|
Name |
Accession |
Description |
Interval |
E-value |
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
532-834 |
0e+00 |
|
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN, and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239244 Cd Length: 299 Bit Score: 554.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPlygpGQSSFLNIE 611
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGR----GQIGFNNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 612 LISEKTAAYWCHSVTELKADFPDNILIASIMCSYNKSDWMELSKMAEASGADALELNLSCPHGMGERGMGLACGQDPELV 691
Cdd:cd02940 77 LISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 692 RNICRWVRQAVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGLMGLKADGTPwPAVGIGRRTTYGGVSGTAIR 771
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTP-PAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25140985 772 PIALRAVTAIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGL 834
Cdd:cd02940 236 PIALRAVSQIARAPePGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
532-1012 |
9.62e-124 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 383.91 E-value: 9.62e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTfsLDKDIVTNVSPRIirgttsGPLYGPGQS--SFLN 609
Cdd:PRK08318 3 DLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKT--LGPPIVNVSSPRF------GALVKEDRRfiGFNN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 610 IELISEKTAAYWCHSVTELKADFPDNILIASIMCSYNKSDWMELSKMAEASGADALELNLSCPHGMGERGMGLACGQDPE 689
Cdd:PRK08318 75 IELITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 690 LVRNICRWVRQAVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGLMGLKADG-TPWPAVGiGrRTTYGGVSGT 768
Cdd:PRK08318 155 LVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRmIPMPIVN-G-KSSHGGYCGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 769 AIRPIALRAVTAIAR--ALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGlkallylksieeL 846
Cdd:PRK08318 233 AVKPIALNMVAEIARdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISG------------L 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 847 ADWdgqsppiishqkgkpvprvaelmgqklpsfgpyleqrkkiiaaskirqkdqntacspLQRKHFNSqkpipaIKDVIG 926
Cdd:PRK08318 301 SHY---------------------------------------------------------MDEKGFAS------LEDMVG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 927 KSLQYLGTFGEMSIMEQVVALIDEEMCINCGKCYMTCNDSGYQAIQFDP-ETHLPTVSDT-CTGCTLCLSVCPIMDCIRM 1004
Cdd:PRK08318 318 LAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDEdGTRTPEVIEEeCVGCNLCAHVCPVEGCITM 397
|
490
....*....|
gi 25140985 1005 VSRAT--PYQ 1012
Cdd:PRK08318 398 GEVKFgkPYA 407
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
53-511 |
1.22e-118 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 371.82 E-value: 1.22e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 53 EKLESNFDDIkHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPT 132
Cdd:PRK11749 17 EERAQNFDEV-APGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 133 SDLCVGGCNLHAAEEgPINIGGLQQFATEvfKAMNIPQIRNPSLPPPEHmpeaysaKIALFGAGPASISCASFLARLGYS 212
Cdd:PRK11749 96 ERLCEGACVRGKKGE-PVAIGRLERYITD--WAMETGWVLFKRAPKTGK-------KVAVIGAGPAGLTAAHRLARKGYD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 213 nITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSTDeMTLSSLKEnGYRAAFIGIGLPEPKKDH 292
Cdd:PRK11749 166 -VTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRD-ITLDELRA-GYDAVFIGTGAGLPRFLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 293 IF-QGLtqvQGFYTSKDFLPLVAKSSktgmcachSPLPSIRG-AVIVLGAGDTAFDCATSALRCGALRVFIVFRKGFVNI 370
Cdd:PRK11749 243 IPgENL---GGVYSAVDFLTRVNQAV--------ADYDLPVGkRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 371 RAVPEEMELAKEEKCEFLPFLSPRKVIVKDGKIVAMQFVRTE---QDETGN-WVEDEEQTVRLKADVVISAFGSVLEDPK 446
Cdd:PRK11749 312 PASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMElgePDASGRrRVPIEGSEFTLPADLVIKAIGQTPNPLI 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25140985 447 VKEALsPIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKHIQAQY 511
Cdd:PRK11749 392 LSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAA 455
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
58-505 |
3.22e-116 |
|
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: 364.46 E-value: 3.22e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 58 NFDDIkHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTsdLCV 137
Cdd:COG0493 4 DFREV-YPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--PCE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 138 GGCNLHAAEEgPINIGGLQQFATEvfKAMNIPQIRNPSLPPPEHmpeaysAKIALFGAGPASISCASFLARLGYSnITIF 217
Cdd:COG0493 81 GACVRGIVDE-PVAIGALERFIAD--KAFEEGWVKPPPPAPRTG------KKVAVVGSGPAGLAAAYQLARAGHE-VTVF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 218 EKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSTDeMTLSSLKENgYRAAFIGIGLPEPKKDHIfQGl 297
Cdd:COG0493 151 EALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKD-ITLDELLEE-FDAVFLATGAGKPRDLGI-PG- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 298 TQVQGFYTSKDFLPLVAKssktgMCACHSPLPsIRGAVIVLGAGDTAFDCATSALRCGALRVFIVFRKGFVNIRAVPEEM 377
Cdd:COG0493 227 EDLKGVHSAMDFLTAVNL-----GEAPDTILA-VGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 378 ELAKEEKCEFLPFLSPRKVIV-KDGKIVAMQFVRTE---QDETGNW--VEDEEQTVRLKADVVISAFGSVLEDPKVKEAL 451
Cdd:COG0493 301 EEALEEGVEFLFLVAPVEIIGdENGRVTGLECVRMElgePDESGRRrpVPIEGSEFTLPADLVILAIGQTPDPSGLEEEL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 25140985 452 SpIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHK 505
Cdd:COG0493 381 G-LELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDR 433
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
535-833 |
9.41e-98 |
|
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 310.05 E-value: 9.41e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 535 VEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDkDIVTNVSPRIIRGTTSGPlYGPGQSSFLNIELIS 614
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLH-PRPGNPLPRVARLPPEGE-SYPEQLGILNSFGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 615 EKTAAYWCHSVTELKADFPDNILIASIMCSyNKSDWMELSKMAEASGADALELNLSCPHGMGERGmglaCGQDPELVRNI 694
Cdd:cd02810 79 NLGLDVWLQDIAKAKKEFPGQPLIASVGGS-SKEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 695 CRWVRQAVRVPFFAKLTPNVT--DIVSIARAAKEGGADGVTATNTVSGLMGLKadgtpwPAVGIGRRTTYGGVSGTAIRP 772
Cdd:cd02810 154 LKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDL------KTVGPGPKRGTGGLSGAPIRP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25140985 773 IALRAVTAIARALP-GFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTG 833
Cdd:cd02810 228 LALRWVARLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
58-511 |
2.45e-86 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 285.76 E-value: 2.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 58 NFDDIkhtTLG--ERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDL 135
Cdd:PRK12831 22 NFEEV---CLGynEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 136 CVGGCNLHAAEEgPINIGGLQQFATEVFKAMNIPQIRNPSLPppehmpeaySAKIALFGAGPASISCASFLARLGYsNIT 215
Cdd:PRK12831 99 CEGKCVLGIKGE-PVAIGKLERFVADWARENGIDLSETEEKK---------GKKVAVIGSGPAGLTCAGDLAKMGY-DVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 216 IFEKQEYVGGLSTSEIPQFRLPYD-VVNFEIELMKDLGVKI----ICGKSLSTDEMtlssLKENGYRAAFIGIGLPEPKk 290
Cdd:PRK12831 168 IFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIetnvVVGKTVTIDEL----LEEEGFDAVFIGSGAGLPK- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 291 dhiFQGL--TQVQGFYTSKDFLPLV--AKSSKTGmcachSPLPSIRGA-VIVLGAGDTAFDCATSALRCGAlRVFIVFRK 365
Cdd:PRK12831 243 ---FMGIpgENLNGVFSANEFLTRVnlMKAYKPE-----YDTPIKVGKkVAVVGGGNVAMDAARTALRLGA-EVHIVYRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 366 GFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KDGKIVAMQFVRT---EQDETGNW--VEDEEQTVRLKADVVISAFG 439
Cdd:PRK12831 314 SEEELPARVEEVHHAKEEGVIFDLLTNPVEILGdENGWVKGMKCIKMelgEPDASGRRrpVEIEGSEFVLEVDTVIMSLG 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25140985 440 SVlEDPKVKEALSPIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKHIQAQY 511
Cdd:PRK12831 394 TS-PNPLISSTTKGLKINKRGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSKKW 464
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
532-855 |
