|
Name |
Accession |
Description |
Interval |
E-value |
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
498-798 |
2.48e-172 |
|
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: 504.13 E-value: 2.48e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 498 DISVEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGFALTKTFSLDKDLVTNVSPRIIRGTTSGHtygpGQGSFLNIE 577
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGR----GQIGFNNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 578 LISEKTMAYWLQSITELKKDYPEKA--SSIMCGFNEQDWTELAKAAEAAGADALELNLSCPHGMGERGMGLACGQNPQLV 655
Cdd:cd02940 77 LISEKPLEYWLKEIRELKKDFPDKIliASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 656 KGICKWVRKAVKIPFFAKLTPNVTDITEIAIAAKEGGADGVTATNTVSGLMGLRGDGSAwPAVGKEKRTTYGGVSGNAIR 735
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTP-PAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1936509173 736 PIALRDVSAIAK-VLPGYPILATGGIDSADAGMQFLHAGASVLQVCSAIQNQDFTVVEDYILGL 798
Cdd:cd02940 236 PIALRAVSQIARaPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
498-968 |
5.33e-121 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 375.82 E-value: 5.33e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 498 DISVEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGFALTKTfsLDKDLVTNVSPRIirgttsGHTYGPGQG--SFLN 575
Cdd:PRK08318 3 DLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKT--LGPPIVNVSSPRF------GALVKEDRRfiGFNN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 576 IELISEKTMAYWLQSITELKKDYPEKA--SSIMCGFNEQDWTELAKAAEAAGADALELNLSCPHGMGERGMGLACGQNPQ 653
Cdd:PRK08318 75 IELITDRPLEVNLREIRRVKRDYPDRAliASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 654 LVKGICKWVRKAVKIPFFAKLTPNVTDITEIAIAAKEGGADGVTATNTVSGLMGLRGDG-SAWPAVGkeKRTTYGGVSGN 732
Cdd:PRK08318 155 LVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRmIPMPIVN--GKSSHGGYCGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 733 AIRPIALRDVSAIAK--VLPGYPILATGGIDSADAGMQFLHAGASVLQVCSAIQNQDFTVVEDYILGLKTllYLEtlqel 810
Cdd:PRK08318 233 AVKPIALNMVAEIARdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSH--YMD----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 811 kswngqspptfkhqlgkpihhheqnlphfgpylkkrhellrkekvkldllsgdllpaparpsyrpQKPIPQVKDVIGRAL 890
Cdd:PRK08318 306 -----------------------------------------------------------------EKGFASLEDMVGLAV 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 891 PMIGSYGDLDNTQQVVALIDEDMCINCGKCYLACNDAGYQAISFD-SKTHIPHVTED-CTGCTLCLSVCPIIDCITMVKR 968
Cdd:PRK08318 321 PNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDeDGTRTPEVIEEeCVGCNLCAHVCPVEGCITMGEV 400
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
63-472 |
1.63e-92 |
|
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: 300.90 E-value: 1.63e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 63 NYYGAAKAIFSDNPLGLTCGMVCPTsdLCVGGCNLyASEEGPINIGGLQQFATEvfKHMKIPQILPPEVLPVSQRhqsyi 142
Cdd:COG0493 53 DYEEALELIHETNPFPEVCGRVCPA--PCEGACVR-GIVDEPVAIGALERFIAD--KAFEEGWVKPPPPAPRTGK----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 143 ssKVALIGCGPASISCATFLARLGY-VnlTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGVKIETGRALSTsD 221
Cdd:COG0493 123 --KVAVVGSGPAGLAAAYQLARAGHeV--TVFEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGK-D 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 222 LTInvtisnmfasQKLKEEgYNAIFIGIGMPDPKVIKVfEGlTEEQGFYTSKGFLPRVAKaskagMCAcKSSLPSLHGNV 301
Cdd:COG0493 198 ITL----------DELLEE-FDAVFLATGAGKPRDLGI-PG-EDLKGVHSAMDFLTAVNL-----GEA-PDTILAVGKRV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 302 IVLGAGDTAFDCATSALRCGAKRVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQVFVKGD-RLTGMEFCRTE-- 378
Cdd:COG0493 259 VVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLFLVAPVEIIGDENgRVTGLECVRMElg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 379 -QDNQGNW----IEDEEQTIrlKADFVISAFGSTiANSDVLKAMEPVRLTPHGTVEVDEETMATSELGVFCGGDLGGTAE 453
Cdd:COG0493 339 ePDESGRRrpvpIEGSEFTL--PADLVILAIGQT-PDPSGLEEELGLELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPS 415
|
410
....*....|....*....
gi 1936509173 454 TTVESVNDGKTAAWHMHRY 472
Cdd:COG0493 416 LVVWAIAEGRKAARAIDRY 434
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
66-477 |
2.47e-92 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 301.33 E-value: 2.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 66 GAAKAIFSDNPLGLTCGMVCPTSDLCVGGCNLYASEEgPINIGGLQQFATE-VFKHMKIPQILPPEvlpvsqrhqsyISS 144
Cdd:PRK11749 74 GAAETILETNPLPAVCGRVCPQERLCEGACVRGKKGE-PVAIGRLERYITDwAMETGWVLFKRAPK-----------TGK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 145 KVALIGCGPASISCATFLARLGYvNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGVKIETGRALSTsdlti 224
Cdd:PRK11749 142 KVAVIGAGPAGLTAAHRLARKGY-DVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGR----- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 225 NVTISNMFasqklkeEGYNAIFIGIGMPDPKVIKVF-EGLteeQGFYTSKGFLPRVAKAskagmcacKSSLPSLHG-NVI 302
Cdd:PRK11749 216 DITLDELR-------AGYDAVFIGTGAGLPRFLGIPgENL---GGVYSAVDFLTRVNQA--------VADYDLPVGkRVV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 303 VLGAGDTAFDCATSALRCGAKRVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQVFVKGDRLTGMEFCRTE---Q 379
Cdd:PRK11749 278 VIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMElgeP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 380 DNQGN---WIEDEEQTirLKADFVISAFGSTiANSDVLKAMEPVRLTPHGTVEVDEETMATSELGVFCGGDLGGTAETTV 456
Cdd:PRK11749 358 DASGRrrvPIEGSEFT--LPADLVIKAIGQT-PNPLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVV 434
|
410 420
....*....|....*....|.
gi 1936509173 457 ESVNDGKTAAWHMHRYIQQKY 477
Cdd:PRK11749 435 WAVGDGKDAAEAIHEYLEGAA 455
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
501-795 |
1.64e-75 |
|
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: 249.96 E-value: 1.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 501 VEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGFALTKTFSLDKDlVTNVSPRIIRGTTSGHTYgPGQGSFLNIELIS 580
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPR-PGNPLPRVARLPPEGESY-PEQLGILNSFGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 581 EKTMAYWLQSITELKKDYPEK---ASsiMCGFNEQDWTELAKAAEAAGADALELNLSCPHGMGERGmglaCGQNPQLVKG 657
Cdd:cd02810 79 NLGLDVWLQDIAKAKKEFPGQpliAS--VGGSSKEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVAN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 658 ICKWVRKAVKIPFFAKLTPNVT--DITEIAIAAKEGGADGVTATNTVSGLMGLRgdgsawPAVGKEKRTTYGGVSGNAIR 735
Cdd:cd02810 153 LLKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDL------KTVGPGPKRGTGGLSGAPIR 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1936509173 736 PIALRDVSAIAKVLP-GYPILATGGIDSADAGMQFLHAGASVLQVCSAIQNQDFTVVEDYI 795
Cdd:cd02810 227 PLALRWVARLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIK 287
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
498-821 |
5.33e-74 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 249.37 E-value: 5.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 498 DISVEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGFALTKTFSLDKDLVTNVSPRIIRGTTSGHTYGPGQG-SFLNI 576
Cdd:PLN02495 10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARLRAGANGSAKGRViGWQNI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 577 ELISEKTMAYWLQSITELKKDYPEKA--SSIMCGFNEQDWTELAKAAEAAGADALELNLSCPHGMGERGMGLACGQNPQL 654
Cdd:PLN02495 90 ELISDRPFETMLAEFKQLKEEYPDRIliASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVGQDCDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 655 VKGICKWVRKAVKIPFFAKLTPNVTDITEIAIAAKEGGADGVTATNTVSGLMG-----LRGDgsawPAVgkEKRTTYGGV 729
Cdd:PLN02495 170 LEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGinldtLRPE----PCV--EGYSTPGGY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 730 SGNAIRPIALRDVSAIAKVL-----PGYPILATGGIDSADAGMQFLHAGASVLQVCSAIQNQDFTVVEDYILGLKTLLYL 804
Cdd:PLN02495 244 SSKAVRPIALAKVMAIAKMMksefpEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKK 323
|
330
....*....|....*..
