|
Name |
Accession |
Description |
Interval |
E-value |
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
527-829 |
0e+00 |
|
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN, and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239244 Cd Length: 299 Bit Score: 550.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 527 DISVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGLDKDLVTNVSPRIVRGTTSGykygPQQGCFLNIE 606
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSG----RGQIGFNNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 607 LISEKRAEYWLKSIGELKRDFPEKIVIASIMCSFNEEDWTELAIKAEQSGADALELNLSCPHGMGERGMGLACGQDPELV 686
Cdd:cd02940 77 LISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 687 EQISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADGGSAINTVQGLMGLKADSTAwPAIGKEQRTTYGGVSGNATR 766
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTP-PAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640763 767 PMALKAISDIANRV-PGFPILGIGGIDSGEVALQFIHAGATVLQICSSVQNQDFTVIEDYCTAL 829
Cdd:cd02940 236 PIALRAVSQIARAPePGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
527-1008 |
1.31e-132 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 407.02 E-value: 1.31e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 527 DISVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGldkDLVTNVSPRivRGTTSGYKYGPQQGcFLNIE 606
Cdd:PRK08318 3 DLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLG---PPIVNVSSP--RFGALVKEDRRFIG-FNNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 607 LISEKRAEYWLKSIGELKRDFPEKIVIASIMCSFNEEDWTELAIKAEQSGADALELNLSCPHGMGERGMGLACGQDPELV 686
Cdd:PRK08318 77 LITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 687 EQISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADGGSAINTVQGLMGLKADS-TAWPAIGKeqRTTYGGVSGNAT 765
Cdd:PRK08318 157 EMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRmIPMPIVNG--KSSHGGYCGPAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 766 RPMALKAISDIAN--RVPGFPILGIGGIDSGEVALQFIHAGATVLQICSSVQNQDFTVIEDYCTALKAllYLKanpppvd 843
Cdd:PRK08318 235 KPIALNMVAEIARdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSH--YMD------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 844 gpfwdgqspptpvhQKGkpvvrltgegkatlgffgpyqrqrdikmaeLRSqkgalwdaeqvkatppasngapnpaprIKD 923
Cdd:PRK08318 306 --------------EKG------------------------------FAS---------------------------LED 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 924 VIGAALDKIGSYNKLDNKQQKVALIDDDMCINCGKCYMTCADSGYQAIEFDKD-THIPHVNDD-CTGCTLCVSVCPIIDC 1001
Cdd:PRK08318 315 MVGLAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDEDgTRTPEVIEEeCVGCNLCAHVCPVEGC 394
|
....*..
gi 24640763 1002 ITMVPKK 1008
Cdd:PRK08318 395 ITMGEVK 401
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
55-507 |
1.09e-109 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 348.32 E-value: 1.09e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 55 TTLANDFSDIkHTTLSERGALEEAARCLKCADAPCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGLTCGMVCPT 134
Cdd:PRK11749 17 EERAQNFDEV-APGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 135 SDLCVGGCNLQASEaGPINIGGLQQFATEVFKKMGVRQRRTPqaeaNPLSQKIALVGGGPASLSCATFLARLGYrDVTIY 214
Cdd:PRK11749 96 ERLCEGACVRGKKG-EPVAIGRLERYITDWAMETGWVLFKRA----PKTGKKVAVIGAGPAGLTAAHRLARKGY-DVTIF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 215 ERRSYLGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRIETGRSLGtKDLTIQGLLStGHDAVFVGIGLPEPKLNPIF-AG 293
Cdd:PRK11749 170 EARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVG-RDITLDELRA-GYDAVFIGTGAGLPRFLGIPgEN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 294 LqpsNGFYTSKNFLPLVSDGskpglcacKAAAGLPKlhG-NVIVLGAGDTAFDCATSALRCGARRVFVVFRKGSSGIRAV 372
Cdd:PRK11749 248 L---GGVYSAVDFLTRVNQA--------VADYDLPV--GkRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPAS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 373 PEEVELARDERCELLPYLSPRKVIVKDGLITAMEFCRTEQNENDE----WVEDEEQTQRLKANFVISAFGSGLEDQDVKA 448
Cdd:PRK11749 315 EEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMELGEPDAsgrrRVPIEGSEFTLPADLVIKAIGQTPNPLILST 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 449 ALA-PLQFRGELpVVDRVTMQSSVKQVFLGGDLAGVANTTVESVNDGKVAAWSIHCQLQG 507
Cdd:PRK11749 395 TPGlELNRWGTI-IADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEG 453
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
58-502 |
4.99e-108 |
|
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: 342.89 E-value: 4.99e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 58 ANDFSDIkHTTLSERGALEEAARCLKCADAPCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGLTCGMVCPTsdL 137
Cdd:COG0493 2 IKDFREV-YPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 138 CVGGCNLQASEaGPINIGGLQQFATEVFKKMGVRQRRTPqaeANPLSQKIALVGGGPASLSCATFLARLGYrDVTIYERR 217
Cdd:COG0493 79 CEGACVRGIVD-EPVAIGALERFIADKAFEEGWVKPPPP---APRTGKKVAVVGSGPAGLAAAYQLARAGH-EVTVFEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 218 SYLGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRIETGRSLGtKDLTIQGLLStGHDAVFVGIGLPEPKLNPIfaglqP- 296
Cdd:COG0493 154 DKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVG-KDITLDELLE-EFDAVFLATGAGKPRDLGI-----Pg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 297 --SNGFYTSKNFLPLVSDGskpglcacKAAAGLPKLHGNVIVLGAGDTAFDCATSALRCGARRVFVVFRKGSSGIRAVPE 374
Cdd:COG0493 227 edLKGVHSAMDFLTAVNLG--------EAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 375 EVELARDERCELLPYLSPRKVIV-KDGLITAMEFCRTEQNENDE-----WVEDEEQTQRLKANFVISAFGSGLEDQDVKA 448
Cdd:COG0493 299 EVEEALEEGVEFLFLVAPVEIIGdENGRVTGLECVRMELGEPDEsgrrrPVPIEGSEFTLPADLVILAIGQTPDPSGLEE 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 24640763 449 ALA-PLQFRGeLPVVDRVTMQSSVKQVFLGGDLAGVANTTVESVNDGKVAAWSIH 502
Cdd:COG0493 379 ELGlELDKRG-TIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAID 432
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
530-827 |
4.34e-85 |
|
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: 276.16 E-value: 4.34e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 530 VEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGLDKDlVTNVSPRIVRGTTSGYKYGPQQGcFLNIELIS 609
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPR-PGNPLPRVARLPPEGESYPEQLG-ILNSFGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 610 EKRAEYWLKSIGELKRDFPEKIVIASIMCSfNEEDWTELAIKAEQSGADALELNLSCPHGMGERGmglaCGQDPELVEQI 689
Cdd:cd02810 79 NLGLDVWLQDIAKAKKEFPGQPLIASVGGS-SKEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 690 SRWVRKAVKLPFFIKLTPNIT--DIVSIAAAAKRGGADGGSAINTVQGLMGLKADstawPAIGKeqRTTYGGVSGNATRP 767
Cdd:cd02810 154 LKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDLKT----VGPGP--KRGTGGLSGAPIRP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640763 768 MALKAISDIANRVP-GFPILGIGGIDSGEVALQFIHAGATVLQICSSVQNQDFTVIEDYCT 827
Cdd:cd02810 228 LALRWVARLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKK 288
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
527-833 |
8.30e-84 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 276.33 E-value: 8.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 527 DISVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGLDKDLVTNVSPRIVRGTTSGY-KYGPQQGCFLNI 605
Cdd:PLN02495 10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARLRAGANgSAKGRVIGWQNI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 606 ELISEKRAEYWLKSIGELKRDFPEKIVIASIMCSFNEEDWTELAIKAEQSGADALELNLSCPHGMGERGMGLACGQDPEL 685
Cdd:PLN02495 90 ELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVGQDCDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 686 VEQISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADGGSAINTVQGLMGLKADsTAWPAIGKEQRTTYGGVSGNAT 765
Cdd:PLN02495 170 LEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLD-TLRPEPCVEGYSTPGGYSSKAV 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24640763 766 RPMALKAISDIANRVPG-FP----ILGIGGIDSGEVALQFIHAGATVLQICSSVQNQDFTVIEDYCTALKALL 833
Cdd:PLN02495 249 RPIALAKVMAIAKMMKSeFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFM 321
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
527-833 |
4.89e-81 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 265.40 E-value: 4.89e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 527 DISVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTfgldkdlVT------NVSPRIVRgtTsgykygPQQG 600
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKT-------VTpepqpgNPRPRLFR--L------PEDS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 601 CFLNIELISEKRAEYWLKSIGELKRdfPEKIVIASIMCSfNEEDWTELAIKAEQSGADALELNLSCPHGmgeRGMGLACG 680
Cdd:COG0167 66 GLINRMGLNNPGVDAFLERLLPAKR--YDVPVIVNIGGN-TVEDYVELARRLADAGADYLELNISCPNT---PGGGRALG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 681 QDPELVEQISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADGGSAINTVQGlMGLKADSTAwPAIGKEqrttYGGV 760
Cdd:COG0167 140 QDPEALAELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLG-RAIDLETRR-PVLANE----AGGL 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640763 761 SGNATRPMALKAISDIANRVPG-FPILGIGGIDSGEVALQFIHAGATVLQICSSVQNQDFTVIEDYCTALKALL 833
Cdd:COG0167 214 SGPALKPIALRMVREVAQAVGGdIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYL 287
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
70-507 |
1.72e-73 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 250.71 E-value: 1.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 70 SERGALEEAARCLKCADAPCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGLTCGMVCPTSDLCVGGCNLQAsEA 149
Cdd:PRK12831 31 NEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQCEGKCVLGI-KG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 150 GPINIGGLQQFATEVFKKMGVRQRRTPQAEanplSQKIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGGLSAAEIP 229
Cdd:PRK12831 110 EPVAIGKLERFVADWARENGIDLSETEEKK----GKKVAVIGSGPAGLTCAGDLAKMGY-DVTIFEALHEPGGVLVYGIP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 230 QYRLPIDA-VNFEIDLVRDLGVRIETGRSLGtKDLTIQGLLS-TGHDAVFVGIGLPEPKLNPIfAGLQpSNGFYTSKNFL 307
Cdd:PRK12831 185 EFRLPKETvVKKEIENIKKLGVKIETNVVVG-KTVTIDELLEeEGFDAVFIGSGAGLPKFMGI-PGEN-LNGVFSANEFL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 308 PLVSDGSkpglcACKAAAGLPKLHGN-VIVLGAGDTAFDCATSALRCGArRVFVVFRKGSSGIRAVPEEVELARDERCEL 386
Cdd:PRK12831 262 TRVNLMK-----AYKPEYDTPIKVGKkVAVVGGGNVAMDAARTALRLGA-EVHIVYRRSEEELPARVEEVHHAKEEGVIF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 387 LPYLSPRKVIV-KDGLITAMEFCRTEQNENDEW-----VEDEEQTQRLKANFVISAFGS-----------GLEdqdvkaa 449