7.64e-86 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 281.73 E-value: 7.64e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIR------GTTSGPLYGpgqs 605
Cdd:PLN02495 10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARlraganGSAKGRVIG---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 606 sFLNIELISEKTAAYWCHSVTELKADFPDNILIASIMCSYNKSDWMELSKMAEASGADALELNLSCPHGMGERGMGLACG 685
Cdd:PLN02495 86 -WQNIELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 686 QDPELVRNICRWVRQAVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGLMGLKADgTPWPAVGIGRRTTYGGV 765
Cdd:PLN02495 165 QDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLD-TLRPEPCVEGYSTPGGY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 766 SGTAIRPIALRAVTAIARALPG-FP----ILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYL 840
Cdd:PLN02495 244 SSKAVRPIALAKVMAIAKMMKSeFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKK 323
|
330
....*....|....*
gi 25140985 841 KSIEELADWDGQSPP 855
Cdd:PLN02495 324 HNFSSIEDFRGASLP 338
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
532-838 |
9.14e-83 |
|
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: 270.02 E-value: 9.14e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKdIVTNVSPRIIRgttsgpLygPGQSSFLNIE 611
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEP-QPGNPRPRLFR------L--PEDSGLINRM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 612 LISEKTAAYWCHSVTELKAdfPDNILIASIMCSyNKSDWMELSKMAEASGADALELNLSCPHGmgeRGMGLACGQDPELV 691
Cdd:COG0167 72 GLNNPGVDAFLERLLPAKR--YDVPVIVNIGGN-TVEDYVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 692 RNICRWVRQAVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGL-MGLKadgTPWPAVGigrrTTYGGVSGTAI 770
Cdd:COG0167 146 AELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRaIDLE---TRRPVLA----NEAGGLSGPAL 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25140985 771 RPIALRAVTAIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:COG0167 219 KPIALRMVREVAQAVGGdIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYL 287
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
67-510 |
1.58e-75 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 264.30 E-value: 1.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 67 LGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNLHAAE 146
Cdd:PRK12778 319 LTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQCESKCIHGKMG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 147 EGPINIGGLQQFATEvFKAMNipqiRNPSLPppeHMPEAYSAKIALFGAGPASISCASFLARLGYsNITIFEKQEYVGGL 226
Cdd:PRK12778 399 EEAVAIGYLERFVAD-YERES----GNISVP---EVAEKNGKKVAVIGSGPAGLSFAGDLAKRGY-DVTVFEALHEIGGV 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 227 STSEIPQFRLPYDVVNFEIELMKDLGVKI----ICGKSLSTDEMtlsslKENGYRAAFI--GIGLPepkkdhIFQGL--T 298
Cdd:PRK12778 470 LKYGIPEFRLPKKIVDVEIENLKKLGVKFetdvIVGKTITIEEL-----EEEGFKGIFIasGAGLP------NFMNIpgE 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 299 QVQGFYTSKDFLPLV------AKSSKTgmcachsplPSIRG-AVIVLGAGDTAFDCATSALRCGALRVFIVFRKGFVNIR 371
Cdd:PRK12778 539 NSNGVMSSNEYLTRVnlmdaaSPDSDT---------PIKFGkKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMP 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 372 AVPEEMELAKEEKCEFLPFLSPRKVI------VKDGKIVAMQFvrTEQDETGNW--VEDEEQTVRLKADVVISAFGsVLE 443
Cdd:PRK12778 610 ARLEEVKHAKEEGIEFLTLHNPIEYLadekgwVKQVVLQKMEL--GEPDASGRRrpVAIPGSTFTVDVDLVIVSVG-VSP 686
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25140985 444 DPKVKEALSPIKFNRWGLPEVNPEtMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKHIQAQ 510
Cdd:PRK12778 687 NPLVPSSIPGLELNRKGTIVVDEE-MQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
58-499 |
1.70e-63 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 223.12 E-value: 1.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 58 NFDDIkHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSdlCV 137
Cdd:PRK12810 26 DFKEF-YEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAP--CE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 138 GGCNLhAAEEGPINIGGLQQFATEvfKAMNIPQIRnpslppPEHmPEAYSAK-IALFGAGPASISCASFLARLGYSnITI 216
Cdd:PRK12810 103 GACTL-NINFGPVTIKNIERYIID--KAFEEGWVK------PDP-PVKRTGKkVAVVGSGPAGLAAADQLARAGHK-VTV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 217 FEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSTDeMTLSSLKENgYRAAFIGIG--------LPEP 288
Cdd:PRK12810 172 FERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKD-ITAEELLAE-YDAVFLGTGaykprdlgIPGR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 289 KKDHIFQGLtqvqgfytskDFLPLVAKSsktgmCACHSPLPSIRGA---VIVLGAGDTAFDCATSALRCGALRVfIVFrk 365
Cdd:PRK12810 250 DLDGVHFAM----------DFLIQNTRR-----VLGDETEPFISAKgkhVVVIGGGDTGMDCVGTAIRQGAKSV-TQR-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 366 gfvNIRAVP----------------EEMELAKEEKCEFLPFLSPRKVIVKDGKIVAMQFVRTEQDETGNW-VEDEEQTvr 428
Cdd:PRK12810 312 ---DIMPMPpsrrnknnpwpywpmkLEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGDFEpVEGSEFV-- 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25140985 429 LKADVVISAFGSVLEDPKVKEALSpIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQA 499
Cdd:PRK12810 387 LPADLVLLAMGFTGPEAGLLAQFG-VELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQA 456
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
534-847 |
1.09e-62 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 214.72 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 534 SVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSG-----PLYGPGQSSFL 608
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPRE-GNPPPRVVE-TPGGmlnaiGLQNPGVEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 609 NIELIsektaaywchsvtelKADFPDNILIASIMCSyNKSDWMELSKMAEASGADALELNLSCPHgmgERGMGLACGQDP 688
Cdd:cd04740 79 EELLP---------------WLREFGTPVIASIAGS-TVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 689 ELVRNICRWVRQAVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVSGLmglkadgtpwpAVGIGRRT-----TYG 763
Cdd:cd04740 140 EAVAEIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKGM-----------AIDIETRKpilgnVTG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 764 GVSGTAIRPIALRAVTAIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIEDYCTGLKALL---YL 840
Cdd:cd04740 209 GLSGPAIKPIALRMVYQVYKAV-EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLdeeGI 286
|
....*..
gi 25140985 841 KSIEELA 847
Cdd:cd04740 287 KSIEELV 293
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
532-846 |
1.85e-61 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 211.55 E-value: 1.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSG-----PLYGPGQSS 606
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPRE-GNPTPRIAE-TPGGmlnaiGLQNPGVDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 607 FLNIELISEKtaaywchsvtelKADFPdniLIASImCSYNKSDWMEL-SKMAEASGADALELNLSCPHGMGergMGLACG 685
Cdd:PRK07259 79 FIEEELPWLE------------EFDTP---IIANV-AGSTEEEYAEVaEKLSKAPNVDAIELNISCPNVKH---GGMAFG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 686 QDPELVRNICRWVRQAVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTvsgLMGLKAD-GTPWPAVGigrrTTYGG 764
Cdd:PRK07259 140 TDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAIDiKTRKPILA----NVTGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 765 VSGTAIRPIALRAVTAIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIEDYCTGLKALLY---LK 841
Cdd:PRK07259 213 LSGPAIKPIALRMVYQVYQAV-DIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDkygIK 290
|
....*
gi 25140985 842 SIEEL 846
Cdd:PRK07259 291 SIEEI 295
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
82-518 |
4.25e-57 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 209.20 E-value: 4.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 82 CAD--APCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSdlCVGGCNLHAAEEgPINIGGLQQFA 159
Cdd:PRK12814 97 CGDclGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDE-PVSICALKRYA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 160 TEvfKAMNIPQirnPSLPPPEhmpEAYSAKIALFGAGPASISCASFLARLGYsNITIFEKQEYVGGLSTSEIPQFRLPYD 239
Cdd:PRK12814 174 AD--RDMESAE---RYIPERA---PKSGKKVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGMMRYGIPRFRLPES 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 240 VVNFEIELMKDLGVKIICGKSLSTDeMTLSSLKENgYRAAFIGIGLPEPKKDHIfQGlTQVQGFYTSKDFLPLVAKSSKt 319
