|
Name |
Accession |
Description |
Interval |
E-value |
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
397-699 |
2.57e-176 |
|
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: 511.44 E-value: 2.57e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 397 DISVEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTFALDKDLVTNVSPRIVRGTTAGHnygpQQGSFLNIE 476
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGR----GQIGFNNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 477 LISEKCAAYWLKGIQELKADFPTKIIIASIMCSYNEQDWKTLSKMAQDAGADALELNLSCPHGMGESGMGLACGQKPELV 556
Cdd:cd02940 77 LISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 557 KGISEWVKATVKIPFFIKLTPNITNIVDIATAAYEGGADGVAAINTVSGLMGLSANGTPwPAVGLDKRTTYGGVSGNATR 636
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTP-PAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2117727728 637 PMGLRAVSAVANALS-GFSIMGIGGIDSADVAWQYLQAGASVVQVCSAIQNQDFTLIDDYCTGL 699
Cdd:cd02940 236 PIALRAVSQIARAPEpGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
397-870 |
7.31e-125 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 383.53 E-value: 7.31e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 397 DISVEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTfaLDKDLVTNVSPRIvrgttAGHNYGPQQ-GSFLNI 475
Cdd:PRK08318 3 DLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKT--LGPPIVNVSSPRF-----GALVKEDRRfIGFNNI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 476 ELISEKCAAYWLKGIQELKADFPTKIIIASIMCSYNEQDWKTLSKMAQDAGADALELNLSCPHGMGESGMGLACGQKPEL 555
Cdd:PRK08318 76 ELITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 556 VKGISEWVKATVKIPFFIKLTPNITNIVDIATAAYEGGADGVAAINTVSGLMGLS-ANGTPWPAVglDKRTTYGGVSGNA 634
Cdd:PRK08318 156 VEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDlDRMIPMPIV--NGKSSHGGYCGPA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 635 TRPMGLRAVSAVAN--ALSGFSIMGIGGIDSADVAWQYLQAGASVVQVCSAIQNQDFTLIDDYCTGLKAllYLDgrlprw 712
Cdd:PRK08318 234 VKPIALNMVAEIARdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSH--YMD------ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 713 dgqspptfkhqkgkpvisirnedskalphfgpylkqreeklknlkretilhhngrENGYPTngvqvpskvpkINEMIGRA 792
Cdd:PRK08318 306 -------------------------------------------------------EKGFAS-----------LEDMVGLA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 793 LPRIGAYKKLDNTKQVVALIDDDMCINCGKCYMTCNDSGYQAINFDP--NTHIPTVTDDCTGCTLCLSVCPIIDCITMVP 870
Cdd:PRK08318 320 VPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDEdgTRTPEVIEEECVGCNLCAHVCPVEGCITMGE 399
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
2-374 |
1.65e-80 |
|
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: 267.00 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTsdLCVGGCNLHASEEgSINIGGLQQFATEVFSKMGVKQIRDPQTPTPKnstaKIVLLGAGPASLSCATFLGRLGYD 81
Cdd:COG0493 74 VCPA--PCEGACVRGIVDE-PVAIGALERFIADKAFEEGWVKPPPPAPRTGK----KVAVVGSGPAGLAAAYQLARAGHE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 82 nITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKIETGRSLSKqDITLEKLLKDTKAVFVGIGLPQPKLNPL 161
Cdd:COG0493 147 -VTVFEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGK-DITLDELLEEFDAVFLATGAGKPRDLGI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 162 fkdltPEM---GFYTSKDFLPKVAKASKPgvclckATLPSLKGTVIVLGAGDTAFDCATSALRCGAKKVFVVFRRGFTNI 238
Cdd:COG0493 225 -----PGEdlkGVHSAMDFLTAVNLGEAP------DTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEM 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 239 RAVPEEVSLAVEEKCELVGFLSPHKVNVKE-GKIVSVTFSRTE---QDKNGKW----VQDSEQltTVKANYLISAFGSGL 310
Cdd:COG0493 294 PASKEEVEEALEEGVEFLFLVAPVEIIGDEnGRVTGLECVRMElgePDESGRRrpvpIEGSEF--TLPADLVILAIGQTP 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2117727728 311 eDPDVVEALKPLKFTDQNLPSVDLNTMQSSHASVWVGGDLAGVAETTVEAVNDGKTAAWYMHCF 374
Cdd:COG0493 372 -DPSGLEEELGLELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
400-698 |
7.68e-80 |
|
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: 259.98 E-value: 7.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 400 VEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTFALDKDlVTNVSPRIVRgTTAGHNYGPQQGSFLNIELIS 479
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPR-PGNPLPRVAR-LPPEGESYPEQLGILNSFGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 480 EKCAAYWLKGIQELKADFPTKIIIASIMCSyNEQDWKTLSKMAQDAGADALELNLSCPHGMGESGmglaCGQKPELVKGI 559
Cdd:cd02810 79 NLGLDVWLQDIAKAKKEFPGQPLIASVGGS-SKEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 560 SEWVKATVKIPFFIKLTPNIT--NIVDIATAAYEGGADGVAAINTVSGLMGLSangtpwPAVGLDKRTTYGGVSGNATRP 637
Cdd:cd02810 154 LKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDL------KTVGPGPKRGTGGLSGAPIRP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2117727728 638 MGLRAVSAVANAL-SGFSIMGIGGIDSADVAWQYLQAGASVVQVCSAIQNQDFTLIDDYCTG 698
Cdd:cd02810 228 LALRWVARLAARLqLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
397-703 |
1.38e-78 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 260.16 E-value: 1.38e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 397 DISVEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTFALDKDLVTNVSPRIVR-GTTAGHNYGPQQGSFLNI 475
Cdd:PLN02495 10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARlRAGANGSAKGRVIGWQNI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 476 ELISEKCAAYWLKGIQELKADFPTKIIIASIMCSYNEQDWKTLSKMAQDAGADALELNLSCPHGMGESGMGLACGQKPEL 555
Cdd:PLN02495 90 ELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVGQDCDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 556 VKGISEWVKATVKIPFFIKLTPNITNIVDIATAAYEGGADGVAAINTVSGLMGLSANG-TPWPAVglDKRTTYGGVSGNA 634
Cdd:PLN02495 170 LEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLDTlRPEPCV--EGYSTPGGYSSKA 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2117727728 635 TRPMGLRAVSAVANAL-----SGFSIMGIGGIDSADVAWQYLQAGASVVQVCSAIQNQDFTLIDDYCTGLKALL 703
Cdd:PLN02495 248 VRPIALAKVMAIAKMMksefpEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFM 321
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
397-703 |
1.01e-75 |
|
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: 249.22 E-value: 1.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 397 DISVEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTfaldkdlVT------NVSPRIVRgtTaghnygPQQG 470
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKT-------VTpepqpgNPRPRLFR--L------PEDS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 471 SFLNIELISEKCAAYWLKGIQELKAdfPTKIIIASIMCSyNEQDWKTLSKMAQDAGADALELNLSCPHGmgeSGMGLACG 550
Cdd:COG0167 66 GLINRMGLNNPGVDAFLERLLPAKR--YDVPVIVNIGGN-TVEDYVELARRLADAGADYLELNISCPNT---PGGGRALG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 551 QKPELVKGISEWVKATVKIPFFIKLTPNITNIVDIATAAYEGGADGVAAINTVSGLmglsangtpwpAVGLDKRT----- 625
Cdd:COG0167 140 QDPEALAELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGR-----------AIDLETRRpvlan 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117727728 626 TYGGVSGNATRPMGLRAVSAVANALSG-FSIMGIGGIDSADVAWQYLQAGASVVQVCSAIQNQDFTLIDDYCTGLKALL 703
Cdd:COG0167 209 EAGGLSGPALKPIALRMVREVAQAVGGdIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYL 287
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
2-377 |
2.94e-73 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 248.17 E-value: 2.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTSDLCVGGCNLHASEEgSINIGGLQQFATEVFSKMGVKQirdPQTPTPKNSTAKIVllGAGPASLSCATFLGRLGYD 81