Cdd:PRK12831 336 DLLTNPVEILGdENGWVKGMKCIKMELGEPDASgrrrpVEIEGSEFVLEVDTVIMSLGTspnplissttkGLK------- 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24640763 450 lapLQFRGELpVVDRVTMQSSVKQVFLGGDLAGVANTTVESVNDGKVAAWSIHCQLQG 507
Cdd:PRK12831 409 ---INKRGCI-VADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSK 462
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
69-507 |
6.86e-65 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 234.25 E-value: 6.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 69 LSERGALEEAARCLKCADAPCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGLTCGMVCPTSDLCVGGCNLQASE 148
Cdd:PRK12778 319 LTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQCESKCIHGKMG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 149 AGPINIGGLQQFATEVFKKMGvrQRRTPQ-AEANplSQKIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGGLSAAE 227
Cdd:PRK12778 399 EEAVAIGYLERFVADYERESG--NISVPEvAEKN--GKKVAVIGSGPAGLSFAGDLAKRGY-DVTVFEALHEIGGVLKYG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 228 IPQYRLPIDAVNFEIDLVRDLGVRIETGRSLGtKDLTIQGLLSTGHDAVFV--GIGLPE----PKLNPIfaGLQPSNGFY 301
Cdd:PRK12778 474 IPEFRLPKKIVDVEIENLKKLGVKFETDVIVG-KTITIEELEEEGFKGIFIasGAGLPNfmniPGENSN--GVMSSNEYL 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 302 TSKNFLPLVSDGSKPGLCACKaaaglpklhgNVIVLGAGDTAFDCATSALRCGARRVFVVFRKGSSGIRAVPEEVELARD 381
Cdd:PRK12778 551 TRVNLMDAASPDSDTPIKFGK----------KVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARLEEVKHAKE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 382 ERCELLPYLSPRKVIV-KDGLITAMEFCRTEQNENDEW-----VEDEEQTQRLKANFVISAFGS-----------GLEdq 444
Cdd:PRK12778 621 EGIEFLTLHNPIEYLAdEKGWVKQVVLQKMELGEPDASgrrrpVAIPGSTFTVDVDLVIVSVGVspnplvpssipGLE-- 698
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24640763 445 dvkaalapLQFRGELpVVDRVtMQSSVKQVFLGGDLAGVANTTVESVNDGKVAAWSIHCQLQG 507
Cdd:PRK12778 699 --------LNRKGTI-VVDEE-MQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSS 751
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
529-833 |
3.30e-64 |
|
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: 219.34 E-value: 3.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 529 SVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGLDKDLvTNVSPRIVRgtTSGykygpqqgCFLN-IEL 607
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPRE-GNPPPRVVE--TPG--------GMLNaIGL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 608 iSEKRAEYWLKSIGELKRDFpEKIVIASIMCSfNEEDWTELAIKAEQSGADALELNLSCPHgmgERGMGLACGQDPELVE 687
Cdd:cd04740 70 -QNPGVEAFLEELLPWLREF-GTPVIASIAGS-TVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDPEAVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 688 QISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADGGSAINTvqgLMGLKADS-TAWPAIGkeqrTTYGGVSGNATR 766
Cdd:cd04740 144 EIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINT---LKGMAIDIeTRKPILG----NVTGGLSGPAIK 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640763 767 PMALKAISDIANRVpGFPILGIGGIDSGEVALQFIHAGATVLQICSSVQnQDFTVIEDYCTALKALL 833
Cdd:cd04740 217 PIALRMVYQVYKAV-EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYL 281
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
60-507 |
6.11e-62 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 218.49 E-value: 6.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 60 DFSDIkHTTLSERGALEEAARCLKCADAPCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGLTCGMVCPTSdlCV 139
Cdd:PRK12810 26 DFKEF-YEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAP--CE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 140 GGCNLqASEAGPINIGGLQQFATEVFKKMGVRQrrtPQAEANPLSQKIALVGGGPASLSCATFLARLGYrDVTIYERRSY 219
Cdd:PRK12810 103 GACTL-NINFGPVTIKNIERYIIDKAFEEGWVK---PDPPVKRTGKKVAVVGSGPAGLAAADQLARAGH-KVTVFERADR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 220 LGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRIETGRSLGtKDLTIQGLLSTgHDAVFVGIGLPEP-KLNpiFAGlQPSN 298
Cdd:PRK12810 178 IGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVG-KDITAEELLAE-YDAVFLGTGAYKPrDLG--IPG-RDLD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 299 GFYTSKNFLP-----LVSDGSKPGLCackaAAGlpKlhgNVIVLGAGDTAFDCATSALRCGARRVfVVF----RKGSSGI 369
Cdd:PRK12810 253 GVHFAMDFLIqntrrVLGDETEPFIS----AKG--K---HVVVIGGGDTGMDCVGTAIRQGAKSV-TQRdimpMPPSRRN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 370 RAVPE-------EVELARDERCELLPYLSPRKVIVKDGLITAMEFCRTEQNEND-EWVEDEEQTqrLKANFVISAFGSGL 441
Cdd:PRK12810 323 KNNPWpywpmklEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGDfEPVEGSEFV--LPADLVLLAMGFTG 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640763 442 EDQDVKAALA-PLQFRGELpVVDRVTMQSSVKQVFLGGDLAGVANTTVESVNDGKVAAWSIHCQLQG 507
Cdd:PRK12810 401 PEAGLLAQFGvELDERGRV-AAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMG 466
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
527-810 |
1.25e-61 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 211.93 E-value: 1.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 527 DISVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGLDKDLvTNVSPRIVRgTTSGykygpqqgcFLN-- 604
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPRE-GNPTPRIAE-TPGG---------MLNai 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 605 ------IELISEKrAEYWLKSIgelkrDFPekiVIASImCSFNEEDWTELAIKAEQSG-ADALELNLSCPHGMGergMGL 677
Cdd:PRK07259 70 glqnpgVDAFIEE-ELPWLEEF-----DTP---IIANV-AGSTEEEYAEVAEKLSKAPnVDAIELNISCPNVKH---GGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 678 ACGQDPELVEQISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADGGSAINTvqgLMGLKAD-STAWPAIGkeqrTT 756
Cdd:PRK07259 137 AFGTDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAIDiKTRKPILA----NV 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 24640763 757 YGGVSGNATRPMALKAISDIANRVpGFPILGIGGIDSGEVALQFIHAGATVLQI 810
Cdd:PRK07259 210 TGGLSGPAIKPIALRMVYQVYQAV-DIPIIGMGGISSAEDAIEFIMAGASAVQV 262
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
49-518 |
2.85e-61 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 219.36 E-value: 2.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 49 HAAPPCTTLANDFSDIKHTTLSERgaleeaaRCLKCADA--PCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGL 126
Cdd:PRK12771 14 EAAFDALTLPDGFSDEIATGPWRH-------KCPVYVDQtpPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 127 TCGMVCPTSdlCVGGCNLQASEAgPINIGGLQQFATEvfkkMGVRQRRTPQAEANPLSQKIALVGGGPASLSCATFLARL 206
Cdd:PRK12771 87 VMGRVCYHP--CESGCNRGQVDD-AVGINAVERFLGD----YAIANGWKFPAPAPDTGKRVAVIGGGPAGLSAAYHLRRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 207 GYRdVTIYERRSYLGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRIETGRSLGTkDLTIQgLLSTGHDAVFVGIGLPEPK 286
Cdd:PRK12771 160 GHA-VTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGVEVRLGVRVGE-DITLE-QLEGEFDAVFVAIGAQLGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 287 LNPIFAGlqPSNGFYTSKNFLPLVSDGskpglcackaaaGLPKLHGNVIVLGAGDTAFDCATSALRCGARRVFVVFRKGS 366
Cdd:PRK12771 237 RLPIPGE--DAAGVLDAVDFLRAVGEG------------EPPFLGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 367 SGIRAVPEEVELARDERCELLPYLSPRKVIVKDGLITAMEFCRTEQNENDE--W---VEDEEQTqrLKANFVISAFGSGL 441
Cdd:PRK12771 303 EDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVITVEKMELDEdgRpspVTGEEET--LEADLVVLAIGQDI 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24640763 442 EDQDVKAALAPLQFRGELpVVDRVTMQSSVKQVFLGGDLA-GVANTTVeSVNDGKVAAWSIHCQLQGLPLDTPAALPL 518
Cdd:PRK12771 381 DSAGLESVPGVEVGRGVV-QVDPNFMMTGRPGVFAGGDMVpGPRTVTT-AIGHGKKAARNIDAFLGGEPYEHRPKREI 456
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
528-814 |
2.79e-55 |
|
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: 194.18 E-value: 2.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 528 ISVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGLDKDLvTNVSPRIVRgTTSGykygpqqgcFLNIEL 607
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRP-GYRNPTIVE-TPCG---------MLNAIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 608 ISEKRAEYWLKSIGELKRDFPEKIvIASIMCSfNEEDWTELAIKAEQSG--ADALELNLSCPHGMGergMGLACGQDPEL 685
Cdd:TIGR01037 70 LQNPGVEAFLEELKPVREEFPTPL-IASVYGS-SVEEFAEVAEKLEKAPpyVDAYELNLSCPHVKG---GGIAIGQDPEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 686 VEQISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADGGSAINTvqgLMGLKAD-STAWPAIGkeqrTTYGGVSGNA 764
Cdd:TIGR01037 145 SADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKIDiKTGKPILA----NKTGGLSGPA 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 24640763 765 TRPMALKAISDIANRVpGFPILGIGGIDSGEVALQFIHAGATVLQICSSV 814
Cdd:TIGR01037 218 IKPIALRMVYDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAV 266
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
52-516 |
7.06e-50 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 188.01 E-value: 7.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 52 PPCTTLANDFSDIK--HTTLSE--RGALEE--AARCLKCaDAPCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLG 125
Cdd:PRK12814 62 PACSTAVSEGMVIEteNAELHAmrRQSLERliEQHCGDC-LGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 126 LTCGMVCPTSdlCVGGCNLQASEAgPINIGGLQQFATEvfKKMGVRQRRTPqaEANPLS-QKIALVGGGPASLSCATFLA 204
Cdd:PRK12814 141 GILGRICPAP--CEEACRRHGVDE-PVSICALKRYAAD--RDMESAERYIP--ERAPKSgKKVAIIGAGPAGLTAAYYLL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 205 RLGYrDVTIYERRSYLGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRIETGRSLGtKDLTIQGLlSTGHDAVFVGIGLPE 284
Cdd:PRK12814 214 RKGH-DVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAMGAEFRFNTVFG-RDITLEEL-QKEFDAVLLAVGAQK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 285 PKLNPIfAGlQPSNGFYTSKNFLPLVSDGSKPglcackaaaglpKLHGNVIVLGAGDTAFDCATSALRCGARRVFVVFRK 364
Cdd:PRK12814 291 ASKMGI-PG-EELPGVISGIDFLRNVALGTAL------------HPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 365 GSSGIRAVPEEVELARDERCELLPYLSPRKVIVKDG--LITAMEFcrtEQNENDEW-------VEDEEQTqrLKANFVIS 435
Cdd:PRK12814 357 TREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGglELTAIKM---QQGEPDESgrrrpvpVEGSEFT--LQADTVIS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 436 AFGSGLeDQDVKAALAPLQFRGELPVVDRVTMQSSVKQVFLGGDLAGVANTTVESVNDGKVAAWSIHCQLQGLPLDTPAA 515
Cdd:PRK12814 432 AIGQQV-DPPIAEAAGIGTSRNGTVKVDPETLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGKPVTAPVQ 510
|
.