Cdd:PRK12814 245 VIDADIAPLRAMGAEFRFNTVFGRD-ITLEELQKE-FDAVLLAVGAQKASKMGI-PG-EELPGVISGIDFLRNVALGTA- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 320 gmcachsplPSIRGAVIVLGAGDTAFDCATSALRCGALRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVK 399
Cdd:PRK12814 320 ---------LHPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 400 DGKIVaMQFVRTEQ---DETGNW----VEDEEQTvrLKADVVISAFGSVLeDPKVKEAlSPIKFNRWGLPEVNPETMQTS 472
Cdd:PRK12814 391 EGGLE-LTAIKMQQgepDESGRRrpvpVEGSEFT--LQADTVISAIGQQV-DPPIAEA-AGIGTSRNGTVKVDPETLQTS 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 25140985 473 EPWVFAGGDVVGMANTTVESVNDGKQASWYIHKHIQAQYGTSVPSQ 518
Cdd:PRK12814 466 VAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGKPVTAPVQP 511
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
72-510 |
1.13e-54 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 201.15 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 72 ALREAVRCLKCAdaPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCptSDLCVGGCNL-HAAEegPI 150
Cdd:PRK13984 180 AMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVC--THKCETVCSIgHRGE--PI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 151 NIGGLQQFATEvfkamNIPQIRNPSLPPPEhmPEAYSAKIALFGAGPASISCASFLARLGYsNITIFEKQEYVGGLSTSE 230
Cdd:PRK13984 254 AIRWLKRYIVD-----NVPVEKYSEILDDE--PEKKNKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGVMRYG 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 231 IPQFRLPYDVVNFEIELMKDLGVKIICGKSLSTDeMTLSSLKEnGYRAAFIGIGL------PEPKKDH--IFQGLTQVQG 302
Cdd:PRK13984 326 IPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKD-IPLEELRE-KHDAVFLSTGFtlgrstRIPGTDHpdVIQALPLLRE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 303 FytsKDFLplvakssktgmcACHSPLPSIRGAVIVLGAGDTAFDCATSALRC-----GALRVFIV-FRKGFVNIRAVPEE 376
Cdd:PRK13984 404 I---RDYL------------RGEGPKPKIPRSLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTsLERTFEEMPADMEE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 377 MELAKEEKCEFLPFLSPRKVIVKDGKIVAMQFVRTEQ--DETG--NWVEDEEQTVRLKADVVISAFG-----SVLEDPkV 447
Cdd:PRK13984 469 IEEGLEEGVVIYPGWGPMEVVIENDKVKGVKFKKCVEvfDEEGrfNPKFDESDQIIVEADMVVEAIGqapdySYLPEE-L 547
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25140985 448 KEALspiKFNRwGLPEVNpETMQTSEPWVFAGGDVVGMANtTVESVNDGKQASWYIHKHIQAQ 510
Cdd:PRK13984 548 KSKL---EFVR-GRILTN-EYGQTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYLRKQ 604
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
72-500 |
3.37e-53 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 202.48 E-value: 3.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 72 ALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNLHAAEEgPIN 151
Cdd:PRK12775 326 ALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQCIIAKKHE-SVG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 152 IGGLQQFATEvfkamnipQIRNPSLPPPEHMPEAysAKIALFGAGPASISCASFLARLGySNITIFEKQEYVGGLSTSEI 231
Cdd:PRK12775 405 IGRLERFVGD--------NARAKPVKPPRFSKKL--GKVAICGSGPAGLAAAADLVKYG-VDVTVYEALHVVGGVLQYGI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 232 PQFRLPYDVVNFEIELMKDLGVKI----ICGKSLSTDEMtlssLKENGYRAAFIGIGLPEPKkdhiFQGL-----TQVqg 302
Cdd:PRK12775 474 PSFRLPRDIIDREVQRLVDIGVKIetnkVIGKTFTVPQL----MNDKGFDAVFLGVGAGAPT----FLGIpgefaGQV-- 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 303 fYTSKDFLPLVAKSSKTGMCACHSPLpSIRGAVIVLGAGDTAFDCATSALRCGALRVFIVFRKGFVNIRAVPEEMELAKE 382
Cdd:PRK12775 544 -YSANEFLTRVNLMGGDKFPFLDTPI-SLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKE 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 383 EKCEFLPFLSPRKVIV-KDGKIVAMqfvRTEQDETGnwvEDEEQTVR----------LKADVVISAFGSVlEDPKVKEAL 451
Cdd:PRK12775 622 EGIDFFFLHSPVEIYVdAEGSVRGM---KVEEMELG---EPDEKGRRkpmptgefkdLECDTVIYALGTK-ANPIITQST 694
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 25140985 452 SPIKFNRWGLPEVN----PETMQTSEPWVFAGGDVVGMANTTVESVNDGKQAS 500
Cdd:PRK12775 695 PGLALNKWGNIAADdgklESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAA 747
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
86-504 |
6.88e-53 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 195.09 E-value: 6.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 86 PCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSdlCVGGCNlHAAEEGPINIGGLQQFATEvfka 165
Cdd:PRK12771 48 PCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCN-RGQVDDAVGINAVERFLGD---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 166 mnipQIRNPSLPPPEhmPEAYSAK-IALFGAGPASISCASFLARLGYSnITIFEKQEYVGGLSTSEIPQFRLPYDVVNFE 244
Cdd:PRK12771 121 ----YAIANGWKFPA--PAPDTGKrVAVIGGGPAGLSAAYHLRRMGHA-VTIFEAGPKLGGMMRYGIPAYRLPREVLDAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 245 IELMKDLGVKIICGKSLSTDeMTLSSLkENGYRAAFIGIG------LPEPKKD--HIFQGLtqvqgfytskDFLplvaKS 316
Cdd:PRK12771 194 IQRILDLGVEVRLGVRVGED-ITLEQL-EGEFDAVFVAIGaqlgkrLPIPGEDaaGVLDAV----------DFL----RA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 317 SKTGMcachspLPSIRGAVIVLGAGDTAFDCATSALRCGALRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKV 396
Cdd:PRK12771 258 VGEGE------PPFLGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 397 IVKDGKIVAM---QFVRTEQDETGNWVEDEEQTVRLKADVVISAFG-----SVLEDpkvkealSPIKFNRWGLPEVNPET 468
Cdd:PRK12771 332 EGDENGATGLrviTVEKMELDEDGRPSPVTGEEETLEADLVVLAIGqdidsAGLES-------VPGVEVGRGVVQVDPNF 404
|
410 420 430
....*....|....*....|....*....|....*.
gi 25140985 469 MQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIH 504
Cdd:PRK12771 405 MMTGRPGVFAGGDMVPGPRTVTTAIGHGKKAARNID 440
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
533-846 |
5.45e-52 |
|
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: 184.94 E-value: 5.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 533 ISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSG-----PLYGPGQSSF 607
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRP-GYRNPTIVE-TPCGmlnaiGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 608 LNiELISEKTaaywchsvtelkaDFPDNIlIASImcsYNKS--DWMELSKMAEASG--ADALELNLSCPHGMGergMGLA 683
Cdd:TIGR01037 79 LE-ELKPVRE-------------EFPTPL-IASV---YGSSveEFAEVAEKLEKAPpyVDAYELNLSCPHVKG---GGIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 684 CGQDPELVRNICRWVRQAVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTvsgLMGLKAD---GTPWPAvgigrrT 760
Cdd:TIGR01037 138 IGQDPELSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKIDiktGKPILA------N 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 761 TYGGVSGTAIRPIALRAVTAIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFtVIEDYCTGLKALLY- 839
Cdd:TIGR01037 209 KTGGLSGPAIKPIALRMVYDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKa 286
|
....*....
gi 25140985 840 --LKSIEEL 846
Cdd:TIGR01037 287 egFTSIEEL 295
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
23-500 |
4.15e-51 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 191.39 E-value: 4.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 23 QAHATLRSTAAKKLDKKHWKRNTDKncFTCEKLESNFDDIkHTTLGERGALREAVRCLKCAD-APCQKSCPTSLDIKSFI 101
Cdd:PRK12809 157 KASSDAQPSRSAALLPVNSRKGADK--ISASERKTHFGEI-YCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYI 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 102 TSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNLHAaEEGPINIGGLQQFATEVFKAMN-IPQIRNpSLPPPE 180
Cdd:PRK12809 234 RLVQEGKIIEAAELCHQTSSLPEICGRVCPQDRLCEGACTLKD-HSGAVSIGNLERYITDTALAMGwRPDVSK-VVPRSE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 181 hmpeaysaKIALFGAGPASISCASFLARLGYsNITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKS 260
Cdd:PRK12809 312 --------KVAVIGAGPAGLGCADILARAGV-QVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 261 LSTDeMTLSSLKENgYRAAFIGIG--------LPEPKKDHIFQGLtqvqgfytskdflPLVAKSSKTGMCACHS---PLP 329
Cdd:PRK12809 383 IGRD-ITFSDLTSE-YDAVFIGVGtygmmradLPHEDAPGVIQAL-------------PFLTAHTRQLMGLPESeeyPLT 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 330 SIRGA-VIVLGAGDTAFDCATSALRCGALRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KDGKIVAMQ 407
Cdd:PRK12809 448 DVEGKrVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACdEDGRLTAVG 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 408 FVRTEQDETGNWVEDEEQTV-----RLKADVVISAFGSVLEDPKVKEALSpIKFNRWGL---PEVNPETMQTSEPWVFAG 479
Cdd:PRK12809 528 LIRTAMGEPGPDGRRRPRPVagsefELPADVLIMAFGFQAHAMPWLQGSG-IKLDKWGLiqtGDVGYLPTQTHLKKVFAG 606
|
490 500
....*....|....*....|.
