|
Name |
Accession |
Description |
Interval |
E-value |
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
509-762 |
7.38e-154 |
|
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: 455.59 E-value: 7.38e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 509 DIVTNVSPRIIRGTTSGPmygpGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDS 588
Cdd:cd02940 50 DIVTNVSPRIARLRTSGR----GQIGFNNIELISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 589 GADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSG 668
Cdd:cd02940 126 GADALELNFSCPHGMPERGMGAAVGQDPELVEEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 669 LMGLKSDGTPwPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAI 747
Cdd:cd02940 206 LMGVDLDGTP-PAPGVEGKTTYGGYSGPAVKPIALRAVSQIARAPePGLPISGIGGIESWEDAAEFLLLGASVVQVCTAV 284
|
250
....*....|....*
gi 578798494 748 QNQDFTVIEDYCTGL 762
Cdd:cd02940 285 MNQGFTIVDDMCTGL 299
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
53-508 |
1.58e-118 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 369.89 E-value: 1.58e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 53 EKLENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPT 132
Cdd:PRK11749 17 EERAQNFDEV-APGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 133 SDLCVGGCNLYATEEgPINIGGLQQFATEvfKAMSIPQIRNPSLPPPEKmseaysaKIALFGAGPASISCASFLARLGYs 212
Cdd:PRK11749 96 ERLCEGACVRGKKGE-PVAIGRLERYITD--WAMETGWVLFKRAPKTGK-------KVAVIGAGPAGLTAAHRLARKGY- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 213 DITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNeMTLSTLKEkGYKAAFIGIGLPEPNKDA 292
Cdd:PRK11749 165 DVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRD-ITLDELRA-GYDAVFIGTGAGLPRFLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 293 IF-QGLtqdQGFYTSKDFLPLVAKGSKAgmcachSPLPSIRGVViVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIR 371
Cdd:PRK11749 243 IPgENL---GGVYSAVDFLTRVNQAVAD------YDLPVGKRVV-VIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 372 AVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTE---QDETGKWNE-DEDQMVHLKADVVISAFGSVlSDPKV 447
Cdd:PRK11749 313 ASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMElgePDASGRRRVpIEGSEFTLPADLVIKAIGQT-PNPLI 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578798494 448 KEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQ 508
Cdd:PRK11749 392 LSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLE 452
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
57-506 |
4.16e-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: 365.23 E-value: 4.16e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 57 NNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTsdLC 136
Cdd:COG0493 3 KDFREV-YPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--PC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 137 VGGCNLyATEEGPINIGGLQQFATEvfKAMSIPQIRNPSLPPP-EKmseaysaKIALFGAGPASISCASFLARLGYsDIT 215
Cdd:COG0493 80 EGACVR-GIVDEPVAIGALERFIAD--KAFEEGWVKPPPPAPRtGK-------KVAVVGSGPAGLAAAYQLARAGH-EVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 216 IFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNeMTLSTLKEKgYKAAFIGIG------LPEPN 289
Cdd:COG0493 149 VFEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKD-ITLDELLEE-FDAVFLATGagkprdLGIPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 290 KDAifqgltqdQGFYTSKDFLPLVAKgskagMCACHSPLPsIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVN 369
Cdd:COG0493 227 EDL--------KGVHSAMDFLTAVNL-----GEAPDTILA-VGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 370 IRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRTE---QDETGKWN--EDEDQMVHLKADVVISAFGSVLS 443
Cdd:COG0493 293 MPASKEEVEEALEEGVEFLFLVAPVEIIGdENGRVTGLECVRMElgePDESGRRRpvPIEGSEFTLPADLVILAIGQTPD 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578798494 444 DPKVKEALSpIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKY 506
Cdd:COG0493 373 PSGLEEELG-LELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
510-935 |
9.70e-104 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 329.60 E-value: 9.70e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 510 IVTNVSPRIirgttsGPMYGPGQS--SFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSED 587
Cdd:PRK08318 51 IVNVSSPRF------GALVKEDRRfiGFNNIELITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 588 SGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVS 667
Cdd:PRK08318 125 TGADGIELNFGCPHGMSERGMGSAVGQVPELVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTIN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 668 GLMGLKSDG-TPWPAVGiaKRTTYGGVSGTAIRPIALRAVTSIAR--ALPGFPILATGGIDSAESGLQFLHSGASVLQVC 744
Cdd:PRK08318 205 SITGVDLDRmIPMPIVN--GKSSHGGYCGPAVKPIALNMVAEIARdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVC 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 745 SAIQNQDFTVIEDYCTGlkallylksieeLQDWdgqspatvshqkgkpvpriaelMDKKlpsfgpyleqrkkiiaenkir 824
Cdd:PRK08318 283 TAAMQYGFRIVEDMISG------------LSHY----------------------MDEK--------------------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 825 lkeqnvafsplkrncfipkrPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCYMTCNDSGYQAIQFDPE 904
Cdd:PRK08318 308 --------------------GFASLEDMVGLAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDED 367
|
410 420 430
....*....|....*....|....*....|...
gi 578798494 905 T--HLPTITDTCTGCTLCLSVCPIVDCIKMVSR 935
Cdd:PRK08318 368 GtrTPEVIEEECVGCNLCAHVCPVEGCITMGEV 400
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
58-508 |
1.55e-84 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 279.98 E-value: 1.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 58 NFDDIkhtTLG--ERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDL 135
Cdd:PRK12831 22 NFEEV---CLGynEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 136 CVGGCNLYATEEgPINIGGLQQFATEVFKAMSIPQIrnpslPPPEKMSEaysaKIALFGAGPASISCASFLARLGYsDIT 215
Cdd:PRK12831 99 CEGKCVLGIKGE-PVAIGKLERFVADWARENGIDLS-----ETEEKKGK----KVAVIGSGPAGLTCAGDLAKMGY-DVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 216 IFEKQEYVGGLSTSEIPQFRLPYD-VVNFEIELMKDLGVKI----ICGKSLSVNEMtlstLKEKGYKAAFIGI--GLPEp 288
Cdd:PRK12831 168 IFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIetnvVVGKTVTIDEL----LEEEGFDAVFIGSgaGLPK- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 289 nkdaiFQGL--TQDQGFYTSKDFLPLVAKGsKAGMCACHSPLPSIRGVVIVlGAGDTAFDCATSALRCGArRVFIVFRKG 366
Cdd:PRK12831 243 -----FMGIpgENLNGVFSANEFLTRVNLM-KAYKPEYDTPIKVGKKVAVV-GGGNVAMDAARTALRLGA-EVHIVYRRS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 367 FVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRT---EQDETGKWN--EDEDQMVHLKADVVISAFGS 440
Cdd:PRK12831 315 EEELPARVEEVHHAKEEGVIFDLLTNPVEILGdENGWVKGMKCIKMelgEPDASGRRRpvEIEGSEFVLEVDTVIMSLGT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578798494 441 VlSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQ 508
Cdd:PRK12831 395 S-PNPLISSTTKGLKINKRGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLS 461
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
508-761 |
4.87e-82 |
|
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: 266.91 E-value: 4.87e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 508 QDIVTNVSPRIIRGTTSGPmYGPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSyNKNDWTELAKKSED 587
Cdd:cd02810 45 HPRPGNPLPRVARLPPEGE-SYPEQLGILNSFGLPNLGLDVWLQDIAKAKKEFPGQPLIASVGGS-SKEDYVELARKIER 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 588 SGADALELNLSCPHGMGERGmglaCGQDPELVRNICRWVRQAVQIPFFAKLTPNVT--DIVSIARAAKEGGANGVTATNT 665
Cdd:cd02810 123 AGAKALELNLSCPNVGGGRQ----LGQDPEAVANLLKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 666 VSGLMGLKsdgtpwPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALP-GFPILATGGIDSAESGLQFLHSGASVLQVC 744
Cdd:cd02810 199 ISGRVVDL------KTVGPGPKRGTGGLSGAPIRPLALRWVARLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVA 272
|
250
....*....|....*..