Cdd:PRK11749 92 VCPQERLCEGACVRGKKGE-PVAIGRLERYITDWAMETGWVL---FKRAPKTGKKVAVI--GAGPAGLTAAHRLARKGYD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 82 nITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKIETGRSLSKqDITLEKLLKDTKAVFVGIGLPQPKLNPL 161
Cdd:PRK11749 166 -VTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGR-DITLDELRAGYDAVFIGTGAGLPRFLGI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 162 F-KDLTpemGFYTSKDFLPKVAKAskpgvclcKATLPSLKG-TVIVLGAGDTAFDCATSALRCGAKKVFVVFRRGFTNIR 239
Cdd:PRK11749 244 PgENLG---GVYSAVDFLTRVNQA--------VADYDLPVGkRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMP 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 240 AVPEEVSLAVEEKCELVGFLSPHKVNVKEGKIVSVTFSRTE---QDKNGK---WVQDSEqlTTVKANYLISAFGSGLEDP 313
Cdd:PRK11749 313 ASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMElgePDASGRrrvPIEGSE--FTLPADLVIKAIGQTPNPL 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2117727728 314 dVVEALKPLKFTDQNLPSVDLNTMQSSHASVWVGGDLAGVAETTVEAVNDGKTAAWYMHCFLEG 377
Cdd:PRK11749 391 -ILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEG 453
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
397-684 |
1.94e-53 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 188.05 E-value: 1.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 397 DISVEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTFALDKDLvTNVSPRIVRgTTAGhnygpqqgsFLN-- 474
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPRE-GNPTPRIAE-TPGG---------MLNai 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 475 ------IELISEKcAAYWLKgiqelKADFPtkiIIASImCSYNEQDWKTLSKMAQDAG-ADALELNLSCPHGMGesgMGL 547
Cdd:PRK07259 70 glqnpgVDAFIEE-ELPWLE-----EFDTP---IIANV-AGSTEEEYAEVAEKLSKAPnVDAIELNISCPNVKH---GGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 548 ACGQKPELVKGISEWVKATVKIPFFIKLTPNITNIVDIATAAYEGGADGVAAINTVSGlMGLSANgTPWPAVGldkrTTY 627
Cdd:PRK07259 137 AFGTDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINTLKG-MAIDIK-TRKPILA----NVT 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2117727728 628 GGVSGNATRPMGLRAVSAVANALSgFSIMGIGGIDSADVAWQYLQAGASVVQVCSAI 684
Cdd:PRK07259 211 GGLSGPAIKPIALRMVYQVYQAVD-IPIIGMGGISSAEDAIEFIMAGASAVQVGTAN 266
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
399-703 |
1.15e-52 |
|
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: 185.83 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 399 SVEMCGLKFENPFGLASAPPATTTAMiRRAFEQGWA-YTVTKTFALDKDLvTNVSPRIVRgTTAGhnygpqqgsFLN-IE 476
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEEL-SRVADLGKLgAIVTKSITLEPRE-GNPPPRVVE-TPGG---------MLNaIG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 477 LiSEKCAAYWLKGIQELKADFPTKIIiASIMCSyNEQDWKTLSKMAQDAGADALELNLSCPHgmgESGMGLACGQKPELV 556
Cdd:cd04740 69 L-QNPGVEAFLEELLPWLREFGTPVI-ASIAGS-TVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDPEAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 557 KGISEWVKATVKIPFFIKLTPNITNIVDIATAAYEGGADGVAAINTVSGLmglsangtpwpAVGLDKRT-----TYGGVS 631
Cdd:cd04740 143 AEIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKGM-----------AIDIETRKpilgnVTGGLS 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2117727728 632 GNATRPMGLRAVSAVANALSgFSIMGIGGIDSADVAWQYLQAGASVVQVCSAIQnQDFTLIDDYCTGLKALL 703
Cdd:cd04740 212 GPAIKPIALRMVYQVYKAVE-IPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYL 281
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
2-388 |
1.69e-49 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 184.31 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTSdlCVGGCNlHASEEGSINIGGLQQFATEVFSKMGVKqirdpqTPTPKNSTAKIVL-LGAGPASLSCATFLGRLGY 80
Cdd:PRK12771 91 VCYHP--CESGCN-RGQVDDAVGINAVERFLGDYAIANGWK------FPAPAPDTGKRVAvIGGGPAGLSAAYHLRRMGH 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 81 DnITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKIETGRSLSKqDITLEKLLKDTKAVFVGIGLPQPKLNP 160
Cdd:PRK12771 162 A-VTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGVEVRLGVRVGE-DITLEQLEGEFDAVFVAIGAQLGKRLP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 161 LFKDLTPemGFYTSKDFLPKVAKASKpgvclckatlPSLKGTVIVLGAGDTAFDCATSALRCGAKKVFVVFRRGFTNIRA 240
Cdd:PRK12771 240 IPGEDAA--GVLDAVDFLRAVGEGEP----------PFLGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 241 VPEEVSLAVEEKCELVGFLSPHKVNVKEGKIVSVTFSRTEQ---DKNGKWVQDSEQLTTVKANYLISAFG-----SGLED 312
Cdd:PRK12771 308 HDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVITVEKmelDEDGRPSPVTGEEETLEADLVVLAIGqdidsAGLES 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2117727728 313 PDVVEALKPLKftdqnlpSVDLNTMQSSHASVWVGGDLAGVAETTVEAVNDGKTAAWYMHCFLEGLPLTTTPKLPL 388
Cdd:PRK12771 388 VPGVEVGRGVV-------QVDPNFMMTGRPGVFAGGDMVPGPRTVTTAIGHGKKAARNIDAFLGGEPYEHRPKREI 456
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
2-377 |
1.17e-47 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 176.75 E-value: 1.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTSDLCVGGCNLHASEEgSINIGGLQQFATEVFSKMGVKQIrdpqtPTPKNSTAKIVLLGAGPASLSCATFLGRLGYD 81
Cdd:PRK12831 92 VCPQESQCEGKCVLGIKGE-PVAIGKLERFVADWARENGIDLS-----ETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 82 nITIYEKQDFVGGLSTSEIPQYRLPIS-VVNFEIQLVKDLGVKIETGRSLSKQdITLEKLLKDT--KAVFVGIGLPQPKl 158
Cdd:PRK12831 166 -VTIFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKT-VTIDELLEEEgfDAVFIGSGAGLPK- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 159 nplFKDLTPE--MGFYTSKDFLPKV--AKASKPGVclckATlPSLKGT-VIVLGAGDTAFDCATSALRCGAkKVFVVFRR 233
Cdd:PRK12831 243 ---FMGIPGEnlNGVFSANEFLTRVnlMKAYKPEY----DT-PIKVGKkVAVVGGGNVAMDAARTALRLGA-EVHIVYRR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 234 GFTNIRAVPEEVSLAVEEKCELVGFLSPHKVNVKE-GKIVSVTFSRT---EQDKNGKW----VQDSEqlTTVKANYLISA 305
Cdd:PRK12831 314 SEEELPARVEEVHHAKEEGVIFDLLTNPVEILGDEnGWVKGMKCIKMelgEPDASGRRrpveIEGSE--FVLEVDTVIMS 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2117727728 306 FGSGlEDPDVVEALKPLKFTDQNLPSVDLNTMQSSHASVWVGGDLAGVAETTVEAVNDGKTAAWYMHCFLEG 377
Cdd:PRK12831 392 LGTS-PNPLISSTTKGLKINKRGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSK 462
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
398-684 |
7.87e-47 |
|
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: 169.53 E-value: 7.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 398 ISVEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTFALDKDLvTNVSPRIVRgTTAGhnygpqqgsFLNIEL 477
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRP-GYRNPTIVE-TPCG---------MLNAIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 478 ISEKCAAYWLKGIQELKADFPTKIIiASIMCSyNEQDWKTLSKMAQDAG--ADALELNLSCPHGMGesgMGLACGQKPEL 555
Cdd:TIGR01037 70 LQNPGVEAFLEELKPVREEFPTPLI-ASVYGS-SVEEFAEVAEKLEKAPpyVDAYELNLSCPHVKG---GGIAIGQDPEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 556 VKGISEWVKATVKIPFFIKLTPNITNIVDIATAAYEGGADGVAAINTVSGLMGLSANGTPwpavglDKRTTYGGVSGNAT 635
Cdd:TIGR01037 145 SADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMKIDIKTGKP------ILANKTGGLSGPAI 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2117727728 636 RPMGLRAVSAVANALsGFSIMGIGGIDSADVAWQYLQAGASVVQVCSAI 684
Cdd:TIGR01037 219 KPIALRMVYDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAV 266
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
2-377 |
1.31e-45 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 171.12 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTSdlCVGGCNLhASEEGSINIGGLQQFATEVFSKMGVKQIRDPQTPTPKnstaKIVLLGAGPASLSCATFLGRLGYD 81