gi 25140985 480 GDVVGMANTTVESVNDGKQAS 500
Cdd:PRK12809 607 GDAVHGADLVVTAMAAGRQAA 627
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
19-500 |
3.39e-46 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 176.86 E-value: 3.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 19 NPRVQAHATLRSTAAKKLDK-KHWKRNTDKNCFTCEKLESNFDDIKHTTLGERgALREAVRCLKCAD-APCQKSCPTSLD 96
Cdd:PRK12769 167 QPWHASTAAQEMPAMSKVEQmQATPPRGEPDKLAIEARKTGFDEIYLPFRADQ-AQREASRCLKCGEhSICEWTCPLHNH 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 97 IKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNLHAaEEGPINIGGLQQFATEVFKAM----NIPQIR 172
Cdd:PRK12769 246 IPQWIELVKAGNIDAAVELSHQTNSLPEITGRVCPQDRLCEGACTLRD-EYGAVTIGNIERYISDQALAKgwrpDLSQVT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 173 nPSlpppehmpeaySAKIALFGAGPASISCASFLARLGYSnITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLG 252
Cdd:PRK12769 325 -KS-----------DKRVAIIGAGPAGLACADVLARNGVA-VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMG 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 253 VKIICGKSLSTDeMTLSSLKENgYRAAFIGIGLPEPKKDHIFQglTQVQGFYtskDFLPLVAKSSKTGM---CACHSPLP 329
Cdd:PRK12769 392 IEFELNCEVGKD-ISLESLLED-YDAVFVGVGTYRSMKAGLPN--EDAPGVY---DALPFLIANTKQVMgleELPEEPFI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 330 SIRGA-VIVLGAGDTAFDCATSALRCGALRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKD-GKIVAMQ 407
Cdd:PRK12769 465 NTAGLnVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEqGHVCGIR 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 408 FVRT---EQDETGNW----VEDEEQTvrLKADVVISAFG-SVLEDPKVKEAlsPIKFNRWGLPEVNPET---MQTSEPWV 476
Cdd:PRK12769 545 FLRTrlgEPDAQGRRrpvpIPGSEFV--MPADAVIMAFGfNPHGMPWLESH--GVTVDKWGRIIADVESqyrYQTSNPKI 620
|
490 500
....*....|....*....|....
gi 25140985 477 FAGGDVVGMANTTVESVNDGKQAS 500
Cdd:PRK12769 621 FAGGDAVRGADLVVTAMAEGRHAA 644
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
58-168 |
1.92e-44 |
|
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.
Pssm-ID: 434132 [Multi-domain] Cd Length: 113 Bit Score: 156.16 E-value: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 58 NFDDIkHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCV 137
Cdd:pfam14691 4 NFEEV-ALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQCE 82
|
90 100 110
....*....|....*....|....*....|.
gi 25140985 138 GGCNLHAAEEGPINIGGLQQFATEVFKAMNI 168
Cdd:pfam14691 83 GACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
75-507 |
1.38e-40 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 162.31 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 75 EAVRCLKCADAPCQ------------KSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNl 142
Cdd:PRK12779 186 EVMRDKQCDDKPCElgvlvqgkaepkGGCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCT- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 143 HAAEegPINIGGLQQFATEVFKAMNiPQIRNPSLPPPEHMPEAYSAKIALFGAGPASISCASFLARLGYSnITIFEKQEY 222
Cdd:PRK12779 265 HTKR--PIEIGQLEWYLPQHEKLVN-PNANERFAGRISPWAAAVKPPIAVVGSGPSGLINAYLLAVEGFP-VTVFEAFHD 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 223 VGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKI----ICGKSlstdeMTLSSLKENGYRAAFIGIGLPEPKkdhiFQGL- 297
Cdd:PRK12779 341 LGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFvknfVVGKT-----ATLEDLKAAGFWKIFVGTGAGLPT----FMNVp 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 298 -TQVQGFYTSKDFLPLVaksskTGMCACH----SPLPSIRGA-VIVLGAGDTAFDCATSALRCGALrVFIVFRKGFVNIR 371
Cdd:PRK12779 412 gEHLLGVMSANEFLTRV-----NLMRGLDddyeTPLPEVKGKeVFVIGGGNTAMDAARTAKRLGGN-VTIVYRRTKSEMP 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 372 AVPEEMELAKEEKCEFLPFLSPRKVIvKDGKivaMQFVRT---------EQDETGNWV-EDEEQTVRLKADVVISAFGSV 441
Cdd:PRK12779 486 ARVEELHHALEEGINLAVLRAPREFI-GDDH---THFVTHalldvnelgEPDKSGRRSpKPTGEIERVPVDLVIMALGNT 561
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25140985 442 lEDPKVKEALSPIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMANTTVESVNDGKQASWYIHKHI 507
Cdd:PRK12779 562 -ANPIMKDAEPGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAAKEIVGEI 626
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
534-838 |
1.43e-34 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 134.01 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 534 SVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKDiVTNVSPRIIRgTTSGPLYGPGqssFLNIELi 613
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQ-PGNPTPRVFR-LPEGVLNRMG---LNNPGL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 614 sEKTAAYWCHSVTELKADFPdniliaSIMCSYNKSDWMELSKMAEASG--ADALELNLSCPHGMGERgmglACGQDPELV 691
Cdd:pfam01180 77 -DAVLAELLKRRKEYPRPDL------GINLSKAGMTVDDYVEVARKIGpfADYIELNVSCPNTPGLR----ALQTDPELA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 692 RNICRWVRQAVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATN-TVSGLMGLKADGTPWPAVGigrRTTYGGVSGTAI 770
Cdd:pfam01180 146 AILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINaTNTTVRGMRIDLKTEKPIL---ANGTGGLSGPPI 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25140985 771 RPIALRAVTAIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:pfam01180 223 KPIALKVIRELYQRTgPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
189-510 |
1.56e-32 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 130.11 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 189 KIALFGAGPASISCASFLARLGYSnITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGV------KIICGKSLS 262
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYLACLGYE-VHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVvfhtrtKVCCGEPLH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 263 TDE--------MTLSSLKENgYRAAFIGIGLPEPKKDHIfQGlTQVQGFYTSKDFLpLVAKSSKTGMcACHSPLPSIRGA 334
Cdd:PRK12770 99 EEEgdefveriVSLEELVKK-YDAVLIATGTWKSRKLGI-PG-EDLPGVYSALEYL-FRIRAAKLGY-LPWEKVPPVEGK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 335 -VIVLGAGDTAFDCATSALRCGALRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIvKDGKIVAMQFVRT-- 411
Cdd:PRK12770 174 kVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRII-GEGRVEGVELAKMrl 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 412 -EQDETGNW----VEDEEQTvrLKADVVISAFGSVLEDPKVKEALSpIKFNRWGLPEVNpETMQTSEPWVFAGGDVVGMA 486
Cdd:PRK12770 253 gEPDESGRPrpvpIPGSEFV--LEADTVVFAIGEIPTPPFAKECLG-IELNRKGEIVVD-EKHMTSREGVFAAGDVVTGP 328
|
330 340
....*....|....*....|....
gi 25140985 487 NTTVESVNDGKQASWYIHKHIQAQ 510
Cdd:PRK12770 329 SKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
946-1004 |
7.73e-29 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 434137 [Multi-domain] Cd Length: 59 Bit Score: 109.68 E-value: 7.73e-29
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 25140985 946 ALIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTVSDTCTGCTLCLSVCPIMDCIRM 1004
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDDCITM 59
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
662-819 |
4.70e-23 |
|
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.
Pssm-ID: 240089 Cd Length: 327 Bit Score: 101.42 E-value: 4.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 662 ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAV-----RVPFFAKLTPNVTD--IVSIARAAKEGGADGVTA 734
Cdd:cd04738 161 ADYLVVNVSSPNTPGLRDL-----QGKEALRELLTAVKEERnklgkKVPLLVKIAPDLSDeeLEDIADVALEHGVDGIIA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 735 TNTV---SGLMGLKAdgtpwpavgigrRTTYGGVSGTAIRPIALRAVTAIARALPG-FPILATGGIDSAESGLQFLHSGA 810
Cdd:cd04738 236 TNTTisrPGLLRSPL------------ANETGGLSGAPLKERSTEVLRELYKLTGGkIPIIGVGGISSGEDAYEKIRAGA 303
|
....*....
gi 25140985 811 SVLQVCSAI 819
Cdd:cd04738 304 SLVQLYTGL 312
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
559-817 |
2.06e-20 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 90.34 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 559 MIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRgttsgplygpgqssflnielisektaaywchsvteLKADFPDNILI 638
Cdd:cd04722 17 LAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLK-----------------------------------EVAAETDLPLG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 639 ASIMCSYNKSDWMELSKMAEASGADALELNLSCPHGmgergmglacgqdPELVRNICRWVRQAVR-VPFFAKLTPNVTDI 717
Cdd:cd04722 62 VQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL-------------AREDLELIRELREAVPdVKVVVKLSPTGELA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 718 vsiARAAKEGGADGVTATNtvsglmglkadgtpwpavgigrrttYGGVSGTAIRPIALRAVTAIARALPGFPILATGGID 797
Cdd:cd04722 129 ---AAAAEEAGVDEVGLGN-------------------------GGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGIN 180
|
250 260
....*....|....*....|
gi 25140985 798 SAESGLQFLHSGASVLQVCS 817
Cdd:cd04722 181 DPEDAAEALALGADGVIVGS 200
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
662-838 |
2.69e-19 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 90.61 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 662 ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAV-----RVPFFAKLTPNVTD--IVSIARAAKEGGADGVTA 734
Cdd:PRK05286 170 ADYFTVNISSPNTPGLRDL-----QYGEALDELLAALKEAQaelhgYVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 735 TNTV---SGLMGLK-ADGTpwpavgigrrttyGGVSGTAIRPIALRAVTAIARALPG-FPILATGGIDSAESGLQFLHSG 809
Cdd:PRK05286 245 TNTTlsrDGLKGLPnADEA-------------GGLSGRPLFERSTEVIRRLYKELGGrLPIIGVGGIDSAEDAYEKIRAG 311
|
170 180
....*....|....*....|....*....