gi 578798494 745 SAIQNQDFTVIEDYCTG 761
Cdd:cd02810 273 TALMWDGPDVIRKIKKE 289
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
57-508 |
7.19e-78 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 269.69 E-value: 7.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 57 NNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLC 136
Cdd:PRK12778 310 NRFEEV-NLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQC 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 137 VGGCNLYATEEGPINIGGLQQFATEVFKamsipQIRNPSLPppeKMSEAYSAKIALFGAGPASISCASFLARLGYsDITI 216
Cdd:PRK12778 389 ESKCIHGKMGEEAVAIGYLERFVADYER-----ESGNISVP---EVAEKNGKKVAVIGSGPAGLSFAGDLAKRGY-DVTV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 217 FEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKI----ICGKSLSVNEMtlstlKEKGYKAAFIGIGLPEPNkda 292
Cdd:PRK12778 460 FEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFetdvIVGKTITIEEL-----EEEGFKGIFIASGAGLPN--- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 293 iFQGLTQDQ--GFYTSKDFLplvakgSKAGMCACHSPL---PSIRG-VVIVLGAGDTAFDCATSALRCGARRVFIVFRKG 366
Cdd:PRK12778 532 -FMNIPGENsnGVMSSNEYL------TRVNLMDAASPDsdtPIKFGkKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRS 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 367 FVNIRAVPEEMELAKEEKCEFLPFLSPRKVI------VKGGRIVAMQFvrTEQDETGKWN--EDEDQMVHLKADVVISAF 438
Cdd:PRK12778 605 EEEMPARLEEVKHAKEEGIEFLTLHNPIEYLadekgwVKQVVLQKMEL--GEPDASGRRRpvAIPGSTFTVDVDLVIVSV 682
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 439 GsVLSDPKVKEALSPIKFNRWGLPEVDPEtMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQ 508
Cdd:PRK12778 683 G-VSPNPLVPSSIPGLELNRKGTIVVDEE-MQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLS 750
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
513-766 |
1.02e-65 |
|
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: 222.64 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 513 NVSPRIIRgtTsgpmygPGQSSFLNIELISEKTAAYWCQSVTELKAdfPDNIVIASIMCSyNKNDWTELAKKSEDSGADA 592
Cdd:COG0167 53 NPRPRLFR--L------PEDSGLINRMGLNNPGVDAFLERLLPAKR--YDVPVIVNIGGN-TVEDYVELARRLADAGADY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 593 LELNLSCPHGmgeRGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLmgl 672
Cdd:COG0167 122 LELNISCPNT---PGGGRALGQDPEALAELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGR--- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 673 ksdgtpwpAVGIAKRT-----TYGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSA 746
Cdd:COG0167 196 --------AIDLETRRpvlanEAGGLSGPALKPIALRMVREVAQAVGGdIPIIGVGGISTAEDALEFILAGASAVQVGTA 267
|
250 260
....*....|....*....|
gi 578798494 747 IQNQDFTVIEDYCTGLKALL 766
Cdd:COG0167 268 LFYEGPGLVRRIIRGLEAYL 287
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
511-781 |
1.61e-64 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 222.41 E-value: 1.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 511 VTNVSPRIIR------GTTSGPMYGpgqssFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKK 584
Cdd:PLN02495 61 VINVTPRYARlraganGSAKGRVIG-----WQNIELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIER 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 585 SEDSGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATN 664
Cdd:PLN02495 136 VEETGVDALEINFSCPHGMPERKMGAAVGQDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAIN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 665 TVSGLMGLKSDgTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPG-FP----ILATGGIDSAESGLQFLHSGAS 739
Cdd:PLN02495 216 TIMSVMGINLD-TLRPEPCVEGYSTPGGYSSKAVRPIALAKVMAIAKMMKSeFPedrsLSGIGGVETGGDAAEFILLGAD 294
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 578798494 740 VLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQS 781
Cdd:PLN02495 295 TVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSSIEDFRGAS 336
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
58-506 |
1.29e-63 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 222.73 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 58 NFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCV 137
Cdd:PRK12810 26 DFKEF-YEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAP--CE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 138 GGCNLyATEEGPINIGGLQQFATEvfKAMSIPQIRnpslppPEKMSEAYSAKIALFGAGPASISCASFLARLGYsDITIF 217
Cdd:PRK12810 103 GACTL-NINFGPVTIKNIERYIID--KAFEEGWVK------PDPPVKRTGKKVAVVGSGPAGLAAADQLARAGH-KVTVF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 218 EKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNeMTLSTLKEKgYKAAFIGIG------LPEPNKD 291
Cdd:PRK12810 173 ERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKD-ITAEELLAE-YDAVFLGTGaykprdLGIPGRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 292 AifqgltqdQGFYTSKDFLP--------------LVAKGSKagmcachsplpsirgvVIVLGAGDTAFDCATSALRCGAR 357
Cdd:PRK12810 251 L--------DGVHFAMDFLIqntrrvlgdetepfISAKGKH----------------VVVIGGGDTGMDCVGTAIRQGAK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 358 RVfIVFrkgfvNIRAVP----------------EEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEqdetgkWNE 421
Cdd:PRK12810 307 SV-TQR-----DIMPMPpsrrnknnpwpywpmkLEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTE------LGE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 422 DEDQMV-----HLKADVVISAFGSVLSDPKVKEALSpIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDG 496
Cdd:PRK12810 375 GDFEPVegsefVLPADLVLLAMGFTGPEAGLLAQFG-VELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEG 453
|
490
....*....|
gi 578798494 497 KQASWYIHKY 506
Cdd:PRK12810 454 RQAARAIDAY 463
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
82-530 |
1.90e-56 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 206.89 E-value: 1.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 82 CAD--APCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCVGGCNLYATEEgPINIGGLQQFA 159
Cdd:PRK12814 97 CGDclGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDE-PVSICALKRYA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 160 TEvfKAMSIPQirnPSLPPPEKMSeaySAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYD 239
Cdd:PRK12814 174 AD--RDMESAE---RYIPERAPKS---GKKVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGMMRYGIPRFRLPES 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 240 VVNFEIELMKDLGVKIICGKSLSvNEMTLSTLKeKGYKAAFIGIGLPEPNKDAIfQGlTQDQGFYTSKDFLPLVAKGSKa 319
Cdd:PRK12814 245 VIDADIAPLRAMGAEFRFNTVFG-RDITLEELQ-KEFDAVLLAVGAQKASKMGI-PG-EELPGVISGIDFLRNVALGTA- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 320 gmcachsplPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVK 399
Cdd:PRK12814 320 ---------LHPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 400 GGRIVaMQFVRTEQ---DETGKWNED--EDQMVHLKADVVISAFGSVLsDPKVKEAlSPIKFNRWGLPEVDPETMQTSEA 474
Cdd:PRK12814 391 EGGLE-LTAIKMQQgepDESGRRRPVpvEGSEFTLQADTVISAIGQQV-DPPIAEA-AGIGTSRNGTVKVDPETLQTSVA 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 578798494 475 WVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQDIVTNVSPRIIRGTtsgpmYGP 530
Cdd:PRK12814 468 GVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGKPVTAPVQPFNSS-----YGP 518
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
72-508 |
2.34e-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: 2.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 72 ALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCnLYATEEGPIN 151
Cdd:PRK12775 326 ALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQC-IIAKKHESVG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 152 IGGLQQFATEVFKAmsipqirNPSLPPpeKMSEAYsAKIALFGAGPASISCASFLARLGySDITIFEKQEYVGGLSTSEI 231