gi 24640763 516 L 516
Cdd:PRK12814 511 P 511
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
13-562 |
1.56e-49 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 190.92 E-value: 1.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 13 DIEDLLSLNPRVKTQ-----------CSVvpTKQT-KENKKHWKRNADhAAPPCTTL--------ANDFSDIkHTTLSER 72
Cdd:PRK12775 249 DFKELHARQKRFKSQedranedyahvCNL--EKQLfEEGKRNYKKLKT-LVPHQTPMperdaverARNFKEV-NLGYSLE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 73 GALEEAARCLKCADAPCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGLTCGMVCPTSDLCVGGCnLQASEAGPI 152
Cdd:PRK12775 325 DALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQC-IIAKKHESV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 153 NIGGLQQFATEvfkkmgvrQRRTPQAEANPLSQ---KIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGGLSAAEIP 229
Cdd:PRK12775 404 GIGRLERFVGD--------NARAKPVKPPRFSKklgKVAICGSGPAGLAAAADLVKYGV-DVTVYEALHVVGGVLQYGIP 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 230 QYRLPIDAVNFEIDLVRDLGVRIETGRSLGtKDLTIQGLLS-TGHDAVFVGIGLPEPKLNPI---FAG-LQPSNGFYTSK 304
Cdd:PRK12775 475 SFRLPRDIIDREVQRLVDIGVKIETNKVIG-KTFTVPQLMNdKGFDAVFLGVGAGAPTFLGIpgeFAGqVYSANEFLTRV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 305 NFLplvsDGSKPGLCACKAAAGlpklhGNVIVLGAGDTAFDCATSALRCGARRVFVVFRKGSSGIRAVPEEVELARDERC 384
Cdd:PRK12775 554 NLM----GGDKFPFLDTPISLG-----KSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGI 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 385 ELLPYLSPRKVIV-KDGLITAMEFCRTEQNENDEWVEDE----EQTQRLKANFVISAFGSGLEDQDVKA--ALApLQFRG 457
Cdd:PRK12775 625 DFFFLHSPVEIYVdAEGSVRGMKVEEMELGEPDEKGRRKpmptGEFKDLECDTVIYALGTKANPIITQStpGLA-LNKWG 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 458 ELPVVDRV---TMQSSVKQVFLGGDLAGVANTTVESVNDGKVAAWSIHCQLQglpldTPAALPLFYTDIDAvdisvemcg 534
Cdd:PRK12775 704 NIAADDGKlesTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYLR-----LGKKWPITAEEAAA--------- 769
|
570 580
....*....|....*....|....*...
gi 24640763 535 irFENPFGLASAPPTTSTAMIRRAFEQG 562
Cdd:PRK12775 770 --FQPGKLLPAIELHTHAGAVAAGAETG 795
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
58-170 |
2.11e-45 |
|
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.
Pssm-ID: 434132 [Multi-domain] Cd Length: 113 Bit Score: 158.86 E-value: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 58 ANDFSDIkHTTLSERGALEEAARCLKCADAPCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGLTCGMVCPTSDL 137
Cdd:pfam14691 2 IKNFEEV-ALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 24640763 138 CVGGCNLQASEAGPINIGGLQQFATEVFKKMGV 170
Cdd:pfam14691 81 CEGACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
22-501 |
9.18e-45 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 172.62 E-value: 9.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 22 PRVKTQCSVvPTKQTKENKKHWKRNADHAAPPCTTLANDFSDIKHTtLSERGALEEAARCLKCAD-APCQKSCPTQLDIK 100
Cdd:PRK12769 170 HASTAAQEM-PAMSKVEQMQATPPRGEPDKLAIEARKTGFDEIYLP-FRADQAQREASRCLKCGEhSICEWTCPLHNHIP 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 101 SFITSIANKNFYGAAKAIFSDNPLGLTCGMVCPTSDLCVGGCNLQaSEAGPINIGGLQQFATEVFKKMGVRqrrtPQ-AE 179
Cdd:PRK12769 248 QWIELVKAGNIDAAVELSHQTNSLPEITGRVCPQDRLCEGACTLR-DEYGAVTIGNIERYISDQALAKGWR----PDlSQ 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 180 ANPLSQKIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRIETGRSLG 259
Cdd:PRK12769 323 VTKSDKRVAIIGAGPAGLACADVLARNGV-AVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 260 tKDLTIQGLLSTgHDAVFVGIGlpepKLNPIFAGL--QPSNGFYTSKNFLplvsdgskpgLCACKAAAGLPKLHG----- 332
Cdd:PRK12769 402 -KDISLESLLED-YDAVFVGVG----TYRSMKAGLpnEDAPGVYDALPFL----------IANTKQVMGLEELPEepfin 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 333 ----NVIVLGAGDTAFDCATSALRCGARRVFVVFRKGSSGIRAVPEEVELARDERCELLPYLSPRKVIVKD-GLITAMEF 407
Cdd:PRK12769 466 taglNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEqGHVCGIRF 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 408 CRTEQNENDEW-------VEDEEQTQrlKANFVISAFG------SGLEDQDVKaalAPLQFRGELPVVDRVTMQSSVKQV 474
Cdd:PRK12769 546 LRTRLGEPDAQgrrrpvpIPGSEFVM--PADAVIMAFGfnphgmPWLESHGVT---VDKWGRIIADVESQYRYQTSNPKI 620
|
490 500
....*....|....*....|....*..