gi 1936509173 805 ETLQELKSWNGQSPPTF 821
Cdd:PLN02495 324 HNFSSIEDFRGASLPYF 340
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
498-802 |
3.94e-68 |
|
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: 229.57 E-value: 3.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 498 DISVEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGFALTKTfsldkdlVT------NVSPRIIRgttsghTygPGQG 571
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKT-------VTpepqpgNPRPRLFR------L--PEDS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 572 SFLNIELISEKTMAYWLQSITELKKDYPEKASSIMcGFNEQDWTELAKAAEAAGADALELNLSCPHGmgeRGMGLACGQN 651
Cdd:COG0167 66 GLINRMGLNNPGVDAFLERLLPAKRYDVPVIVNIG-GNTVEDYVELARRLADAGADYLELNISCPNT---PGGGRALGQD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 652 PQLVKGICKWVRKAVKIPFFAKLTPNVTDITEIAIAAKEGGADGVTATNTVSGL-MGLRgdgSAWPAVGKEkrttYGGVS 730
Cdd:COG0167 142 PEALAELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRaIDLE---TRRPVLANE----AGGLS 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1936509173 731 GNAIRPIALRDVSAIAKVLPG-YPILATGGIDSADAGMQFLHAGASVLQVCSAIQNQDFTVVEDYILGLKTLL 802
Cdd:COG0167 215 GPALKPIALRMVREVAQAVGGdIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYL 287
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
57-477 |
1.67e-65 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 228.36 E-value: 1.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 57 SALMATNYYGAAKAIFSDNPLGLTCGMVCPTSDLCVGGCNLYASEEgPINIGGLQQFATEVFKHMKIPQILPPEvlpvsQ 136
Cdd:PRK12831 65 SKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQCEGKCVLGIKGE-PVAIGKLERFVADWARENGIDLSETEE-----K 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 137 RHQsyissKVALIGCGPASISCATFLARLGYvNLTIFEKQNYIGGLSSSEIPQYRLPYD-VVDFEIALMQDLGVKIET-- 213
Cdd:PRK12831 139 KGK-----KVAVIGSGPAGLTCAGDLAKMGY-DVTIFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIETnv 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 214 --GRALSTSDLtinvtisnmfasqkLKEEGYNAIFIGIGMPDPKvikvFEGLTEEQ--GFYTSKGFLPRV--AKASKAGm 287
Cdd:PRK12831 213 vvGKTVTIDEL--------------LEEEGFDAVFIGSGAGLPK----FMGIPGENlnGVFSANEFLTRVnlMKAYKPE- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 288 cackSSLPSLHGN-VIVLGAGDTAFDCATSALRCGAKrVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPrqVFVKG 366
Cdd:PRK12831 274 ----YDTPIKVGKkVAVVGGGNVAMDAARTALRLGAE-VHIVYRRSEEELPARVEEVHHAKEEGVIFDLLTNP--VEILG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 367 D---RLTGMEFCRT---EQDNQGNW--IEDEEQTIRLKADFVISAFGsTIANSDVLKAMEPVRLTPHGTVEVDEETMATS 438
Cdd:PRK12831 347 DengWVKGMKCIKMelgEPDASGRRrpVEIEGSEFVLEVDTVIMSLG-TSPNPLISSTTKGLKINKRGCIVADEETGLTS 425
|
410 420 430
....*....|....*....|....*....|....*....
gi 1936509173 439 ELGVFCGGDLGGTAETTVESVNDGKTAAWHMHRYIQQKY 477
Cdd:PRK12831 426 KEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSKKW 464
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
63-476 |
4.59e-60 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 219.61 E-value: 4.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 63 NYYGAAKAIFSDNPLGLTCGMVCPTSDLCVGGCNLYASEEGPINIGGLQQFATEVFKhmKIPQILPPEVLPVSQRhqsyi 142
Cdd:PRK12778 360 NFLEAAKILKETSALPAVCGRVCPQEKQCESKCIHGKMGEEAVAIGYLERFVADYER--ESGNISVPEVAEKNGK----- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 143 ssKVALIGCGPASISCATFLARLGYvNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGVKIETgralstsDL 222
Cdd:PRK12778 433 --KVAVIGSGPAGLSFAGDLAKRGY-DVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFET-------DV 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 223 TINVTISnmfaSQKLKEEGYNAIFIGIGMPDPKvikvFEGLTEEQ--GFYTSKGFLPRV--AKASKAGmcackSSLPSLH 298
Cdd:PRK12778 503 IVGKTIT----IEELEEEGFKGIFIASGAGLPN----FMNIPGENsnGVMSSNEYLTRVnlMDAASPD-----SDTPIKF 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 299 G-NVIVLGAGDTAFDCATSALRCGAKRVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQV------FVKGDRLTG 371
Cdd:PRK12778 570 GkKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARLEEVKHAKEEGIEFLTLHNPIEYladekgWVKQVVLQK 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 372 MEFcrTEQDNQGNW--IEDEEQTIRLKADFVISAFGSTiANSDVLKAMEPVRLTPHGTVEVDEETMATSElGVFCGGDLG 449
Cdd:PRK12778 650 MEL--GEPDASGRRrpVAIPGSTFTVDVDLVIVSVGVS-PNPLVPSSIPGLELNRKGTIVVDEEMQSSIP-GIYAGGDIV 725
|
410 420
....*....|....*....|....*..
gi 1936509173 450 GTAETTVESVNDGKTAAWHMHRYIQQK 476
Cdd:PRK12778 726 RGGATVILAMGDGKRAAAAIDEYLSSK 752
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
500-802 |
1.84e-51 |
|
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: 183.13 E-value: 1.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 500 SVEMCGLKFENPFGLASAPPTTSSSMiHRAFEQGW-GFALTKTFSLDKDLvTNVSPRIIRgTTSGhtygpgqgsFLN-IE 577
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEEL-SRVADLGKlGAIVTKSITLEPRE-GNPPPRVVE-TPGG---------MLNaIG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 578 LiSEKTMAYWLQSITELKKDYPEKA-SSIMcGFNEQDWTELAKAAEAAGADALELNLSCPHgmgERGMGLACGQNPQLVK 656
Cdd:cd04740 69 L-QNPGVEAFLEELLPWLREFGTPViASIA-GSTVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDPEAVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 657 GICKWVRKAVKIPFFAKLTPNVTDITEIAIAAKEGGADGVTATNTvsgLMGLRGD-GSAWPAVGkekrTTYGGVSGNAIR 735
Cdd:cd04740 144 EIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINT---LKGMAIDiETRKPILG----NVTGGLSGPAIK 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1936509173 736 PIALRDVSAIAKVLpGYPILATGGIDSADAGMQFLHAGASVLQVCSAIQnQDFTVVEDYILGLKTLL 802
Cdd:cd04740 217 PIALRMVYQVYKAV-EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYL 281
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
498-810 |
2.66e-50 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 179.96 E-value: 2.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 498 DISVEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGFALTKTFSLDKDLvTNVSPRIIRgTTSGhtygpgqgsFLNie 577
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPRE-GNPTPRIAE-TPGG---------MLN-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 578 lisektmAYWLQ--SITE-LKKDYPEKAS-------SImCGFNEQDWTELAKA-AEAAGADALELNLSCPHGMGergMGL 646
Cdd:PRK07259 68 -------AIGLQnpGVDAfIEEELPWLEEfdtpiiaNV-AGSTEEEYAEVAEKlSKAPNVDAIELNISCPNVKH---GGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 647 ACGQNPQLVKGICKWVRKAVKIPFFAKLTPNVTDITEIAIAAKEGGADGVTATNTvsgLMGLRGD-GSAWPAVGkekrTT 725
Cdd:PRK07259 137 AFGTDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAIDiKTRKPILA----NV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 726 YGGVSGNAIRPIALRDVSAIAKVLpGYPILATGGIDSADAGMQFLHAGASVLQVCSAIQnQDFTVVEDYILGLKTLLY-- 803
Cdd:PRK07259 210 TGGLSGPAIKPIALRMVYQVYQAV-DIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDky 287
|
....*...
gi 1936509173 804 -LETLQEL 810
Cdd:PRK07259 288 gIKSIEEI 295
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
61-472 |
1.72e-49 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 185.08 E-value: 1.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 61 ATNYYGAAKAIFSDNPLGLTCGMVCPTSdlCVGGCNlYASEEGPINIGGLQQFATEvfkhMKIPQILPPEVLPVSQRHqs 140
Cdd:PRK12771 68 GGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCN-RGQVDDAVGINAVERFLGD----YAIANGWKFPAPAPDTGK-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 141 yissKVALIGCGPASISCATFLARLGYvNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGVKIETGRALSTs 220
Cdd:PRK12771 139 ----RVAVIGGGPAGLSAAYHLRRMGH-AVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGVEVRLGVRVGE- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 221 DLTINvtisnmfasqKLkEEGYNAIFIGIGMPDPKVIKVfEGlTEEQGFYTSKGFLPRVAKASKagmcacksslPSLHGN 300
Cdd:PRK12771 213 DITLE----------QL-EGEFDAVFVAIGAQLGKRLPI-PG-EDAAGVLDAVDFLRAVGEGEP----------PFLGKR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 301 VIVLGAGDTAFDCATSALRCGAKRVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQVFVKGDRLTGMEFCRTEQ- 379
Cdd:PRK12771 270 VVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVITVEKm 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 380 -DNQGNW---IEDEEQTIrlKADFVISAFGSTIaNSDVLKAMEPVRlTPHGTVEVDEETMATSELGVFCGGDLGGTAETT 455
Cdd:PRK12771 350 eLDEDGRpspVTGEEETL--EADLVVLAIGQDI-DSAGLESVPGVE-VGRGVVQVDPNFMMTGRPGVFAGGDMVPGPRTV 425
|
410
....*....|....*..