Cdd:PRK12810 96 VCPAP--CEGACTL-NINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGK----KVAVVGSGPAGLAAADQLARAGHK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 82 nITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKIETGRSLSKqDITLEKLLKDTKAVFVGIGLPQP-KLNP 160
Cdd:PRK12810 169 -VTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGK-DITAEELLAEYDAVFLGTGAYKPrDLGI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 161 LFKDLTpemGFYTSKDFLP---KVAKASKPGVCLckatlpSLKG-TVIVLGAGDTAFDCATSALRCGAKKvfvVFRRGFT 236
Cdd:PRK12810 247 PGRDLD---GVHFAMDFLIqntRRVLGDETEPFI------SAKGkHVVVIGGGDTGMDCVGTAIRQGAKS---VTQRDIM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 237 NIRAVPE-------------EVSLAVEEKCELVGFLSPHKVNVKEGKIVSVTFSRTE-QDKNGKWVQDSEQltTVKANYL 302
Cdd:PRK12810 315 PMPPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTElGEGDFEPVEGSEF--VLPADLV 392
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2117727728 303 ISAFGSGLEDPDVVEALKpLKFTDQNLPSVDLNTMQSSHASVWVGGDLAGVAETTVEAVNDGKTAAWYMHCFLEG 377
Cdd:PRK12810 393 LLAMGFTGPEAGLLAQFG-VELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMG 466
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
2-377 |
1.89e-43 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 169.54 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTSDLCVGGCNLHASEEGSINIGGLQQFATEVFSKMGvkQIRDPQTpTPKNStAKIVLLGAGPASLSCATFLGRLGYD 81
Cdd:PRK12778 381 VCPQEKQCESKCIHGKMGEEAVAIGYLERFVADYERESG--NISVPEV-AEKNG-KKVAVIGSGPAGLSFAGDLAKRGYD 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 82 nITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKIET----GRSLSKQDITLEKLlkdtKAVFV--GIGLPQ 155
Cdd:PRK12778 457 -VTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETdvivGKTITIEELEEEGF----KGIFIasGAGLPN 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 156 pklnplFKDLTPE--MGFYTSKDFLPKV--AKASKPGVclckATLPSLKGTVIVLGAGDTAFDCATSALRCGAKKVFVVF 231
Cdd:PRK12778 532 ------FMNIPGEnsNGVMSSNEYLTRVnlMDAASPDS----DTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIVY 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 232 RRGFTNIRAVPEEVSLAVEEKCELVGFLSPHKVNVKE-GKIVSVTFSRT---EQDKNGKW----VQDSEQltTVKANYLI 303
Cdd:PRK12778 602 RRSEEEMPARLEEVKHAKEEGIEFLTLHNPIEYLADEkGWVKQVVLQKMelgEPDASGRRrpvaIPGSTF--TVDVDLVI 679
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2117727728 304 SAFGSGlEDPDVVEALKPLKFTDQNLPSVDLNtMQSSHASVWVGGDLAGVAETTVEAVNDGKTAAWYMHCFLEG 377
Cdd:PRK12778 680 VSVGVS-PNPLVPSSIPGLELNRKGTIVVDEE-MQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSS 751
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
2-386 |
4.16e-43 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 167.21 E-value: 4.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTSdlCVGGCNLHASEEgSINIGGLQQFATEVFSKMGvkqirDPQTPTPKNSTAKIV-LLGAGPASLSCATFLGRLGY 80
Cdd:PRK12814 146 ICPAP--CEEACRRHGVDE-PVSICALKRYAADRDMESA-----ERYIPERAPKSGKKVaIIGAGPAGLTAAYYLLRKGH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 81 DnITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKIETGRSLSKqDITLEKLLKDTKAVFVGIGLPQP-KLN 159
Cdd:PRK12814 218 D-VTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAMGAEFRFNTVFGR-DITLEELQKEFDAVLLAVGAQKAsKMG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 160 PLFKDLTpemGFYTSKDFLPKVA--KASKPGvclckatlpslkGTVIVLGAGDTAFDCATSALRCGAKKVFVVFRRGFTN 237
Cdd:PRK12814 296 IPGEELP---GVISGIDFLRNVAlgTALHPG------------KKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 238 IRAVPEEVSLAVEEKCELVGFLSPHKVNVKEG--KIVSVTFSRTEQDKNGKW----VQDSEqlTTVKANYLISAFGSGLE 311
Cdd:PRK12814 361 MPANRAEIEEALAEGVSLRELAAPVSIERSEGglELTAIKMQQGEPDESGRRrpvpVEGSE--FTLQADTVISAIGQQVD 438
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2117727728 312 DPdvVEALKPLKFTDQNLPSVDLNTMQSSHASVWVGGDLAGVAETTVEAVNDGKTAAWYMHCFLEGLPLTTTPKL 386
Cdd:PRK12814 439 PP--IAEAAGIGTSRNGTVKVDPETLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGKPVTAPVQP 511
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
399-703 |
3.82e-33 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 129.78 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 399 SVEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTFALDKDlVTNVSPRIVRgttaghnygpQQGSFLN-IEL 477
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQ-PGNPTPRVFR----------LPEGVLNrMGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 478 ISEKCAAYWLKGIQELKADFPTKI-IIASIMCSYNEQDWKTLSKMAQDagADALELNLSCPHGMGesgmGLACGQKPELV 556
Cdd:pfam01180 72 NNPGLDAVLAELLKRRKEYPRPDLgINLSKAGMTVDDYVEVARKIGPF--ADYIELNVSCPNTPG----LRALQTDPELA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 557 KGISEWVKATVKIPFFIKLTPNITNIVDIATAAYEGGADGVAAIN----TVSGLM-------GLSANGTpwpavgldkrt 625
Cdd:pfam01180 146 AILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINatntTVRGMRidlktekPILANGT----------- 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117727728 626 tyGGVSGNATRPMGLRAVSAVANALSG-FSIMGIGGIDSADVAWQYLQAGASVVQVCSAIQNQDFTLIDDYCTGLKALL 703
Cdd:pfam01180 215 --GGLSGPPIKPIALKVIRELYQRTGPeIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
2-368 |
1.65e-32 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 134.87 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTSDLCVGGCNLHaSEEGSINIGGLQQFATEVFSKMGVKqirdPQTPTPKNSTAKIVLLGAGPASLSCATFLGRLGYd 81
Cdd:PRK12769 278 VCPQDRLCEGACTLR-DEYGAVTIGNIERYISDQALAKGWR----PDLSQVTKSDKRVAIIGAGPAGLACADVLARNGV- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 82 NITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKIETGRSLSKqDITLEKLLKDTKAVFVGIGLPQPKLNPL 161
Cdd:PRK12769 352 AVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGK-DISLESLLEDYDAVFVGVGTYRSMKAGL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 162 FKDLTPemGFYtskDFLPKVAKASKPGVCLckATLP-----SLKG-TVIVLGAGDTAFDCATSALRCGAKKVFVVFRRGF 235
Cdd:PRK12769 431 PNEDAP--GVY---DALPFLIANTKQVMGL--EELPeepfiNTAGlNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 236 TNIRAVPEEVSLAVEEKCELVGFLSPHKVNVKE-GKIVSVTFSRT---EQDKNGKW----VQDSEQLttVKANYLISAFG 307
Cdd:PRK12769 504 ANMPGSKKEVKNAREEGANFEFNVQPVALELNEqGHVCGIRFLRTrlgEPDAQGRRrpvpIPGSEFV--MPADAVIMAFG 581
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 308 ------SGLEDPDVvealkplKFTDQN---LPSVDLNTMQSSHASVWVGGDLAGVAETTVEAVNDGKTAA 368
Cdd:PRK12769 582 fnphgmPWLESHGV-------TVDKWGriiADVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAA 644
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
2-435 |
2.26e-32 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 135.84 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTSDLCVGGCNLHASEEgSINIGGLQQFATEvfskmgvkQIRDPQTPTPK--NSTAKIVLLGAGPASLSCATFLGRLG 79
Cdd:PRK12775 383 VCPQETQCEAQCIIAKKHE-SVGIGRLERFVGD--------NARAKPVKPPRfsKKLGKVAICGSGPAGLAAAADLVKYG 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 80 YDnITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKIETGRSLSKQdITLEKLLKDT--KAVFVGIGLPQPK 157
Cdd:PRK12775 454 VD-VTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKT-FTVPQLMNDKgfDAVFLGVGAGAPT 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 158 lnplFKDLTPEMG--FYTSKDFLPKVAKASKpGVCLCKATLPSLKGTVIVLGAGDTAFDCATSALRCGAKKVFVVFRRGF 235
Cdd:PRK12775 532 ----FLGIPGEFAgqVYSANEFLTRVNLMGG-DKFPFLDTPISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSE 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 236 TNIRAVPEEVSLAVEEKCELVGFLSPHKVNVKE-GKIVSVTFSRTE----QDKNGKWVQDSEQLTTVKANYLISAFGSgl 310