gi 24640763 475 FLGGDLAGVANTTVESVNDGKVAAWSI 501
Cdd:PRK12769 621 FAGGDAVRGADLVVTAMAEGRHAAQGI 647
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
70-501 |
4.00e-43 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 166.87 E-value: 4.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 70 SERGALEEAARCLKCAdaPCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGLTCGMVCptSDLCVGGCNLqASEA 149
Cdd:PRK13984 176 SKEQAMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVC--THKCETVCSI-GHRG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 150 GPINIGGLQQFATEvfkkmGVRQRRTPQA---EANPLSQKIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGGLSAA 226
Cdd:PRK13984 251 EPIAIRWLKRYIVD-----NVPVEKYSEIlddEPEKKNKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGVMRY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 227 EIPQYRLPIDAVNFEIDLVRDLGVRIETGRSLGtKDLTIQGlLSTGHDAVFVGIGLPEPKLNPIfaglqPSNGFYTSKNF 306
Cdd:PRK13984 325 GIPSYRLPDEALDKDIAFIEALGVKIHLNTRVG-KDIPLEE-LREKHDAVFLSTGFTLGRSTRI-----PGTDHPDVIQA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 307 LPLV--------SDGSKpglcackaaaglPKLHGNVIVLGAGDTAFDCATSALRC-----GARRVFVVFRKGS-SGIRAV 372
Cdd:PRK13984 398 LPLLreirdylrGEGPK------------PKIPRSLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTSLERTfEEMPAD 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 373 PEEVELARDERCELLPYLSPRKVIVKDGLITAMEF--CRTEQNENDEWVE--DEEQTQRLKANFVISAFGSG----LEDQ 444
Cdd:PRK13984 466 MEEIEEGLEEGVVIYPGWGPMEVVIENDKVKGVKFkkCVEVFDEEGRFNPkfDESDQIIVEADMVVEAIGQApdysYLPE 545
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24640763 445 DVKAAlapLQF-RGELPVVDrvTMQSSVKQVFLGGDLAGVANtTVESVNDGKVAAWSI 501
Cdd:PRK13984 546 ELKSK---LEFvRGRILTNE--YGQTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGI 597
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
59-498 |
3.24e-40 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 158.65 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 59 NDFSDIkHTTLSERGALEEAARCLKCAD-APCQKSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGLTCGMVCPTSDL 137
Cdd:PRK12809 189 THFGEI-YCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 138 CVGGCNLQaSEAGPINIGGLQQFATEVFKKMGVRqrrtPQ-AEANPLSQKIALVGGGPASLSCATFLARLGYRdVTIYER 216
Cdd:PRK12809 268 CEGACTLK-DHSGAVSIGNLERYITDTALAMGWR----PDvSKVVPRSEKVAVIGAGPAGLGCADILARAGVQ-VDVFDR 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 217 RSYLGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRIETGRSLGtKDLTIQGLLSTgHDAVFVGIGlpepKLNPIFAGLQP 296
Cdd:PRK12809 342 HPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIG-RDITFSDLTSE-YDAVFIGVG----TYGMMRADLPH 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 297 SN--GFYTSKNFLplvsdgskpgLCACKAAAGLPK--------LHG-NVIVLGAGDTAFDCATSALRCGARRVFVVFRKG 365
Cdd:PRK12809 416 EDapGVIQALPFL----------TAHTRQLMGLPEseeypltdVEGkRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRD 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 366 SSGIRAVPEEVELARDERCELLPYLSPRKVIV-KDGLITAMEFCRTEQNENDewvEDEEQTQR--------LKANFVISA 436
Cdd:PRK12809 486 EVSMPGSRKEVVNAREEGVEFQFNVQPQYIACdEDGRLTAVGLIRTAMGEPG---PDGRRRPRpvagsefeLPADVLIMA 562
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24640763 437 FGSGLEDQD-VKAALAPLQFRGELPV--VDRVTMQSSVKQVFLGGDLAGVANTTVESVNDGKVAA 498
Cdd:PRK12809 563 FGFQAHAMPwLQGSGIKLDKWGLIQTgdVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAA 627
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
529-833 |
1.69e-38 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 145.57 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 529 SVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGLDKDlVTNVSPRIVRgTTSGY--KYG-PQQGCFLNI 605
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQ-PGNPTPRVFR-LPEGVlnRMGlNNPGLDAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 606 ELISEKRAEYWLKSIGelkrdfpekiVIASIMCSfNEEDWTELAIKAeQSGADALELNLSCPHGMGERgmglACGQDPEL 685
Cdd:pfam01180 81 AELLKRRKEYPRPDLG----------INLSKAGM-TVDDYVEVARKI-GPFADYIELNVSCPNTPGLR----ALQTDPEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 686 VEQISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADGGSAINTVQG-LMGLKADSTAWPAIGKEQrttYGGVSGNA 764
Cdd:pfam01180 145 AAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINATNTtVRGMRIDLKTEKPILANG---TGGLSGPP 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 765 TRPMALKAISDIANRV-PGFPILGIGGIDSGEVALQFIHAGATVLQICSSVQNQDFTVIEDYCTALKALL 833
Cdd:pfam01180 222 IKPIALKVIRELYQRTgPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
77-501 |
4.60e-33 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 138.43 E-value: 4.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 77 EAARCLKCADAPCQ------------KSCPTQLDIKSFITSIANKNFYGAAKAIFSDNPLGLTCGMVCPTSDLCVGGCNL 144
Cdd:PRK12779 186 EVMRDKQCDDKPCElgvlvqgkaepkGGCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTH 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 145 QASeagPINIGGLQQFATEVFKKMG----VRQ--RRTPQAEANplSQKIALVGGGPASLSCATFLARLGYrDVTIYERRS 218
Cdd:PRK12779 266 TKR---PIEIGQLEWYLPQHEKLVNpnanERFagRISPWAAAV--KPPIAVVGSGPSGLINAYLLAVEGF-PVTVFEAFH 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 219 YLGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRIETGRSLGtKDLTIQGLLSTGHDAVFVGIGLPEPKLNPI----FAGL 294
Cdd:PRK12779 340 DLGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFVKNFVVG-KTATLEDLKAAGFWKIFVGTGAGLPTFMNVpgehLLGV 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 295 QPSNGFYTSKNFLP-LVSDGSKPglcackaaagLPKLHG-NVIVLGAGDTAFDCATSALRCGArRVFVVFRKGSSGIRAV 372
Cdd:PRK12779 419 MSANEFLTRVNLMRgLDDDYETP----------LPEVKGkEVFVIGGGNTAMDAARTAKRLGG-NVTIVYRRTKSEMPAR 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 373 PEEVELARDERCELLPYLSPRKVI--VKDGLITAMEFCRTEQNENDEWVEDEEQ----TQRLKANFVISAFGSGLED--Q 444
Cdd:PRK12779 488 VEELHHALEEGINLAVLRAPREFIgdDHTHFVTHALLDVNELGEPDKSGRRSPKptgeIERVPVDLVIMALGNTANPimK 567
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 24640763 445 DVKAALAPLQFrGELpVVDRVTMQSSVKQVFLGGDLAGVANTTVESVNDGKVAAWSI 501
Cdd:PRK12779 568 DAEPGLKTNKW-GTI-EVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAAKEI 622
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
946-1004 |
2.47e-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: 110.83 E-value: 2.47e-29
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 24640763 946 ALIDDDMCINCGKCYMTCADSGYQAIEFDKDTHIPHVNDDCTGCTLCVSVCPIIDCITM 1004
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDDCITM 59
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
512-813 |
2.85e-22 |
|
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.
Pssm-ID: 240089 Cd Length: 327 Bit Score: 99.11 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 512 TPAALPLFYTDIDAvdiSVEMCGIRFENPFGLAsappttstA-------MIRRAFEQGWGFVVTKTfgldkdlVT----- 579
Cdd:cd04738 26 PPLLLLLVYDDPRL---EVEVFGLTFPNPVGLA--------AgfdknaeAIDALLALGFGFVEVGT-------VTprpqp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 580 -NVSPR----------IVRgttsgykYGpqqgcFLN--IELISEKRAEYWLK------SIGELKRDFPEKIViasimcsf 640
Cdd:cd04738 88 gNPKPRlfrlpedealINR-------MG-----FNNdgADAVAKRLKKRRPRggplgvNIGKNKDTPLEDAV-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 641 neEDWTELaIKAEQSGADALELNLSCPHGMGERGMglacgQDPELVEQISRWVRKAV-----KLPFFIKLTPNITD--IV 713
Cdd:cd04738 148 --EDYVIG-VRKLGPYADYLVVNVSSPNTPGLRDL-----QGKEALRELLTAVKEERnklgkKVPLLVKIAPDLSDeeLE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 714 SIAAAAKRGGADGGSAINTVqglmgLKADSTAWPAIGKEQrttyGGVSGNATRPMALKAISDIANRVPG-FPILGIGGID 792
Cdd:cd04738 220 DIADVALEHGVDGIIATNTT-----ISRPGLLRSPLANET----GGLSGAPLKERSTEVLRELYKLTGGkIPIIGVGGIS 290
|
330 340
....*....|....*....|.
gi 24640763 793 SGEVALQFIHAGATVLQICSS 813
Cdd:cd04738 291 SGEDAYEKIRAGASLVQLYTG 311
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
186-507 |
1.85e-21 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 97.37 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 186 KIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRI------------- 252
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYLACLGY-EVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFhtrtkvccgeplh 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 253 -ETGRSLGTKDLTIQGLLStGHDAVFVG--------IGLPEPKLNPIFAGLQPSNGFYTSKnfLPLVSDGSKPglcacka 323
Cdd:PRK12770 99 eEEGDEFVERIVSLEELVK-KYDAVLIAtgtwksrkLGIPGEDLPGVYSALEYLFRIRAAK--LGYLPWEKVP------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 324 aaglPKLHGNVIVLGAGDTAFDCATSALRCGARRVFVVFRKGSSGIRAVPEEVELARDERCELLPYLSPRKVIvKDGLIT 403
Cdd:PRK12770 169 ----PVEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRII-GEGRVE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 404 AMEFCRTEQNENDEW-------VEDEEQTqrLKANFVISAFG----SGLEDQDVKAALAPlqfRGELPVVDRvtMQSSVK 472
Cdd:PRK12770 244 GVELAKMRLGEPDESgrprpvpIPGSEFV--LEADTVVFAIGeiptPPFAKECLGIELNR---KGEIVVDEK--HMTSRE 316
|
330 340 350
....*....|....*....|....*....|....*
gi 24640763 473 QVFLGGDLAGVANTTVESVNDGKVAAWSIHCQLQG 507
Cdd:PRK12770 317 GVFAAGDVVTGPSKIGKAIKSGLRAAQSIHEWLDL 351
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
657-813 |
1.09e-17 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 85.60 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 657 ADALELNLSCPHGMGERGMglacgQDPELVEQISRWVRKAVKL-----PFFIKLTPNITD--IVSIAAAAKRGGADGGSA 729
Cdd:PRK05286 170 ADYFTVNISSPNTPGLRDL-----QYGEALDELLAALKEAQAElhgyvPLLVKIAPDLSDeeLDDIADLALEHGIDGVIA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 730 INTV---QGLMGLKadstawpaIGKEQrttyGGVSGNATRPMALKAISDIANRVPG-FPILGIGGIDSGEVALQFIHAGA 805
Cdd:PRK05286 245 TNTTlsrDGLKGLP--------NADEA----GGLSGRPLFERSTEVIRRLYKELGGrLPIIGVGGIDSAEDAYEKIRAGA 312
|
....*...