gi 1936509173 456 VESVNDGKTAAWHMHRY 472
Cdd:PRK12771 426 TTAIGHGKKAARNIDAF 442
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
499-783 |
7.08e-48 |
|
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: 173.00 E-value: 7.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 499 ISVEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGFALTKTFSLDKDLvTNVSPRIIRGTtsghtygpgqGSFLNIEL 578
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRP-GYRNPTIVETP----------CGMLNAIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 579 ISEKTMAYWLQSITELKKDYPEKASSIMCGFNEQDWTELAKA--AEAAGADALELNLSCPHGMGergMGLACGQNPQLVK 656
Cdd:TIGR01037 70 LQNPGVEAFLEELKPVREEFPTPLIASVYGSSVEEFAEVAEKleKAPPYVDAYELNLSCPHVKG---GGIAIGQDPELSA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 657 GICKWVRKAVKIPFFAKLTPNVTDITEIAIAAKEGGADGVTATNTvsgLMGLRGD-GSAWPAVGkekrTTYGGVSGNAIR 735
Cdd:TIGR01037 147 DVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKIDiKTGKPILA----NKTGGLSGPAIK 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1936509173 736 PIALRDVSAIAKVLpGYPILATGGIDSADAGMQFLHAGASVLQVCSAI 783
Cdd:TIGR01037 220 PIALRMVYDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAV 266
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
63-474 |
1.05e-47 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 177.28 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 63 NYYGAAKAIFSDNPLGLTCGMVCPTSdlCVGGCNLyASEEGPINIGGLQQFATEvfKHMKIPQILPpeVLPVSQRHQsyi 142
Cdd:PRK12810 75 RWEEAAERLHQTNNFPEFTGRVCPAP--CEGACTL-NINFGPVTIKNIERYIID--KAFEEGWVKP--DPPVKRTGK--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 143 ssKVALIGCGPASISCATFLARLGyVNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGVKIETGralstsdL 222
Cdd:PRK12810 145 --KVAVVGSGPAGLAAADQLARAG-HKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTN-------V 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 223 TINVTISnmfaSQKLKEEgYNAIFIGIGMPDPKVIKVfEGltEE-QGFYTSKGFLP----RVAKASKAGMcacksslPSL 297
Cdd:PRK12810 215 EVGKDIT----AEELLAE-YDAVFLGTGAYKPRDLGI-PG--RDlDGVHFAMDFLIqntrRVLGDETEPF-------ISA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 298 HG-NVIVLGAGDTAFDCATSALRCGAKRVfVVF---------RKGFTNIRAVPEEMEL--AREEKCEFLPFLSPRQVFVK 365
Cdd:PRK12810 280 KGkHVVVIGGGDTGMDCVGTAIRQGAKSV-TQRdimpmppsrRNKNNPWPYWPMKLEVsnAHEEGVEREFNVQTKEFEGE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 366 GDRLTGMEFCRTE-QDNQGNWIEDEEQTIrlKADFVISAFGSTIANSDVLKAMEpVRLTPHGTVEVDEETMATSELGVFC 444
Cdd:PRK12810 359 NGKVTGVKVVRTElGEGDFEPVEGSEFVL--PADLVLLAMGFTGPEAGLLAQFG-VELDERGRVAAPDNAYQTSNPKVFA 435
|
410 420 430
....*....|....*....|....*....|
gi 1936509173 445 GGDLGGTAETTVESVNDGKTAAWHMHRYIQ 474
Cdd:PRK12810 436 AGDMRRGQSLVVWAIAEGRQAARAIDAYLM 465
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
66-533 |
2.25e-42 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 168.20 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 66 GAAKAIFSDNPLGLTCGMVCPTSDLCVGGCnLYASEEGPINIGGLQQFateVFKHMKIPQILPPEVlpvsqrhqSYISSK 145
Cdd:PRK12775 365 GALEVIYEASIFPSICGRVCPQETQCEAQC-IIAKKHESVGIGRLERF---VGDNARAKPVKPPRF--------SKKLGK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 146 VALIGCGPASISCATFLARLGyVNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGVKIETGRALSTSdLTIN 225
Cdd:PRK12775 433 VAICGSGPAGLAAAADLVKYG-VDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKT-FTVP 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 226 vtisnmfasQKLKEEGYNAIFIGIGMPDPKvikvFEGLTEEQG--FYTSKGFLPRVaKASKAGMCACKSSLPSLHGNVIV 303
Cdd:PRK12775 511 ---------QLMNDKGFDAVFLGVGAGAPT----FLGIPGEFAgqVYSANEFLTRV-NLMGGDKFPFLDTPISLGKSVVV 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 304 LGAGDTAFDCATSALRCGAKRVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQVF------VKGDRLTGMEFCRT 377
Cdd:PRK12775 577 IGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGIDFFFLHSPVEIYvdaegsVRGMKVEEMELGEP 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 378 EQDNQGNWIEDEEqTIRLKADFVISAFGsTIANSDVLKAMEPVRLTPHGTVEVD----EETMATSELGVFCGGDLGGTAE 453
Cdd:PRK12775 657 DEKGRRKPMPTGE-FKDLECDTVIYALG-TKANPIITQSTPGLALNKWGNIAADdgklESTQSTNLPGVFAGGDIVTGGA 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 454 TTVESVNDGKTAAWHMHRYIqqkyglgtpetpRLPKFYtPIDLVDISvemcglKFENPFGLASAPPTTSSSMIHRAFEQG 533
Cdd:PRK12775 735 TVILAMGAGRRAARSIATYL------------RLGKKW-PITAEEAA------AFQPGKLLPAIELHTHAGAVAAGAETG 795
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
57-488 |
6.26e-39 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 154.89 E-value: 6.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 57 SALMATNYYGAAKAIFSDNPLGLTCGMVCPTSdlCVGGCNLYASEEgPINIGGLQQFATEvfKHMKIPQILPPEVLPVSQ 136
Cdd:PRK12814 119 AAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDE-PVSICALKRYAAD--RDMESAERYIPERAPKSG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 137 RHqsyisskVALIGCGPASISCATFLARLGYvNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGVKIETGRA 216
Cdd:PRK12814 194 KK-------VAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAMGAEFRFNTV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 217 LStSDLTInvtisnmfasQKLKEEgYNAIFIGIGMPDPKVIKVfEGlTEEQGFYTSKGFLPRVAKASKagmcacksslPS 296
Cdd:PRK12814 266 FG-RDITL----------EELQKE-FDAVLLAVGAQKASKMGI-PG-EELPGVISGIDFLRNVALGTA----------LH 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 297 LHGNVIVLGAGDTAFDCATSALRCGAKRVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQVFVKGDRL--TGMEF 374
Cdd:PRK12814 322 PGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGGLelTAIKM 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 375 CRTEQDNQGNW----IEDEEQTIrlKADFVISAFGSTIansDVLKAMEP-VRLTPHGTVEVDEETMATSELGVFCGGDLG 449
Cdd:PRK12814 402 QQGEPDESGRRrpvpVEGSEFTL--QADTVISAIGQQV---DPPIAEAAgIGTSRNGTVKVDPETLQTSVAGVFAGGDCV 476
|
410 420 430
....*....|....*....|....*....|....*....