gi 25140985 810 ASVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:PRK05286 312 ASLVQIYSGLIYEGPGLVKEIVRGLARLL 340
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
535-838 |
2.48e-18 |
|
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: 86.61 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 535 VEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGFALTKTFSLDKdivtnvspriiRGTTSGPLYGPGQSSFLNIELIS 614
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAG-----------RPGNPEPRYYAFPLGSINSLGLP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 615 EKTAAYWCHSVTElkadfpdnilIASIMCSYNKSDWMELSKMAE-------------ASGADALELNLSCPH--GMGERG 679
Cdd:cd04741 70 NLGLDYYLEYIRT----------ISDGLPGSAKPFFISVTGSAEdiaamykkiaahqKQFPLAMELNLSCPNvpGKPPPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 680 MglacgqDPELVRNICRWVRQAVRVPFFAKLTPnVTDIVSIARAAK--EGGADG---VTATNTV-SGLMgLKADGTpwpA 753
Cdd:cd04741 140 Y------DFDATLEYLTAVKAAYSIPVGVKTPP-YTDPAQFDTLAEalNAFACPisfITATNTLgNGLV-LDPERE---T 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 754 VGIGRRTTYGGVSGTAIRPIALRAVTAIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCT 832
Cdd:cd04741 209 VVLKPKTGFGGLAGAYLHPLALGNVRTFRRLLPSeIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEK 288
|
....*.
gi 25140985 833 GLKALL 838
Cdd:cd04741 289 ELEDIW 294
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
532-852 |
8.94e-18 |
|
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.
Pssm-ID: 240090 Cd Length: 325 Bit Score: 85.74 E-value: 8.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 532 DISVEMAGLRFPNPFGLASATPATSTPMIRRAFEAGWGfALTkTFSLDKDIVTNVSPRIIRGTTSGPLYGPGQSSFLNIE 611
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAG-AIV-LPSLFEEQIEREAQELDRFLTYGSSFAEALSYFPEYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 612 LISEKTAAYWCHsVTELKA--DFPdniLIASIMCSYNkSDWMELSKMAEASGADALELNLscphgmgergmgLACGQDPE 689
Cdd:cd04739 79 RYNLGPEEYLEL-IRRAKRavSIP---VIASLNGVSA-GGWVDYARQIEEAGADALELNI------------YALPTDPD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 690 LVRN--------ICRWVRQAVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVsglmglkadgtPWPAVGIGRRTT 761
Cdd:cd04739 142 ISGAeveqryldILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRF-----------YQPDIDLETLEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 762 YGGV--SGTAIRPIALRAVtAIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLY 839
Cdd:cd04739 211 VPNLllSSPAEIRLPLRWI-AILSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWME 289
|
330
....*....|...
gi 25140985 840 LKSIEELADWDGQ 852
Cdd:cd04739 290 EHGYESVQQLRGS 302
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
535-818 |
1.56e-17 |
|
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: 85.22 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 535 VEMAGLRFPNPFGLASATPATSTpMIRRAFEAGWGFALTKTFSlDKDIVTNVSPRIIRGttsgplygPGQSSFLNIELIS 614
Cdd:TIGR01036 48 VTVLGLKFPNPLGLAAGFDKDGE-AIDALGAMGFGFLEIGTVT-PKPQPGNPRPRLFRL--------IEDEALINRMGFN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 615 EKTAAYWCHSVTELKADFPDNILIAS---IMCSYNKSDWMELSKMAEASgADALELNLSCPHGMGERGMglacgQDPELV 691
Cdd:TIGR01036 118 NHGADVLVERLKRARYKGPIGINIGKnkdTPSEDAKEDYAACLRKLGPL-ADYLVVNVSSPNTPGLRDL-----QYKAEL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 692 RNICRWVRQ-------AVRVPFFAKLTPNVT--DIVSIARAAKEGGADGVTATNTV---SGLMGLKADGTPwpavgigrr 759
Cdd:TIGR01036 192 RDLLTAVKQeqdglrrVHRVPVLVKIAPDLTesDLEDIADSLVELGIDGVIATNTTvsrSLVQGPKNSDET--------- 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25140985 760 ttyGGVSGtaiRPIALRAVTAIAR---ALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSA 818
Cdd:TIGR01036 263 ---GGLSG---KPLQDKSTEIIRRlyaELQGrLPIIGVGGISSAQDALEKIRAGASLLQIYSG 319
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
532-852 |
3.45e-17 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 84.15 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 532 DISVEMAGLRFPNPFgLASATPAT-STPMIRRAFEAGWGFALTKtfSLDKDIVTNVSPRIIRGTTSGPLYGPGQSSFLNI 610
Cdd:PRK07565 2 DLSTTYLGLTLRNPL-VASASPLSeSVDNVKRLEDAGAGAVVLK--SLFEEQIRHEAAELDRHLTHGTESFAEALDYFPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 611 ELISE-KTAAYWCHsVTELKA--DFPdniLIASIMCSYNkSDWMELSKMAEASGADALELNLSCPHGmgerGMGLACGQD 687
Cdd:PRK07565 79 PAKFYvGPEEYLEL-IRRAKEavDIP---VIASLNGSSA-GGWVDYARQIEQAGADALELNIYYLPT----DPDISGAEV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 688 PELVRNICRWVRQAVRVPFFAKLTPNVTDIVSIARAAKEGGADGVTATNTVsglmglkadgtPWPAVGIGRRTTYGGV-- 765
Cdd:PRK07565 150 EQRYLDILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRF-----------YQPDIDLETLEVVPGLvl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 766 SGTAIRPIALRAVtAIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEE 845
Cdd:PRK07565 219 STPAELRLPLRWI-AILSGRVGADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERHGYES 297
|
....*..
gi 25140985 846 LADWDGQ 852
Cdd:PRK07565 298 LQQFRGS 304
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
620-852 |
2.44e-13 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 71.91 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 620 YWCHSVTELKADFPDNILIASI--MCsynKSDWMELSKMAEASG-ADALELNLSCPHGMGERGMGLacgqDPELVRNICR 696
Cdd:PRK02506 78 YYLDYVLELQKKGPNKPHFLSVvgLS---PEETHTILKKIQASDfNGLVELNLSCPNVPGKPQIAY----DFETTEQILE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 697 WVRQAVRVPFFAKLTPNVtDIVSIARAA---KEGGADGVTATNTV-SGLMGLKADGTpwpaVGIGRRTTYGGVSGTAIRP 772
Cdd:PRK02506 151 EVFTYFTKPLGVKLPPYF-DIVHFDQAAaifNKFPLAFVNCINSIgNGLVIDPEDET----VVIKPKNGFGGIGGDYIKP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 773 IALRAVTAIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELADWDG 851
Cdd:PRK02506 226 TALANVRAFYQRLnPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRG 305
|
.
gi 25140985 852 Q 852
Cdd:PRK02506 306 K 306
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
948-1008 |
2.85e-11 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 60.45 E-value: 2.85e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25140985 948 IDEEMCINCGKCYMTCNDsgyQAIQFDPETHLPTVSDTCTGCTLCLSVCPImDCIRMVSRA 1008
Cdd:COG1144 27 VDEDKCIGCGLCWIVCPD---GAIRVDDGKYYGIDYDYCKGCGICAEVCPV-KAIEMVPEE 83
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
945-1007 |
8.52e-11 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 58.59 E-value: 8.52e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25140985 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVSDTCTGCTLCLSVCPiMDCIRMVSR 1007
Cdd:COG1149 5 IPVIDEEKCIGCGLCVEVCP---EGAIKLDDGGAPVVDPDLCTGCGACVGVCP-TGAITLEER 63
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
189-482 |
1.75e-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: 63.11 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 189 KIALFGAGPASISCASFLARLGYSnITIFEKQE---YVGGLSTSEIPQFRLPYDVVNFEIELMKDL---------GVKII 256
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGK-VTLIEDEGtcpYGGCVLSKALLGAAEAPEIASLWADLYKRKeevvkklnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 257 CGKS----------LSTDEMTLSSLKENGYRAAFIGIG-------LPEPKKDHIFQGLTqvqgfYTSKDFLPLVAKSSKt 319
Cdd:pfam07992 81 LGTEvvsidpgakkVVLEELVDGDGETITYDRLVIATGarprlppIPGVELNVGFLVRT-----LDSAEALRLKLLPKR- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 320 gmcachsplpsirgaVIVLGAGDTAFDCATSALRCGAlRVFIVFRKGFVNiRAVPEEMELAKEEKceflpfLSPRKVIVK 399
Cdd:pfam07992 155 ---------------VVVVGGGYIGVELAAALAKLGK-EVTLIEALDRLL-RAFDEEISAALEKA------LEKNGVEVR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 400 DGKIVamqfVRTEQDETGNWVEDEEQTvRLKADVVISAFGSVLEDPKVKEAlsPIKFNRWGLPEVNpETMQTSEPWVFAG 479
Cdd:pfam07992 212 LGTSV----KEIIGDGDGVEVILKDGT-EIDADLVVVAIGRRPNTELLEAA--GLELDERGGIVVD-EYLRTSVPGIYAA 283
|
...