Cdd:PRK12775 405 IGRLERFVGDNARA-------KPVKPP--RFSKKL-GKVAICGSGPAGLAAAADLVKYG-VDVTVYEALHVVGGVLQYGI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 232 PQFRLPYDVVNFEIELMKDLGVKI----ICGKSLSVNEMtlstLKEKGYKAAFIGIGLPEPNkdaiFQGLTQDQG--FYT 305
Cdd:PRK12775 474 PSFRLPRDIIDREVQRLVDIGVKIetnkVIGKTFTVPQL----MNDKGFDAVFLGVGAGAPT----FLGIPGEFAgqVYS 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 306 SKDFLPLVAKGSKAGMCACHSPLpSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKC 385
Cdd:PRK12775 546 ANEFLTRVNLMGGDKFPFLDTPI-SLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGI 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 386 EFLPFLSPRKVI------VKGGRIVAMQFvrTEQDETGKWNE-DEDQMVHLKADVVISAFGSVlSDPKVKEALSPIKFNR 458
Cdd:PRK12775 625 DFFFLHSPVEIYvdaegsVRGMKVEEMEL--GEPDEKGRRKPmPTGEFKDLECDTVIYALGTK-ANPIITQSTPGLALNK 701
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 578798494 459 WGLPEVD----PETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQ 508
Cdd:PRK12775 702 WGNIAADdgklESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYLR 755
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
559-774 |
2.02e-55 |
|
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: 193.92 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 559 DFPDNIVIASIMCSyNKNDWTELAKKSEDSGADALELNLSCPHgmgERGMGLACGQDPELVRNICRWVRQAVQIPFFAKL 638
Cdd:cd04740 86 REFGTPVIASIAGS-TVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDPEAVAEIVKAVKKATDVPVIVKL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 639 TPNVTDIVSIARAAKEGGANGVTATNTVSGLmglksdgtpwpAVGIAKRT-----TYGGVSGTAIRPIALRAVTSIARAL 713
Cdd:cd04740 162 TPNVTDIVEIARAAEEAGADGLTLINTLKGM-----------AIDIETRKpilgnVTGGLSGPAIKPIALRMVYQVYKAV 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578798494 714 pGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIEDYCTGLKALL---YLKSIEEL 774
Cdd:cd04740 231 -EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLdeeGIKSIEEL 292
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
557-774 |
1.07e-54 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 192.29 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 557 KADFPdniVIASImCSYNKNDWTELAKKSEDSG-ADALELNLSCPHGMGergMGLACGQDPELVRNICRWVRQAVQIPFF 635
Cdd:PRK07259 89 EFDTP---IIANV-AGSTEEEYAEVAEKLSKAPnVDAIELNISCPNVKH---GGMAFGTDPELAYEVVKAVKEVVKVPVI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 636 AKLTPNVTDIVSIARAAKEGGANGVTATNTvsgLMGLKSDgtpwpavgIAKR-----TTYGGVSGTAIRPIALRAVTSIA 710
Cdd:PRK07259 162 VKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAID--------IKTRkpilaNVTGGLSGPAIKPIALRMVYQVY 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578798494 711 RALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIEDYCTGLKALLY---LKSIEEL 774
Cdd:PRK07259 231 QAV-DIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDkygIKSIEEI 295
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
86-506 |
8.53e-54 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 197.40 E-value: 8.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 86 PCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCVGGCNlYATEEGPINIGGLQQFATEVFKA 165
Cdd:PRK12771 48 PCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCN-RGQVDDAVGINAVERFLGDYAIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 166 msipqiRNPSLPPPEKMSeaySAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEI 245
Cdd:PRK12771 125 ------NGWKFPAPAPDT---GKRVAVIGGGPAGLSAAYHLRRMGH-AVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 246 ELMKDLGVKIICGKSLSVNeMTLSTLkEKGYKAAFIGIG------LPEPNKDAifqgltqdQGFYTSKDFLPLVAKGSKa 319
Cdd:PRK12771 195 QRILDLGVEVRLGVRVGED-ITLEQL-EGEFDAVFVAIGaqlgkrLPIPGEDA--------AGVLDAVDFLRAVGEGEP- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 320 gmcachsplPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVK 399
Cdd:PRK12771 264 ---------PFLGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 400 GGRIVAM---QFVRTEQDETGKWNEDEDQMVHLKADVVISAFGSVlSDPKVKEALSPIKFNRwGLPEVDPETMQTSEAWV 476
Cdd:PRK12771 335 ENGATGLrviTVEKMELDEDGRPSPVTGEEETLEADLVVLAIGQD-IDSAGLESVPGVEVGR-GVVQVDPNFMMTGRPGV 412
|
410 420 430
....*....|....*....|....*....|
gi 578798494 477 FAGGDVVGLANTTVESVNDGKQASWYIHKY 506
Cdd:PRK12771 413 FAGGDMVPGPRTVTTAIGHGKKAARNIDAF 442
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
72-507 |
1.89e-51 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 191.52 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 72 ALREAMRCLKCAdaPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCptSDLCVGGCNLYATEEgPIN 151
Cdd:PRK13984 180 AMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVC--THKCETVCSIGHRGE-PIA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 152 IGGLQQFATEVFKAMSIPQIRNpsLPPPEKmseaySAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEI 231
Cdd:PRK13984 255 IRWLKRYIVDNVPVEKYSEILD--DEPEKK-----NKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGVMRYGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 232 PQFRLPYDVVNFEIELMKDLGVKIICGKSLsVNEMTLSTLKEKgYKAAFIGIGL--------PEPNKDAIFQGLTQdqgF 303
Cdd:PRK13984 327 PSYRLPDEALDKDIAFIEALGVKIHLNTRV-GKDIPLEELREK-HDAVFLSTGFtlgrstriPGTDHPDVIQALPL---L 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 304 YTSKDFLplvaKGSkagmcachSPLPSIRGVVIVLGAGDTAFDCATSALRC-----GARRVFIV-FRKGFVNIRAVPEEM 377
Cdd:PRK13984 402 REIRDYL----RGE--------GPKPKIPRSLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTsLERTFEEMPADMEEI 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 378 ELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQ--DETGKWNE--DEDQMVHLKADVVISAFG-----SVLSDPkVK 448
Cdd:PRK13984 470 EEGLEEGVVIYPGWGPMEVVIENDKVKGVKFKKCVEvfDEEGRFNPkfDESDQIIVEADMVVEAIGqapdySYLPEE-LK 548
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 578798494 449 EALspiKFNRwGLPEVDpETMQTSEAWVFAGGDVVGlANTTVESVNDGKQASWYIHKYV 507
Cdd:PRK13984 549 SKL---EFVR-GRILTN-EYGQTSIPWLFAGGDIVH-GPDIIHGVADGYWAAEGIDMYL 601
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
53-500 |
2.51e-49 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 186.00 E-value: 2.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 53 EKLENNFDDIkHTTLGERGALREAMRCLKCAD-APCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCP 131
Cdd:PRK12809 185 SERKTHFGEI-YCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 132 TSDLCVGGCNLyATEEGPINIGGLQQFATEVFKAMS-IPQIRNPSlppPEKmseaysAKIALFGAGPASISCASFLARLG 210
Cdd:PRK12809 264 QDRLCEGACTL-KDHSGAVSIGNLERYITDTALAMGwRPDVSKVV---PRS------EKVAVIGAGPAGLGCADILARAG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 211 YSdITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSvNEMTLSTLKEKgYKAAFIGIG------ 284
Cdd:PRK12809 334 VQ-VDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIG-RDITFSDLTSE-YDAVFIGVGtygmmr 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 285 --LPEPNKDAIFQGLtqdqgfytskdflPLVAKGSKAGMCACHS---PLPSIRGV-VIVLGAGDTAFDCATSALRCGARR 358
Cdd:PRK12809 411 adLPHEDAPGVIQAL-------------PFLTAHTRQLMGLPESeeyPLTDVEGKrVVVLGGGDTTMDCLRTSIRLNAAS 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 359 VFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRTEQDETGKWNEDEDQMV-----HLKAD 432
Cdd:PRK12809 478 VTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACdEDGRLTAVGLIRTAMGEPGPDGRRRPRPVagsefELPAD 557
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578798494 433 VVISAFGSVLSDPKVKEALSpIKFNRWGL---PEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQAS 500
Cdd:PRK12809 558 VLIMAFGFQAHAMPWLQGSG-IKLDKWGLiqtGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAA 627
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