gi 1936509173 450 GTAETTVESVNDGKTAAWHMHRYIQQKyglgTPETPRLP 488
Cdd:PRK12814 477 TGADIAINAVEQGKRAAHAIDLFLNGK----PVTAPVQP 511
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
63-476 |
2.16e-36 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 146.45 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 63 NYYGAAKAIFSDNPLGLTCGMVCptSDLCVGGCNLYASEEgPINIGGLQQFATEVFKHMKIPQILPPEVLPVSQrhqsyi 142
Cdd:PRK13984 214 DLEEGLRWLYKTNPLSMVCGRVC--THKCETVCSIGHRGE-PIAIRWLKRYIVDNVPVEKYSEILDDEPEKKNK------ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 143 ssKVALIGCGPASISCATFLARLGYvNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGVKIETgralstsdl 222
Cdd:PRK13984 285 --KVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHL--------- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 223 tiNVTISNMFASQKLKeEGYNAIFIGIG--------MP---DPKVIKVFEGLTEEQGFYTSKGFLPRVAKaskagmcack 291
Cdd:PRK13984 353 --NTRVGKDIPLEELR-EKHDAVFLSTGftlgrstrIPgtdHPDVIQALPLLREIRDYLRGEGPKPKIPR---------- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 292 sslpslhgNVIVLGAGDTAFDCATSALRC-----GAKRVFVV-FRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQVFVK 365
Cdd:PRK13984 420 --------SLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTsLERTFEEMPADMEEIEEGLEEGVVIYPGWGPMEVVIE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 366 GDRLTGMEF--CRTEQDNQG--NWIEDEEQTIRLKADFVISAFGSTIANS----DVLKAMEPVRltphGTVEVDEETMaT 437
Cdd:PRK13984 492 NDKVKGVKFkkCVEVFDEEGrfNPKFDESDQIIVEADMVVEAIGQAPDYSylpeELKSKLEFVR----GRILTNEYGQ-T 566
|
410 420 430
....*....|....*....|....*....|....*....
gi 1936509173 438 SELGVFCGGDLGGTAEtTVESVNDGKTAAWHMHRYIQQK 476
Cdd:PRK13984 567 SIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYLRKQ 604
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
500-802 |
1.80e-35 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 136.71 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 500 SVEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGFALTKTFSLDKDlVTNVSPRIIRgttsghTYGpgqgSFLN-IEL 578
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQ-PGNPTPRVFR------LPE----GVLNrMGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 579 ISEKTMAYwLQSITELKKDYPEKASSIMCGFN---EQDWTELAKAAEAAGADaLELNLSCPHGMGERgmglACGQNPQLV 655
Cdd:pfam01180 72 NNPGLDAV-LAELLKRRKEYPRPDLGINLSKAgmtVDDYVEVARKIGPFADY-IELNVSCPNTPGLR----ALQTDPELA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 656 KGICKWVRKAVKIPFFAKLTPNVTDITEIAIAAKEGGADGVTATN-TVSGLMGLRGDGSAWPAVGKEKrttYGGVSGNAI 734
Cdd:pfam01180 146 AILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINaTNTTVRGMRIDLKTEKPILANG---TGGLSGPPI 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1936509173 735 RPIALRDVSAIAKVL-PGYPILATGGIDSADAGMQFLHAGASVLQVCSAIQNQDFTVVEDYILGLKTLL 802
Cdd:pfam01180 223 KPIALKVIRELYQRTgPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
67-478 |
3.95e-34 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 139.78 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 67 AAKAIFSDNPLGLTCGMVCPTSDLCVGGCNLyASEEGPINIGGLQQFATEVFKHMKipqiLPPEVLPVSQRHQsyissKV 146
Cdd:PRK12809 244 AAELCHQTSSLPEICGRVCPQDRLCEGACTL-KDHSGAVSIGNLERYITDTALAMG----WRPDVSKVVPRSE-----KV 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 147 ALIGCGPASISCATFLARLGyVNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGVKI----ETGRALSTSDL 222
Cdd:PRK12809 314 AVIGAGPAGLGCADILARAG-VQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFhlncEIGRDITFSDL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 223 TinvtisnmfasqklkeEGYNAIFIGIG--------MPD---PKVIKVfeglteeqgfytskgfLPRVAKASKAGMCACK 291
Cdd:PRK12809 393 T----------------SEYDAVFIGVGtygmmradLPHedaPGVIQA----------------LPFLTAHTRQLMGLPE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 292 SS---LPSLHG-NVIVLGAGDTAFDCATSALRCGAKRVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQVFVKGD 367
Cdd:PRK12809 441 SEeypLTDVEGkRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDED 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 368 -RLTGMEFCRTEQDNQGNWIEDEEQTI-----RLKADFVISAFGSTIANSDVLKAMEpVRLTPHGTVE---VDEETMATS 438
Cdd:PRK12809 521 gRLTAVGLIRTAMGEPGPDGRRRPRPVagsefELPADVLIMAFGFQAHAMPWLQGSG-IKLDKWGLIQtgdVGYLPTQTH 599
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1936509173 439 ELGVFCGGDLGGTAETTVESVNDGKTAAWHMHRYIQQKYG 478
Cdd:PRK12809 600 LKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFDTKAS 639
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
59-466 |
2.88e-31 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 132.65 E-value: 2.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 59 LMATNYYGAA-KAIFSDNPLGLTCGMVCPTSDLCVGGCnlyASEEGPINIGGLQQFATEvfkHMKI--PQILPPEVLPVS 135
Cdd:PRK12779 226 LLGNGKHREAlELIESCNPLPNVTGRVCPQELQCQGVC---THTKRPIEIGQLEWYLPQ---HEKLvnPNANERFAGRIS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 136 QrHQSYISSKVALIGCGPASISCATFLARLGYvNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGvkietGR 215
Cdd:PRK12779 300 P-WAAAVKPPIAVVGSGPSGLINAYLLAVEGF-PVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLG-----GR 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 216 ALStsdltiNVTISNMFASQKLKEEGYNAIFIGIGMPDPKVIKV-FEGLTeeqGFYTSKGFLPRVaKASKAGMCACKSSL 294
Cdd:PRK12779 373 FVK------NFVVGKTATLEDLKAAGFWKIFVGTGAGLPTFMNVpGEHLL---GVMSANEFLTRV-NLMRGLDDDYETPL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 295 PSLHG-NVIVLGAGDTAFDCATSALRCGAKrVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQV-------FVKG 366
Cdd:PRK12779 443 PEVKGkEVFVIGGGNTAMDAARTAKRLGGN-VTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFigddhthFVTH 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 367 DRLTGMEFcrTEQDNQGNWI-EDEEQTIRLKADFVISAFGSTiANSdVLKAMEP-VRLTPHGTVEVDEETMATSELGVFC 444
Cdd:PRK12779 522 ALLDVNEL--GEPDKSGRRSpKPTGEIERVPVDLVIMALGNT-ANP-IMKDAEPgLKTNKWGTIEVEKGSQRTSIKGVYS 597
|
410 420
....*....|....*....|..
gi 1936509173 445 GGDLGGTAETTVESVNDGKTAA 466
Cdd:PRK12779 598 GGDAARGGSTAIRAAGDGQAAA 619
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
907-965 |
3.47e-31 |
|
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: 116.23 E-value: 3.47e-31
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1936509173 907 ALIDEDMCINCGKCYLACNDAGYQAISFDSKTHIPHVTEDCTGCTLCLSVCPIIDCITM 965
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDDCITM 59
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
145-476 |
1.96e-30 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 123.56 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 145 KVALIGCGPASISCATFLARLGYvNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGV------KIETGRALS 218
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYLACLGY-EVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVvfhtrtKVCCGEPLH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 219 TSDltinvtiSNMFASQK--LKE--EGYNAIFIGIGMPDPKVIKV-FEGLteeQGFYTSKGFLPRVaKASKAGMCACKSS 293
Cdd:PRK12770 99 EEE-------GDEFVERIvsLEElvKKYDAVLIATGTWKSRKLGIpGEDL---PGVYSALEYLFRI-RAAKLGYLPWEKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 294 LPSLHGNVIVLGAGDTAFDCATSALRCGAKRVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQvFVKGDRLTGME 373
Cdd:PRK12770 168 PPVEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVR-IIGEGRVEGVE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 374 FCRT---EQDNQGNW----IEDEEQTIrlKADFVISAFGStIANSDVLKAMEPVRLTPHGTVEVDEETMaTSELGVFCGG 446
Cdd:PRK12770 247 LAKMrlgEPDESGRPrpvpIPGSEFVL--EADTVVFAIGE-IPTPPFAKECLGIELNRKGEIVVDEKHM-TSREGVFAAG 322
|
330 340 350
....*....|....*....|....*....|....*.