gi 25140985 480 GDV 482
Cdd:pfam07992 284 GDC 286
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
940-1005 |
5.74e-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: 59.04 E-value: 5.74e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25140985 940 IMEQVVALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVSDTCTGCTLCLSVCPImDCIRMV 1005
Cdd:TIGR01944 102 IQPPMVALIDEDNCIGCTKCIQACP---VDAIVGAAKAMHTVIADECTGCDLCVEPCPT-DCIEMI 163
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
945-1009 |
4.30e-09 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 57.26 E-value: 4.30e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25140985 945 VALIDEEMCINCGKCYMTCNdsgYQAIqFDPETHLPTV-SDTCTGCTLCLSVCPImDCIRMVSRAT 1009
Cdd:PRK05113 108 VAFIDEDNCIGCTKCIQACP---VDAI-VGATKAMHTViSDLCTGCDLCVAPCPT-DCIEMIPVAE 168
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
944-1008 |
5.47e-09 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 57.81 E-value: 5.47e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25140985 944 VVALIDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTVS-DTCTGCTLCLSVCPiMDCIRMVSRA 1008
Cdd:COG1145 175 AKAVIDAEKCIGCGLCVKVC---PTGAIRLKDGKPQIVVDpDKCIGCGACVKVCP-VGAISLEPKE 236
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
940-1011 |
9.51e-09 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 57.31 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 940 IMEQVVALI-----DEEMCINCGKCYmtcndsgyQAIQFD----PETHLPTV-SDTCTGCTLCLSVCPiMDCIRMVSRAT 1009
Cdd:COG2878 121 IKDCRAAVIggpkgCEYGCIGCGDCI--------KACPFDaivgAAKGMHTVdEDKCTGCGLCVEACP-VDCIEMVPVSP 191
|
..
gi 25140985 1010 PY 1011
Cdd:COG2878 192 TV 193
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
945-1005 |
1.83e-08 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 56.73 E-value: 1.83e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25140985 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVSDTCTGCTLCLSVCPImDCIRMV 1005
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACP---VDAIVGAPKQMHTVLADLCTGCDLCVPPCPV-DCIDMV 135
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
646-810 |
2.95e-08 |
|
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: 55.58 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 646 NKSDWM-ELSKMAEASGADALELNLSCP-----HGmgerGMGLACGQDPELVRNICRWVRQAVRVPFFAK---LTPNVTD 716
Cdd:cd02801 64 SDPETLaEAAKIVEELGADGIDLNMGCPspkvtKG----GAGAALLKDPELVAEIVRAVREAVPIPVTVKirlGWDDEEE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 717 IVSIARAAKEGGADGVtatnTVSGlmglkadgtpwpavgigrRTT---YggvsgtaiRPIALRAVTAIARALPGFPILAT 793
Cdd:cd02801 140 TLELAKALEDAGASAL----TVHG------------------RTReqrY--------SGPADWDYIAEIKEAVSIPVIAN 189
|
170
....*....|....*...
gi 25140985 794 GGIDSAESGLQFL-HSGA 810
Cdd:cd02801 190 GDIFSLEDALRCLeQTGV 207
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
646-810 |
5.21e-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: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 646 NKSDWM-ELSKMAEASGADALELNLSCPHGMGERGMGLAC-GQDPELVRNICRWVRQAVRVPFFAKLT----PNVTDIVS 719
Cdd:pfam01207 63 SDPALLaEAAKLVEDRGADGIDINMGCPSKKVTRGGGGAAlLRNPDLVAQIVKAVVKAVGIPVTVKIRigwdDSHENAVE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 720 IARAAKEGGADGVtatnTVSGlmglkadgtpwpavgigrRTTYGGVSGTAirpiALRAVTAIARALPgFPILATGGIDSA 799
Cdd:pfam01207 143 IAKIVEDAGAQAL----TVHG------------------RTRAQNYEGTA----DWDAIKQVKQAVS-IPVIANGDITDP 195
|
170
....*....|..
gi 25140985 800 ESGLQFL-HSGA 810
Cdd:pfam01207 196 EDAQRCLaYTGA 207
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
533-818 |
6.87e-08 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 55.90 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 533 ISVEMAGLRFPNPFGLASATPATStpmirRAFEA----GWGFALTKTfsldkdiVT------NVSPRIIRGTTSGPLYGP 602
Cdd:PLN02826 74 LGVEVWGRTFSNPIGLAAGFDKNA-----EAVEGllglGFGFVEIGS-------VTplpqpgNPKPRVFRLREEGAIINR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 603 GQSSFLNIELISEKTAAY-----------WCHSVTELKADFPDNILIASIMCSYNKsdwmeLSKMAEA----------SG 661
Cdd:PLN02826 142 YGFNSEGIVAVAKRLGAQhgkrkldetssSSFSSDDVKAGGKAGPGILGVNLGKNK-----TSEDAAAdyvqgvralsQY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 662 ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVR---------QAVRVPFFAKLTPNVT--DIVSIARAAKEGGAD 730
Cdd:PLN02826 217 ADYLVINVSSPNTPGLRKL-----QGRKQLKDLLKKVLaardemqwgEEGPPPLLVKIAPDLSkeDLEDIAAVALALGID 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 731 GVTATNTVSGlmglkadgTPWPAVGIGRRTTYGGVSGTAIRPIALRAVTAIARALPG-FPILATGGIDSAESGLQFLHSG 809
Cdd:PLN02826 292 GLIISNTTIS--------RPDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGkIPLVGCGGVSSGEDAYKKIRAG 363
|
....*....
gi 25140985 810 ASVLQVCSA 818
Cdd:PLN02826 364 ASLVQLYTA 372
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
649-810 |
1.30e-07 |
|
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: 54.71 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 649 DWM-ELSKMAEASGADALELNLSCP------HGMGergmglAC-GQDPELVRNICRWVRQAVRVPFFAK----LTPNVTD 716
Cdd:COG0042 74 EELaEAARIAEELGADEIDINMGCPvkkvtkGGAG------AAlLRDPELVAEIVKAVVEAVDVPVTVKirlgWDDDDEN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 717 IVSIARAAKEGGADGV-----TATNTVSGlmglKADgtpWPAVGigrrttyggvsgtairpiALRAVTAIaralpgfPIL 791
Cdd:COG0042 148 ALEFARIAEDAGAAALtvhgrTREQRYKG----PAD---WDAIA------------------RVKEAVSI-------PVI 195
|
170 180
....*....|....*....|
gi 25140985 792 ATGGIDSAESGLQFL-HSGA 810
Cdd:COG0042 196 GNGDIFSPEDAKRMLeETGC 215
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
948-1008 |
1.47e-07 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 49.32 E-value: 1.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25140985 948 IDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTV--SDTCTGCTLCLSVCPiMDCIRMVSRA 1008
Cdd:COG1146 5 IDTDKCIGCGACVEVC---PVDVLELDEEGKKALVinPEECIGCGACELVCP-VGAITVEDDE 63
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
194-238 |
1.48e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 49.45 E-value: 1.48e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 25140985 194 GAGPASISCASFLARLGYSnITIFEKQEYVGGLSTS-EIPQFRLPY 238
Cdd:pfam13450 3 GAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSyRVPGYVFDY 47
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
931-1005 |
2.02e-07 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 50.86 E-value: 2.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25140985 931 YLGTFGEMSIMEQVVALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVSDTCTGCTLCLSVCPiMDCIRMV 1005
Cdd:cd10549 58 ELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCP---VDAITLEDELEIVIDKEKCIGCGICAEVCP-VNAIKLV 128
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
948-997 |
8.67e-07 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 46.86 E-value: 8.67e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 25140985 948 IDEEMCINCGKCYMTC--NDSGYQAIQFDPET-HLPTVSDTCTGCTLCLSVCP 997
Cdd:pfam13237 4 IDPDKCIGCGRCTAACpaGLTRVGAIVERLEGeAVRIGVWKCIGCGACVEACP 56
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
953-997 |
9.93e-07 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 46.37 E-value: 9.93e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 25140985 953 CINCGKCYMTCNdsgYQAIQFDPETHLPTV------SDTCTGCTLCLSVCP 997
Cdd:pfam12838 1 CIGCGACVAACP---VGAITLDEVGEKKGTktvvidPERCVGCGACVAVCP 48
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
950-1004 |
1.15e-06 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 46.66 E-value: 1.15e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 25140985 950 EEMCINCGKCYMTCNdsgYQAIQFDPETHLPTV---SDTCTGCTLCLSVCPiMDCIRM 1004