Cdd:PRK12775 607 AEAPARIEEIRHAKEEGIDFFFLHSPVEIYVDAeGSVRGMKVEEMElgepDEKGRRKPMPTGEFKDLECDTVIYALGT-- 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 311 edpdvvealKPLKFTDQNLPSVDLN--------------TMQSSHASVWVGGDLAGVAETTVEAVNDGKTAAWYMHCFle 376
Cdd:PRK12775 685 ---------KANPIITQSTPGLALNkwgniaaddgklesTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATY-- 753
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2117727728 377 glpLTTTPKLPLFYTEIDNvdisvemcglkFENPFGLASAPPATTTAMIRRAFEQGWAY 435
Cdd:PRK12775 754 ---LRLGKKWPITAEEAAA-----------FQPGKLLPAIELHTHAGAVAAGAETGVAT 798
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
810-868 |
3.20e-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: 3.20e-31
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2117727728 810 ALIDDDMCINCGKCYMTCNDSGYQAINFDPNTHIPTVTDDCTGCTLCLSVCPIIDCITM 868
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDDCITM 59
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
2-371 |
7.88e-31 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 129.38 E-value: 7.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTSDLCVGGCNLHaSEEGSINIGGLQQFATEVFSKMGVKQirDPQTPTPKNStaKIVLLGAGPASLSCATFLGRLGYd 81
Cdd:PRK12809 261 VCPQDRLCEGACTLK-DHSGAVSIGNLERYITDTALAMGWRP--DVSKVVPRSE--KVAVIGAGPAGLGCADILARAGV- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 82 NITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKI----ETGRslskqDITLEKLLKDTKAVFVGIG----- 152
Cdd:PRK12809 335 QVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFhlncEIGR-----DITFSDLTSEYDAVFIGVGtygmm 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 153 ---LPQPKLNPLFKDLtPEMGFYTsKDFLPKVAKASKPgvclckatLPSLKG-TVIVLGAGDTAFDCATSALRCGAKKVF 228
Cdd:PRK12809 410 radLPHEDAPGVIQAL-PFLTAHT-RQLMGLPESEEYP--------LTDVEGkRVVVLGGGDTTMDCLRTSIRLNAASVT 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 229 VVFRRGFTNIRAVPEEVSLAVEEKCELVGFLSPHKVNVKE-GKIVSVTFSRTEQDKNG-------KWVQDSEqlTTVKAN 300
Cdd:PRK12809 480 CAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACDEdGRLTAVGLIRTAMGEPGpdgrrrpRPVAGSE--FELPAD 557
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2117727728 301 YLISAFGSGLEDPDVVEAL--KPLKFTDQNLPSVDLNTMQSSHASVWVGGDLAGVAETTVEAVNDGKTAAWYM 371
Cdd:PRK12809 558 VLIMAFGFQAHAMPWLQGSgiKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM 630
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
45-377 |
1.61e-27 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 115.09 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 45 RDPQTPTPKnstaKIVLLGAGPASLSCATFLGRLGYDnITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKI 124
Cdd:PRK12770 11 KEKPPPTGK----KVAIIGAGPAGLAAAGYLACLGYE-VHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 125 --------------ETGRSLSKQDITLEKLLKDTKAVFVGIGLPQP-KLNPLFKDLTpemGFYTSKDFLPKVaKASKPGV 189
Cdd:PRK12770 86 htrtkvccgeplheEEGDEFVERIVSLEELVKKYDAVLIATGTWKSrKLGIPGEDLP---GVYSALEYLFRI-RAAKLGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 190 cLCKATLPSLKG-TVIVLGAGDTAFDCATSALRCGAKKVFVVFRRGFTNIRAVPEEVSLAVEEKCELVGFLSPHKVnVKE 268
Cdd:PRK12770 162 -LPWEKVPPVEGkKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRI-IGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 269 GKIVSVTFSRT---EQDKNGKW----VQDSEqlTTVKANYLISAFGSgLEDPDVVEALKPLKFTDQNLPSVDlNTMQSSH 341
Cdd:PRK12770 240 GRVEGVELAKMrlgEPDESGRPrpvpIPGSE--FVLEADTVVFAIGE-IPTPPFAKECLGIELNRKGEIVVD-EKHMTSR 315
|
330 340 350
....*....|....*....|....*....|....*.
gi 2117727728 342 ASVWVGGDLAGVAETTVEAVNDGKTAAWYMHCFLEG 377
Cdd:PRK12770 316 EGVFAAGDVVTGPSKIGKAIKSGLRAAQSIHEWLDL 351
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
42-368 |
3.01e-25 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 111.78 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 42 KQIRDPQTPtPKNstAKIVLLGAGPASLSCATFLGRLGYDnITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLG 121
Cdd:PRK13984 272 SEILDDEPE-KKN--KKVAIVGSGPAGLSAAYFLATMGYE-VTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALG 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 122 VKIETGRSLSKqDITLEKLLKDTKAVFVGIGL------PQP--------KLNPLFKDLtpemgfytsKDFL----PKvak 183
Cdd:PRK13984 348 VKIHLNTRVGK-DIPLEELREKHDAVFLSTGFtlgrstRIPgtdhpdviQALPLLREI---------RDYLrgegPK--- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 184 askpgvclckatlPSLKGTVIVLGAGDTAFDCATSALRC-----GAKKVFVV-FRRGFTNIRAVPEEVSLAVEEKCELVG 257
Cdd:PRK13984 415 -------------PKIPRSLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTsLERTFEEMPADMEEIEEGLEEGVVIYP 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 258 FLSPHKVNVKEGKIVSVTFSRTEQ--DKNGKWVQ--DSEQLTTVKANYLISAFGSGLEDPDVVEALKP-LKFtdqNLPSV 332
Cdd:PRK13984 482 GWGPMEVVIENDKVKGVKFKKCVEvfDEEGRFNPkfDESDQIIVEADMVVEAIGQAPDYSYLPEELKSkLEF---VRGRI 558
|
330 340 350
....*....|....*....|....*....|....*..
gi 2117727728 333 DLNTM-QSSHASVWVGGDLAGvAETTVEAVNDGKTAA 368
Cdd:PRK13984 559 LTNEYgQTSIPWLFAGGDIVH-GPDIIHGVADGYWAA 594
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
2-368 |
6.94e-21 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 98.75 E-value: 6.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 2 VCPTSDLCVGGCnlhASEEGSINIGGLQQFATEvFSKMGVKQIRDPQT--PTPKNSTAK--IVLLGAGPASLSCATFLGR 77
Cdd:PRK12779 252 VCPQELQCQGVC---THTKRPIEIGQLEWYLPQ-HEKLVNPNANERFAgrISPWAAAVKppIAVVGSGPSGLINAYLLAV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 78 LGYDnITIYEKQDFVGGLSTSEIPQYRLPISVVNFEIQLVKDLGVKIET----GRSLSKQDITLEKLLKdtkaVFVGIGL 153
Cdd:PRK12779 328 EGFP-VTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFVKnfvvGKTATLEDLKAAGFWK----IFVGTGA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 154 PQPKlnplFKDLTPE--MGFYTSKDFLPKV--AKASKPGVclcKATLPSLKG-TVIVLGAGDTAFDCATSALRCGAKkVF 228
Cdd:PRK12779 403 GLPT----FMNVPGEhlLGVMSANEFLTRVnlMRGLDDDY---ETPLPEVKGkEVFVIGGGNTAMDAARTAKRLGGN-VT 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 229 VVFRRGFTNIRAVPEEVSLAVEEKCELVGFLSP------HKVNVKEGKIVSVTfSRTEQDKNGKWV-QDSEQLTTVKANY 301
Cdd:PRK12779 475 IVYRRTKSEMPARVEELHHALEEGINLAVLRAPrefigdDHTHFVTHALLDVN-ELGEPDKSGRRSpKPTGEIERVPVDL 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2117727728 302 LISAFGSGlEDPDVVEALKPLKFTDQNLPSVDLNTMQSSHASVWVGGDLAGVAETTVEAVNDGKTAA 368
Cdd:PRK12779 554 VIMALGNT-ANPIMKDAEPGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAA 619
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
397-684 |
1.37e-19 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 91.08 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 397 DISVEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTfaLDKDLVTNVSPRIVRGTTAGHNYGPQQGSFlnie 476
Cdd:PRK07565 2 DLSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKS--LFEEQIRHEAAELDRHLTHGTESFAEALDY---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 477 lISEKCAAYW-----LKGIQELKA--DFPtkiIIASIMCSYNEQdWKTLSKMAQDAGADALELNLScphgMGESGMGLAC 549
Cdd:PRK07565 76 -FPEPAKFYVgpeeyLELIRRAKEavDIP---VIASLNGSSAGG-WVDYARQIEQAGADALELNIY----YLPTDPDISG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 550 GQKPELVKGISEWVKATVKIPFFIKLTPNITNIVDIATAAYEGGADGVAAINTVsglmglsangtPWPAVGLDKRTTYGG 629
Cdd:PRK07565 147 AEVEQRYLDILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRF-----------YQPDIDLETLEVVPG 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2117727728 630 V---SGNATRpMGLRAVsAVANALSGFSIMGIGGIDSADVAWQYLQAGASVVQVCSAI 684
Cdd:PRK07565 216 LvlsTPAELR-LPLRWI-AILSGRVGADLAATTGVHDAEDVIKMLLAGADVVMIASAL 271
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
397-684 |
3.30e-19 |
|
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.