gi 1936509173 447 D------LGGTAettvesVNDGKTAAWHMHRYIQQK 476
Cdd:PRK12770 323 DvvtgpsKIGKA------IKSGLRAAQSIHEWLDLK 352
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
81-473 |
3.00e-30 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 127.94 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 81 CGMVCPTSDLCVGGCNLyASEEGPINIGGLQQFATEVFKHMKIPQILPpEVLPVSQRhqsyisskVALIGCGPASISCAT 160
Cdd:PRK12769 275 TGRVCPQDRLCEGACTL-RDEYGAVTIGNIERYISDQALAKGWRPDLS-QVTKSDKR--------VAIIGAGPAGLACAD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 161 FLARLGyVNLTIFEKQNYIGGLSSSEIPQYRLPYDVVDFEIALMQDLGVKI----ETGRALSTSDLTinvtisnmfasqk 236
Cdd:PRK12769 345 VLARNG-VAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFelncEVGKDISLESLL------------- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 237 lkeEGYNAIFIGIGMPdpKVIKVfeGLTEE--QGFYTSKGFLprVAKASKAGMCACKSSLP--SLHG-NVIVLGAGDTAF 311
Cdd:PRK12769 411 ---EDYDAVFVGVGTY--RSMKA--GLPNEdaPGVYDALPFL--IANTKQVMGLEELPEEPfiNTAGlNVVVLGGGDTAM 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 312 DCATSALRCGAKRVFVVFRKGFTNIRAVPEEMELAREEKCEFLPFLSPRQVFVKGD-RLTGMEFCRT---EQDNQGNW-- 385
Cdd:PRK12769 482 DCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELNEQgHVCGIRFLRTrlgEPDAQGRRrp 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 386 --IEDEEQTIrlKADFVISAFGSTIANSDVLKAMEpVRLTPHGTVEVDEET---MATSELGVFCGGDLGGTAETTVESVN 460
Cdd:PRK12769 562 vpIPGSEFVM--PADAVIMAFGFNPHGMPWLESHG-VTVDKWGRIIADVESqyrYQTSNPKIFAGGDAVRGADLVVTAMA 638
|
410
....*....|...
gi 1936509173 461 DGKTAAWHMHRYI 473
Cdd:PRK12769 639 EGRHAAQGIIDWL 651
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
63-123 |
1.61e-20 |
|
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: 87.59 E-value: 1.61e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1936509173 63 NYYGAAKAIFSDNPLGLTCGMVCPTSDLCVGGCNLYASEEGPINIGGLQQFATEVFKHMKI 123
Cdd:pfam14691 53 NFEGAARIILETNPLPAICGRVCPQERQCEGACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
501-799 |
1.12e-17 |
|
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240092 Cd Length: 294 Bit Score: 84.68 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 501 VEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGFALTKTFSLDkdlvtnvsPRiiRGTTSGHTYGPGQGSFLNIELiS 580
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLA--------GR--PGNPEPRYYAFPLGSINSLGL-P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 581 EKTMAYWLQSITELKKDYPEKASSI---MCGFNE--QDWTELAKAAEAAGADALELNLSCPH--GMGERGmglACGqnPQ 653
Cdd:cd04741 70 NLGLDYYLEYIRTISDGLPGSAKPFfisVTGSAEdiAAMYKKIAAHQKQFPLAMELNLSCPNvpGKPPPA---YDF--DA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 654 LVKgICKWVRKAVKIPFFAKLTPnVTDIT--EIAIAAKEGGADG---VTATNTV-SGLMGlrgDGSAWPAVGKEKrTTYG 727
Cdd:cd04741 145 TLE-YLTAVKAAYSIPVGVKTPP-YTDPAqfDTLAEALNAFACPisfITATNTLgNGLVL---DPERETVVLKPK-TGFG 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1936509173 728 GVSGNAIRPIALRDVSAIAKVLPGY-PILATGGIDSADAGMQFLHAGASVLQVCSAIQNQDFTVVEDYILGLK 799
Cdd:cd04741 219 GLAGAYLHPLALGNVRTFRRLLPSEiQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELE 291
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
629-783 |
3.30e-17 |
|
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: 84.09 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 629 LELNLSCPHGMGERGMglacgQNPQLVKGICKWVRKAV-----KIPFFAKLTPNVTD--ITEIAIAAKEGGADGVTATNT 701
Cdd:cd04738 164 LVVNVSSPNTPGLRDL-----QGKEALRELLTAVKEERnklgkKVPLLVKIAPDLSDeeLEDIADVALEHGVDGIIATNT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 702 VSGLMGLRGdgsawpavgKEKRTTYGGVSGNAIRPIALRDVSAIAKVLPG-YPILATGGIDSADAGMQFLHAGASVLQVC 780
Cdd:cd04738 239 TISRPGLLR---------SPLANETGGLSGAPLKERSTEVLRELYKLTGGkIPIIGVGGISSGEDAYEKIRAGASLVQLY 309
|
...
gi 1936509173 781 SAI 783
Cdd:cd04738 310 TGL 312
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
909-968 |
3.82e-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: 68.54 E-value: 3.82e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 909 IDEDMCINCGKCYLACNDagyQAISFDSKTHIPHVTEDCTGCTLCLSVCPiIDCITMVKR 968
Cdd:COG1144 27 VDEDKCIGCGLCWIVCPD---GAIRVDDGKYYGIDYDYCKGCGICAEVCP-VKAIEMVPE 82
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
629-782 |
9.54e-14 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 73.66 E-value: 9.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 629 LELNLSCPHGMGERGMglacgQNPQLVKGICKWVRKAVK-----IPFFAKLTPNVTD--ITEIAIAAKEGGADGVTATNT 701
Cdd:PRK05286 173 FTVNISSPNTPGLRDL-----QYGEALDELLAALKEAQAelhgyVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIATNT 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 702 V---SGLMGLRGDGSAwpavgkekrttyGGVSGNAIRPIALRDVSAIAKVLPG-YPILATGGIDSADAGMQFLHAGASVL 777
Cdd:PRK05286 248 TlsrDGLKGLPNADEA------------GGLSGRPLFERSTEVIRRLYKELGGrLPIIGVGGIDSAEDAYEKIRAGASLV 315
|
....*
gi 1936509173 778 QVCSA 782
Cdd:PRK05286 316 QIYSG 320
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
906-970 |
7.17e-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: 64.36 E-value: 7.17e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1936509173 906 VALIDEDMCINCGKCYLACNdagYQAISFDSKTHIPHVTEDCTGCTLCLSVCPiIDCITMVKRVI 970
Cdd:COG1149 5 IPVIDEEKCIGCGLCVEVCP---EGAIKLDDGGAPVVDPDLCTGCGACVGVCP-TGAITLEEREA 65
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
905-970 |
4.78e-12 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 67.06 E-value: 4.78e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1936509173 905 VVALIDEDMCINCGKCYLACndaGYQAISF-DSKTHIPHVTEDCTGCTLCLSVCPiIDCITMVKRVI 970
Cdd:COG1145 175 AKAVIDAEKCIGCGLCVKVC---PTGAIRLkDGKPQIVVDPDKCIGCGACVKVCP-VGAISLEPKEI 237
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
906-988 |
6.19e-12 |
|
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: 66.94 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 906 VALI-----DEDMCINCGKCYLACNdagYQAISFDSKtHIPHVTED-CTGCTLCLSVCPiIDCITMVK---RVIPYTPKR 976
Cdd:COG2878 126 AAVIggpkgCEYGCIGCGDCIKACP---FDAIVGAAK-GMHTVDEDkCTGCGLCVEACP-VDCIEMVPvspTVVVSSWDK 200
|
90
....*....|..
gi 1936509173 977 GIPVVSMKGITA 988
Cdd:COG2878 201 GKAVRKVVGCIG 212
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
906-975 |
1.70e-11 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 64.20 E-value: 1.70e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 906 VALIDEDMCINCGKCYLACNdagYQAISFDSKTHIPHVTEDCTGCTLCLSVCPiIDCITMVKrvIPYTPK 975
Cdd:PRK05113 108 VAFIDEDNCIGCTKCIQACP---VDAIVGATKAMHTVISDLCTGCDLCVAPCP-TDCIEMIP--VAETPD 171
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
884-967 |
2.02e-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: 63.28 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 884 DVIGRALPMIGSYGDLDNTQQ-VVALIDEDMCINCGKCYLACNdagYQAISFDSKtHIPHVTED-CTGCTLCLSVCPiID 961
Cdd:TIGR01944 84 ELLGVEPIPQPLDADAGTIQPpMVALIDEDNCIGCTKCIQACP---VDAIVGAAK-AMHTVIADeCTGCDLCVEPCP-TD 158
|
....*.
gi 1936509173 962 CITMVK 967
Cdd:TIGR01944 159 CIEMIP 164
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
301-476 |
6.36e-11 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 64.76 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 301 VIVLGAGDTAFDcatSALRCG--AKRVFVVFRKGftNIRAVPEEMELAREekCEFLPFLSPRQVF-VKGD-RLTGMEFCR 376
Cdd:COG0492 144 VVVVGGGDSALE---EALYLTkfASKVTLIHRRD--ELRASKILVERLRA--NPKIEVLWNTEVTeIEGDgRVEGVTLKN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 377 TeqdnqgnwieDEEQTIRLKADFVISAFGStIANSDVLKAMEpVRLTPHGTVEVDeETMATSELGVFCGGDL-GGTAETT 455
Cdd:COG0492 217 V----------KTGEEKELEVDGVFVAIGL-KPNTELLKGLG-LELDEDGYIVVD-EDMETSVPGVFAAGDVrDYKYRQA 283
|
170 180
....*....|....*....|.