gi 24640763 806 TVLQICSS 813
Cdd:PRK05286 313 SLVQIYSG 320
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
527-812 |
1.02e-16 |
|
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: 82.66 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 527 DISVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFgLDKDLVT---NVSPRIVRGTTS--GYKYGPQQGC 601
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSL-FEEQIEReaqELDRFLTYGSSFaeALSYFPEYGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 602 FlnielisEKRAEYWLKSIGELKR--DFPekiVIASIMCSFNEEdWTELAIKAEQSGADALELNLscphgmgergmgLAC 679
Cdd:cd04739 80 Y-------NLGPEEYLELIRRAKRavSIP---VIASLNGVSAGG-WVDYARQIEEAGADALELNI------------YAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 680 GQDPEL----VEQ----ISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADGGSAIN----------TVQGLMGLKA 741
Cdd:cd04739 137 PTDPDIsgaeVEQryldILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNrfyqpdidleTLEVVPNLLL 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640763 742 DSTAwpaigkEQRTTyggvsgnatrpmaLKAISDIANRVPGfPILGIGGIDSGEVALQFIHAGATVLQICS 812
Cdd:cd04739 217 SSPA------EIRLP-------------LRWIAILSGRVKA-SLAASGGVHDAEDVVKYLLAGADVVMTTS 267
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
527-726 |
6.55e-16 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 80.30 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 527 DISVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTfgLDKDLVTNVSPRIVRGTTSGYKYGPQQGCFLNIE 606
Cdd:PRK07565 2 DLSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKS--LFEEQIRHEAAELDRHLTHGTESFAEALDYFPEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 607 LISEKRAEYWLKSIGELKR--DFPekiVIASIMCSFNEEdWTELAIKAEQSGADALELNLSCPHGmgergmglacgqDPE 684
Cdd:PRK07565 80 AKFYVGPEEYLELIRRAKEavDIP---VIASLNGSSAGG-WVDYARQIEQAGADALELNIYYLPT------------DPD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24640763 685 L----VEQ----ISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADG 726
Cdd:PRK07565 144 IsgaeVEQryldILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADG 193
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
948-1008 |
2.59e-14 |
|
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: 68.93 E-value: 2.59e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640763 948 IDDDMCINCGKCYMTCADsgyQAIEFDKDTHIPHVNDDCTGCTLCVSVCPiIDCITMVPKK 1008
Cdd:COG1144 27 VDEDKCIGCGLCWIVCPD---GAIRVDDGKYYGIDYDYCKGCGICAEVCP-VKAIEMVPEE 83
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
944-1012 |
1.53e-13 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 66.29 E-value: 1.53e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24640763 944 KVALIDDDMCINCGKCYMTCAdsgYQAIEFDKDTHIPHVNDDCTGCTLCVSVCPiIDCITMVPKKIPHV 1012
Cdd:COG1149 4 KIPVIDEEKCIGCGLCVEVCP---EGAIKLDDGGAPVVDPDLCTGCGACVGVCP-TGAITLEEREAGKI 68
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
530-824 |
1.72e-13 |
|
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: 72.36 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 530 VEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGLDKdLVTNVSPRIVRGTTSGykygpqqgcfLNIELIS 609
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAG-RPGNPEPRYYAFPLGS----------INSLGLP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 610 EKRAEYWLKSIGELKRDFPE--KIVIASIMCSFNEEDWTELAIKAEQS-GADALELNLSCPH--GMGERGMglacgqDPE 684
Cdd:cd04741 70 NLGLDYYLEYIRTISDGLPGsaKPFFISVTGSAEDIAAMYKKIAAHQKqFPLAMELNLSCPNvpGKPPPAY------DFD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 685 LVEQISRWVRKAVKLPFFIKLTPnITDIVSIAAAAKRGGADGGS-----AINTV-QGLMgLKADSTAwPAIgkEQRTTYG 758
Cdd:cd04741 144 ATLEYLTAVKAAYSIPVGVKTPP-YTDPAQFDTLAEALNAFACPisfitATNTLgNGLV-LDPERET-VVL--KPKTGFG 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640763 759 GVSGNATRPMALKAISDIANRVPG-FPILGIGGIDSGEVALQFIHAGATVLQICSSVQNQDFTVIED 824
Cdd:cd04741 219 GLAGAYLHPLALGNVRTFRRLLPSeIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFAR 285
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
527-836 |
2.57e-13 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 71.91 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 527 DISVEMCGIRFENPFGLASAPP-TTSTAMIRRAFEQGwGFVVTKTFGLDKDlVTNVSPRIVRgttsgYKYG-------PQ 598
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGVYcMTKEELEEVEASAA-GAFVTKSATLEPR-PGNPEPRYAD-----TPLGsinsmglPN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 599 QGcflnielisekrAEYWLKSIGELKRDFPEKIVIASIMcSFNEEDWTELAIKAEQSG-ADALELNLSCPHGMGERGMGL 677
Cdd:PRK02506 74 LG------------FDYYLDYVLELQKKGPNKPHFLSVV-GLSPEETHTILKKIQASDfNGLVELNLSCPNVPGKPQIAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 678 acgqDPELVEQISRWVRKAVKLPFFIKLTPNItDIVSIAAAA---KRGGADGGSAINTV-QGLMGLKADSTAW--PAIGk 751
Cdd:PRK02506 141 ----DFETTEQILEEVFTYFTKPLGVKLPPYF-DIVHFDQAAaifNKFPLAFVNCINSIgNGLVIDPEDETVVikPKNG- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 752 eqrttYGGVSGNATRPMALKAISDIANRV-PGFPILGIGGIDSGEVALQFIHAGATVLQICSSVQNQDFTVIEDYCTALK 830
Cdd:PRK02506 215 -----FGGIGGDYIKPTALANVRAFYQRLnPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELK 289
|
....*.
gi 24640763 831 ALLYLK 836
Cdd:PRK02506 290 AIMAEK 295
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
887-1009 |
6.64e-13 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 69.75 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 887 KMAELRSQKGALWDAEQVKATPPASNGAPNPAPRIKDVIGAALDKIGSYNKLDNKQQKVALIDDDMCINCGKCYMTCads 966
Cdd:COG1145 118 VKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVC--- 194
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 24640763 967 GYQAIEFDKDTHIPHVN-DDCTGCTLCVSVCPiIDCITMVPKKI 1009
Cdd:COG1145 195 PTGAIRLKDGKPQIVVDpDKCIGCGACVKVCP-VGAISLEPKEI 237
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
513-812 |
8.97e-13 |
|
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273408 Cd Length: 335 Bit Score: 70.58 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 513 PAALPLFYTDIDAVD-ISVEMCGIRFENPFGLASAPPTTSTAmIRRAFEQGWGFVVTKTFgLDKDLVTNVSPRIVR---- 587
Cdd:TIGR01036 30 TPFLALLRSLFGASDpLEVTVLGLKFPNPLGLAAGFDKDGEA-IDALGAMGFGFLEIGTV-TPKPQPGNPRPRLFRlied 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 588 -GTTSGYKYGPQQGCFLNIELiseKRAEYWLK---SIGELKRDFPEKIViasimcsfneEDWTELAIKAeQSGADALELN 663
Cdd:TIGR01036 108 eALINRMGFNNHGADVLVERL---KRARYKGPigiNIGKNKDTPSEDAK----------EDYAACLRKL-GPLADYLVVN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 664 LSCPHGMGERGMGLACGQDPEL--VEQISRWVRKAVKLPFFIKLTPNIT--DIVSIAAAAKRGGADGGSAINTVqglmgL 739
Cdd:TIGR01036 174 VSSPNTPGLRDLQYKAELRDLLtaVKQEQDGLRRVHRVPVLVKIAPDLTesDLEDIADSLVELGIDGVIATNTT-----V 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640763 740 KADSTAWPAIGKEQrttyGGVSGnatRPMALKA---ISDIANRVPG-FPILGIGGIDSGEVALQFIHAGATVLQICS 812
Cdd:TIGR01036 249 SRSLVQGPKNSDET----GGLSG---KPLQDKSteiIRRLYAELQGrLPIIGVGGISSAQDALEKIRAGASLLQIYS 318
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
553-812 |
3.53e-12 |
|
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: 66.46 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 553 AMIRRAFEQGWGFVVTKTFGLDKDLVTNVSPRIVRgttsgykygpqqgcflnielisekraeywlksigeLKRDFPEKIV 632
Cdd:cd04722 16 ELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLK-----------------------------------EVAAETDLPL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 633 IASIMCSFNEEDWTELAIKAEQSGADALELNLSCPHGMGErgmglacgqDPELVeqisRWVRKAV-KLPFFIKLTPNITD 711
Cdd:cd04722 61 GVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYLARE---------DLELI----RELREAVpDVKVVVKLSPTGEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 712 IvsiAAAAKRGGADGgsaINTvqglmglkadstawpaigkeqrTTYGGVSGNATRPMALKAISDIANRVPGFPILGIGGI 791
Cdd:cd04722 128 A---AAAAEEAGVDE---VGL----------------------GNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGI 179
|
250 260
....*....|....*....|.
gi 24640763 792 DSGEVALQFIHAGATVLQICS 812
Cdd:cd04722 180 NDPEDAAEALALGADGVIVGS 200
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
940-1006 |
2.80e-11 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 63.81 E-value: 2.80e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24640763 940 NKQQKVALIDDDMCINCGKCymtcadsgYQAIEFD------KDTHIPhVNDDCTGCTLCVSVCPiIDCITMVP 1006
Cdd:PRK05113 103 TPARKVAFIDEDNCIGCTKC--------IQACPVDaivgatKAMHTV-ISDLCTGCDLCVAPCP-TDCIEMIP 165
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
897-1007 |
9.02e-11 |
|
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: 61.35 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 897 ALWDAEQVKATPPasnGAPNPAPRIKDVIGAALDKIGSYNKLDNKQQ-KVALIDDDMCINCGKCYMTC-ADSgyqAIEFD 974
Cdd:TIGR01944 61 AIAEGEAINKCPP---GGEAVILALAELLGVEPIPQPLDADAGTIQPpMVALIDEDNCIGCTKCIQACpVDA---IVGAA 134
|
90 100 110
....*....|....*....|....*....|...
gi 24640763 975 KDTHIPhVNDDCTGCTLCVSVCPiIDCITMVPK 1007
Cdd:TIGR01944 135 KAMHTV-IADECTGCDLCVEPCP-TDCIEMIPV 165
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
944-1014 |
1.61e-10 |
|
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: 62.70 E-value: 1.61e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640763 944 KVALI-----DDDMCINCGKCYMTCAdsgYQAIEFDKDtHIPHVNDD-CTGCTLCVSVCPiIDCITMVPKKIPHVIK 1014
Cdd:COG2878 125 RAAVIggpkgCEYGCIGCGDCIKACP---FDAIVGAAK-GMHTVDEDkCTGCGLCVEACP-VDCIEMVPVSPTVVVS 196
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
948-1008 |
5.69e-10 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 56.26 E-value: 5.69e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24640763 948 IDDDMCINCGKCYMTCadsGYQAIEFDKDTHIPHV--NDDCTGCTLCVSVCPiIDCITMVPKK 1008
Cdd:COG1146 5 IDTDKCIGCGACVEVC---PVDVLELDEEGKKALVinPEECIGCGACELVCP-VGAITVEDDE 63
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
931-1005 |
9.23e-09 |
|
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: 54.71 E-value: 9.23e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24640763 931 KIGSYNKLDNKQQKVALIDDDMCINCGKCYMTCAdsgYQAIEFDKDTHIPHVNDDCTGCTLCVSVCPiIDCITMV 1005
Cdd:cd10549 58 ELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCP---VDAITLEDELEIVIDKEKCIGCGICAEVCP-VNAIKLV 128
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
946-1018 |
1.52e-08 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 52.43 E-value: 1.52e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640763 946 ALIDDDMCINCGKCYMTCAdsgYQAIEFDKDTHipHVNDD-CTGCTLCVSVCPiIDCITMVPKKIPHVIKRGVE 1018
Cdd:COG2768 6 PYVDEEKCIGCGACVKVCP---VGAISIEDGKA--VIDPEkCIGCGACIEVCP-VGAIKIEWEEDEEFQEKMAE 73
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
657-810 |
2.79e-08 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 57.44 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 657 ADALELNLSCPHGMGERgmglacgqDPELVEQISRWVRK------------AVKLPFFIKLTPNIT--DIVSIAAAAKRG 722
Cdd:PLN02826 217 ADYLVINVSSPNTPGLR--------KLQGRKQLKDLLKKvlaardemqwgeEGPPPLLVKIAPDLSkeDLEDIAAVALAL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 723 GADGGSAINTvqglmglkADSTAWPAIGKEQRTTYGGVSGNATRPMALKAISDIANRVPG-FPILGIGGIDSGEVALQFI 801
Cdd:PLN02826 289 GIDGLIISNT--------TISRPDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGkIPLVGCGGVSSGEDAYKKI 360
|
....*....