Pssm-ID: 240090 Cd Length: 325 Bit Score: 89.60 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 397 DISVEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTFaLDKDLVT---NVSPRIVRGTTAGH--NYGPQQGS 471
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSL-FEEQIEReaqELDRFLTYGSSFAEalSYFPEYGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 472 FlniELISEKcaayWLKGIQELKA--DFPtkiIIASIMCSYNEQdWKTLSKMAQDAGADALELNLS-CPHGMGESG---- 544
Cdd:cd04739 80 Y---NLGPEE----YLELIRRAKRavSIP---VIASLNGVSAGG-WVDYARQIEEAGADALELNIYaLPTDPDISGaeve 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 545 -MGLacgqkpELVKGisewVKATVKIPFFIKLTPNITNIVDIATAAYEGGADGVAAINTVsglmglsangtPWPAVGLDK 623
Cdd:cd04739 149 qRYL------DILRA----VKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRF-----------YQPDIDLET 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2117727728 624 RTTYGGV----SGNATRPmgLRAVsAVANALSGFSIMGIGGIDSADVAWQYLQAGASVVQVCSAI 684
Cdd:cd04739 208 LEVVPNLllssPAEIRLP--LRWI-AILSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTSAL 269
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
527-684 |
1.47e-18 |
|
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: 87.94 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 527 ADALELNLSCP--HGmgesgmgLACGQKPE-LVKGISEWVKAT----VKIPFFIKLTPNITN--IVDIATAAYEGGADGV 597
Cdd:cd04738 161 ADYLVVNVSSPntPG-------LRDLQGKEaLRELLTAVKEERnklgKKVPLLVKIAPDLSDeeLEDIADVALEHGVDGI 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 598 AAINTVSGLMGLSANgtpwpavglDKRTTYGGVSGNATRPMGLRAVSAVANALSG-FSIMGIGGIDSADVAWQYLQAGAS 676
Cdd:cd04738 234 IATNTTISRPGLLRS---------PLANETGGLSGAPLKERSTEVLRELYKLTGGkIPIIGVGGISSGEDAYEKIRAGAS 304
|
....*...
gi 2117727728 677 VVQVCSAI 684
Cdd:cd04738 305 LVQLYTGL 312
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
400-703 |
2.31e-18 |
|
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240092 Cd Length: 294 Bit Score: 86.61 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 400 VEMCGLKFENPFGLASAPPATTTAMIRRAFEQGWAYTVTKTFALDkdlvtnvsPRivRGTTAGHNYGPQQGSFLNIELiS 479
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLA--------GR--PGNPEPRYYAFPLGSINSLGL-P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 480 EKCAAYWLKGIQELKADFPT--KIIIASIMCSYnEQDWKTLSKMA--QDAGADALELNLSCPHGMGESGMGlACGqkpEL 555
Cdd:cd04741 70 NLGLDYYLEYIRTISDGLPGsaKPFFISVTGSA-EDIAAMYKKIAahQKQFPLAMELNLSCPNVPGKPPPA-YDF---DA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 556 VKGISEWVKATVKIPFFIKLTPnITNIV--DIATAAYEGGADGVA---AINTV-SGLMgLSANGTpwpAVGLDKRTTYGG 629
Cdd:cd04741 145 TLEYLTAVKAAYSIPVGVKTPP-YTDPAqfDTLAEALNAFACPISfitATNTLgNGLV-LDPERE---TVVLKPKTGFGG 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2117727728 630 VSGNATRPMGLRAVSAVANAL-SGFSIMGIGGIDSADVAWQYLQAGASVVQVCSAIQNQDFTLIDDYCTGLKALL 703
Cdd:cd04741 220 LAGAYLHPLALGNVRTFRRLLpSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
527-707 |
3.31e-16 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 80.98 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 527 ADALELNLSCPhgmgeSGMGLACGQKPELVKGISEWVKATVK-----IPFFIKLTPNITN--IVDIATAAYEGGADGVAA 599
Cdd:PRK05286 170 ADYFTVNISSP-----NTPGLRDLQYGEALDELLAALKEAQAelhgyVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 600 INTV---SGLMGLSANGTPwpavgldkrttyGGVSGnatRPMGLRA---VSAVANALSG-FSIMGIGGIDSADVAWQYLQ 672
Cdd:PRK05286 245 TNTTlsrDGLKGLPNADEA------------GGLSG---RPLFERStevIRRLYKELGGrLPIIGVGGIDSAEDAYEKIR 309
|
170 180 190
....*....|....*....|....*....|....*
gi 2117727728 673 AGASVVQVCSAIQNQDFTLIDDYCTGLKALLYLDG 707
Cdd:PRK05286 310 AGASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
794-872 |
6.20e-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: 67.77 E-value: 6.20e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117727728 794 PRIGAYKKLDNTKQVVALIDDDMCINCGKCYMTCNDsgyQAINFDPNTHIPTVTDDCTGCTLCLSVCPiIDCITMVPKT 872
Cdd:COG1144 9 PGGTAAYKTGGWRVERPVVDEDKCIGCGLCWIVCPD---GAIRVDDGKYYGIDYDYCKGCGICAEVCP-VKAIEMVPEE 83
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
784-871 |
3.60e-12 |
|
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: 65.20 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 784 KINEMIGRALPRIGAYKKLDNTKQ-VVALIDDDMCINCGKCYMTCNdsgYQAINFDPNtHIPTV-TDDCTGCTLCLSVCP 861
Cdd:TIGR01944 81 ALAELLGVEPIPQPLDADAGTIQPpMVALIDEDNCIGCTKCIQACP---VDAIVGAAK-AMHTViADECTGCDLCVEPCP 156
|
90
....*....|
gi 2117727728 862 iIDCITMVPK 871
Cdd:TIGR01944 157 -TDCIEMIPV 165
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
740-873 |
3.79e-12 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 67.06 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 740 PHFGPYLKQREEKLKNLKRETILHHNGRENGYPTNGVQVPSKVPKINEMIGRALPRIGAYKKLDNTKQVVALIDDDMCIN 819
Cdd:COG1145 107 AGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIG 186
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2117727728 820 CGKCYMTCndsGYQAINFDPNTHIPTV-TDDCTGCTLCLSVCPiIDCITMVPKTI 873
Cdd:COG1145 187 CGLCVKVC---PTGAIRLKDGKPQIVVdPDKCIGCGACVKVCP-VGAISLEPKEI 237
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
809-876 |
6.19e-12 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 61.67 E-value: 6.19e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2117727728 809 VALIDDDMCINCGKCYMTCNdsgYQAINFDPNTHIPTVTDDCTGCTLCLSVCPiIDCITMVPKTIPHV 876
Cdd:COG1149 5 IPVIDEEKCIGCGLCVEVCP---EGAIKLDDGGAPVVDPDLCTGCGACVGVCP-TGAITLEEREAGKI 68
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
784-870 |
1.77e-11 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 64.20 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 784 KINEMIGRALPRIGAYKKLDNTKQVVALIDDDMCINCGKCYMTCNdsgYQAInFDPNTHIPTV-TDDCTGCTLCLSVCPi 862
Cdd:PRK05113 83 KLAELLGVEPQPLDGEAQEATPARKVAFIDEDNCIGCTKCIQACP---VDAI-VGATKAMHTViSDLCTGCDLCVAPCP- 157
|
....*...
