|
Name |
Accession |
Description |
Interval |
E-value |
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
532-834 |
0e+00 |
|
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN, and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239244 Cd Length: 299 Bit Score: 550.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPmygpGQSSFLNIE 611
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGR----GQIGFNNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 612 LISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACGQDPELV 691
Cdd:cd02940 77 LISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 692 RNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDGTPwPAVGIAKRTTYGGVSGTAIR 771
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTP-PAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578798496 772 PIALRAVTSIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGL 834
Cdd:cd02940 236 PIALRAVSQIARAPePGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
53-513 |
2.16e-120 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 372.98 E-value: 2.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 53 EKLENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPT 132
Cdd:PRK11749 17 EERAQNFDEV-APGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 133 SDLCVGGCNLYATEEgPINIGGLQQFATEvfKAMSIPQIRNPSLPPPEKmseaysaKIALFGAGPASISCASFLARLGYs 212
Cdd:PRK11749 96 ERLCEGACVRGKKGE-PVAIGRLERYITD--WAMETGWVLFKRAPKTGK-------KVAVIGAGPAGLTAAHRLARKGY- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 213 DITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNeMTLSTLKEkGYKAAFIGIGLPEPNKDA 292
Cdd:PRK11749 165 DVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRD-ITLDELRA-GYDAVFIGTGAGLPRFLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 293 IF-QGLtqdQGFYTSKDFLPLVAKGSKAgmcachSPLPSIRGVViVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIR 371
Cdd:PRK11749 243 IPgENL---GGVYSAVDFLTRVNQAVAD------YDLPVGKRVV-VIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 372 AVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTE---QDETGKWNE-DEDQMVHLKADVVISAFGSVlSDPKV 447
Cdd:PRK11749 313 ASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMElgePDASGRRRVpIEGSEFTLPADLVIKAIGQT-PNPLI 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578798496 448 KEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQYGA 513
Cdd:PRK11749 392 LSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAASA 457
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
57-506 |
3.06e-118 |
|
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: 366.38 E-value: 3.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 57 NNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTsdLC 136
Cdd:COG0493 3 KDFREV-YPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--PC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 137 VGGCNLyATEEGPINIGGLQQFATEvfKAMSIPQIRNPSLPPP-EKmseaysaKIALFGAGPASISCASFLARLGYsDIT 215
Cdd:COG0493 80 EGACVR-GIVDEPVAIGALERFIAD--KAFEEGWVKPPPPAPRtGK-------KVAVVGSGPAGLAAAYQLARAGH-EVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 216 IFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNeMTLSTLKEKgYKAAFIGIG------LPEPN 289
Cdd:COG0493 149 VFEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKD-ITLDELLEE-FDAVFLATGagkprdLGIPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 290 KDAifqgltqdQGFYTSKDFLPLVAKgskagMCACHSPLPsIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVN 369
Cdd:COG0493 227 EDL--------KGVHSAMDFLTAVNL-----GEAPDTILA-VGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 370 IRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRTE---QDETGKWN--EDEDQMVHLKADVVISAFGSVLS 443
Cdd:COG0493 293 MPASKEEVEEALEEGVEFLFLVAPVEIIGdENGRVTGLECVRMElgePDESGRRRpvPIEGSEFTLPADLVILAIGQTPD 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578798496 444 DPKVKEALSpIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKY 506
Cdd:COG0493 373 PSGLEEELG-LELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
532-858 |
1.75e-102 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 324.59 E-value: 1.75e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTfsLDKDIVTNVSPRIirgttsGPMYGPGQS--SFLN 609
Cdd:PRK08318 3 DLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKT--LGPPIVNVSSPRF------GALVKEDRRfiGFNN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 610 IELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACGQDPE 689
Cdd:PRK08318 75 IELITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 690 LVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDG-TPWPAVGiaKRTTYGGVSGT 768
Cdd:PRK08318 155 LVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRmIPMPIVN--GKSSHGGYCGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 769 AIRPIALRAVTSIAR--ALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEEL 846
Cdd:PRK08318 233 AVKPIALNMVAEIARdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASL 312
|
330
....*....|..