Cdd:COG1143 1 EDKCIGCGLCVRVCP---VDAITIEDGEPGKVYvidPDKCIGCGLCVEVCP-TGAISM 54
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
939-997 |
1.46e-06 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 46.58 E-value: 1.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 25140985 939 SIMEQVVALIDEEMCINCGKCYMTCNDsgyQAIQFDpETHLPTVSDTCTGCTLCLSVCP 997
Cdd:COG2221 3 GIIGTWPPKIDEEKCIGCGLCVAVCPT---GAISLD-DGKLVIDEEKCIGCGACIRVCP 57
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
948-1008 |
1.80e-06 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 46.57 E-value: 1.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25140985 948 IDEEMCINCGKCYMTCN----DSGYQAIQFDPethlptvsDTCTGCTLCLSVCPImDCIRMVSRA 1008
Cdd:COG4231 19 IDEDKCTGCGACVKVCPadaiEEGDGKAVIDP--------DLCIGCGSCVQVCPV-DAIKLEKRV 74
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
947-1005 |
2.08e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 47.96 E-value: 2.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 25140985 947 LIDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTVSDTCTGCTLCLSVCPiMDCIRMV 1005
Cdd:cd10550 76 VVDEDKCIGCGMCVEAC---PFGAIRVDPETGKAIKCDLCGGDPACVKVCP-TGALEFV 130
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
945-1005 |
2.80e-06 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 47.77 E-value: 2.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHlptVSDTCTGC---------TLCLSVCPImDCIRMV 1005
Cdd:cd04410 74 IVLIDEDKCIGCGSCVEACP---YGAIVFDPEPG---KAVKCDLCgdrldeglePACVKACPT-GALTFG 136
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
944-1004 |
8.25e-06 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 44.72 E-value: 8.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25140985 944 VVALIDEEMCINCGKCYMTCNdsgYQAIQFDPETHLpTVSDTCTGCTLCLSVCPiMDCIRM 1004
Cdd:COG2768 4 GKPYVDEEKCIGCGACVKVCP---VGAISIEDGKAV-IDPEKCIGCGACIEVCP-VGAIKI 59
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
945-1005 |
8.77e-06 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 46.45 E-value: 8.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25140985 945 VALIDEEMCINCGKCYMTCNdsgYQAIqFDPETHLPTV-SDTCTGCTLCLSVCPImDCIRMV 1005
Cdd:PRK08764 79 VAWIVEADCIGCTKCIQACP---VDAI-VGGAKHMHTViAPLCTGCELCVPACPV-DCIELH 135
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
945-997 |
9.17e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 46.86 E-value: 9.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 945 VALIDEEMCIN------CGKCYMTCNDSGYqAIQFDPETHLPTV-SDTCTGCTLCLSVCP 997
Cdd:cd16373 85 VAVIDKDRCLAwqggtdCGVCVEACPTEAI-AIVLEDDVLRPVVdEDKCVGCGLCEYVCP 143
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
949-1005 |
1.38e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 45.73 E-value: 1.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 25140985 949 DEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVsdtCTGCTLCLSVCPiMDCIRMV 1005
Cdd:cd16370 81 DKEKCIGCGNCVKACI---VGAIFWDEETNKPII---CIHCGYCARYCP-HDVLAME 130
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
335-484 |
1.78e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 47.81 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 335 VIVLGAGDTAFDCATSALRCGAlRVFIVFRKGfvNIRAVPEEMELAKE-EKCEFLPflspRKVIVK---DGKIVAMQFVR 410
Cdd:COG0492 144 VVVVGGGDSALEEALYLTKFAS-KVTLIHRRD--ELRASKILVERLRAnPKIEVLW----NTEVTEiegDGRVEGVTLKN 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25140985 411 TEQDETgnwvedeeqtVRLKADVVISAFGSvleDPK---VKEAlsPIKFNRWGLPEVNpETMQTSEPWVFAGGDVVG 484
Cdd:COG0492 217 VKTGEE----------KELEVDGVFVAIGL---KPNtelLKGL--GLELDEDGYIVVD-EDMETSVPGVFAAGDVRD 277
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
194-252 |
1.79e-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: 1.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25140985 194 GAGPASISCASFLARLGYSnITIFEKQEYVGG-LSTSEIPQFRL---PYDVVNFEI--ELMKDLG 252
Cdd:COG1233 10 GAGIGGLAAAALLARAGYR-VTVLEKNDTPGGrARTFERPGFRFdvgPSVLTMPGVleRLFRELG 73
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
926-997 |
1.79e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 48.70 E-value: 1.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25140985 926 GKSLQYLGtfGEMSIMEQVVALIDEEMCINCGKCYMTCNdsgYQAIQFDpETHLPTVSDT-CTGCTLCLSVCP 997
Cdd:COG1148 473 ARAIQLLS--KGELGVEPSVAEVDPEKCTGCGRCVEVCP---YGAISID-EKGVAEVNPAlCKGCGTCAAACP 539
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
190-484 |
4.64e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 47.09 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 190 IALFGAGPASISCASFLARLGYsNITIFEKQEYvGG-------------LSTSEI-------PQFRLPYDV--VNF---- 243
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGK-KVALIEKGPL-GGtclnvgcipskalIAAAEAfheakhaEEFGIHADGpkIDFkkvm 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 244 --------------EIELMKDLGVKIICGKSLSTDEMTLSsLKENGYRAAFIGI----------GLPEPKKDHIfqgltq 299
Cdd:PRK06292 84 arvrrerdrfvggvVEGLEKKPKIDKIKGTARFVDPNTVE-VNGERIEAKNIVIatgsrvppipGVWLILGDRL------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 300 vqgfYTSKDFLPLvakssktgmcachSPLPSirgAVIVLGAG----DTAFdcATSALrcGAlRVFIVFRKGFVniraVP- 374
Cdd:PRK06292 157 ----LTSDDAFEL-------------DKLPK---SLAVIGGGviglELGQ--ALSRL--GV-KVTVFERGDRI----LPl 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 375 EEMELAKEekceFLPFLSPRKVIVKDGKIVAmqfVRTEQDETGNWVEDEEQTVRLKADVVISAFG--SVLEDPKVKEAls 452
Cdd:PRK06292 208 EDPEVSKQ----AQKILSKEFKIKLGAKVTS---VEKSGDEKVEELEKGGKTETIEADYVLVATGrrPNTDGLGLENT-- 278
|
330 340 350
....*....|....*....|....*....|..
gi 25140985 453 PIKFNRWGLPEVNPeTMQTSEPWVFAGGDVVG 484
Cdd:PRK06292 279 GIELDERGRPVVDE-HTQTSVPGIYAAGDVNG 309
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
407-503 |
4.71e-05 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 47.00 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 407 QFVRTEQDETGNWV--EDEEQTVRLKADVVISAFGSVledPKVK----EALSpIKFNRWGLPEVNpETMQTSEPWVFAGG 480
Cdd:COG1249 231 KVTSVEKTGDGVTVtlEDGGGEEAVEADKVLVATGRR---PNTDglglEAAG-VELDERGGIKVD-EYLRTSVPGIYAIG 305
|
90 100
....*....|....*....|...
gi 25140985 481 DVVGMANTTVESVNDGKQASWYI 503
Cdd:COG1249 306 DVTGGPQLAHVASAEGRVAAENI 328
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
948-1016 |
9.35e-05 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 43.15 E-value: 9.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25140985 948 IDEEMCINCGKCYMTCNdsgYQAIQFDPETHLPTVS----DTCTGCTLCLSVCPImDCIRMVSRATPYQPKRG 1016
Cdd:cd10549 3 YDPEKCIGCGICVKACP---TDAIELGPNGAIARGPeideDKCVFCGACVEVCPT-GAIELTPEGKEYVPKEK 71
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
948-1011 |
1.24e-04 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 42.77 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25140985 948 IDEEMCINCGKCYMTCndsGYQAIQFDPETHLPTVS--------DTCTGCTLCLSVCPImDCIRMVSRATPY 1011
Cdd:cd10549 37 IDEDKCVFCGACVEVC---PTGAIELTPEGKEYVPKekeaeideEKCIGCGLCVKVCPV-DAITLEDELEIV 104
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
952-1002 |
1.63e-04 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 40.23 E-value: 1.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 25140985 952 MCINCGKCYMTCNDSGYQAIQFDPETHLPTVSDTCTGCTLCLSVCPiMDCI 1002
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQTIRGDIAGLACIGCGACVDACP-RGAI 50
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
621-733 |
1.99e-04 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 44.58 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 621 WCHSVTELKADFPDNILIASIMCSYNKSDWM-ELSKMAEASGADALELNLSCPHGMGERGM-GLACGQDPELVRNICRWV 698
Cdd:PRK10415 49 WESDKSRLRMVHIDEPGIRTVQIAGSDPKEMaDAARINVESGAQIIDINMGCPAKKVNRKLaGSALLQYPDLVKSILTEV 128
|
90 100 110
....*....|....*....|....*....|....*....