30-500 |
2.40e-45 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 174.16 E-value: 2.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 30 STSAKKLDKKHW--KRNPDKNCFNCEKleNNFDDIKHTTLGERgALREAMRCLKCAD-APCQKSCPTNLDIKSFITSIAN 106
Cdd:PRK12769 179 PAMSKVEQMQATppRGEPDKLAIEARK--TGFDEIYLPFRADQ-AQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 107 KNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLyATEEGPINIGGLQQFATEVFKAMSIpqirNPSLPPPEKMSEay 186
Cdd:PRK12769 256 GNIDAAVELSHQTNSLPEITGRVCPQDRLCEGACTL-RDEYGAVTIGNIERYISDQALAKGW----RPDLSQVTKSDK-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 187 saKIALFGAGPASISCASFLARLGYSdITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKII----CGKSLS 262
Cdd:PRK12769 329 --RVAIIGAGPAGLACADVLARNGVA-VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFElnceVGKDIS 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 263 vnemtLSTLKEKgYKAAFIGIGLPE------PNKDAifqgltqdQGFYtskDFLPLVAKGSKAGM---CACHSPLPSIRG 333
Cdd:PRK12769 406 -----LESLLED-YDAVFVGVGTYRsmkaglPNEDA--------PGVY---DALPFLIANTKQVMgleELPEEPFINTAG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 334 V-VIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRT 411
Cdd:PRK12769 469 LnVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELnEQGHVCGIRFLRT 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 412 ---EQDETGKWNED--EDQMVHLKADVVISAFG-SVLSDPKVKEAlsPIKFNRWGLPEVDPET---MQTSEAWVFAGGDV 482
Cdd:PRK12769 549 rlgEPDAQGRRRPVpiPGSEFVMPADAVIMAFGfNPHGMPWLESH--GVTVDKWGRIIADVESqyrYQTSNPKIFAGGDA 626
|
490
....*....|....*...
gi 578798494 483 VGLANTTVESVNDGKQAS 500
Cdd:PRK12769 627 VRGADLVVTAMAEGRHAA 644
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
559-774 |
5.09e-45 |
|
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: 164.52 E-value: 5.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 559 DFPDNIvIASIMCSyNKNDWTELAKKSEDSG--ADALELNLSCPHGMGergMGLACGQDPELVRNICRWVRQAVQIPFFA 636
Cdd:TIGR01037 88 EFPTPL-IASVYGS-SVEEFAEVAEKLEKAPpyVDAYELNLSCPHVKG---GGIAIGQDPELSADVVKAVKDKTDVPVFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 637 KLTPNVTDIVSIARAAKEGGANGVTATNTvsgLMGLKSD---GTPWPAvgiakrTTYGGVSGTAIRPIALRAVTSIARAL 713
Cdd:TIGR01037 163 KLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKIDiktGKPILA------NKTGGLSGPAIKPIALRMVYDVYKMV 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578798494 714 pGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFtVIEDYCTGLKALLY---LKSIEEL 774
Cdd:TIGR01037 234 -DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKaegFTSIEEL 295
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
56-168 |
1.87e-43 |
|
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: 153.08 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 56 ENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDL 135
Cdd:pfam14691 2 IKNFEEV-ALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 578798494 136 CVGGCNLYATEEGPINIGGLQQFATEVFKAMSI 168
Cdd:pfam14691 81 CEGACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
75-500 |
4.56e-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: 4.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 75 EAMRCLKCADAPCQ------------KSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCnl 142
Cdd:PRK12779 186 EVMRDKQCDDKPCElgvlvqgkaepkGGCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVC-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 143 yATEEGPINIGGLQQFATEVFKAMSiPQIRNPSLPPPEKMSEAYSAKIALFGAGPASISCASFLARLGYSdITIFEKQEY 222
Cdd:PRK12779 264 -THTKRPIEIGQLEWYLPQHEKLVN-PNANERFAGRISPWAAAVKPPIAVVGSGPSGLINAYLLAVEGFP-VTVFEAFHD 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 223 VGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKI----ICGKSlsvneMTLSTLKEKGYKAAFIGIGLPEPNkdaiFQGLT 298
Cdd:PRK12779 341 LGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFvknfVVGKT-----ATLEDLKAAGFWKIFVGTGAGLPT----FMNVP 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 299 QDQ--GFYTSKDFLPLV--AKGSKAGMcacHSPLPSIRGV-VIVLGAGDTAFDCATSALRCGARrVFIVFRKGFVNIRAV 373
Cdd:PRK12779 412 GEHllGVMSANEFLTRVnlMRGLDDDY---ETPLPEVKGKeVFVIGGGNTAMDAARTAKRLGGN-VTIVYRRTKSEMPAR 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 374 PEEMELAKEEKCEFLPFLSPRKVI-------VKGGRIVAMQFvrTEQDETGKWN-EDEDQMVHLKADVVISAFGSVlSDP 445
Cdd:PRK12779 488 VEELHHALEEGINLAVLRAPREFIgddhthfVTHALLDVNEL--GEPDKSGRRSpKPTGEIERVPVDLVIMALGNT-ANP 564
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 578798494 446 KVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQAS 500
Cdd:PRK12779 565 IMKDAEPGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAA 619
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
189-506 |
6.50e-33 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 130.88 E-value: 6.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGV------KIICGKSLS 262
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYLACLGY-EVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVvfhtrtKVCCGEPLH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 263 VNE--------MTLSTLKEKgYKAAFIGIGLPEPNKDAIfQGlTQDQGFYTSKDFLpLVAKGSKAGMcACHSPLPSIRG- 333
Cdd:PRK12770 99 EEEgdefveriVSLEELVKK-YDAVLIATGTWKSRKLGI-PG-EDLPGVYSALEYL-FRIRAAKLGY-LPWEKVPPVEGk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 334 VVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIvKGGRIVAMQFVRT-- 411
Cdd:PRK12770 174 KVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRII-GEGRVEGVELAKMrl 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 412 -EQDETGKWNED--EDQMVHLKADVVISAFGSVLSDPKVKEALSpIKFNRWGLPEVDpETMQTSEAWVFAGGDVV----- 483
Cdd:PRK12770 253 gEPDESGRPRPVpiPGSEFVLEADTVVFAIGEIPTPPFAKECLG-IELNRKGEIVVD-EKHMTSREGVFAAGDVVtgpsk 330
|
330 340
....*....|....*....|....
gi 578798494 484 -GLAnttvesVNDGKQASWYIHKY 506
Cdd:PRK12770 331 iGKA------IKSGLRAAQSIHEW 348
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
577-766 |
4.41e-29 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 118.22 E-value: 4.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 577 DWTELAKKSEDSgADALELNLSCPHGMGERgmglACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGG 656
Cdd:pfam01180 108 DYVEVARKIGPF-ADYIELNVSCPNTPGLR----ALQTDPELAAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 657 ANGVTATN----TVSGlMGLKSDGTPwpavGIAKRTTyGGVSGTAIRPIALRAVTSIARAL-PGFPILATGGIDSAESGL 731
Cdd:pfam01180 183 EDGLDGINatntTVRG-MRIDLKTEK----PILANGT-GGLSGPPIKPIALKVIRELYQRTgPEIPIIGVGGIESGEDAL 256
|
170 180 190
....*....|....*....|....*....|....*
gi 578798494 732 QFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALL 766
Cdd:pfam01180 257 EKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
874-932 |
5.59e-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: 106.98 E-value: 5.59e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 578798494 874 AMIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKM 932
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDDCITM 59
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
590-747 |
1.99e-21 |
|
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: 96.41 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 590 ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAV-----QIPFFAKLTPNVTD--IVSIARAAKEGGANGVTA 662
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDL-----QGKEALRELLTAVKEERnklgkKVPLLVKIAPDLSDeeLEDIADVALEHGVDGIIA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 663 TNTVSGLMGLKSDgtpwpavgiAKRTTYGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLHSGASVL 741
Cdd:cd04738 236 TNTTISRPGLLRS---------PLANETGGLSGAPLKERSTEVLRELYKLTGGkIPIIGVGGISSGEDAYEKIRAGASLV 306
|
....*.