gi 578798496 847 QDWDGQSPATVS 858
Cdd:PRK08318 313 EDMVGLAVPNVT 324
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
535-833 |
1.66e-98 |
|
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 309.28 E-value: 1.66e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 535 VEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDkDIVTNVSPRIIRGTTSGPmYGPGQSSFLNIELIS 614
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLH-PRPGNPLPRVARLPPEGE-SYPEQLGILNSFGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 615 EKTAAYWCQSVTELKADFPDNIVIASIMCSyNKNDWTELAKKSEDSGADALELNLSCPHGMGERGmglaCGQDPELVRNI 694
Cdd:cd02810 79 NLGLDVWLQDIAKAKKEFPGQPLIASVGGS-SKEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 695 CRWVRQAVQIPFFAKLTPNVT--DIVSIARAAKEGGANGVTATNTVSGLMGLKsdgtpwPAVGIAKRTTYGGVSGTAIRP 772
Cdd:cd02810 154 LKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDL------KTVGPGPKRGTGGLSGAPIRP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798496 773 IALRAVTSIARALP-GFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTG 833
Cdd:cd02810 228 LALRWVARLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
58-511 |
2.82e-86 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 283.45 E-value: 2.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 58 NFDDIkhtTLG--ERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDL 135
Cdd:PRK12831 22 NFEEV---CLGynEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 136 CVGGCNLYATEEgPINIGGLQQFATEVFKAMSIPQIrnpslPPPEKMSEaysaKIALFGAGPASISCASFLARLGYsDIT 215
Cdd:PRK12831 99 CEGKCVLGIKGE-PVAIGKLERFVADWARENGIDLS-----ETEEKKGK----KVAVIGSGPAGLTCAGDLAKMGY-DVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 216 IFEKQEYVGGLSTSEIPQFRLPYD-VVNFEIELMKDLGVKI----ICGKSLSVNEMtlstLKEKGYKAAFIGI--GLPEp 288
Cdd:PRK12831 168 IFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIetnvVVGKTVTIDEL----LEEEGFDAVFIGSgaGLPK- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 289 nkdaiFQGL--TQDQGFYTSKDFLPLVAKGsKAGMCACHSPLPSIRGVVIVlGAGDTAFDCATSALRCGArRVFIVFRKG 366
Cdd:PRK12831 243 -----FMGIpgENLNGVFSANEFLTRVNLM-KAYKPEYDTPIKVGKKVAVV-GGGNVAMDAARTALRLGA-EVHIVYRRS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 367 FVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRT---EQDETGKWN--EDEDQMVHLKADVVISAFGS 440
Cdd:PRK12831 315 EEELPARVEEVHHAKEEGVIFDLLTNPVEILGdENGWVKGMKCIKMelgEPDASGRRRpvEIEGSEFVLEVDTVIMSLGT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578798496 441 VlSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQY 511
Cdd:PRK12831 395 S-PNPLISSTTKGLKINKRGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSKKW 464
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
532-853 |
3.93e-85 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 277.49 E-value: 3.93e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIR------GTTSGPMYGpgqs 605
Cdd:PLN02495 10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARlraganGSAKGRVIG---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 606 sFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACG 685
Cdd:PLN02495 86 -WQNIELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 686 QDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDgTPWPAVGIAKRTTYGGV 765
Cdd:PLN02495 165 QDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLD-TLRPEPCVEGYSTPGGY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 766 SGTAIRPIALRAVTSIARALPG-FP----ILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYL 840
Cdd:PLN02495 244 SSKAVRPIALAKVMAIAKMMKSeFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKK 323
|
330
....*....|...