gi 1936509173 456 VESVNDGKTAAWHMHRYIQQK 476
Cdd:COG0492 284 ATAAGEGAIAALSAARYLEPL 304
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
629-782 |
2.79e-10 |
|
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: 62.88 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 629 LELNLSCPHGMGERGMGLACGQNPQL--VKGICKWVRKAVKIPFFAKLTPNVT--DITEIAIAAKEGGADGVTATNTVSG 704
Cdd:TIGR01036 170 LVVNVSSPNTPGLRDLQYKAELRDLLtaVKQEQDGLRRVHRVPVLVKIAPDLTesDLEDIADSLVELGIDGVIATNTTVS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 705 LMGLRGdgsawPAVGKEKrttyGGVSGnaiRPIALRDVSAI---AKVLPG-YPILATGGIDSADAGMQFLHAGASVLQVC 780
Cdd:TIGR01036 250 RSLVQG-----PKNSDET----GGLSG---KPLQDKSTEIIrrlYAELQGrLPIIGVGGISSAQDALEKIRAGASLLQIY 317
|
..
gi 1936509173 781 SA 782
Cdd:TIGR01036 318 SG 319
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
909-969 |
2.70e-09 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 54.33 E-value: 2.70e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1936509173 909 IDEDMCINCGKCYLACndaGYQAISFDSKTHIPHVT--EDCTGCTLCLSVCPiIDCITMVKRV 969
Cdd:COG1146 5 IDTDKCIGCGACVEVC---PVDVLELDEEGKKALVInpEECIGCGACELVCP-VGAITVEDDE 63
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
899-969 |
5.21e-09 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 53.89 E-value: 5.21e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1936509173 899 LDN-TQQVVALIDEDMCINCGKCYLACNdagyqAISFDSKTHIPHVTED-CTGCTLCLSVCPiIDCITMVKRV 969
Cdd:COG4231 8 LDNrTTAMRYVIDEDKCTGCGACVKVCP-----ADAIEEGDGKAVIDPDlCIGCGSCVQVCP-VDAIKLEKRV 74
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
906-966 |
6.70e-09 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 57.88 E-value: 6.70e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1936509173 906 VALIDEDMCINCGKCYLACNdagYQAISFDSKTHIPHVTEDCTGCTLCLSVCPiIDCITMV 966
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACP---VDAIVGAPKQMHTVLADLCTGCDLCVPPCP-VDCIDMV 135
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
145-462 |
6.74e-09 |
|
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: 58.48 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 145 KVALIGCGPASISCATFLARLGYvNLTIFEKQN---YIGGLSSSEIPQYRLPYDVVDFEIALMQDL-------------- 207
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGG-KVTLIEDEGtcpYGGCVLSKALLGAAEAPEIASLWADLYKRKeevvkklnngievl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 208 ----GVKIETGRAlstsdltiNVTISNMFASqKLKEEGYNAIFIGIGMPdPKVIKVfEGLTEEQGF----YTSKGFLprv 279
Cdd:pfam07992 81 lgteVVSIDPGAK--------KVVLEELVDG-DGETITYDRLVIATGAR-PRLPPI-PGVELNVGFlvrtLDSAEAL--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 280 akaskagmcacksSLPSLHGNVIVLGAGDTAFDCATSALRCGAKRVFVVFRKGFTniRAVPEE-----MELAREEKCEFl 354
Cdd:pfam07992 147 -------------RLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLL--RAFDEEisaalEKALEKNGVEV- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 355 pflsprqvfvkgdrLTGMEFCRTEQDNQGNWIEDEEQTiRLKADFVISAFGsTIANSDVLKAMePVRLTPHGTVEVDeET 434
Cdd:pfam07992 211 --------------RLGTSVKEIIGDGDGVEVILKDGT-EIDADLVVVAIG-RRPNTELLEAA-GLELDERGGIVVD-EY 272
|
330 340
....*....|....*....|....*....
gi 1936509173 435 MATSELGVFCGGDLG-GTAETTVESVNDG 462
Cdd:pfam07992 273 LRTSVPGIYAAGDCRvGGPELAQNAVAQG 301
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
644-781 |
1.59e-08 |
|
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: 55.67 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 644 MGLACGQNPQLVKGICKWVRKAV-KIPFFAKLTPNVTDIteiAIAAKEGGADGVTATNTvsglMGLRGDGSAWPAVGKEK 722
Cdd:cd04722 90 IHGAVGYLAREDLELIRELREAVpDVKVVVKLSPTGELA---AAAAEEAGVDEVGLGNG----GGGGGGRDAVPIADLLL 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1936509173 723 RTTYGGVSGnairpialrdvsaiakvlpgyPILATGGIDSADAGMQFLHAGASVLQVCS 781
Cdd:cd04722 163 ILAKRGSKV---------------------PVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
586-784 |
3.41e-08 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 56.50 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 586 YWLQSITELKKDYPEKAS--SIMcGFNEQD-WTELAKAAEAAGADALELNLSCPHGMGERGMGLACGQNPQLVKGICKWV 662
Cdd:PRK02506 78 YYLDYVLELQKKGPNKPHflSVV-GLSPEEtHTILKKIQASDFNGLVELNLSCPNVPGKPQIAYDFETTEQILEEVFTYF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 663 RKavkiPFFAKLTPNVtDITEIAIAA---KEGGADGVTATNTVSGlmGLRGDGSAWPAVGKEKrTTYGGVSGNAIRPIAL 739
Cdd:PRK02506 157 TK----PLGVKLPPYF-DIVHFDQAAaifNKFPLAFVNCINSIGN--GLVIDPEDETVVIKPK-NGFGGIGGDYIKPTAL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1936509173 740 RDVSAIAKVL-PGYPILATGGIDS-ADAGMQFLhAGASVLQVCSAIQ 784
Cdd:PRK02506 229 ANVRAFYQRLnPSIQIIGTGGVKTgRDAFEHIL-CGASMVQVGTALH 274
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
909-958 |
4.40e-08 |
|
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: 50.33 E-value: 4.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1936509173 909 IDEDMCINCGKCYLAC--NDAGYQAISFDSKT-HIPHVTEDCTGCTLCLSVCP 958
Cdd:pfam13237 4 IDPDKCIGCGRCTAACpaGLTRVGAIVERLEGeAVRIGVWKCIGCGACVEACP 56
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
911-971 |
9.88e-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: 49.74 E-value: 9.88e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1936509173 911 EDMCINCGKCYLACNdagYQAISFDSKTHIPHVT---EDCTGCTLCLSVCPiIDCITMVKRVIP 971
Cdd:COG1143 1 EDKCIGCGLCVRVCP---VDAITIEDGEPGKVYVidpDKCIGCGLCVEVCP-TGAISMTPFELA 60
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
914-958 |
1.24e-07 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 49.06 E-value: 1.24e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1936509173 914 CINCGKCYLACNdagYQAISFDSKTHIP------HVTEDCTGCTLCLSVCP 958
Cdd:pfam12838 1 CIGCGACVAACP---VGAITLDEVGEKKgtktvvIDPERCVGCGACVAVCP 48
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
909-958 |
1.58e-07 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 49.28 E-value: 1.58e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1936509173 909 IDEDMCINCGKCYLACNDagyQAISFDSKThiPHVTED-CTGCTLCLSVCP 958
Cdd:COG2221 12 IDEEKCIGCGLCVAVCPT---GAISLDDGK--LVIDEEkCIGCGACIRVCP 57
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
907-966 |
1.61e-07 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 51.24 E-value: 1.61e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 907 ALIDEDMCINCGKCYLACNdagYQAISFDSKTHIPHVTEDCTGCTLCLSVCPiIDCITMV 966
Cdd:cd10549 73 AEIDEEKCIGCGLCVKVCP---VDAITLEDELEIVIDKEKCIGCGICAEVCP-VNAIKLV 128
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
498-821 |
2.56e-07 |
|
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: 53.77 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 498 DISVEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGfALTkTFSLDKDLVTNVSPRIIRGTTSGHTYGPGQGSFLNIE 577
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAG-AIV-LPSLFEEQIEREAQELDRFLTYGSSFAEALSYFPEYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 578 LISEKTMAYwLQSITELKK--DYPEKASsiMCGFNEQDWTELAKAAEAAGADALELNLscpHGMGERgMGLACGQNPQLV 655
Cdd:cd04739 79 RYNLGPEEY-LELIRRAKRavSIPVIAS--LNGVSAGGWVDYARQIEEAGADALELNI---YALPTD-PDISGAEVEQRY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 656 KGICKWVRKAVKIPFFAKLTPNVTDITEIAIAAKEGGADGVTATN-------------TVSGLmglrgdgsawpavgkek 722
Cdd:cd04739 152 LDILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNrfyqpdidletleVVPNL----------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 723 RTTYGGVSGNAIRPIALrdvsAIAKVlpGYPILATGGIDSADAGMQFLHAGASVLQVCSAIQNQDFTVVEDYILGLKTll 802
Cdd:cd04739 215 LLSSPAEIRLPLRWIAI----LSGRV--KASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEA-- 286
|
330 340
....*....|....*....|....*...