gi 578798494 742 QVCSAI 747
Cdd:cd04738 307 QLYTGL 312
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
553-745 |
8.15e-18 |
|
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: 82.63 E-value: 8.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 553 VTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGmgergmglacgqdPELVRNICRWVRQAV-Q 631
Cdd:cd04722 48 VLKEVAAETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL-------------AREDLELIRELREAVpD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 632 IPFFAKLTPNVTDIvsiARAAKEGGANGVTATNtvsglmglksdgtpwpavgiakrttYGGVSGTAIRPIALRAVTSIAR 711
Cdd:cd04722 115 VKVVVKLSPTGELA---AAAAEEAGVDEVGLGN-------------------------GGGGGGGRDAVPIADLLLILAK 166
|
170 180 190
....*....|....*....|....*....|....
gi 578798494 712 ALPGFPILATGGIDSAESGLQFLHSGASVLQVCS 745
Cdd:cd04722 167 RGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
565-780 |
1.44e-17 |
|
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.
Pssm-ID: 240090 Cd Length: 325 Bit Score: 84.97 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 565 VIASIMCSYNkNDWTELAKKSEDSGADALELNLscphgmgergmgLACGQDPELVRN--------ICRWVRQAVQIPFFA 636
Cdd:cd04739 102 VIASLNGVSA-GGWVDYARQIEEAGADALELNI------------YALPTDPDISGAeveqryldILRAVKSAVTIPVAV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 637 KLTPNVTDIVSIARAAKEGGANGVTATNTVsglmglksdgtPWPAVGIAKRTTYGGVS-------GTAIRPIAlravtsI 709
Cdd:cd04739 169 KLSPFFSALAHMAKQLDAAGADGLVLFNRF-----------YQPDIDLETLEVVPNLLlsspaeiRLPLRWIA------I 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578798494 710 ARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQ 780
Cdd:cd04739 232 LSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHGYESVQQLRGS 302
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
590-766 |
3.27e-17 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 84.06 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 590 ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAVQ-----IPFFAKLTPNVTD--IVSIARAAKEGGANGVTA 662
Cdd:PRK05286 170 ADYFTVNISSPNTPGLRDL-----QYGEALDELLAALKEAQAelhgyVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 663 TNTV---SGLMGLKsdgtpwpavgIAKRTtyGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLHSGA 738
Cdd:PRK05286 245 TNTTlsrDGLKGLP----------NADEA--GGLSGRPLFERSTEVIRRLYKELGGrLPIIGVGGIDSAEDAYEKIRAGA 312
|
170 180
....*....|....*....|....*...
gi 578798494 739 SVLQVCSAIQNQDFTVIEDYCTGLKALL 766
Cdd:PRK05286 313 SLVQIYSGLIYEGPGLVKEIVRGLARLL 340
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
585-766 |
3.47e-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: 83.14 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 585 SEDSGADALELNLSCPH--GMGERGMglacgqDPELVRNICRWVRQAVQIPFFAKLTPnVTDIVSIARAAK-----EGGA 657
Cdd:cd04741 115 HQKQFPLAMELNLSCPNvpGKPPPAY------DFDATLEYLTAVKAAYSIPVGVKTPP-YTDPAQFDTLAEalnafACPI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 658 NGVTATNTV-SGLMgLKSDGTpwpAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLH 735
Cdd:cd04741 188 SFITATNTLgNGLV-LDPERE---TVVLKPKTGFGGLAGAYLHPLALGNVRTFRRLLPSeIQIIGVGGVLDGRGAFRMRL 263
|
170 180 190
....*....|....*....|....*....|.
gi 578798494 736 SGASVLQVCSAIQNQDFTVIEDYCTGLKALL 766
Cdd:cd04741 264 AGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
565-780 |
1.22e-16 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 82.22 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 565 VIASIMCSYNkNDWTELAKKSEDSGADALELNLSCPHGmgerGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTD 644
Cdd:PRK07565 104 VIASLNGSSA-GGWVDYARQIEQAGADALELNIYYLPT----DPDISGAEVEQRYLDILRAVKSAVSIPVAVKLSPYFSN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 645 IVSIARAAKEGGANGVTATNTVsglmglksdgtPWPAVGIAKRTTYGGV--SGTAIRPIALRAVtSIARALPGFPILATG 722
Cdd:PRK07565 179 LANMAKRLDAAGADGLVLFNRF-----------YQPDIDLETLEVVPGLvlSTPAELRLPLRWI-AILSGRVGADLAATT 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578798494 723 GIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQ 780
Cdd:PRK07565 247 GVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYESLQQFRGS 304
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
575-746 |
3.99e-13 |
|
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: 71.74 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 575 KNDWTELAKKSED---------SGADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAVQI-------PFFAKL 638
Cdd:TIGR01036 143 KNKDTPSEDAKEDyaaclrklgPLADYLVVNVSSPNTPGLRDL-----QYKAELRDLLTAVKQEQDGlrrvhrvPVLVKI 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 639 TPNVT--DIVSIARAAKEGGANGVTATNTV---SGLMGLKSDGTPwpavgiakrttyGGVSGtaiRPIALRAVTSIAR-- 711
Cdd:TIGR01036 218 APDLTesDLEDIADSLVELGIDGVIATNTTvsrSLVQGPKNSDET------------GGLSG---KPLQDKSTEIIRRly 282
|
170 180 190
....*....|....*....|....*....|....*..