gi 578798496 841 KSIEELQDWDGQS 853
Cdd:PLN02495 324 HNFSSIEDFRGAS 336
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
532-838 |
1.62e-82 |
|
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: 267.32 E-value: 1.62e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKdIVTNVSPRIIRgtTsgpmygPGQSSFLNIE 611
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEP-QPGNPRPRLFR--L------PEDSGLINRM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 612 LISEKTAAYWCQSVTELKAdfPDNIVIASIMCSyNKNDWTELAKKSEDSGADALELNLSCPHGmgeRGMGLACGQDPELV 691
Cdd:COG0167 72 GLNNPGVDAFLERLLPAKR--YDVPVIVNIGGN-TVEDYVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 692 RNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLmglksdgtpwpAVGIAKRT-----TYGGVS 766
Cdd:COG0167 146 AELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGR-----------AIDLETRRpvlanEAGGLS 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578798496 767 GTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:COG0167 215 GPALKPIALRMVREVAQAVGGdIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYL 287
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
57-510 |
1.78e-79 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 273.16 E-value: 1.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 57 NNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLC 136
Cdd:PRK12778 310 NRFEEV-NLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQC 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 137 VGGCNLYATEEGPINIGGLQQFATEVFKamsipQIRNPSLPppeKMSEAYSAKIALFGAGPASISCASFLARLGYsDITI 216
Cdd:PRK12778 389 ESKCIHGKMGEEAVAIGYLERFVADYER-----ESGNISVP---EVAEKNGKKVAVIGSGPAGLSFAGDLAKRGY-DVTV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 217 FEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKI----ICGKSLSVNEMtlstlKEKGYKAAFIGIGLPEPNkda 292
Cdd:PRK12778 460 FEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFetdvIVGKTITIEEL-----EEEGFKGIFIASGAGLPN--- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 293 iFQGLTQDQ--GFYTSKDFLplvakgSKAGMCACHSPL---PSIRG-VVIVLGAGDTAFDCATSALRCGARRVFIVFRKG 366
Cdd:PRK12778 532 -FMNIPGENsnGVMSSNEYL------TRVNLMDAASPDsdtPIKFGkKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRS 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 367 FVNIRAVPEEMELAKEEKCEFLPFLSPRKVI------VKGGRIVAMQFvrTEQDETGKWN--EDEDQMVHLKADVVISAF 438
Cdd:PRK12778 605 EEEMPARLEEVKHAKEEGIEFLTLHNPIEYLadekgwVKQVVLQKMEL--GEPDASGRRRpvAIPGSTFTVDVDLVIVSV 682
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798496 439 GsVLSDPKVKEALSPIKFNRWGLPEVDPEtMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQ 510
Cdd:PRK12778 683 G-VSPNPLVPSSIPGLELNRKGTIVVDEE-MQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
58-506 |
6.99e-64 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 222.73 E-value: 6.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 58 NFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCV 137
Cdd:PRK12810 26 DFKEF-YEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAP--CE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 138 GGCNLyATEEGPINIGGLQQFATEvfKAMSIPQIRnpslppPEKMSEAYSAKIALFGAGPASISCASFLARLGYsDITIF 217
Cdd:PRK12810 103 GACTL-NINFGPVTIKNIERYIID--KAFEEGWVK------PDPPVKRTGKKVAVVGSGPAGLAAADQLARAGH-KVTVF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 218 EKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNeMTLSTLKEKgYKAAFIGIG------LPEPNKD 291
Cdd:PRK12810 173 ERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKD-ITAEELLAE-YDAVFLGTGaykprdLGIPGRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 292 AifqgltqdQGFYTSKDFLP--------------LVAKGSKagmcachsplpsirgvVIVLGAGDTAFDCATSALRCGAR 357