gi 1936509173 803 YLE-----TLQELK---SW-NGQSPPTF 821
Cdd:cd04739 287 WMEehgyeSVQQLRgsmSQkNVPDPAAF 314
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
905-958 |
3.62e-07 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 48.57 E-value: 3.62e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1936509173 905 VVALIDEDMCINCGKCYLACNdagYQAISFDSKTHIPHvTEDCTGCTLCLSVCP 958
Cdd:COG2768 4 GKPYVDEEKCIGCGACVKVCP---VGAISIEDGKAVID-PEKCIGCGACIEVCP 53
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
906-966 |
5.42e-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: 49.69 E-value: 5.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 906 VALIDEDMCINCGKCYLACNdagYQAISFDSKTHIPhvtEDCTGC---------TLCLSVCPiIDCITMV 966
Cdd:cd04410 74 IVLIDEDKCIGCGSCVEACP---YGAIVFDPEPGKA---VKCDLCgdrldeglePACVKACP-TGALTFG 136
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
906-958 |
7.55e-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: 7.55e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 906 VALIDEDMCIN------CGKCYLACNDAGYqAISFDSKTHIPHVTED-CTGCTLCLSVCP 958
Cdd:cd16373 85 VAVIDKDRCLAwqggtdCGVCVEACPTEAI-AIVLEDDVLRPVVDEDkCVGCGLCEYVCP 143
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
149-194 |
2.19e-06 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 45.99 E-value: 2.19e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1936509173 149 IGCGPASISCATFLARLGYvNLTIFEKQNYIGGLSSS-EIPQYRLPY 194
Cdd:pfam13450 2 VGAGLAGLVAAALLAKRGF-RVLVLEKRDRLGGNAYSyRVPGYVFDY 47
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
498-783 |
3.44e-06 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 50.25 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 498 DISVEMCGLKFENPFGLASAPPTTSSSMIHRAFEQGWGFALTKtfSLDKDLVTNVSPRIIRGTTSGHTYGPGQGSFlnie 577
Cdd:PRK07565 2 DLSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLK--SLFEEQIRHEAAELDRHLTHGTESFAEALDY---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 578 lISEKTMAYW-----LQSITELKK--DYPEKASsiMCGFNEQDWTELAKAAEAAGADALELNLSCPHGmgerGMGLACGQ 650
Cdd:PRK07565 76 -FPEPAKFYVgpeeyLELIRRAKEavDIPVIAS--LNGSSAGGWVDYARQIEQAGADALELNIYYLPT----DPDISGAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 651 NPQLVKGICKWVRKAVKIPFFAKLTPNVTDITEIAIAAKEGGADG------------------VTATNTVS----GLMGL 708
Cdd:PRK07565 149 VEQRYLDILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGlvlfnrfyqpdidletleVVPGLVLStpaeLRLPL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1936509173 709 RgdgsaWPAVgkekrtTYGGVsgnairpialrdvsaiakvlpGYPILATGGIDSADAGMQFLHAGASVLQVCSAI 783
Cdd:PRK07565 229 R-----WIAI------LSGRV---------------------GADLAATTGVHDAEDVIKMLLAGADVVMIASAL 271
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
889-966 |
3.57e-06 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 47.61 E-value: 3.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1936509173 889 ALPMIGSYGDldNTQQVVALIDEDMCINCGKCYLACNdagYQAISFDSKtHIPHVTED-CTGCTLCLSVCPiIDCITMV 966
Cdd:PRK08764 64 ARPYDRSRGT--HKLPQVAWIVEADCIGCTKCIQACP---VDAIVGGAK-HMHTVIAPlCTGCELCVPACP-VDCIELH 135
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
909-972 |
7.04e-06 |
|
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: 46.24 E-value: 7.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1936509173 909 IDEDMCINCGKCYLAC-------NDAGYQAISFDSKTHIPHvtEDCTGCTLCLSVCPiIDCITMVKRVIPY 972
Cdd:cd10549 37 IDEDKCVFCGACVEVCptgaielTPEGKEYVPKEKEAEIDE--EKCIGCGLCVKVCP-VDAITLEDELEIV 104
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
905-958 |
1.25e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 49.09 E-value: 1.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1936509173 905 VVALIDEDMCINCGKCYLACNdagYQAISFDSKTHIPHVTEDCTGCTLCLSVCP 958
Cdd:COG1148 489 SVAEVDPEKCTGCGRCVEVCP---YGAISIDEKGVAEVNPALCKGCGTCAAACP 539
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
909-981 |
2.16e-05 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 48.10 E-value: 2.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1936509173 909 IDEDMCINCGKCYLACndaGYQAISFDSKtHIPHVTEDCTGCTLCLSVCP-----IIDCITMVKRVIpytpKRGIPVV 981
Cdd:COG4624 88 RDKEKCKNCYPCVRAC---PVKAIKVDDG-KAEIDEEKCISCGQCVAVCPfgaitEKSDIEKVKKAL----KDPEKVV 157
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
629-782 |
2.35e-05 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 47.81 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 629 LELNLSCPHGMGERGMglacgQNPQLVKGICKWVRKA---------VKIPFFAKLTPNVT--DITEIAIAAKEGGADGVT 697
Cdd:PLN02826 220 LVINVSSPNTPGLRKL-----QGRKQLKDLLKKVLAArdemqwgeeGPPPLLVKIAPDLSkeDLEDIAAVALALGIDGLI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 698 ATNTVSGlmglRGDgsawPAVGKEKRTTYGGVSGNAIRPIALRDVSAIAKVLPG-YPILATGGIDSADAGMQFLHAGASV 776
Cdd:PLN02826 295 ISNTTIS----RPD----SVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGkIPLVGCGGVSSGEDAYKKIRAGASL 366
|
....*.
gi 1936509173 777 LQVCSA 782
Cdd:PLN02826 367 VQLYTA 372
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
913-958 |
3.29e-05 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 42.16 E-value: 3.29e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1936509173 913 MCINCGKCYLACNDAGYQAISFDSKTHIPHVTEDCTGCTLCLSVCP 958
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQTIRGDIAGLACIGCGACVDACP 46
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
910-967 |
4.85e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 44.19 E-value: 4.85e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1936509173 910 DEDMCINCGKCYLACNdagYQAISFDSKTHIPHVtedCTGCTLCLSVCPiIDCITMVK 967
Cdd:cd16370 81 DKEKCIGCGNCVKACI---VGAIFWDEETNKPII---CIHCGYCARYCP-HDVLAMEE 131
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
909-977 |
5.13e-05 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 43.92 E-value: 5.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1936509173 909 IDEDMCINCGKCYLACNdagYQAISFDSKTHI---PHVTED-CTGCTLCLSVCPiIDCITMVKRVIPYTPKRG 977
Cdd:cd10549 3 YDPEKCIGCGICVKACP---TDAIELGPNGAIargPEIDEDkCVFCGACVEVCP-TGAIELTPEGKEYVPKEK 71
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
912-958 |
1.24e-04 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 42.81 E-value: 1.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1936509173 912 DMCINCGKCYLACNDAGYqaISFDSKthIPHVTED-CTGCTLCLSVCP 958
Cdd:PRK09625 59 EICINCFNCWVYCPDAAI--LSRDKK--LKGVDYShCKGCGVCVEVCP 102
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
145-208 |
1.98e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 45.23 E-value: 1.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1936509173 145 KVALIGCGPASISCATFLARLGY-VnlTIFEKQNYIGG-LSSSEIPQYRL---PYDVVDFEIA--LMQDLG 208
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYrV--TVLEKNDTPGGrARTFERPGFRFdvgPSVLTMPGVLerLFRELG 73
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
906-958 |
3.63e-04 |
|
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: 41.55 E-value: 3.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 906 VALIDEDMCINCGKCYLACNDAGYQ-------AISFDSKTHIPHVTEdCTGCTLCLSVCP 958
Cdd:cd16372 2 LLVTDPEKCIGCLQCEEACSKTFFKeedreksCIRITETEGGYAINV-CNQCGECIDVCP 60
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
900-958 |
4.05e-04 |
|
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: 41.41 E-value: 4.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1936509173 900 DNTQQVValIDEDMCINCGKCYLACndaGYQAISFDSKTHIPHVTEDCTGCTLCLSVCP 958
Cdd:cd10550 70 EETGAVV--VDEDKCIGCGMCVEAC---PFGAIRVDPETGKAIKCDLCGGDPACVKVCP 123
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
910-969 |
4.17e-04 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 40.78 E-value: 4.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 910 DEDMCINCGKCYLACNDAgyqAISFDSKTHIPHVTEDCTGCTLCLSVCPiIDCITMVKRV 969
Cdd:PRK09624 49 NRDKCVRCYLCYIYCPEP---AIYLDEEGYPVFDYDYCKGCGICANECP-TKAIEMVRET 104
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
913-959 |
4.64e-04 |
|
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: 41.02 E-value: 4.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1936509173 913 MCINCGK--CYLACNdagYQAISFDSKTHIPHVTED-CTGCTLCLSVCPI 959
Cdd:cd10550 48 VCRQCEDapCVEACP---VGAISRDEETGAVVVDEDkCIGCGMCVEACPF 94
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
913-958 |
6.04e-04 |
|
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: 39.22 E-value: 6.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1936509173 913 MCINCGKCYLAC-----------NDAGYQAISFDSKTHIPHVTED----CTGCTLCLSVCP 958
Cdd:pfam13183 1 RCIRCGACLAACpvylvtggrfpGDPRGGAAALLGRLEALEGLAEglwlCTLCGACTEVCP 61
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
914-970 |
6.09e-04 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 43.00 E-value: 6.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 914 CINCGKCYLACndaGYQAISFDSKthIPHVTED-CTGCTLCLSVCP--IIDCITMVKRVI 970
Cdd:PRK07118 141 CLGLGSCVAAC---PFDAIHIENG--LPVVDEDkCTGCGACVKACPrnVIELIPKSARVF 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
906-966 |
6.38e-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: 43.62 E-value: 6.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1936509173 906 VALIDEDMCiNCGKCYLAC------NDAGYQAISFDSKTHIPHVTED-CTGCTLCLSVCPiIDCITMV 966
Cdd:COG1245 4 IAVVDRDRC-QPKKCNYECikycpvNRTGKEAIEIDEDDGKPVISEElCIGCGICVKKCP-FDAISIV 69
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
906-966 |
7.83e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 7.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1936509173 906 VALIDEDMCiNCGKCYLAC------NDAGYQAISFDSKTHIPHVTED-CTGCTLCLSVCPiIDCITMV 966
Cdd:PRK13409 4 IAVVDYDRC-QPKKCNYECikycpvVRTGEETIEIDEDDGKPVISEElCIGCGICVKKCP-FDAISIV 69
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
944-974 |
8.31e-04 |
|
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: 8.31e-04
10 20 30
....*....|....*....|....*....|.