gi 25140985 699 RQAVRVPFFAKL----TPNVTDIVSIARAAKEGGADGVT 733
Cdd:PRK10415 129 VNAVDVPVTLKIrtgwAPEHRNCVEIAQLAEDCGIQALT 167
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
948-997 |
3.76e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 44.25 E-value: 3.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 25140985 948 IDEEMCINCGKCYMTCndsGYQAIQFDpETHLPTVSDTCTGCTLCLSVCP 997
Cdd:COG4624 88 RDKEKCKNCYPCVRAC---PVKAIKVD-DGKAEIDEEKCISCGQCVAVCP 133
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
937-998 |
4.46e-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: 43.14 E-value: 4.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25140985 937 EMSIMEQVVALIDEEMCINCGKCYMTCNdsgYQAIQFDPeTHLPTVSDTCTGCTLCLSVCPI 998
Cdd:cd03110 50 EEDFVGGKKAFIDQEKCIRCGNCERVCK---FGAILEFF-QKLIVDESLCEGCGACVIICPR 107
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
947-1010 |
6.17e-04 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 41.86 E-value: 6.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25140985 947 LIDEEMCINCGKCYMTCNdsgYQAIQFDPETHlptVSDTCTGC---------TLCLSVCPiMDCIRMVSRATP 1010
Cdd:COG0437 86 LVDYDKCIGCRYCVAACP---YGAPRFNPETG---VVEKCTFCadrldegllPACVEACP-TGALVFGDLDDP 151
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
949-1005 |
6.80e-04 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 40.01 E-value: 6.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 25140985 949 DEEMCINCGKCYMTCNDSgyqAIQFDPETHLPTVSDTCTGCTLCLSVCPiMDCIRMV 1005
Cdd:PRK09624 49 NRDKCVRCYLCYIYCPEP---AIYLDEEGYPVFDYDYCKGCGICANECP-TKAIEMV 101
|
|
| napG |
PRK09476 |
quinol dehydrogenase periplasmic component; Provisional |
947-996 |
9.65e-04 |
|
quinol dehydrogenase periplasmic component; Provisional
Pssm-ID: 236534 [Multi-domain] Cd Length: 254 Bit Score: 42.30 E-value: 9.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25140985 947 LIDEEMCIN-----CGKCYMTCN--DsgyQAI----QFDPETH-----LPTV-SDTCTGCTLCLSVC 996
Cdd:PRK09476 133 LVDQENCLNfqglrCDVCYRVCPliD---KAItlelERNERTGkhaffLPTVhSDACTGCGKCEKAC 196
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
189-252 |
1.02e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 42.95 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25140985 189 KIALFGAGPASISCASFLARLGYSnITIFEKQEYVGGLSTSeipqfrlpYDVVNFEIE---------------LMKDLG 252
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAAS--------FEFGGLPIErfyhhifksdealleLLDELG 70
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
951-1024 |
1.13e-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: 42.76 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 951 EMCINCGKCYMTC---------NDS-------------GYQAIQFDPETHLptVSDTCTGCTLCLSVCPIM-DCIRMVSR 1007
Cdd:COG0247 78 DACVGCGFCRAMCpsykatgdeKDSprgrinllrevleGELPLDLSEEVYE--VLDLCLTCKACETACPSGvDIADLIAE 155
|
90
....*....|....*...
gi 25140985 1008 ATPYQPKRGL-PLAVKPV 1024
Cdd:COG0247 156 ARAQLVERGGrPLRDRLL 173
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
189-230 |
1.31e-03 |
|
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: 42.51 E-value: 1.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 25140985 189 KIALFGAGPASISCASFLARLGYSnITIFEKQEYVGGLSTSE 230
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHE-VTVLEASDRVGGLIRTV 43
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
961-1007 |
1.87e-03 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 39.53 E-value: 1.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 25140985 961 MTCNDS-GYQAIQFDPETH---LPTV-SDTCTGCTLCLSVCPImDCIRMVSR 1007
Cdd:cd10564 89 RSCQDAcPTQAIRFRPRLGgiaLPELdADACTGCGACVSVCPV-GAITLTPL 139
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
951-997 |
1.89e-03 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 39.73 E-value: 1.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 25140985 951 EMCINCGKCYMTCNDSgyqAIQFDPETHLPTVSDTCTGCTLCLSVCP 997
Cdd:PRK09625 59 EICINCFNCWVYCPDA---AILSRDKKLKGVDYSHCKGCGVCVEVCP 102
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
945-997 |
1.93e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 1.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 945 VALIDEEMCiNCGKCYMTC------NDSGYQAIQFDPETHLPTVS-DTCTGCTLCLSVCP 997
Cdd:COG1245 4 IAVVDRDRC-QPKKCNYECikycpvNRTGKEAIEIDEDDGKPVISeELCIGCGICVKKCP 62
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
649-732 |
2.48e-03 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 41.40 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 649 DWMELSKMAEASGADALelNLSCphGMGERGMGLACGQDPELVRNI--CRWVRQAVRVPFFAklTPNVTDIVSIARAAKE 726
Cdd:cd02803 229 EAIEIAKALEEAGVDAL--HVSG--GSYESPPPIIPPPYVPEGYFLelAEKIKKAVKIPVIA--VGGIRDPEVAEEILAE 302
|
....*.
gi 25140985 727 GGADGV 732
Cdd:cd02803 303 GKADLV 308
|
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
945-997 |
4.06e-03 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 38.00 E-value: 4.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 25140985 945 VALIDEEMCINCGKCYMTCNDSgyqAIQFDPETHLPTVSDTCTGCTLCLSVCP 997
Cdd:PRK09623 45 MPVVDESKCVKCYICWKFCPEP---AIYIKEDGYVAIDYDYCKGCGICANECP 94
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
981-1005 |
4.07e-03 |
|
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).
Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 40.23 E-value: 4.07e-03
10 20
....*....|....*....|....*
gi 25140985 981 TVSDTCTGCTLCLSVCPiMDCIRMV 1005
Cdd:NF038196 182 HVTDKCIGCGICAKVCP-VNNIEME 205
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
335-480 |
4.21e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 40.28 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 335 VIVLGAGDTAFDCATSALRCGAlRVFIVFRKGFVNIRA-----------VPEEMELAKEEKCEFLpFLSPRKVIVKDGKI 403
Cdd:pfam13738 158 VVVIGGYNSAVDAALELVRKGA-RVTVLYRGSEWEDRDsdpsyslspdtLNRLEELVKNGKIKAH-FNAEVKEITEVDVS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25140985 404 VAMQFvrteqdetgnwveDEEQTVRLKADVVIsAFG-----SVLEDPKvkealspIKFNRWGLPEVNPETMQTSEPWVFA 478
Cdd:pfam13738 236 YKVHT-------------EDGRKVTSNDDPIL-ATGyhpdlSFLKKGL-------FELDEDGRPVLTEETESTNVPGLFL 294
|
..
gi 25140985 479 GG 480
Cdd:pfam13738 295 AG 296
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
189-227 |
4.36e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 40.64 E-value: 4.36e-03
10 20 30
....*....|....*....|....*....|....*....
gi 25140985 189 KIALFGAGPASISCASFLARLGYSnITIFEKQEYVGGLS 227
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYP-VTVLEADPVVGGIS 43
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
948-1008 |
4.74e-03 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 40.05 E-value: 4.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25140985 948 IDEEMCINCGKCYMTCndsgyqaiqfdpETHLP-----TVSDTCTGCTLCLSVCPImDCIRMVSRA 1008
Cdd:COG0348 207 YDRGDCIDCGLCVKVC------------PMGIDirkgeINQSECINCGRCIDACPK-DAIRFSSRG 259
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
945-1005 |
5.37e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 5.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25140985 945 VALIDEEMCiNCGKCYMTC------NDSGYQAIQFDPETHLPTVS-DTCTGCTLCLSVCPiMDCIRMV 1005
Cdd:PRK13409 4 IAVVDYDRC-QPKKCNYECikycpvVRTGEETIEIDEDDGKPVISeELCIGCGICVKKCP-FDAISIV 69
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
428-487 |
6.90e-03 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 39.79 E-value: 6.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25140985 428 RLKADVVISAFGSVledPKVK-EALSPIKFNRWGLPEVNpETMQTSEPWVFAGGDVVGMAN 487
Cdd:COG0446 206 EIPADLVVVAPGVR---PNTElAKDAGLALGERGWIKVD-ETLQTSDPDVYAAGDCAEVPH 262
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
984-1013 |
7.77e-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: 35.88 E-value: 7.77e-03
10 20 30
....*....|....*....|....*....|
gi 25140985 984 DTCTGCTLCLSVCPiMDCIRMVSRATPYQP 1013
Cdd:COG1143 2 DKCIGCGLCVRVCP-VDAITIEDGEPGKVY 30
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
179-231 |
9.91e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 39.78 E-value: 9.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 25140985 179 PEHMPEaysaKIALFGAGPASISCASFLARLGySNITIFEKQEYVGGLSTSEI 231
Cdd:PRK06292 165 LDKLPK----SLAVIGGGVIGLELGQALSRLG-VKVTVFERGDRILPLEDPEV 212
|
|
| |