gi 578798494 712 -ALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSA 746
Cdd:TIGR01036 283 aELQGrLPIIGVGGISSAQDALEKIRAGASLLQIYSG 319
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
876-936 |
7.45e-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: 64.69 E-value: 7.45e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578798494 876 IDEEMCINCGKCYMTCNDsgyQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMVSRT 936
Cdd:COG1144 27 VDEDKCIGCGLCWIVCPD---GAIRVDDGKYYGIDYDYCKGCGICAEVCP-VKAIEMVPEE 83
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
548-780 |
1.07e-12 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 69.98 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 548 YWCQSVTELKADFPDNIVIASIMcSYNKNDWTELAKKSEDSG-ADALELNLSCPHGMGERGMGLacgqDPELVRNICRWV 626
Cdd:PRK02506 78 YYLDYVLELQKKGPNKPHFLSVV-GLSPEETHTILKKIQASDfNGLVELNLSCPNVPGKPQIAY----DFETTEQILEEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 627 RQAVQIPFFAKLTPNVtDIVSIARAA---KEGGANGVTATNTV-SGLMGLKSDGTpwpaVGIAKRTTYGGVSGTAIRPIA 702
Cdd:PRK02506 153 FTYFTKPLGVKLPPYF-DIVHFDQAAaifNKFPLAFVNCINSIgNGLVIDPEDET----VVIKPKNGFGGIGGDYIKPTA 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578798494 703 LRAVTSIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQ 780
Cdd:PRK02506 228 LANVRAFYQRLnPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRGK 306
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
873-937 |
2.70e-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: 59.74 E-value: 2.70e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578798494 873 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMVSRTT 937
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 |
1.04e-10 |
|
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: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 189 KIALFGAGPASISCASFLARLGYsDITIFEKQE---YVGGLSTSEIPQFRLPYDVVNFEIELMKDL---------GVKII 256
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGG-KVTLIEDEGtcpYGGCVLSKALLGAAEAPEIASLWADLYKRKeevvkklnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 257 CGKS-LSVN----EMTLSTLKEKG-----YKAAFIGIGlPEPNKDAIfQGLTQDQGF----YTSKDFLPLVAKGSKagmc 322
Cdd:pfam07992 81 LGTEvVSIDpgakKVVLEELVDGDgetitYDRLVIATG-ARPRLPPI-PGVELNVGFlvrtLDSAEALRLKLLPKR---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 323 achsplpsirgvVIVLGAGDTAFDCATSALRCGARrVFIVFRKGFVNiRAVPEEMELAKEEKceflpfLSPRKVIVKGGR 402
Cdd:pfam07992 155 ------------VVVVGGGYIGVELAAALAKLGKE-VTLIEALDRLL-RAFDEEISAALEKA------LEKNGVEVRLGT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 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 ... |
873-933 |
2.87e-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: 59.81 E-value: 2.87e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578798494 873 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 933
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACP---VDAIVGAAKAMHTVIADECTGCDLCVEPCP-TDCIEMI 163
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
873-933 |
1.60e-09 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 58.42 E-value: 1.60e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798494 873 VAMIDEEMCINCGKCYMTCNdsgYQAIqFDPETHLPT-ITDTCTGCTLCLSVCPiVDCIKMV 933
Cdd:PRK05113 108 VAFIDEDNCIGCTKCIQACP---VDAI-VGATKAMHTvISDLCTGCDLCVAPCP-TDCIEMI 164
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
873-936 |
2.35e-09 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 59.42 E-value: 2.35e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578798494 873 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMVSRT 936
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACP---VDAIVGAPKQMHTVLADLCTGCDLCVPPCP-VDCIDMVPVT 138
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
873-945 |
3.20e-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: 58.85 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 873 VAMI-----DEEMCINCGKCYmtcndsgyQAIQFD----PETHLPT-ITDTCTGCTLCLSVCPiVDCIKMVsrttPYEPK 942
Cdd:COG2878 126 AAVIggpkgCEYGCIGCGDCI--------KACPFDaivgAAKGMHTvDEDKCTGCGLCVEACP-VDCIEMV----PVSPT 192
|
...
gi 578798494 943 RGV 945
Cdd:COG2878 193 VVV 195
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
868-935 |
4.02e-09 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 58.20 E-value: 4.02e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578798494 868 NVEQVVAMIDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTI-TDTCTGCTLCLSVCPiVDCIKMVSR 935
Cdd:COG1145 171 AIKKAKAVIDAEKCIGCGLCVKVC---PTGAIRLKDGKPQIVVdPDKCIGCGACVKVCP-VGAISLEPK 235
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
859-933 |
3.62e-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: 52.78 E-value: 3.62e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578798494 859 YLGTFGELSNVEQVVAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 933
Cdd:cd10549 58 ELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCP---VDAITLEDELEIVIDKEKCIGCGICAEVCP-VNAIKLV 128
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
579-738 |
5.08e-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: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 579 TELAKKSEDSGADALELNLSCPHGMGERGMGLAC-GQDPELVRNICRWVRQAVQIPFFAKLT----PNVTDIVSIARAAK 653
Cdd:pfam01207 69 AEAAKLVEDRGADGIDINMGCPSKKVTRGGGGAAlLRNPDLVAQIVKAVVKAVGIPVTVKIRigwdDSHENAVEIAKIVE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 654 EGGANGVTatntvsglmglksdgtpwpavgIAKRTTYGGVSGTAirpiALRAVTSIARALPgFPILATGGIDSAESGLQF 733
Cdd:pfam01207 149 DAGAQALT----------------------VHGRTRAQNYEGTA----DWDAIKQVKQAVS-IPVIANGDITDPEDAQRC 201
|
....*.
gi 578798494 734 L-HSGA 738
Cdd:pfam01207 202 LaYTGA 207
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
876-935 |
5.64e-08 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 50.48 E-value: 5.64e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798494 876 IDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTIT--DTCTGCTLCLSVCPiVDCIKMVSR 935
Cdd:COG1146 5 IDTDKCIGCGACVEVC---PVDVLELDEEGKKALVInpEECIGCGACELVCP-VGAITVEDD 62
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
873-935 |
5.70e-08 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 50.81 E-value: 5.70e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578798494 873 VAM---IDEEMCINCGKCYMTCNdsgyqAIQFDPETHLPTI-TDTCTGCTLCLSVCPiVDCIKMVSR 935
Cdd:COG4231 13 TAMryvIDEDKCTGCGACVKVCP-----ADAIEEGDGKAVIdPDLCIGCGSCVQVCP-VDAIKLEKR 73
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
194-238 |
9.78e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 49.84 E-value: 9.78e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 578798494 194 GAGPASISCASFLARLGYsDITIFEKQEYVGGLSTS-EIPQFRLPY 238
Cdd:pfam13450 3 GAGLAGLVAAALLAKRGF-RVLVLEKRDRLGGNAYSyRVPGYVFDY 47
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
582-738 |
2.50e-07 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 52.50 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 582 AKKSEDSGADALELNLSCP-----HGmgerGMGLACGQDPELVRNICRWVRQAVQIPFFAK---LTPNVTDIVSIARAAK 653
Cdd:cd02801 73 AKIVEELGADGIDLNMGCPspkvtKG----GAGAALLKDPELVAEIVRAVREAVPIPVTVKirlGWDDEEETLELAKALE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 654 EGGANGVtatnTVSGlmglksdgtpwpavgiakRTTYGGVSGTA----IRPIalravtsiaRALPGFPILATGGIDSAES 729
Cdd:cd02801 149 DAGASAL----TVHG------------------RTREQRYSGPAdwdyIAEI---------KEAVSIPVIANGDIFSLED 197
|
170
....*....|
gi 578798494 730 GLQFL-HSGA 738
Cdd:cd02801 198 ALRCLeQTGV 207
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
878-932 |
3.92e-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: 48.20 E-value: 3.92e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 578798494 878 EEMCINCGKCYMTCNdsgYQAIQFDPETHLPTIT---DTCTGCTLCLSVCPiVDCIKM 932
Cdd:COG1143 1 EDKCIGCGLCVRVCP---VDAITIEDGEPGKVYVidpDKCIGCGLCVEVCP-TGAISM 54
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
875-933 |
4.56e-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: 49.88 E-value: 4.56e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 578798494 875 MIDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 933
Cdd:cd10550 76 VVDEDKCIGCGMCVEAC---PFGAIRVDPETGKAIKCDLCGGDPACVKVCP-TGALEFV 130
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
854-932 |
4.99e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 53.71 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 854 GKALQYLGTfGELSnVEQVVAMIDEEMCINCGKCYMTCNdsgYQAIQFDpETHLPTITDT-CTGCTLCLSVCPiVDCIKM 932
Cdd:COG1148 473 ARAIQLLSK-GELG-VEPSVAEVDPEKCTGCGRCVEVCP---YGAISID-EKGVAEVNPAlCKGCGTCAAACP-SGAISL 545
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
872-938 |
2.16e-06 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 46.26 E-value: 2.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578798494 872 VVAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLpTITDTCTGCTLCLSVCPiVDCIKMVSRTTP 938
Cdd:COG2768 4 GKPYVDEEKCIGCGACVKVCP---VGAISIEDGKAV-IDPEKCIGCGACIEVCP-VGAIKIEWEEDE 65
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
881-925 |
2.51e-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: 45.21 E-value: 2.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 578798494 881 CINCGKCYMTCNdsgYQAIQFDPETHLPTIT------DTCTGCTLCLSVCP 925
Cdd:pfam12838 1 CIGCGACVAACP---VGAITLDEVGEKKGTKtvvidpERCVGCGACVAVCP 48
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
871-931 |
2.61e-06 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 45.81 E-value: 2.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578798494 871 QVVAMIDEEMCINCGKCYMTCNDsgyQAIQFDpETHLPTITDTCTGCTLCLSVCPiVDCIK 931
Cdd:COG2221 7 TWPPKIDEEKCIGCGLCVAVCPT---GAISLD-DGKLVIDEEKCIGCGACIRVCP-TGAIK 62
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
876-925 |
3.51e-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: 44.93 E-value: 3.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 578798494 876 IDEEMCINCGKCYMTC--NDSGYQAIQFDPET-HLPTITDTCTGCTLCLSVCP 925
Cdd:pfam13237 4 IDPDKCIGCGRCTAACpaGLTRVGAIVERLEGeAVRIGVWKCIGCGACVEACP 56
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
580-738 |
3.72e-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: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 580 ELAKKSEDSGADALELNLSCP------HGMGergmglAC-GQDPELVRNICRWVRQAVQIPFFAK----LTPNVTDIVSI 648
Cdd:COG0042 78 EAARIAEELGADEIDINMGCPvkkvtkGGAG------AAlLRDPELVAEIVKAVVEAVDVPVTVKirlgWDDDDENALEF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 649 ARAAKEGGANGVtatnTVSGlmglksdgtpwpavgiakRTT---YggvSGTA----IRpiALRAVTSIaralpgfPILAT 721
Cdd:COG0042 152 ARIAEDAGAAAL----TVHG------------------RTReqrY---KGPAdwdaIA--RVKEAVSI-------PVIGN 197
|
170
....*....|....*...