gi 1936509173 944 TEDCTGCTLCLSVCPiIDCITMVKRVIPYTP 974
Cdd:COG1143 1 EDKCIGCGLCVRVCP-VDAITIEDGEPGKVY 30
|
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
906-967 |
8.89e-04 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 39.93 E-value: 8.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1936509173 906 VALIDEDMCINCGKCYLAC-------NDAGYQAISFDSkthiphvtedCTGCTLCLSVCPiIDCITMVK 967
Cdd:PRK09623 45 MPVVDESKCVKCYICWKFCpepaiyiKEDGYVAIDYDY----------CKGCGICANECP-TKAITMVK 102
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
909-958 |
1.28e-03 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 41.59 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1936509173 909 IDEDMCINCGKCYLACndagyqaisfdsKTHIP-----HVTEDCTGCTLCLSVCP 958
Cdd:COG0348 207 YDRGDCIDCGLCVKVC------------PMGIDirkgeINQSECINCGRCIDACP 249
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
906-973 |
1.30e-03 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 41.60 E-value: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1936509173 906 VALIDEDMCINCGKCYLACNdagYQAISFDSKThiPHVTED-CTGCTLCLSVCPiIDCITMVKRVIPYT 973
Cdd:cd03110 58 KAFIDQEKCIRCGNCERVCK---FGAILEFFQK--LIVDESlCEGCGACVIICP-RGAIYLKDRDTGKI 120
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
914-960 |
1.69e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 42.29 E-value: 1.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1936509173 914 CINCGKCYLACNDagyQAISFDSKTHIPHVTED-CTGCTLCLSVCPII 960
Cdd:PRK13795 583 CVGCGVCVGACPT---GAIRIEEGKRKISVDEEkCIHCGKCTEVCPVV 627
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
908-958 |
1.72e-03 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 40.70 E-value: 1.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 908 LIDEDMCINCGKCYLACNdagYQAISFDSKTHIPHVtedCTGC---------TLCLSVCP 958
Cdd:COG0437 86 LVDYDKCIGCRYCVAACP---YGAPRFNPETGVVEK---CTFCadrldegllPACVEACP 139
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
923-968 |
1.88e-03 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 39.53 E-value: 1.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1936509173 923 ACNDA-GYQAISF-DSKTHI--PHV-TEDCTGCTLCLSVCPiIDCITMVKR 968
Cdd:cd10564 90 SCQDAcPTQAIRFrPRLGGIalPELdADACTGCGACVSVCP-VGAITLTPL 139
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
942-967 |
3.26e-03 |
|
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).
Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 40.23 E-value: 3.26e-03
10 20
....*....|....*....|....*.
gi 1936509173 942 HVTEDCTGCTLCLSVCPiIDCITMVK 967
Cdd:NF038196 182 HVTDKCIGCGICAKVCP-VNNIEMED 206
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
678-783 |
3.45e-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: 39.92 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 678 VTDITEIAIAAKEGgADGVtatntvsglmglrGDGSAWPAVGKEKRTTYGGVSGnairpialrdVSAIAKVLPGYPILAT 757
Cdd:TIGR00693 103 THNLEELAEAEAEG-ADYI-------------GFGPIFPTPTKKDPAPPAGVEL----------LREIAATLIDIPIVAI 158
|
90 100
....*....|....*....|....*.
gi 1936509173 758 GGIDSADAGmQFLHAGASVLQVCSAI 783
Cdd:TIGR00693 159 GGITLENAA-EVLAAGADGVAVVSAI 183
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
914-958 |
4.25e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 40.30 E-value: 4.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1936509173 914 CINCGKCYLACNDagyQAISF-DSKTHIPHvtEDCTGCTLCLSVCP 958
Cdd:PRK07118 215 CIGCGKCVKACPA---GAITMeNNLAVIDQ--EKCTSCGKCVEKCP 255
|
|
| pyruv_ox_red |
TIGR02176 |
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ... |
912-958 |
5.02e-03 |
|
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.
Pssm-ID: 131231 [Multi-domain] Cd Length: 1165 Bit Score: 40.91 E-value: 5.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 912 DMCINCGKCYLACNDAGYQAISFDS-----------------------KTHIPHVTEDCTGCTLCLSVCP 958
Cdd:TIGR02176 683 DNCIQCNQCAFVCPHAAIRPKLADEeelenapagfksldakgkelegmKFRIQISPLDCTGCGNCVDICP 752
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
914-958 |
5.16e-03 |
|
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: 36.29 E-value: 5.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1936509173 914 CINCGKCYLACndAGYQAISFDSKT-------------HIPHVTEDCTGCTLCLSVCP 958
Cdd:pfam13534 2 CIQCGCCVDEC--PRYLLNGDEPKKlmraaylgdleelQANKVANLCSECGLCEYACP 57
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
908-969 |
5.35e-03 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 38.10 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936509173 908 LIDEDMCINCGKCYLACNDAGY---------------------------------------QAISFDskTHIPHVTED-C 947
Cdd:COG1142 6 IADPEKCIGCRTCEAACAVAHEgeegepflprirvvrkagvsapvqcrhcedapcaevcpvGAITRD--DGAVVVDEEkC 83
|
90 100
....*....|....*....|..
gi 1936509173 948 TGCTLCLSVCPiIDCITMVKRV 969
Cdd:COG1142 84 IGCGLCVLACP-FGAITMVGEK 104
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
907-966 |
5.94e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 39.92 E-value: 5.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1936509173 907 ALIDEDMCINCGKCYLACNDAGYQAISFDSKTHIPHVTED------------CTGCTLCLSVCPiIDCITMV 966
Cdd:PRK07118 163 PVVDEDKCTGCGACVKACPRNVIELIPKSARVFVACNSKDkgkavkkvcevgCIGCGKCVKACP-AGAITME 233
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
145-186 |
7.62e-03 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 39.82 E-value: 7.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1936509173 145 KVALIGCGPASISCATFLARLGYvNLTIFEKQNYIGGLSSSE 186
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTV 43
|
|
| PLN00071 |
PLN00071 |
photosystem I subunit VII; Provisional |
912-959 |
8.82e-03 |
|
photosystem I subunit VII; Provisional
Pssm-ID: 177700 [Multi-domain] Cd Length: 81 Bit Score: 36.46 E-value: 8.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1936509173 912 DMCINCGKCYLACNDAGYQAISFDSK-----THIPHvTEDCTGCTLCLSVCPI 959
Cdd:PLN00071 9 DTCIGCTQCVRACPTDVLEMIPWDGCkakqiASAPR-TEDCVGCKRCESACPT 60
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
906-938 |
8.91e-03 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 35.86 E-value: 8.91e-03
10 20 30
....*....|....*....|....*....|...
gi 1936509173 906 VALIDEDMCINCGKCYLACNdagYQAISFDSKT 938
Cdd:COG2768 34 KAVIDPEKCIGCGACIEVCP---VGAIKIEWEE 63
|
|
| |