Cdd:PRK12810 251 L--------DGVHFAMDFLIqntrrvlgdetepfISAKGKH----------------VVVIGGGDTGMDCVGTAIRQGAK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 358 RVfIVFrkgfvNIRAVP----------------EEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEqdetgkWNE 421
Cdd:PRK12810 307 SV-TQR-----DIMPMPpsrrnknnpwpywpmkLEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTE------LGE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 422 DEDQMV-----HLKADVVISAFGSVLSDPKVKEALSpIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDG 496
Cdd:PRK12810 375 GDFEPVegsefVLPADLVLLAMGFTGPEAGLLAQFG-VELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEG 453
|
490
....*....|
gi 578798496 497 KQASWYIHKY 506
Cdd:PRK12810 454 RQAARAIDAY 463
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
534-846 |
4.28e-62 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 212.02 E-value: 4.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 534 SVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSGPMY-----GPGQSSFL 608
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPRE-GNPPPRVVE-TPGGMLNaiglqNPGVEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 609 NIELIsektaaywcqsvtelKADFPDNIVIASIMCSyNKNDWTELAKKSEDSGADALELNLSCPHgmgERGMGLACGQDP 688
Cdd:cd04740 79 EELLP---------------WLREFGTPVIASIAGS-TVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 689 ELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLmglksdgtpwpAVGIAKRT-----TYG 763
Cdd:cd04740 140 EAVAEIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKGM-----------AIDIETRKpilgnVTG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 764 GVSGTAIRPIALRAVTSIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIEDYCTGLKALL---YL 840
Cdd:cd04740 209 GLSGPAIKPIALRMVYQVYKAV-EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLdeeGI 286
|
....*.
gi 578798496 841 KSIEEL 846
Cdd:cd04740 287 KSIEEL 292
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
532-846 |
1.48e-61 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 210.78 E-value: 1.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSGPM--YG---PGQSS 606
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPRE-GNPTPRIAE-TPGGMLnaIGlqnPGVDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 607 FLNIELISEKtaaywcqsvtelKADFPdniVIASImCSYNKNDWTELAKKSEDSG-ADALELNLSCPHGMGergMGLACG 685
Cdd:PRK07259 79 FIEEELPWLE------------EFDTP---IIANV-AGSTEEEYAEVAEKLSKAPnVDAIELNISCPNVKH---GGMAFG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 686 QDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTvsgLMGLKSDgtpwpavgIAKR-----T 760
Cdd:PRK07259 140 TDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAID--------IKTRkpilaN 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 761 TYGGVSGTAIRPIALRAVTSIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIEDYCTGLKALLY- 839
Cdd:PRK07259 209 VTGGLSGPAIKPIALRMVYQVYQAV-DIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDk 286
|
....*....
gi 578798496 840 --LKSIEEL 846
Cdd:PRK07259 287 ygIKSIEEI 295
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
72-508 |
1.34e-56 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 211.34 E-value: 1.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 72 ALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCnLYATEEGPIN 151
Cdd:PRK12775 326 ALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQC-IIAKKHESVG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 152 IGGLQQFATEVFKAmsipqirNPSLPPpeKMSEAYsAKIALFGAGPASISCASFLARLGySDITIFEKQEYVGGLSTSEI 231
Cdd:PRK12775 405 IGRLERFVGDNARA-------KPVKPP--RFSKKL-GKVAICGSGPAGLAAAADLVKYG-VDVTVYEALHVVGGVLQYGI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 232 PQFRLPYDVVNFEIELMKDLGVKI----ICGKSLSVNEMtlstLKEKGYKAAFIGIGLPEPNkdaiFQGLTQDQG--FYT 305