gi 578798494 722 GGIDSAESGLQFL-HSGA 738
Cdd:COG0042 198 GDIFSPEDAKRMLeETGC 215
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
873-933 |
4.42e-06 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 47.22 E-value: 4.42e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578798494 873 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 933
Cdd:PRK08764 79 VAWIVEADCIGCTKCIQACP---VDAIVGGAKHMHTVIAPLCTGCELCVPACP-VDCIELH 135
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
873-933 |
8.20e-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: 46.23 E-value: 8.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 873 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTItdtCTGC---------TLCLSVCPiVDCIKMV 933
Cdd:cd04410 74 IVLIDEDKCIGCGSCVEACP---YGAIVFDPEPGKAVK---CDLCgdrldeglePACVKACP-TGALTFG 136
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
194-252 |
1.28e-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: 1.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578798494 194 GAGPASISCASFLARLGYsDITIFEKQEYVGG-LSTSEIPQFRL---PYDVVNFEI--ELMKDLG 252
Cdd:COG1233 10 GAGIGGLAAAALLARAGY-RVTVLEKNDTPGGrARTFERPGFRFdvgPSVLTMPGVleRLFRELG 73
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
875-939 |
2.00e-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: 45.08 E-value: 2.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578798494 875 MIDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTIT--------DTCTGCTLCLSVCPiVDCIKMVSRTTPY 939
Cdd:cd10549 36 EIDEDKCVFCGACVEVC---PTGAIELTPEGKEYVPKekeaeideEKCIGCGLCVKVCP-VDAITLEDELEIV 104
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
876-944 |
2.12e-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: 45.08 E-value: 2.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578798494 876 IDEEMCINCGKCYMTCNdsgYQAIQFDP----ETHLPTITDTCTGCTLCLSVCPiVDCIKMVSRTTPYEPKRG 944
Cdd:cd10549 3 YDPEKCIGCGICVKACP---TDAIELGPngaiARGPEIDEDKCVFCGACVEVCP-TGAIELTPEGKEYVPKEK 71
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
590-746 |
2.37e-05 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 47.81 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 590 ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVR---------QAVQIPFFAKLTPNVT--DIVSIARAAKEGGAN 658
Cdd:PLN02826 217 ADYLVINVSSPNTPGLRKL-----QGRKQLKDLLKKVLaardemqwgEEGPPPLLVKIAPDLSkeDLEDIAAVALALGID 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 659 GVTATNTvsglmglkSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLHSG 737
Cdd:PLN02826 292 GLIISNT--------TISRPDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGkIPLVGCGGVSSGEDAYKKIRAG 363
|
....*....
gi 578798494 738 ASVLQVCSA 746
Cdd:PLN02826 364 ASLVQLYTA 372
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
576-780 |
3.06e-05 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 47.27 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 576 NDWTELAKKSEDSGADALELNLSCPHGMGERGM-GLACGQDPELVRNICRWVRQAVQIPFFAKL----TPNVTDIVSIAR 650
Cdd:PRK10415 77 KEMADAARINVESGAQIIDINMGCPAKKVNRKLaGSALLQYPDLVKSILTEVVNAVDVPVTLKIrtgwAPEHRNCVEIAQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 651 AAKEGGANGVTatntvsglmglksdgtpwpavgIAKRTTYGGVSGTA----IRpiALRAVTSIaralpgfPILATGGIDS 726
Cdd:PRK10415 157 LAEDCGIQALT----------------------IHGRTRACLFNGEAeydsIR--AVKQKVSI-------PVIANGDITD 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578798494 727 AESGLQFL-HSGASVLQVCSAIQNQD--FTVIEDYC-TG----------LKALLyLKSIEELQDWDGQ 780
Cdd:PRK10415 206 PLKARAVLdYTGADALMIGRAAQGRPwiFREIQHYLdTGellpplplaeVKRLL-CAHVRELHDFYGP 272
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
873-925 |
3.75e-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: 44.94 E-value: 3.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 873 VAMIDEEMCIN------CGKCYMTCNDSGYqAIQFDPETHLPTI-TDTCTGCTLCLSVCP 925
Cdd:cd16373 85 VAVIDKDRCLAwqggtdCGVCVEACPTEAI-AIVLEDDVLRPVVdEDKCVGCGLCEYVCP 143
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
194-510 |
4.21e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 46.65 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 194 GAGPASISCASFLARLGYSdITIFEKQEyVGGlstseipQFRLPYDVVNF-----EI---ELMKDL-------GVKIICG 258
Cdd:COG0492 7 GAGPAGLTAAIYAARAGLK-TLVIEGGE-PGG-------QLATTKEIENYpgfpeGIsgpELAERLreqaerfGAEILLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 259 KslsVNEMTLStlkekgykaafigiglpepnkDAIFQGLTQDQGFYTSKDFLplVAKGSKAGmcacHSPLPSI-----RG 333
Cdd:COG0492 78 E---VTSVDKD---------------------DGPFRVTTDDGTEYEAKAVI--IATGAGPR----KLGLPGEeefegRG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 334 V---------------VIVLGAGDTAFDcatSALRCG--ARRVFIVFRKGfvNIRAVPEEMELAKE-EKCEFLPflspRK 395
Cdd:COG0492 128 VsycatcdgfffrgkdVVVVGGGDSALE---EALYLTkfASKVTLIHRRD--ELRASKILVERLRAnPKIEVLW----NT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 396 VI--VKG-GRIVAMQFVRTEQDETgkwnededqmVHLKADVVISAFGSV-LSDPkVKEAlsPIKFNRWGLPEVDpETMQT 471
Cdd:COG0492 199 EVteIEGdGRVEGVTLKNVKTGEE----------KELEVDGVFVAIGLKpNTEL-LKGL--GLELDEDGYIVVD-EDMET 264
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 578798494 472 SEAWVFAGGDVVG----LANTtveSVNDGKQASWYIHKYVQDI 510
Cdd:COG0492 265 SVPGVFAAGDVRDykyrQAAT---AAGEGAIAALSAARYLEPL 304
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
877-933 |
5.05e-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: 43.80 E-value: 5.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 578798494 877 DEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTItdtCTGCTLCLSVCPiVDCIKMV 933
Cdd:cd16370 81 DKEKCIGCGNCVKACI---VGAIFWDEETNKPII---CIHCGYCARYCP-HDVLAME 130
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
872-933 |
1.12e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 45.79 E-value: 1.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578798494 872 VVAMIDEEMCINCGKCYMTCndsGYQAIQFDpETHLPTITDTCTGCTLCLSVCP-----IVDCIKMV 933
Cdd:COG4624 84 PSIIRDKEKCKNCYPCVRAC---PVKAIKVD-DGKAEIDEEKCISCGQCVAVCPfgaitEKSDIEKV 146
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
877-936 |
2.87e-04 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 41.17 E-value: 2.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 877 DEEMCINCGKCYMTCNDSgyqAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMVSRT 936
Cdd:PRK09624 49 NRDKCVRCYLCYIYCPEP---AIYLDEEGYPVFDYDYCKGCGICANECP-TKAIEMVRET 104
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
189-230 |
4.72e-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: 4.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 578798494 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSE 230
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTV 43
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
