQNQD--FTVIEDYC-TG----------LKALLyLKSIEELQDWDGQ 852
Cdd:PRK10415 206 PLKARAVLdYTGADALMIGRAAQGRPwiFREIQHYLdTGellpplplaeVKRLL-CAHVRELHDFYGP 272
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
949-1005 |
3.65e-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: 44.57 E-value: 3.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 119943098 949 DEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTItdtCTGCTLCLSVCPiVDCIKMV 1005
Cdd:cd16370 81 DKEKCIGCGNCVKACI---VGAIFWDEETNKPII---CIHCGYCARYCP-HDVLAME 130
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
194-510 |
4.24e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 46.65 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 194 GAGPASISCASFLARLGYSdITIFEKQEyVGGlstseipQFRLPYDVVNF-----EI---ELMKDL-------GVKIICG 258
Cdd:COG0492 7 GAGPAGLTAAIYAARAGLK-TLVIEGGE-PGG-------QLATTKEIENYpgfpeGIsgpELAERLreqaerfGAEILLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 259 KslsVNEMTLStlkekgykaafigiglpepnkDAIFQGLTQDQGFYTSKDFLplVAKGSKAGmcacHSPLPSI-----RG 333
Cdd:COG0492 78 E---VTSVDKD---------------------DGPFRVTTDDGTEYEAKAVI--IATGAGPR----KLGLPGEeefegRG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 334 V---------------VIVLGAGDTAFDcatSALRCG--ARRVFIVFRKGfvNIRAVPEEMELAKE-EKCEFLPflspRK 395
Cdd:COG0492 128 VsycatcdgfffrgkdVVVVGGGDSALE---EALYLTkfASKVTLIHRRD--ELRASKILVERLRAnPKIEVLW----NT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 396 VI--VKG-GRIVAMQFVRTEQDETgkwnededqmVHLKADVVISAFGSV-LSDPkVKEAlsPIKFNRWGLPEVDpETMQT 471
Cdd:COG0492 199 EVteIEGdGRVEGVTLKNVKTGEE----------KELEVDGVFVAIGLKpNTEL-LKGL--GLELDEDGYIVVD-EDMET 264
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 119943098 472 SEAWVFAGGDVVG----LANTtveSVNDGKQASWYIHKYVQSQ 510
Cdd:COG0492 265 SVPGVFAAGDVRDykyrQAAT---AAGEGAIAALSAARYLEPL 304
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
944-1005 |
9.79e-05 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 46.17 E-value: 9.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119943098 944 VVAMIDEEMCINCGKCYMTCndsGYQAIQFDpETHLPTITDTCTGCTLCLSVCP-----IVDCIKMV 1005
Cdd:COG4624 84 PSIIRDKEKCKNCYPCVRAC---PVKAIKVD-DGKAEIDEEKCISCGQCVAVCPfgaitEKSDIEKV 146
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
949-1008 |
2.70e-04 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 41.17 E-value: 2.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 949 DEEMCINCGKCYMTCNDSgyqAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMVSRT 1008
Cdd:PRK09624 49 NRDKCVRCYLCYIYCPEP---AIYLDEEGYPVFDYDYCKGCGICANECP-TKAIEMVRET 104
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
961-1007 |
4.02e-04 |
|
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: 41.46 E-value: 4.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 119943098 961 MTCNDS-GYQAIQFDPETH---LPTI-TDTCTGCTLCLSVCPiVDCIKMVSR 1007
Cdd:cd10564 89 RSCQDAcPTQAIRFRPRLGgiaLPELdADACTGCGACVSVCP-VGAITLTPL 139
|
|
| 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 119943098 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSE 230
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTV 43
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
945-1005 |
5.35e-04 |
|
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: 44.00 E-value: 5.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119943098 945 VAMIDEEMCiNCGKCYMTC------NDSGYQAIQFDPETHLPTIT-DTCTGCTLCLSVCPIvDCIKMV 1005
Cdd:COG1245 4 IAVVDRDRC-QPKKCNYECikycpvNRTGKEAIEIDEDDGKPVISeELCIGCGICVKKCPF-DAISIV 69
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
945-998 |
5.95e-04 |
|
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: 42.76 E-value: 5.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 119943098 945 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPeTHLPTITDTCTGCTLCLSVCPI 998
Cdd:cd03110 58 KAFIDQEKCIRCGNCERVCK---FGAILEFF-QKLIVDESLCEGCGACVIICPR 107
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
952-1002 |
7.08e-04 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 38.30 E-value: 7.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 119943098 952 MCINCGKCYMTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCI 1002
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQTIRGDIAGLACIGCGACVDACP-RGAI 50
|
|
| 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 119943098 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSeipqfrlpYDVVNFEIE---------------LMKDLG 252
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGH-EVTVFEADDQLGGLAAS--------FEFGGLPIErfyhhifksdealleLLDELG 70
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
951-997 |
8.19e-04 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 40.50 E-value: 8.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 119943098 951 EMCINCGKCYMTCNDSgyqAIQFDPETHLPTITDTCTGCTLCLSVCP 997
Cdd:PRK09625 59 EICINCFNCWVYCPDA---AILSRDKKLKGVDYSHCKGCGVCVEVCP 102
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
945-997 |
1.00e-03 |
|
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: 319894 [Multi-domain] Cd Length: 125 Bit Score: 40.01 E-value: 1.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 945 VAMIDEEMCINCGKCYMTCNDSGYQ-------AIQFDPETHLPTITdTCTGCTLCLSVCP 997
Cdd:cd16372 2 LLVTDPEKCIGCLQCEEACSKTFFKeedreksCIRITETEGGYAIN-VCNQCGECIDVCP 60
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
947-1010 |
1.32e-03 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 41.09 E-value: 1.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119943098 947 MIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTItdtCTGC---------TLCLSVCPiVDCIKMVSRTTP 1010
Cdd:COG0437 86 LVDYDKCIGCRYCVAACP---YGAPRFNPETGVVEK---CTFCadrldegllPACVEACP-TGALVFGDLDDP 151
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
407-503 |
1.77e-03 |
|
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: 42.00 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 407 QFVRTEQDETGKW--NEDEDQMVHLKADVVISAFGSVlsdPKVK----EALSpIKFNRWGLPEVDpETMQTSEAWVFAGG 480
Cdd:COG1249 231 KVTSVEKTGDGVTvtLEDGGGEEAVEADKVLVATGRR---PNTDglglEAAG-VELDERGGIKVD-EYLRTSVPGIYAIG 305
|
90 100
....*....|....*....|...