gi 24640763 802 HAGATVLQI 810
Cdd:PLN02826 361 RAGASLVQL 369
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
953-1010 |
3.59e-08 |
|
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: 50.90 E-value: 3.59e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640763 953 CINCGKCYMTCAdsgYQAIEFDKDTH--IPHVN-DDCTGCTLCVSVCPiIDCITMVPKKIP 1010
Cdd:COG1143 4 CIGCGLCVRVCP---VDAITIEDGEPgkVYVIDpDKCIGCGLCVEVCP-TGAISMTPFELA 60
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
953-997 |
5.17e-08 |
|
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: 50.22 E-value: 5.17e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 24640763 953 CINCGKCYMTCAdsgYQAIEFDKDTHIP------HVNDDCTGCTLCVSVCP 997
Cdd:pfam12838 1 CIGCGACVAACP---VGAITLDEVGEKKgtktvvIDPERCVGCGACVAVCP 48
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
190-234 |
5.23e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 50.61 E-value: 5.23e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 24640763 190 VGGGPASLSCATFLARLGYRdVTIYERRSYLGGLSA-AEIPQYRLP 234
Cdd:pfam13450 2 VGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYsYRVPGYVFD 46
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
184-232 |
6.65e-08 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 56.40 E-value: 6.65e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 24640763 184 SQKIALVGGGPASLSCATFLARLGYRdVTIYERRSYLGG-LSAAEIPQYR 232
Cdd:COG1233 3 MYDVVVIGAGIGGLAAAALLARAGYR-VTVLEKNDTPGGrARTFERPGFR 51
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
945-1006 |
6.67e-08 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 55.19 E-value: 6.67e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24640763 945 VALIDDDMCINCGKCYMTC-ADSGYQAiefDKDTHIPhVNDDCTGCTLCVSVCPiIDCITMVP 1006
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACpVDAIVGA---PKQMHTV-LADLCTGCDLCVPPCP-VDCIDMVP 136
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
186-479 |
1.04e-07 |
|
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: 54.63 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 186 KIALVGGGPASLSCATFLARLGYRdVTIYERRS------------YLGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRIE 253
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGK-VTLIEDEGtcpyggcvlskaLLGAAEAPEIASLWADLYKRKEEVVKKLNNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 254 TGRS-----LGTKDLTIQGLLSTG-----HDAVFVGIG-------LPEPKLNPIFAGLqpsngFYTSKNFLplvSDGSKP 316
Cdd:pfam07992 81 LGTEvvsidPGAKKVVLEELVDGDgetitYDRLVIATGarprlppIPGVELNVGFLVR-----TLDSAEAL---RLKLLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 317 glcackaaaglpklhGNVIVLGAGDTAFDCATSALRCGArRVFVVFRkGSSGIRAVPEEVElardERCEllpylsprKVI 396
Cdd:pfam07992 153 ---------------KRVVVVGGGYIGVELAAALAKLGK-EVTLIEA-LDRLLRAFDEEIS----AALE--------KAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 397 VKDG--LITAMEFCRTEQNENDEWVEDEEqTQRLKANFVISAFGSGLEDQDVKAALAPLQFRGELpVVDRvTMQSSVKQV 474
Cdd:pfam07992 204 EKNGveVRLGTSVKEIIGDGDGVEVILKD-GTEIDADLVVVAIGRRPNTELLEAAGLELDERGGI-VVDE-YLRTSVPGI 280
|
....*
gi 24640763 475 FLGGD 479
Cdd:pfam07992 281 YAAGD 285
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
937-1005 |
1.30e-07 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 49.66 E-value: 1.30e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640763 937 KLDNKQQKVAL-IDDDMCINCGKCYMTCAdsgyqAIEFDKDTHIPHVNDD-CTGCTLCVSVCPiIDCITMV 1005
Cdd:COG4231 7 ILDNRTTAMRYvIDEDKCTGCGACVKVCP-----ADAIEEGDGKAVIDPDlCIGCGSCVQVCP-VDAIKLE 71
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
948-997 |
2.00e-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: 48.79 E-value: 2.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 24640763 948 IDDDMCINCGKCYMTC--ADSGYQAIEFDKDT-HIPHVNDDCTGCTLCVSVCP 997
Cdd:pfam13237 4 IDPDKCIGCGRCTAACpaGLTRVGAIVERLEGeAVRIGVWKCIGCGACVEACP 56
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
184-285 |
2.12e-07 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 54.48 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 184 SQKIALVGGGPASLSCATFLARLGYRdVTIYERRSYLGGLSAA-EIPQYRLPIDA---------VNFeIDLVRDLGVRie 253
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFR-VTLLEARPRLGGRARSfPDPDTGLPIDNgqhvllgcyRNT-LDLLRRIGAA-- 78
|
90 100 110
....*....|....*....|....*....|..
gi 24640763 254 tGRSLGTKDLTIqgLLSTGHDAVFVGIGLPEP 285
Cdd:COG3349 79 -DNLVGPEPLQF--PLPGGRRWTLRAPRLPAP 107
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
945-1005 |
3.42e-07 |
|
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: 50.47 E-value: 3.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 945 VALIDDDMCINCGKCYMTCAdsgYQAIEFDKDTHIPHvndDCTGC---------TLCVSVCPiIDCITMV 1005
Cdd:cd04410 74 IVLIDEDKCIGCGSCVEACP---YGAIVFDPEPGKAV---KCDLCgdrldeglePACVKACP-TGALTFG 136
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
948-1013 |
4.08e-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: 50.09 E-value: 4.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640763 948 IDDDMCINCGKCYMTCADSGYQAIEFDKDTHIPHVN-----DDCTGCTLCVSVCPiIDCITMVpKKIPHVI 1013
Cdd:cd10549 37 IDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEKEaeideEKCIGCGLCVKVCP-VDAITLE-DELEIVI 105
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
948-1019 |
7.29e-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: 49.32 E-value: 7.29e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24640763 948 IDDDMCINCGKCYMTCAdsgYQAIEFDKDTHI---PHVNDD-CTGCTLCVSVCPiIDCITMVPKKIPHVIKRGVEE 1019
Cdd:cd10549 3 YDPEKCIGCGICVKACP---TDAIELGPNGAIargPEIDEDkCVFCGACVEVCP-TGAIELTPEGKEYVPKEKEAE 74
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
945-997 |
7.49e-07 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 49.95 E-value: 7.49e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 945 VALIDDDMCIN------CGKCYMTCADSGYqAIEFDKDTHIPHVNDD-CTGCTLCVSVCP 997
Cdd:cd16373 85 VAVIDKDRCLAwqggtdCGVCVEACPTEAI-AIVLEDDVLRPVVDEDkCVGCGLCEYVCP 143
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
948-997 |
9.35e-07 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 46.97 E-value: 9.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 24640763 948 IDDDMCINCGKCYMTCADsgyQAIEFDKDThiPHVNDD-CTGCTLCVSVCP 997
Cdd:COG2221 12 IDEEKCIGCGLCVAVCPT---GAISLDDGK--LVIDEEkCIGCGACIRVCP 57
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
186-251 |
1.12e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 52.20 E-value: 1.12e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24640763 186 KIALVGGGPASLSCATFLARLGYRdVTIYERRSYLGGLSAA-EIPQYRL--------PIDAvnFEIDLVRDLGVR 251
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAASfEFGGLPIerfyhhifKSDE--ALLELLDELGLE 72
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
628-725 |
1.20e-06 |
|
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: 51.56 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 628 PEKIVIAsiMCSFNEEDW--------------TELAIKAEQSGADALELNLSCPHGMGERGMGLAC-GQDPELVEQISRW 692
Cdd:pfam01207 39 PEKVRIR--MLSELEEPTplavqlggsdpallAEAAKLVEDRGADGIDINMGCPSKKVTRGGGGAAlLRNPDLVAQIVKA 116
|
90 100 110
....*....|....*....|....*....|....*..
gi 24640763 693 VRKAVKLPFFIKLTPNITD----IVSIAAAAKRGGAD 725
Cdd:pfam01207 117 VVKAVGIPVTVKIRIGWDDshenAVEIAKIVEDAGAQ 153
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
184-255 |
1.56e-06 |
|
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: 51.76 E-value: 1.56e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24640763 184 SQKIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGGLSAAeipqyrlpidavnFEIDlvrdlGVRIETG 255
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRT-------------VEVD-----GFRIDRG 53
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
945-997 |
1.67e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 51.78 E-value: 1.67e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 24640763 945 VALIDDDMCINCGKCYMTCAdsgYQAIEFDKDtHIPHVND-DCTGCTLCVSVCP 997
Cdd:COG1148 490 VAEVDPEKCTGCGRCVEVCP---YGAISIDEK-GVAEVNPaLCKGCGTCAAACP 539
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
951-997 |
3.75e-06 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 47.43 E-value: 3.75e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 24640763 951 DMCINCGKCYMTCADSgyqAIEfDKDTHIPHVN-DDCTGCTLCVSVCP 997
Cdd:PRK09625 59 EICINCFNCWVYCPDA---AIL-SRDKKLKGVDySHCKGCGVCVEVCP 102
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
181-282 |
7.38e-06 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 49.79 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 181 NPLSQKIALVGGGPASLSCATFLARLGYRdVTIYERRSYLGGLSAAEIPQY-------RLPIDaVNFEIDLVRDLGVRIE 253
Cdd:PRK06292 166 DKLPKSLAVIGGGVIGLELGQALSRLGVK-VTVFERGDRILPLEDPEVSKQaqkilskEFKIK-LGAKVTSVEKSGDEKV 243
|
90 100 110
....*....|....*....|....*....|..