Cdd:PRK12775 474 PSFRLPRDIIDREVQRLVDIGVKIetnkVIGKTFTVPQL----MNDKGFDAVFLGVGAGAPT----FLGIPGEFAgqVYS 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 306 SKDFLPLVAKGSKAGMCACHSPLpSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKC 385
Cdd:PRK12775 546 ANEFLTRVNLMGGDKFPFLDTPI-SLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGI 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 386 EFLPFLSPRKVI------VKGGRIVAMQFvrTEQDETGKWNE-DEDQMVHLKADVVISAFGSVlSDPKVKEALSPIKFNR 458
Cdd:PRK12775 625 DFFFLHSPVEIYvdaegsVRGMKVEEMEL--GEPDEKGRRKPmPTGEFKDLECDTVIYALGTK-ANPIITQSTPGLALNK 701
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 578798496 459 WGLPEVD----PETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQ 508
Cdd:PRK12775 702 WGNIAADdgklESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYLR 755
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
82-519 |
1.41e-56 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 206.50 E-value: 1.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 82 CAD--APCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCVGGCNLYATEEgPINIGGLQQFA 159
Cdd:PRK12814 97 CGDclGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDE-PVSICALKRYA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 160 TEvfKAMSIPQirnPSLPPPEKMSeaySAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYD 239
Cdd:PRK12814 174 AD--RDMESAE---RYIPERAPKS---GKKVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGMMRYGIPRFRLPES 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 240 VVNFEIELMKDLGVKIICGKSLSvNEMTLSTLKeKGYKAAFIGIGLPEPNKDAIfQGlTQDQGFYTSKDFLPLVAKGSKa 319
Cdd:PRK12814 245 VIDADIAPLRAMGAEFRFNTVFG-RDITLEELQ-KEFDAVLLAVGAQKASKMGI-PG-EELPGVISGIDFLRNVALGTA- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 320 gmcachsplPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVK 399
Cdd:PRK12814 320 ---------LHPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 400 GGRIVaMQFVRTEQ---DETGKWNED--EDQMVHLKADVVISAFGSVLsDPKVKEAlSPIKFNRWGLPEVDPETMQTSEA 474
Cdd:PRK12814 391 EGGLE-LTAIKMQQgepDESGRRRPVpvEGSEFTLQADTVISAIGQQV-DPPIAEA-AGIGTSRNGTVKVDPETLQTSVA 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 578798496 475 WVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQsqyGASVSAKP 519
Cdd:PRK12814 468 GVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLN---GKPVTAPV 509
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
86-506 |
1.30e-54 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 198.95 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 86 PCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCVGGCNlYATEEGPINIGGLQQFATEVFKA 165
Cdd:PRK12771 48 PCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCN-RGQVDDAVGINAVERFLGDYAIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 166 msipqiRNPSLPPPEKMSeaySAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEI 245
Cdd:PRK12771 125 ------NGWKFPAPAPDT---GKRVAVIGGGPAGLSAAYHLRRMGH-AVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 246 ELMKDLGVKIICGKSLSVNeMTLSTLkEKGYKAAFIGIG------LPEPNKDAifqgltqdQGFYTSKDFLPLVAKGSKa 319
Cdd:PRK12771 195 QRILDLGVEVRLGVRVGED-ITLEQL-EGEFDAVFVAIGaqlgkrLPIPGEDA--------AGVLDAVDFLRAVGEGEP- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 320 gmcachsplPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVK 399
Cdd:PRK12771 264 ---------PFLGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 400 GGRIVAM---QFVRTEQDETGKWNEDEDQMVHLKADVVISAFGSVlSDPKVKEALSPIKFNRwGLPEVDPETMQTSEAWV 476
Cdd:PRK12771 335 ENGATGLrviTVEKMELDEDGRPSPVTGEEETLEADLVVLAIGQD-IDSAGLESVPGVEVGR-GVVQVDPNFMMTGRPGV 412
|
410 420 430
....*....|....*....|....*....|
gi 578798496 477 FAGGDVVGLANTTVESVNDGKQASWYIHKY 506
Cdd:PRK12771 413 FAGGDMVPGPRTVTTAIGHGKKAARNIDAF 442
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
72-510 |