gi 119943098 481 DVVGLANTTVESVNDGKQASWYI 503
Cdd:COG1249 306 DVTGGPQLAHVASAEGRVAAENI 328
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
896-1005 |
2.11e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 41.78 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 896 RLKEQNVAFSPLKRNCFIP----KRPIPTIKDVIGkalqylgTFGELsnveqVVAMIDEE------------MCINCGKC 959
Cdd:PRK12771 451 RPKREIVKFDKLNLWYFTDapraQRPELDADERVG-------DFDEV-----LGGLTEEEarqeaarclscgNCFECDNC 518
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 119943098 960 YMTCNDsgyQAIQ-FDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 1005
Cdd:PRK12771 519 YGACPQ---DAIIkLGPGRRYHFDYDKCTGCHICADVCP-CGAIEMG 561
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
983-1013 |
2.87e-03 |
|
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: 37.03 E-value: 2.87e-03
10 20 30
....*....|....*....|....*....|.
gi 119943098 983 TDTCTGCTLCLSVCPiVDCIKMVSRTTPYEP 1013
Cdd:COG1143 1 EDKCIGCGLCVRVCP-VDAITIEDGEPGKVY 30
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
951-1020 |
3.31e-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: 41.22 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119943098 951 EMCINCGKCYMTC---------NDS-------------GYQAIQFDPET--HLptitDTCTGCTLCLSVCPI-VDCIKMV 1005
Cdd:COG0247 78 DACVGCGFCRAMCpsykatgdeKDSprgrinllrevleGELPLDLSEEVyeVL----DLCLTCKACETACPSgVDIADLI 153
|
90
....*....|....*.
gi 119943098 1006 SRTTP-YEPKRGVPLS 1020
Cdd:COG0247 154 AEARAqLVERGGRPLR 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
945-1005 |
3.41e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 3.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119943098 945 VAMIDEEMCiNCGKCYMTC------NDSGYQAIQFDPETHLPTIT-DTCTGCTLCLSVCPIvDCIKMV 1005
Cdd:PRK13409 4 IAVVDYDRC-QPKKCNYECikycpvVRTGEETIEIDEDDGKPVISeELCIGCGICVKKCPF-DAISIV 69
|
|
| 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 119943098 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLS 227
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGIS 43
|
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
945-1005 |
4.56e-03 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 37.62 E-value: 4.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119943098 945 VAMIDEEMCINCGKCYMTCNDSgyqAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 1005
Cdd:PRK09623 45 MPVVDESKCVKCYICWKFCPEP---AIYIKEDGYVAIDYDYCKGCGICANECP-TKAITMV 101
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
982-1015 |
6.08e-03 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 36.23 E-value: 6.08e-03
10 20 30
....*....|....*....|....*....|....
gi 119943098 982 ITDTCTGCTLCLSVCPiVDCIKMVSRTTPYEPKR 1015
Cdd:COG1146 6 DTDKCIGCGACVEVCP-VDVLELDEEGKKALVIN 38
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
948-1007 |
6.09e-03 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 39.66 E-value: 6.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119943098 948 IDEEMCINCGKCYMTCndsgyqaiqfdpETHLP-----TITDTCTGCTLCLSVCPiVDCIKMVSR 1007
Cdd:COG0348 207 YDRGDCIDCGLCVKVC------------PMGIDirkgeINQSECINCGRCIDACP-KDAIRFSSR 258
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
981-1005 |
7.49e-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: 39.46 E-value: 7.49e-03
10 20
....*....|....*....|....*
gi 119943098 981 TITDTCTGCTLCLSVCPiVDCIKMV 1005
Cdd:NF038196 182 HVTDKCIGCGICAKVCP-VNNIEME 205
|
|
| |