gi 24640763 254 TGRSLGTKDLTIQG---LLSTGHDAVFVGIGL 282
Cdd:PRK06292 244 EELEKGGKTETIEAdyvLVATGRRPNTDGLGL 275
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
618-802 |
7.63e-06 |
|
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: 48.26 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 618 KSIGELKRDFPEKIVIASImCSFNEEDWTELAIKAEQSGADALELNLSCP-----HGmgerGMGLACGQDPELVEQISRW 692
Cdd:cd02801 43 KRLRLLTRNPEERPLIVQL-GGSDPETLAEAAKIVEELGADGIDLNMGCPspkvtKG----GAGAALLKDPELVAEIVRA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 693 VRKAVKLPFFIK------LTPNITDIVSIAAAAkrggadGGSAInTVQGlmglkadSTAWpaigkeQRTTyggvsGNATr 766
Cdd:cd02801 118 VREAVPIPVTVKirlgwdDEEETLELAKALEDA------GASAL-TVHG-------RTRE------QRYS-----GPAD- 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 24640763 767 pmaLKAISDIANRVPgFPILGIGGIDSGEVALQFIH 802
Cdd:cd02801 172 ---WDYIAEIKEAVS-IPVIANGDIFSLEDALRCLE 203
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
186-502 |
8.79e-06 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 48.96 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 186 KIALVGGGPASLSCATFLARLGyRDVTIYERRS-------------YLG---GLSAAEIPQyRLPIDAVNFEIDLVRDLG 249
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAG-LKTLVIEGGEpggqlattkeienYPGfpeGISGPELAE-RLREQAERFGAEILLEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 250 VRIE---TGRSLGTKDLTIqglLSTghDAVFVGIGLPEPKLNpiFAGLQPSNGFytsknflplvsdgskpGLCACkAAAG 326
Cdd:COG0492 80 TSVDkddGPFRVTTDDGTE---YEA--KAVIIATGAGPRKLG--LPGEEEFEGR----------------GVSYC-ATCD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 327 LPKLHG-NVIVLGAGDTAFDcatSALRCG--ARRVFVVFRKGSsgIRAVPEEVELARD-ERCELLpylsPRKVIVK---D 399
Cdd:COG0492 136 GFFFRGkDVVVVGGGDSALE---EALYLTkfASKVTLIHRRDE--LRASKILVERLRAnPKIEVL----WNTEVTEiegD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 400 GLITAMEFCRTEQNEndewvedeeqTQRLKANFVISAFGS-----GLEDQDVKaaLAPlqfRGELpVVDRvTMQSSVKQV 474
Cdd:COG0492 207 GRVEGVTLKNVKTGE----------EKELEVDGVFVAIGLkpnteLLKGLGLE--LDE---DGYI-VVDE-DMETSVPGV 269
|
330 340 350
....*....|....*....|....*....|..
gi 24640763 475 FLGGDlagVANTTVE----SVNDGKVAAWSIH 502
Cdd:COG0492 270 FAAGD---VRDYKYRqaatAAGEGAIAALSAA 298
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
184-250 |
1.09e-05 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 48.96 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 184 SQKIALVGGGPASLSCATFLARlgYRDVTIYERRSYLGGLSA---AEIPQYRLPIDA---V-------NFeIDLVRDLGV 250
Cdd:COG2907 3 RMRIAVIGSGISGLTAAWLLSR--RHDVTLFEANDRLGGHTHtvdVDLDGRTVPVDTgfiVfnertypNL-TALFAELGV 79
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
897-998 |
1.75e-05 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 48.53 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 897 ALWDAEQVKATPPASNGAPNPAPRIKDVIGAALDKIGSYNKLDNKQQKVALIDD--DMCINCGKCYMTC---------AD 965
Cdd:COG0247 22 FLELELGKIKYAFDPDNKLNPGKIGLLNPGVELLGDGDLHDKNLKTLPWKELLDalDACVGCGFCRAMCpsykatgdeKD 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24640763 966 S-------------GYQAIEFDKDTHipHVNDDCTGCTLCVSVCPI 998
Cdd:COG0247 102 SprgrinllrevleGELPLDLSEEVY--EVLDLCLTCKACETACPS 145
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
186-258 |
3.76e-05 |
|
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: 425450 [Multi-domain] Cd Length: 80 Bit Score: 42.96 E-value: 3.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24640763 186 KIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGGLSAAEIPQYRLpidavnfeiDLVRDLGVRIETGRSL 258
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGS-KVTVVERRDRLLPGFDPEIAKILQ---------EKLEKNGIEFLLNTTV 63
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
147-281 |
4.55e-05 |
|
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: 46.54 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 147 SEAGPINIGGLQQFATEVFKKMGVRQRrtpqAEANPLSQKIALVGGGPASLSCATFLARLGyRDVTIYERRSYLGGlsaa 226
Cdd:pfam07992 119 ARPRLPPIPGVELNVGFLVRTLDSAEA----LRLKLLPKRVVVVGGGYIGVELAAALAKLG-KEVTLIEALDRLLR---- 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24640763 227 eipqyRLPIDAVNFEIDLVRDLGVRIETGRSLGT---KDLTIQGLLSTGH----DAVFVGIG 281
Cdd:pfam07992 190 -----AFDEEISAALEKALEKNGVEVRLGTSVKEiigDGDGVEVILKDGTeidaDLVVVAIG 246
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
647-799 |
5.35e-05 |
|
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: 46.24 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 647 ELAIKAEQSGADALELNLSCP------HGMGergmglAC-GQDPELVEQISRWVRKAVKLPFFIKL-------TPNITDI 712
Cdd:COG0042 78 EAARIAEELGADEIDINMGCPvkkvtkGGAG------AAlLRDPELVAEIVKAVVEAVDVPVTVKIrlgwdddDENALEF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 713 VSIAAAAkrgGADggsAInTV------QGLMGlKADstaWPAIGkeqrttyggvsgnatrpmALKAISDIanrvpgfPIL 786
Cdd:COG0042 152 ARIAEDA---GAA---AL-TVhgrtreQRYKG-PAD---WDAIA------------------RVKEAVSI-------PVI 195
|
170
....*....|...
gi 24640763 787 GIGGIDSGEVALQ 799
Cdd:COG0042 196 GNGDIFSPEDAKR 208
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
952-997 |
5.80e-05 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 41.39 E-value: 5.80e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 24640763 952 MCINCGKCYMTCADSGYQAIEFDKDTHIPHVNDDCTGCTLCVSVCP 997
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQTIRGDIAGLACIGCGACVDACP 46
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
940-997 |
7.47e-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: 319872 [Multi-domain] Cd Length: 130 Bit Score: 43.33 E-value: 7.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 24640763 940 NKQQKVALIDDDMCINCGKCYMTCAdsgYQAIEFDKDTHIPHVNDDCTGCTLCVSVCP 997
Cdd:cd10550 69 DEETGAVVVDEDKCIGCGMCVEACP---FGAIRVDPETGKAIKCDLCGGDPACVKVCP 123
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
944-1009 |
9.41e-05 |
|
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: 45.07 E-value: 9.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24640763 944 KVALIDDDMCINCGKCYMTCAdsgYQAIEFDKDtHIPHVNDDCTGCTLCVSVCPiIDCITMVPKKI 1009
Cdd:cd03110 57 KKAFIDQEKCIRCGNCERVCK---FGAILEFFQ-KLIVDESLCEGCGACVIICP-RGAIYLKDRDT 117
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
167-225 |
1.07e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 46.01 E-value: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24640763 167 KMGV---RQRRTPQAEANPLSQKIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGGLSA 225
Cdd:COG1148 120 RMAVakaKLLEPLEPIKVPVNKRALVIGGGIAGMTAALELAEQGY-EVYLVEKEPELGGRAA 180
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
948-997 |
1.09e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 45.79 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 24640763 948 IDDDMCINCGKCYMTCadsGYQAIEFDkDTHIPHVNDDCTGCTLCVSVCP 997
Cdd:COG4624 88 RDKEKCKNCYPCVRAC---PVKAIKVD-DGKAEIDEEKCISCGQCVAVCP 133
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
961-1007 |
1.52e-04 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 43.00 E-value: 1.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 24640763 961 MTCADS-GYQAIEF-DKDTHI--PHVNDD-CTGCTLCVSVCPiIDCITMVPK 1007
Cdd:cd10564 89 RSCQDAcPTQAIRFrPRLGGIalPELDADaCTGCGACVSVCP-VGAITLTPL 139
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
947-997 |
1.78e-04 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 43.40 E-value: 1.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 947 LIDDDMCINCGKCYMTCAdsgYQAIEFDKDTHIPHVnddCTGC---------TLCVSVCP 997
Cdd:COG0437 86 LVDYDKCIGCRYCVAACP---YGAPRFNPETGVVEK---CTFCadrldegllPACVEACP 139
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
901-1005 |
2.10e-04 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 42.22 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 901 AEQVKATPPASNGAPNPAPRIKDVIGAALDKigsyNKLDNKQQKVALIDDDMCINCGKCYMTCADSGYqaIEFDKDTHIP 980
Cdd:PRK08764 39 EATIDRCPPGGDAGARALAQVLGVPARPYDR----SRGTHKLPQVAWIVEADCIGCTKCIQACPVDAI--VGGAKHMHTV 112
|
90 100
....*....|....*....|....*
gi 24640763 981 hVNDDCTGCTLCVSVCPiIDCITMV 1005
Cdd:PRK08764 113 -IAPLCTGCELCVPACP-VDCIELH 135
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
949-1005 |
2.22e-04 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 41.55 E-value: 2.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24640763 949 DDDMCINCGKCYMTCADSgyqAIEFDKDTHIPHVNDDCTGCTLCVSVCPiIDCITMV 1005
Cdd:PRK09624 49 NRDKCVRCYLCYIYCPEP---AIYLDEEGYPVFDYDYCKGCGICANECP-TKAIEMV 101
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
182-225 |
2.73e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 44.88 E-value: 2.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 24640763 182 PLSQKIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGGLSA 225
Cdd:PRK07208 2 TNKKSVVIIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGISR 44
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
981-1009 |
2.85e-04 |
|
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: 43.69 E-value: 2.85e-04
10 20
....*....|....*....|....*....