2.98e-53 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 196.14 E-value: 2.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 72 ALREAMRCLKCAdaPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCptSDLCVGGCNLYATEEgPIN 151
Cdd:PRK13984 180 AMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVC--THKCETVCSIGHRGE-PIA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 152 IGGLQQFATEVFKAMSIPQIRNpsLPPPEKmseaySAKIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEI 231
Cdd:PRK13984 255 IRWLKRYIVDNVPVEKYSEILD--DEPEKK-----NKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGVMRYGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 232 PQFRLPYDVVNFEIELMKDLGVKIICGKSLsVNEMTLSTLKEKgYKAAFIGIGL--------PEPNKDAIFQGLTQdqgF 303
Cdd:PRK13984 327 PSYRLPDEALDKDIAFIEALGVKIHLNTRV-GKDIPLEELREK-HDAVFLSTGFtlgrstriPGTDHPDVIQALPL---L 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 304 YTSKDFLplvaKGSkagmcachSPLPSIRGVVIVLGAGDTAFDCATSALRC-----GARRVFIV-FRKGFVNIRAVPEEM 377
Cdd:PRK13984 402 REIRDYL----RGE--------GPKPKIPRSLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTsLERTFEEMPADMEEI 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 378 ELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQ--DETGKWNE--DEDQMVHLKADVVISAFG-----SVLSDPkVK 448
Cdd:PRK13984 470 EEGLEEGVVIYPGWGPMEVVIENDKVKGVKFKKCVEvfDEEGRFNPkfDESDQIIVEADMVVEAIGqapdySYLPEE-LK 548
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578798496 449 EALspiKFNRwGLPEVDpETMQTSEAWVFAGGDVVGlANTTVESVNDGKQASWYIHKYVQSQ 510
Cdd:PRK13984 549 SKL---EFVR-GRILTN-EYGQTSIPWLFAGGDIVH-GPDIIHGVADGYWAAEGIDMYLRKQ 604
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
533-846 |
1.31e-51 |
|
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: 183.01 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 533 ISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIvTNVSPRIIRgTTSG-----PMYGPGQSSF 607
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRP-GYRNPTIVE-TPCGmlnaiGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 608 LNiELISEKTaaywcqsvtelkaDFPDNIvIASIMCSyNKNDWTELAKKSEDSG--ADALELNLSCPHGMGergMGLACG 685
Cdd:TIGR01037 79 LE-ELKPVRE-------------EFPTPL-IASVYGS-SVEEFAEVAEKLEKAPpyVDAYELNLSCPHVKG---GGIAIG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 686 QDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTvsgLMGLKSD---GTPWPAvgiakrTTY 762
Cdd:TIGR01037 140 QDPELSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKIDiktGKPILA------NKT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 763 GGVSGTAIRPIALRAVTSIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFtVIEDYCTGLKALLY--- 839
Cdd:TIGR01037 211 GGLSGPAIKPIALRMVYDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKaeg 288
|
....*..
gi 578798496 840 LKSIEEL 846
Cdd:TIGR01037 289 FTSIEEL 295
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
53-500 |
5.25e-50 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 187.54 E-value: 5.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 53 EKLENNFDDIkHTTLGERGALREAMRCLKCAD-APCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCP 131
Cdd:PRK12809 185 SERKTHFGEI-YCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 132 TSDLCVGGCNLyATEEGPINIGGLQQFATEVFKAMS-IPQIRNPSlppPEKmseaysAKIALFGAGPASISCASFLARLG 210
Cdd:PRK12809 264 QDRLCEGACTL-KDHSGAVSIGNLERYITDTALAMGwRPDVSKVV---PRS------EKVAVIGAGPAGLGCADILARAG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 211 YSdITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSvNEMTLSTLKEKgYKAAFIGIG------ 284
Cdd:PRK12809 334 VQ-VDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIG-RDITFSDLTSE-YDAVFIGVGtygmmr 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 285 --LPEPNKDAIFQGLtqdqgfytskdflPLVAKGSKAGMCACHS---PLPSIRGV-VIVLGAGDTAFDCATSALRCGARR 358