gi 2117727728 863 IDCITMVP 870
Cdd:PRK05113 158 TDCIEMIP 165
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
380-683 |
4.91e-11 |
|
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: 65.19 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 380 LTTTPKLPLFYTEIDNVD-ISVEMCGLKFENPFGLASAPPATTTAmIRRAFEQGWAY----TVTktfalDKDLVTNVSPR 454
Cdd:TIGR01036 27 GTGTPFLALLRSLFGASDpLEVTVLGLKFPNPLGLAAGFDKDGEA-IDALGAMGFGFleigTVT-----PKPQPGNPRPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 455 IVRGttaghnygPQQGSFLNIELISEKCAAYWLKGIQELKADFPTKIIIASIMCSYNEQ---DWKTLSKMAQdAGADALE 531
Cdd:TIGR01036 101 LFRL--------IEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKNKDTPSEDakeDYAACLRKLG-PLADYLV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 532 LNLSCPHGMGESGMGLACGQKPEL--VKGISEWVKATVKIPFFIKLTPNIT--NIVDIATAAYEGGADGVAAINTVsglm 607
Cdd:TIGR01036 172 VNVSSPNTPGLRDLQYKAELRDLLtaVKQEQDGLRRVHRVPVLVKIAPDLTesDLEDIADSLVELGIDGVIATNTT---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 608 gLSANGTPWPAVGLDKrttyGGVSGnatRPMGLRAVSAV---ANALSGFS-IMGIGGIDSADVAWQYLQAGASVVQVCSA 683
Cdd:TIGR01036 248 -VSRSLVQGPKNSDET----GGLSG---KPLQDKSTEIIrrlYAELQGRLpIIGVGGISSAQDALEKIRAGASLLQIYSG 319
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
809-878 |
5.60e-10 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 60.78 E-value: 5.60e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2117727728 809 VALI-----DDDMCINCGKCYMTCNdsgYQAINFDPNtHIPTV-TDDCTGCTLCLSVCPiIDCITMVPKTIPHVIK 878
Cdd:COG2878 126 AAVIggpkgCEYGCIGCGDCIKACP---FDAIVGAAK-GMHTVdEDKCTGCGLCVEACP-VDCIEMVPVSPTVVVS 196
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
492-682 |
5.81e-10 |
|
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: 59.91 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 492 ELKADFPTKIIIASIMCSYNEQDWKTLSKMAQDAGADALELNLSCPHGMGESgmglacgqkPELVKGIsewVKATVKIPF 571
Cdd:cd04722 50 KEVAAETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYLARED---------LELIREL---REAVPDVKV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 572 FIKLTPNITnivDIATAAYEGGADGVAAINTvsglMGLSANGTPWPAVGLDKRTtyggvsgnatrpmglravsavANALS 651
Cdd:cd04722 118 VVKLSPTGE---LAAAAAEEAGVDEVGLGNG----GGGGGGRDAVPIADLLLIL---------------------AKRGS 169
|
170 180 190
....*....|....*....|....*....|.
gi 2117727728 652 GFSIMGIGGIDSADVAWQYLQAGASVVQVCS 682
Cdd:cd04722 170 KVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
809-872 |
2.17e-09 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 59.42 E-value: 2.17e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2117727728 809 VALIDDDMCINCGKCYMTCNdsgYQAINFDPNTHIPTVTDDCTGCTLCLSVCPiIDCITMVPKT 872
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACP---VDAIVGAPKQMHTVLADLCTGCDLCVPPCP-VDCIDMVPVT 138
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
58-364 |
6.76e-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: 58.10 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 58 KIVLLGAGPASLSCATFLGRLGYDnITIYEKQD---FVGGLSTSEIPQYRLPISVVNFEIQLVKDL---------GVKIE 125
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGK-VTLIEDEGtcpYGGCVLSKALLGAAEAPEIASLWADLYKRKeevvkklnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 126 TGRS-----LSKQDITLEKLLKDT------KAVFVGIG-------LPQPKLNPLFKDLTpemgfYTSKDFLpkvakaskp 187
Cdd:pfam07992 81 LGTEvvsidPGAKKVVLEELVDGDgetityDRLVIATGarprlppIPGVELNVGFLVRT-----LDSAEAL--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 188 gvclckaTLPSLKGTVIVLGAGDTAFDCATSALRCGaKKVFVVFRRGFTNiRAVPEEVSLAVEEKcelvgfLSPHKVNVK 267
Cdd:pfam07992 147 -------RLKLLPKRVVVVGGGYIGVELAAALAKLG-KEVTLIEALDRLL-RAFDEEISAALEKA------LEKNGVEVR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 268 EGkivsVTFSRTEQDKNGKWVQDSEQlTTVKANYLISAFGSGLeDPDVVEALKpLKFTDQNLPSVDlNTMQSSHASVWVG 347
Cdd:pfam07992 212 LG----TSVKEIIGDGDGVEVILKDG-TEIDADLVVVAIGRRP-NTELLEAAG-LELDERGGIVVD-EYLRTSVPGIYAA 283
|
330
....*....|....*...
gi 2117727728 348 GDLA-GVAETTVEAVNDG 364
Cdd:pfam07992 284 GDCRvGGPELAQNAVAQG 301
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
812-871 |
1.10e-08 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 52.40 E-value: 1.10e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2117727728 812 IDDDMCINCGKCYMTC-------NDSGYQAINFDPnthiptvtDDCTGCTLCLSVCPiIDCITMVPK 871
Cdd:COG1146 5 IDTDKCIGCGACVEVCpvdvlelDEEGKKALVINP--------EECIGCGACELVCP-VGAITVEDD 62
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
398-707 |
1.35e-08 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 58.21 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 398 ISVEMCGLKFENPFGLASAPPATTTAmIRRAFEQGWAY----TVTKtfaldKDLVTNVSPRIVRGttaghnygPQQGSFL 473
Cdd:PLN02826 74 LGVEVWGRTFSNPIGLAAGFDKNAEA-VEGLLGLGFGFveigSVTP-----LPQPGNPKPRVFRL--------REEGAII 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 474 N--------IELISEKCAAY-----------WLKGIQELKADFPTKIIIASIMCSYNeqdwKTLSKMAQD--AG------ 526
Cdd:PLN02826 140 NrygfnsegIVAVAKRLGAQhgkrkldetssSSFSSDDVKAGGKAGPGILGVNLGKN----KTSEDAAADyvQGvralsq 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 527 -ADALELNLSCPhgmgeSGMGLACGQKPELVKGISEWVKAT---------VKIPFFIKLTPNIT--NIVDIATAAYEGGA 594
Cdd:PLN02826 216 yADYLVINVSSP-----NTPGLRKLQGRKQLKDLLKKVLAArdemqwgeeGPPPLLVKIAPDLSkeDLEDIAAVALALGI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 595 DGVAAINTvsglmglsANGTPWPAVGLDKRTTYGGVSGNATRPMGLRAVSAVANALSG-FSIMGIGGIDSADVAWQYLQA 673
Cdd:PLN02826 291 DGLIISNT--------TISRPDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGkIPLVGCGGVSSGEDAYKKIRA 362
|
330 340 350
....*....|....*....|....*....|....