gi 24640763 981 HVNDDCTGCTLCVSVCPiIDCITMVPKKI 1009
Cdd:NF038196 182 HVTDKCIGCGICAKVCP-VNNIEMEDGKP 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
945-1005 |
4.31e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.00 E-value: 4.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24640763 945 VALIDDDMCiNCGKCYMTCAD------SGYQAIEFDKDTHIPHVNDD-CTGCTLCVSVCPiIDCITMV 1005
Cdd:COG1245 4 IAVVDRDRC-QPKKCNYECIKycpvnrTGKEAIEIDEDDGKPVISEElCIGCGICVKKCP-FDAISIV 69
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
945-1005 |
5.20e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 5.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24640763 945 VALIDDDMCiNCGKCYMTCAD------SGYQAIEFDKDTHIPHVNDD-CTGCTLCVSVCPiIDCITMV 1005
Cdd:PRK13409 4 IAVVDYDRC-QPKKCNYECIKycpvvrTGEETIEIDEDDGKPVISEElCIGCGICVKKCP-FDAISIV 69
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
185-290 |
5.64e-04 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 43.18 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 185 QKIALVGGGPASLSCATFLARLGyRDVTIYERRSylgGLSAAEIPQYRL------------PIDAVNFEiDLVRdlGVRI 252
Cdd:COG0492 142 KDVVVVGGGDSALEEALYLTKFA-SKVTLIHRRD---ELRASKILVERLranpkievlwntEVTEIEGD-GRVE--GVTL 214
|
90 100 110
....*....|....*....|....*....|....*...
gi 24640763 253 ETGRSLGTKDLTIqgllstghDAVFVGIGLpEPKLNPI 290
Cdd:COG0492 215 KNVKTGEEKELEV--------DGVFVAIGL-KPNTELL 243
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
952-1012 |
5.84e-04 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 41.18 E-value: 5.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640763 952 MCINC--GKCYMTCAdsgYQAIEFDKDthIPHVNDD-CTGCTLCVSVCPiIDCITMVPKKIPHV 1012
Cdd:COG1142 51 QCRHCedAPCAEVCP---VGAITRDDG--AVVVDEEkCIGCGLCVLACP-FGAITMVGEKSRAV 108
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
948-997 |
6.31e-04 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 42.74 E-value: 6.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24640763 948 IDDDMCINCGKCYMTCAdsgyqaiefdkdTHIP-----HVNDDCTGCTLCVSVCP 997
Cdd:COG0348 207 YDRGDCIDCGLCVKVCP------------MGIDirkgeINQSECINCGRCIDACP 249
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
953-997 |
7.54e-04 |
|
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: 433287 [Multi-domain] Cd Length: 61 Bit Score: 38.60 E-value: 7.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 24640763 953 CINCGKCYMTCA---------DSGYQAIEFDK--DTHIPHVNDDCTGCTLCVSVCP 997
Cdd:pfam13534 2 CIQCGCCVDECPryllngdepKKLMRAAYLGDleELQANKVANLCSECGLCEYACP 57
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
186-218 |
9.64e-04 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 42.62 E-value: 9.64e-04
10 20 30
....*....|....*....|....*....|...
gi 24640763 186 KIALVGGGPASLSCATFLARLGYRdVTIYERRS 218
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIR-VTVVERAP 36
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
984-1010 |
1.01e-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: 38.57 E-value: 1.01e-03
10 20
....*....|....*....|....*..
gi 24640763 984 DDCTGCTLCVSVCPiIDCITMVPKKIP 1010
Cdd:COG1143 2 DKCIGCGLCVRVCP-VDAITIEDGEPG 27
|
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
945-1005 |
1.07e-03 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 39.54 E-value: 1.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640763 945 VALIDDDMCINCGKCYMTCADSgyqAIEFDKDTHIPHVNDDCTGCTLCVSVCPiIDCITMV 1005
Cdd:PRK09623 45 MPVVDESKCVKCYICWKFCPEP---AIYIKEDGYVAIDYDYCKGCGICANECP-TKAITMV 101
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
186-253 |
1.13e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 42.60 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24640763 186 KIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGG----LSAAEIPQY------RLPIDAVNFeIDLVRDLGVRIE 253
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGL-DVTVLEARDRVGGrvwtLRFGDDGLYaelgamRIPPSHTNL-LALARELGLPLE 84
|
|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
953-997 |
1.14e-03 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 38.24 E-value: 1.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24640763 953 CINCGKCYMTC---------------ADSGYQAIEFDKDTHI---PHVNDDCTGCTLCVSVCP 997
Cdd:pfam13484 1 CGSCGKCIDACptgaivgpegvldarRCISYLTIEKKGLIPDelrCLLGNRCYGCDICQDVCP 63
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
944-997 |
1.23e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 40.01 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640763 944 KVALIDDDMCINCGKCYMTCADSGYQ-------AIEFDKDTHIPHVNdDCTGCTLCVSVCP 997
Cdd:cd16372 1 KLLVTDPEKCIGCLQCEEACSKTFFKeedreksCIRITETEGGYAIN-VCNQCGECIDVCP 60
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
952-997 |
1.36e-03 |
|
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: 433017 [Multi-domain] Cd Length: 64 Bit Score: 38.06 E-value: 1.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640763 952 MCINCGKCYMTC-----------ADSGYQAIEFDKDTHIPHVNDD----CTGCTLCVSVCP 997
Cdd:pfam13183 1 RCIRCGACLAACpvylvtggrfpGDPRGGAAALLGRLEALEGLAEglwlCTLCGACTEVCP 61
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
767-832 |
1.69e-03 |
|
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 273222 [Multi-domain] Cd Length: 196 Bit Score: 40.70 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24640763 767 PMALKAISDIANRVPGFPILGIGGIDSGEVAlQFIHAGATVLQICSSVqnqdfTVIEDYCTALKAL 832
Cdd:TIGR00693 137 PAGVELLREIAATLIDIPIVAIGGITLENAA-EVLAAGADGVAVVSAI-----MQAADPKAAAKRL 196
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
977-1009 |
1.90e-03 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 37.72 E-value: 1.90e-03
10 20 30
....*....|....*....|....*....|....
gi 24640763 977 THIPHVNDD-CTGCTLCVSVCPiIDCITMVPKKI 1009
Cdd:COG2221 7 TWPPKIDEEkCIGCGLCVAVCP-TGAISLDDGKL 39
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
952-1006 |
2.33e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 41.78 E-value: 2.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 24640763 952 MCINCGKCYMTCADsgyQAIEFDKDTHIPHVN-DDCTGCTLCVSVCPiidC--ITMVP 1006
Cdd:PRK12771 511 NCFECDNCYGACPQ---DAIIKLGPGRRYHFDyDKCTGCHICADVCP---CgaIEMGP 562
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
644-723 |
2.81e-03 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 41.11 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 644 DWTELAIKAE---QSGADALELNLSCPHGMGERGM-GLACGQDPELVEQISRWVRKAVKLPFFIKL----TPNITDIVSI 715
Cdd:PRK10415 75 DPKEMADAARinvESGAQIIDINMGCPAKKVNRKLaGSALLQYPDLVKSILTEVVNAVDVPVTLKIrtgwAPEHRNCVEI 154
|
....*...
gi 24640763 716 AAAAKRGG 723
Cdd:PRK10415 155 AQLAEDCG 162
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
953-1008 |
2.84e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 40.69 E-value: 2.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24640763 953 CINCGKCYMTCAdsgYQAIEFDKDthIPHVNDD-CTGCTLCVSVCPiIDCITMVPKK 1008
Cdd:PRK07118 141 CLGLGSCVAACP---FDAIHIENG--LPVVDEDkCTGCGACVKACP-RNVIELIPKS 191
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
948-997 |
3.55e-03 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 38.87 E-value: 3.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24640763 948 IDDDMCINCGKCYMTCAdsgYQAIEFD--KDTHIPHVNDDCTGCT---LCVSVCP 997
Cdd:COG1142 78 VDEEKCIGCGLCVLACP---FGAITMVgeKSRAVAVKCDLCGGREggpACVEACP 129
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
186-281 |
4.20e-03 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 41.08 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640763 186 KIALVGGGPASLSCATFLARLG-YRDVTIYER-RSY-------------LGGLSAAEIPQYRLPIDAVNF--EIDLVRDl 248
Cdd:PRK08255 2 RIVCIGGGPAGLYFALLMKLLDpAHEVTVVERnRPYdtfgwgvvfsdatLGNLRAADPVSAAAIGDAFNHwdDIDVHFK- 80
|
90 100 110
....*....|....*....|....*....|...
gi 24640763 249 GVRIETGrslgtkdltiqgllstGHDavFVGIG 281
Cdd:PRK08255 81 GRRIRSG----------------GHG--FAGIG 95
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
952-998 |
4.39e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 38.33 E-value: 4.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 24640763 952 MCINCGK--CYMTCAdsgYQAIEFDKDTHIPHVNDD-CTGCTLCVSVCPI 998
Cdd:cd10550 48 VCRQCEDapCVEACP---VGAISRDEETGAVVVDEDkCIGCGMCVEACPF 94
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| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
953-997 |
6.03e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 39.92 E-value: 6.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 24640763 953 CINCGKCYMTCADsgyQAIEFDKDthIPHVN-DDCTGCTLCVSVCP 997
Cdd:PRK07118 215 CIGCGKCVKACPA---GAITMENN--LAVIDqEKCTSCGKCVEKCP 255
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| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
186-222 |
7.41e-03 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 40.17 E-value: 7.41e-03
10 20 30
....*....|....*....|....*....|....*..
gi 24640763 186 KIALVGGGPASLSCATFLARLGYrDVTIYERRSYLGG 222
Cdd:PLN02487 77 KVAIIGAGLAGMSTAVELLDQGH-EVDIYESRPFIGG 112
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| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
192-221 |
8.13e-03 |
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Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 39.57 E-value: 8.13e-03
10 20 30
....*....|....*....|....*....|
gi 24640763 192 GGPASLSCATFLARLGYrDVTIYERRSYLG 221
Cdd:COG0644 1 AGPAGSAAARRLARAGL-SVLLLEKGSFPG 29
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| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
983-1009 |
9.00e-03 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 36.17 E-value: 9.00e-03
10 20
....*....|....*....|....*..
gi 24640763 983 NDDCTGCTLCVSVCPiIDCITMVPKKI 1009
Cdd:COG4231 21 EDKCTGCGACVKVCP-ADAIEEGDGKA 46
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