873-933 |
5.07e-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: 5.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578798494 873 VAMIDEEMCiNCGKCYMTC------NDSGYQAIQFDPETHLPTIT-DTCTGCTLCLSVCPIvDCIKMV 933
Cdd:COG1245 4 IAVVDRDRC-QPKKCNYECikycpvNRTGKEAIEIDEDDGKPVISeELCIGCGICVKKCPF-DAISIV 69
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
889-935 |
5.39e-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: 41.08 E-value: 5.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 578798494 889 MTCNDS-GYQAIQFDPETH---LPTI-TDTCTGCTLCLSVCPiVDCIKMVSR 935
Cdd:cd10564 89 RSCQDAcPTQAIRFRPRLGgiaLPELdADACTGCGACVSVCP-VGAITLTPL 139
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
873-926 |
6.38e-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: 42.37 E-value: 6.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 578798494 873 VAMIDEEMCINCGKCYMTCNdsgYQAIQFDPeTHLPTITDTCTGCTLCLSVCPI 926
Cdd:cd03110 58 KAFIDQEKCIRCGNCERVCK---FGAILEFF-QKLIVDESLCEGCGACVIICPR 107
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
189-252 |
6.85e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 43.34 E-value: 6.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578798494 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSeipqfrlpYDVVNFEIE---------------LMKDLG 252
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGH-EVTVFEADDQLGGLAAS--------FEFGGLPIErfyhhifksdealleLLDELG 70
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
879-925 |
9.27e-04 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 40.50 E-value: 9.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 578798494 879 EMCINCGKCYMTCNDSgyqAIQFDPETHLPTITDTCTGCTLCLSVCP 925
Cdd:PRK09625 59 EICINCFNCWVYCPDA---AILSRDKKLKGVDYSHCKGCGVCVEVCP 102
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
880-930 |
1.14e-03 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 37.92 E-value: 1.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 578798494 880 MCINCGKCYMTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCI 930
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQTIRGDIAGLACIGCGACVDACP-RGAI 50
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
873-925 |
1.34e-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: 39.63 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 873 VAMIDEEMCINCGKCYMTCNDSGYQ-------AIQFDPETHLPTITdTCTGCTLCLSVCP 925
Cdd:cd16372 2 LLVTDPEKCIGCLQCEEACSKTFFKeedreksCIRITETEGGYAIN-VCNQCGECIDVCP 60
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
407-503 |
1.63e-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: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 407 QFVRTEQDETGKW--NEDEDQMVHLKADVVISAFGSVlsdPKVK----EALSpIKFNRWGLPEVDpETMQTSEAWVFAGG 480
Cdd:COG1249 231 KVTSVEKTGDGVTvtLEDGGGEEAVEADKVLVATGRR---PNTDglglEAAG-VELDERGGIKVD-EYLRTSVPGIYAIG 305
|
90 100
....*....|....*....|...
gi 578798494 481 DVVGLANTTVESVNDGKQASWYI 503
Cdd:COG1249 306 DVTGGPQLAHVASAEGRVAAENI 328
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
875-925 |
1.82e-03 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 40.31 E-value: 1.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 875 MIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTItdtCTGC---------TLCLSVCP 925
Cdd:COG0437 86 LVDYDKCIGCRYCVAACP---YGAPRFNPETGVVEK---CTFCadrldegllPACVEACP 139
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
824-933 |
2.24e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 41.78 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 824 RLKEQNVAFSPLKRNCFIP----KRPIPTIKDVIGkalqylgTFGELsnveqVVAMIDEE------------MCINCGKC 887
Cdd:PRK12771 451 RPKREIVKFDKLNLWYFTDapraQRPELDADERVG-------DFDEV-----LGGLTEEEarqeaarclscgNCFECDNC 518
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 578798494 888 YMTCNDsgyQAIQ-FDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 933
Cdd:PRK12771 519 YGACPQ---DAIIkLGPGRRYHFDYDKCTGCHICADVCP-CGAIEMG 561
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
873-933 |
3.13e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 3.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578798494 873 VAMIDEEMCiNCGKCYMTC------NDSGYQAIQFDPETHLPTIT-DTCTGCTLCLSVCPIvDCIKMV 933
Cdd:PRK13409 4 IAVVDYDRC-QPKKCNYECikycpvVRTGEETIEIDEDDGKPVISeELCIGCGICVKKCPF-DAISIV 69
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
189-227 |
3.55e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 41.03 E-value: 3.55e-03
10 20 30
....*....|....*....|....*....|....*....
gi 578798494 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLS 227
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGIS 43
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
911-941 |
3.88e-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: 36.65 E-value: 3.88e-03
10 20 30
....*....|....*....|....*....|.
gi 578798494 911 TDTCTGCTLCLSVCPiVDCIKMVSRTTPYEP 941
Cdd:COG1143 1 EDKCIGCGLCVRVCP-VDAITIEDGEPGKVY 30
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
879-948 |
3.93e-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: 40.83 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798494 879 EMCINCGKCYMTC---------NDS-------------GYQAIQFDPET--HLptitDTCTGCTLCLSVCPI-VDCIKMV 933
Cdd:COG0247 78 DACVGCGFCRAMCpsykatgdeKDSprgrinllrevleGELPLDLSEEVyeVL----DLCLTCKACETACPSgVDIADLI 153
|
90
....*....|....*.
gi 578798494 934 SRTTP-YEPKRGVPLS 948
Cdd:COG0247 154 AEARAqLVERGGRPLR 169
|
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
873-933 |
4.70e-03 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 37.62 E-value: 4.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578798494 873 VAMIDEEMCINCGKCYMTCNDSgyqAIQFDPETHLPTITDTCTGCTLCLSVCPiVDCIKMV 933
Cdd:PRK09623 45 MPVVDESKCVKCYICWKFCPEP---AIYIKEDGYVAIDYDYCKGCGICANECP-TKAITMV 101
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
876-935 |
5.50e-03 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 39.66 E-value: 5.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578798494 876 IDEEMCINCGKCYMTCndsgyqaiqfdpETHLP-----TITDTCTGCTLCLSVCPiVDCIKMVSR 935
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 ... |
909-933 |
7.96e-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: 39.07 E-value: 7.96e-03
10 20
....*....|....*....|....*
gi 578798494 909 TITDTCTGCTLCLSVCPiVDCIKMV 933
Cdd:NF038196 182 HVTDKCIGCGICAKVCP-VNNIEME 205
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
910-943 |
8.62e-03 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 35.84 E-value: 8.62e-03
10 20 30
....*....|....*....|....*....|....
gi 578798494 910 ITDTCTGCTLCLSVCPiVDCIKMVSRTTPYEPKR 943
Cdd:COG1146 6 DTDKCIGCGACVEVCP-VDVLELDEEGKKALVIN 38
|
|
| |