gi 2117727728 674 GASVVQVCSAIQNQDFTLIDDYCTGLKALLYLDG 707
Cdd:PLN02826 363 GASLVQLYTAFAYEGPALIPRIKAELAACLERDG 396
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
1-41 |
1.42e-08 |
|
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: 53.31 E-value: 1.42e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2117727728 1 MVCPTSDLCVGGCNLHASEEGSINIGGLQQFATEVFSKMGV 41
Cdd:pfam14691 73 RVCPQERQCEGACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
397-685 |
2.56e-08 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 56.50 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 397 DISVEMCGLKFENPFGLASAPpATTTAMIRRAFEQGWAYT-VTKTFALDKDlVTNVSPRIvrgttAGHNYG-------PQ 468
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGV-YCMTKEELEEVEASAAGAfVTKSATLEPR-PGNPEPRY-----ADTPLGsinsmglPN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 469 QGsflnielisekcAAYWLKGIQELKADFPTKIIIASIMcSYNEQDWKTLSKMAQDAG-ADALELNLSCPHGMGESGMGL 547
Cdd:PRK02506 74 LG------------FDYYLDYVLELQKKGPNKPHFLSVV-GLSPEETHTILKKIQASDfNGLVELNLSCPNVPGKPQIAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 548 acgqKPELVKGISEWVKATVKIPFFIKLTPNItNIVDIATAAY---EGGADGVAAINTV-SGLMGLSANGTpwpaVGLDK 623
Cdd:PRK02506 141 ----DFETTEQILEEVFTYFTKPLGVKLPPYF-DIVHFDQAAAifnKFPLAFVNCINSIgNGLVIDPEDET----VVIKP 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2117727728 624 RTTYGGVSGNATRPMGLRAVSAVANAL-SGFSIMGIGGIDSADVAWQYLQAGASVVQVCSAIQ 685
Cdd:PRK02506 212 KNGFGGIGGDYIKPTALANVRAFYQRLnPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALH 274
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
812-861 |
9.72e-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: 49.56 E-value: 9.72e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2117727728 812 IDDDMCINCGKCYMTC--NDSGYQAINFDP-NTHIPTVTDDCTGCTLCLSVCP 861
Cdd:pfam13237 4 IDPDKCIGCGRCTAACpaGLTRVGAIVERLeGEAVRIGVWKCIGCGACVEACP 56
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
799-869 |
1.11e-07 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 49.66 E-value: 1.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2117727728 799 YKKLDN-TKQVVALIDDDMCINCGKCYMTCndsGYQAINFDPNTHIpTVTDDCTGCTLCLSVCPiIDCITMV 869
Cdd:COG4231 5 VKILDNrTTAMRYVIDEDKCTGCGACVKVC---PADAIEEGDGKAV-IDPDLCIGCGSCVQVCP-VDAIKLE 71
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
792-869 |
1.33e-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: 1.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2117727728 792 ALPRIGAYKKLDNtKQVVALIDDDMCINCGKCYMTCNdsgYQAINFDPNTHIPTVTDDCTGCTLCLSVCPiIDCITMV 869
Cdd:cd10549 56 AIELTPEGKEYVP-KEKEAEIDEEKCIGCGLCVKVCP---VDAITLEDELEIVIDKEKCIGCGICAEVCP-VNAIKLV 128
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
817-874 |
1.77e-07 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 48.97 E-value: 1.77e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2117727728 817 CINCGKCYMTCNdsgYQAINFDPNTHIPTVT---DDCTGCTLCLSVCPiIDCITMVPKTIP 874
Cdd:COG1143 4 CIGCGLCVRVCP---VDAITIEDGEPGKVYVidpDKCIGCGLCVEVCP-TGAISMTPFELA 60
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
817-861 |
2.91e-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: 47.91 E-value: 2.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2117727728 817 CINCGKCYMTCNdsgYQAINFDPNTHIPTVT------DDCTGCTLCLSVCP 861
Cdd:pfam12838 1 CIGCGACVAACP---VGAITLDEVGEKKGTKtvvidpERCVGCGACVAVCP 48
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
808-879 |
6.82e-07 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 47.42 E-value: 6.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2117727728 808 VVALIDDDMCINCGKCYMTCNdsgYQAINFDPNTHIpTVTDDCTGCTLCLSVCPiIDCITMVPKTIPHVIKR 879
Cdd:COG2768 4 GKPYVDEEKCIGCGACVKVCP---VGAISIEDGKAV-IDPEKCIGCGACIEVCP-VGAIKIEWEEDEEFQEK 70
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
62-106 |
6.95e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 47.14 E-value: 6.95e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2117727728 62 LGAGPASLSCATFLGRLGYDnITIYEKQDFVGGLSTS-EIPQYRLP 106
Cdd:pfam13450 2 VGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSyRVPGYVFD 46
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
58-379 |
3.60e-06 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 49.73 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 58 KIVLLGAGPASLSCATFLGRLGYdNITIYEKqDFVGG--LSTSEI---PQYRLPIS----VVNFEIQlVKDLGVKIETGR 128
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGL-KTLVIEG-GEPGGqlATTKEIenyPGFPEGISgpelAERLREQ-AERFGAEILLEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 129 --SLSKQD----ITLEKLLK-DTKAVFVGIGLPQPKLNplfkdltpemgfytskdfLPKVAKASKPGVCLCkAT--LPSL 199
Cdd:COG0492 79 vtSVDKDDgpfrVTTDDGTEyEAKAVIIATGAGPRKLG------------------LPGEEEFEGRGVSYC-ATcdGFFF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 200 KG-TVIVLGAGDTAFDcatSALRCG--AKKVFVVFRRGftNIRAVPEEVSLAveEKCELVGFLSPHKVN--VKEGKIVSV 274
Cdd:COG0492 140 RGkDVVVVGGGDSALE---EALYLTkfASKVTLIHRRD--ELRASKILVERL--RANPKIEVLWNTEVTeiEGDGRVEGV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 275 TFSRTeqdkngkwvqDSEQLTTVKANYLISAFGSgleDP--DVVEALKpLKFTDQNLPSVDlNTMQSSHASVWVGGDlag 352
Cdd:COG0492 213 TLKNV----------KTGEEKELEVDGVFVAIGL---KPntELLKGLG-LELDEDGYIVVD-EDMETSVPGVFAAGD--- 274
|
330 340 350
....*....|....*....|....*....|.
gi 2117727728 353 VAETTVE----AVNDGKTAAWYMHCFLEGLP 379
Cdd:COG0492 275 VRDYKYRqaatAAGEGAIAALSAARYLEPLK 305
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
809-869 |
4.17e-06 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 47.00 E-value: 4.17e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 809 VALIDDDMCINCGKCYMTCNdsgYQAINFDPNTHIPtvtDDCTGC---------TLCLSVCPiIDCITMV 869
Cdd:cd04410 74 IVLIDEDKCIGCGSCVEACP---YGAIVFDPEPGKA---VKCDLCgdrldeglePACVKACP-TGALTFG 136
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
812-861 |
4.40e-06 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 45.04 E-value: 4.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2117727728 812 IDDDMCINCGKCYMTCNDsgyQAINFDpNTHIPTVTDDCTGCTLCLSVCP 861
Cdd:COG2221 12 IDEEKCIGCGLCVAVCPT---GAISLD-DGKLVIDEEKCIGCGACIRVCP 57
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
812-883 |
2.51e-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: 44.70 E-value: 2.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2117727728 812 IDDDMCINCGKCYMTCNdsgYQAINFDPNTHIPTVT----DDCTGCTLCLSVCPiIDCITMVPKTIPHVIKRGQSV 883
Cdd:cd10549 3 YDPEKCIGCGICVKACP---TDAIELGPNGAIARGPeideDKCVFCGACVEVCP-TGAIELTPEGKEYVPKEKEAE 74
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
520-598 |
2.56e-05 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 46.33 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 520 KMAQDAGADALELNLSCP------HGMGeSGMgLacgQKPELVKGISEWVKATVKIPFFIK---LTPNITNIVDIATAAY 590
Cdd:cd02801 74 KIVEELGADGIDLNMGCPspkvtkGGAG-AAL-L---KDPELVAEIVRAVREAVPIPVTVKirlGWDDEEETLELAKALE 148
|
....*...
gi 2117727728 591 EGGADGVA 598
Cdd:cd02801 149 DAGASALT 156
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
54-104 |
2.60e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 47.92 E-value: 2.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2117727728 54 NSTAKIVLLGAGPASLSCATFLGRLGYDnITIYEKQDFVGG-LSTSEIPQYR 104
Cdd:COG1233 1 MMMYDVVVIGAGIGGLAAAALLARAGYR-VTVLEKNDTPGGrARTFERPGFR 51
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
809-861 |
3.08e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 44.94 E-value: 3.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 809 VALIDDDMCIN------CGKCYMTCNDSGYqAINFDPNTHIPTV-TDDCTGCTLCLSVCP 861
Cdd:cd16373 85 VAVIDKDRCLAwqggtdCGVCVEACPTEAI-AIVLEDDVLRPVVdEDKCVGCGLCEYVCP 143
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
58-99 |
3.92e-05 |
|
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: 47.13 E-value: 3.92e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2117727728 58 KIVLLGAGPASLSCATFLGRLGYDnITIYEKQDFVGGLSTSE 99
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHE-VTVLEASDRVGGLIRTV 43
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
809-869 |
4.22e-05 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 44.14 E-value: 4.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2117727728 809 VALIDDDMCINCGKCYMTCNdsgYQAInFDPNTHIPTVTDD-CTGCTLCLSVCPiIDCITMV 869
Cdd:PRK08764 79 VAWIVEADCIGCTKCIQACP---VDAI-VGGAKHMHTVIAPlCTGCELCVPACP-VDCIELH 135
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
808-861 |
4.73e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 47.16 E-value: 4.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2117727728 808 VVALIDDDMCINCGKCYMTCNdsgYQAINFDPNTHIPTVTDDCTGCTLCLSVCP 861
Cdd:COG1148 489 SVAEVDPEKCTGCGRCVEVCP---YGAISIDEKGVAEVNPALCKGCGTCAAACP 539
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
807-871 |
8.38e-05 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 43.39 E-value: 8.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2117727728 807 QVVALIDDDmCIN-----CgkcyMTCNDS-GYQAINFDPNTH---IPTV-TDDCTGCTLCLSVCPiIDCITMVPK 871
Cdd:cd10564 71 PLRAEIGDS-CLAlqgveC----RSCQDAcPTQAIRFRPRLGgiaLPELdADACTGCGACVSVCP-VGAITLTPL 139
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
812-877 |
1.24e-04 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 42.77 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2117727728 812 IDDDMCINCGKCYMTCndsGYQAINFDPNTHIPTVT--------DDCTGCTLCLSVCPiIDCITMVPKtIPHVI 877
Cdd:cd10549 37 IDEDKCVFCGACVEVC---PTGAIELTPEGKEYVPKekeaeideEKCIGCGLCVKVCP-VDAITLEDE-LEIVI 105
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
806-861 |
2.00e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 45.02 E-value: 2.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2117727728 806 KQVVALIDDDMCINCGKCYMTCndsGYQAINFDpNTHIPTVTDDCTGCTLCLSVCP 861
Cdd:COG4624 82 RGPSIIRDKEKCKNCYPCVRAC---PVKAIKVD-DGKAEIDEEKCISCGQCVAVCP 133
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
520-598 |
2.03e-04 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 44.31 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 520 KMAQDAGADALELNLSCP------HGMGeSGMgLacgQKPELVKGISEWVKATVKIPFFIK----LTPNITNIVDIATAA 589
Cdd:COG0042 81 RIAEELGADEIDINMGCPvkkvtkGGAG-AAL-L---RDPELVAEIVKAVVEAVDVPVTVKirlgWDDDDENALEFARIA 155
|
....*....
gi 2117727728 590 YEGGADGVA 598
Cdd:COG0042 156 EDAGAAALT 164
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
58-96 |
2.24e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 44.88 E-value: 2.24e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2117727728 58 KIVLLGAGPASLSCATFLGRLGYDnITIYEKQDFVGGLS 96
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYP-VTVLEADPVVGGIS 43
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
817-861 |
2.80e-04 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 39.75 E-value: 2.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2117727728 817 CINCGKCYMTCnDSgYQAINFDP-------------NTHIPTVTDDCTGCTLCLSVCP 861
Cdd:pfam13534 2 CIQCGCCVDEC-PR-YLLNGDEPkklmraaylgdleELQANKVANLCSECGLCEYACP 57
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
816-861 |
2.92e-04 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 39.46 E-value: 2.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2117727728 816 MCINCGKCYMTCNDSGYQAINFDPNTHIPTVTDDCTGCTLCLSVCP 861
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQTIRGDIAGLACIGCGACVDACP 46
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
520-598 |
3.36e-04 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 43.85 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 520 KMAQDAGADALELNLSCP-HGMGESGMGLACGQKPELVKGISEWVKATVKIPFFIKLTPNI----TNIVDIATAAYEGGA 594
Cdd:pfam01207 73 KLVEDRGADGIDINMGCPsKKVTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGWddshENAVEIAKIVEDAGA 152
|
....
gi 2117727728 595 DGVA 598
Cdd:pfam01207 153 QALT 156
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
58-98 |
8.80e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 42.57 E-value: 8.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2117727728 58 KIVLLGAGPASLSCATFLGRLGYDnITIYEKQDFVGGLSTS 98
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAAS 40
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
813-872 |
9.38e-04 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 39.63 E-value: 9.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 813 DDDMCINCGKCYMTCNDSgyqAINFDPNTHIPTVTDDCTGCTLCLSVCPiIDCITMVPKT 872
Cdd:PRK09624 49 NRDKCVRCYLCYIYCPEP---AIYLDEEGYPVFDYDYCKGCGICANECP-TKAIEMVRET 104
|
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
809-869 |
1.13e-03 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 39.16 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2117727728 809 VALIDDDMCINCGKCYMTCNDSgyqAINFDPNTHIPTVTDDCTGCTLCLSVCPiIDCITMV 869
Cdd:PRK09623 45 MPVVDESKCVKCYICWKFCPEP---AIYIKEDGYVAIDYDYCKGCGICANECP-TKAITMV 101
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
815-861 |
1.19e-03 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 40.12 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2117727728 815 DMCINCGKCYMTCNDSGY-------QAINFDpntHiptvtddCTGCTLCLSVCP 861
Cdd:PRK09625 59 EICINCFNCWVYCPDAAIlsrdkklKGVDYS---H-------CKGCGVCVEVCP 102
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
809-862 |
1.94e-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: 40.83 E-value: 1.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2117727728 809 VALIDDDMCINCGKCYMTCNdsgYQAINFDPNtHIPTVTDDCTGCTLCLSVCPI 862
Cdd:cd03110 58 KAFIDQEKCIRCGNCERVCK---FGAILEFFQ-KLIVDESLCEGCGACVIICPR 107
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
847-871 |
2.18e-03 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 37.42 E-value: 2.18e-03
10 20
....*....|....*....|....*
gi 2117727728 847 TDDCTGCTLCLSVCPiIDCITMVPK 871
Cdd:COG1143 1 EDKCIGCGLCVRVCP-VDAITIEDG 24
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
51-94 |
2.36e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 41.45 E-value: 2.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2117727728 51 TPKNSTAKIVLLGAGPASLSCATFLGRLGYDnITIYEKQDFVGG 94
Cdd:COG1231 2 SRRARGKDVVIVGAGLAGLAAARELRKAGLD-VTVLEARDRVGG 44
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
568-684 |
2.92e-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: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 568 KIPFFIkltpniTNIVDIATAAyegGADGV------------AAINTVSGLMGLSANGTPWPAVGLDKRTTYGGVsG--- 632
Cdd:TIGR00693 57 GVPFIV------NDRVDLALAL---GADGVhlgqddlpaseaRALLGPDKIIGVSTHNLEELAEAEAEGADYIGF-Gpif 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2117727728 633 ------NATRPMGLRAVSAVANALSGFSIMGIGGIDSADVAwQYLQAGASVVQVCSAI 684
Cdd:TIGR00693 127 ptptkkDPAPPAGVELLREIAATLIDIPIVAIGGITLENAA-EVLAAGADGVAVVSAI 183
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
812-861 |
3.10e-03 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 40.43 E-value: 3.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2117727728 812 IDDDMCINCGKCYMTCndsgyqainfdPnTHIP-----TVTDDCTGCTLCLSVCP 861
Cdd:COG0348 207 YDRGDCIDCGLCVKVC-----------P-MGIDirkgeINQSECINCGRCIDACP 249
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
482-530 |
3.43e-03 |
|
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.
Pssm-ID: 240077 [Multi-domain] Cd Length: 202 Bit Score: 39.87 E-value: 3.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2117727728 482 CAAYWLKGIQELKADFPTKIIIAsimcsyneqDWKTL------SKMAQDAGADAL 530
Cdd:cd04726 36 IKSEGMEAVRALREAFPDKIIVA---------DLKTAdagaleAEMAFKAGADIV 81
|
|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
817-861 |
4.20e-03 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 36.70 E-value: 4.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2117727728 817 CINCGKCYMTCndsGYQAI-----NFDPNTHIPTVTDD----------------CTGCTLCLSVCP 861
Cdd:pfam13484 1 CGSCGKCIDAC---PTGAIvgpegVLDARRCISYLTIEkkglipdelrcllgnrCYGCDICQDVCP 63
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
845-869 |
5.80e-03 |
|
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).
Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 39.46 E-value: 5.80e-03
10 20
....*....|....*....|....*
gi 2117727728 845 TVTDDCTGCTLCLSVCPiIDCITMV 869
Cdd:NF038196 182 HVTDKCIGCGICAKVCP-VNNIEME 205
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
811-861 |
7.61e-03 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 38.39 E-value: 7.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 811 LIDDDMCINCGKCYMTCNdsgYQAINFDPNTHIPTVtddCTGC---------TLCLSVCP 861
Cdd:COG0437 86 LVDYDKCIGCRYCVAACP---YGAPRFNPETGVVEK---CTFCadrldegllPACVEACP 139
|
|
| DMSOR_beta_like |
cd16367 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
809-869 |
7.98e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319889 [Multi-domain] Cd Length: 138 Bit Score: 37.67 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117727728 809 VALIDDDMCINCGKCYMTCNDS--GYQAINFD----PNTHIPT----------------------------VTDDCTGCT 854
Cdd:cd16367 13 LLVIDLDRCIRCDNCEKACADThdGHSRLDRNglrfGNLLVPTacrhcvdpvcmigcptgaihrddggevvISDACCGCG 92
|
90
....*....|....*
gi 2117727728 855 LCLSVCPiIDCITMV 869
Cdd:cd16367 93 NCASACP-YGAIQMV 106
|
|
| |