Cdd:PRK12809 411 adLPHEDAPGVIQAL-------------PFLTAHTRQLMGLPESeeyPLTDVEGKrVVVLGGGDTTMDCLRTSIRLNAAS 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 359 VFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRTEQDETGKWNEDEDQMV-----HLKAD 432
Cdd:PRK12809 478 VTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACdEDGRLTAVGLIRTAMGEPGPDGRRRPRPVagsefELPAD 557
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578798496 433 VVISAFGSVLSDPKVKEALSpIKFNRWGL---PEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQAS 500
Cdd:PRK12809 558 VLIMAFGFQAHAMPWLQGSG-IKLDKWGLiqtGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAA 627
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
30-500 |
3.08e-46 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 176.48 E-value: 3.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 30 STSAKKLDKKHW--KRNPDKNCFNCEKleNNFDDIKHTTLGERgALREAMRCLKCAD-APCQKSCPTNLDIKSFITSIAN 106
Cdd:PRK12769 179 PAMSKVEQMQATppRGEPDKLAIEARK--TGFDEIYLPFRADQ-AQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 107 KNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLyATEEGPINIGGLQQFATEVFKAMSIpqirNPSLPPPEKMSEay 186
Cdd:PRK12769 256 GNIDAAVELSHQTNSLPEITGRVCPQDRLCEGACTL-RDEYGAVTIGNIERYISDQALAKGW----RPDLSQVTKSDK-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 187 saKIALFGAGPASISCASFLARLGYSdITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKII----CGKSLS 262
Cdd:PRK12769 329 --RVAIIGAGPAGLACADVLARNGVA-VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFElnceVGKDIS 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 263 vnemtLSTLKEKgYKAAFIGIGLPE------PNKDAifqgltqdQGFYtskDFLPLVAKGSKAGM---CACHSPLPSIRG 333
Cdd:PRK12769 406 -----LESLLED-YDAVFVGVGTYRsmkaglPNEDA--------PGVY---DALPFLIANTKQVMgleELPEEPFINTAG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 334 V-VIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIV-KGGRIVAMQFVRT 411
Cdd:PRK12769 469 LnVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELnEQGHVCGIRFLRT 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 412 ---EQDETGKWNED--EDQMVHLKADVVISAFG-SVLSDPKVKEAlsPIKFNRWGLPEVDPET---MQTSEAWVFAGGDV 482
Cdd:PRK12769 549 rlgEPDAQGRRRPVpiPGSEFVMPADAVIMAFGfNPHGMPWLESH--GVTVDKWGRIIADVESqyrYQTSNPKIFAGGDA 626
|
490
....*....|....*...
gi 578798496 483 VGLANTTVESVNDGKQAS 500
Cdd:PRK12769 627 VRGADLVVTAMAEGRHAA 644
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
56-168 |
1.07e-44 |
|
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.
Pssm-ID: 434132 [Multi-domain] Cd Length: 113 Bit Score: 156.55 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 56 ENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDL 135
Cdd:pfam14691 2 IKNFEEV-ALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 578798496 136 CVGGCNLYATEEGPINIGGLQQFATEVFKAMSI 168
Cdd:pfam14691 81 CEGACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
75-500 |
3.53e-40 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 160.38 E-value: 3.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 75 EAMRCLKCADAPCQ------------KSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCnl 142
Cdd:PRK12779 186 EVMRDKQCDDKPCElgvlvqgkaepkGGCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVC-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 143 yATEEGPINIGGLQQFATEVFKAMSiPQIRNPSLPPPEKMSEAYSAKIALFGAGPASISCASFLARLGYSdITIFEKQEY 222
Cdd:PRK12779 264 -THTKRPIEIGQLEWYLPQHEKLVN-PNANERFAGRISPWAAAVKPPIAVVGSGPSGLINAYLLAVEGFP-VTVFEAFHD 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 223 VGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKI----ICGKSlsvneMTLSTLKEKGYKAAFIGIGLPEPNkdaiFQGLT 298
Cdd:PRK12779 341 LGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFvknfVVGKT-----ATLEDLKAAGFWKIFVGTGAGLPT----FMNVP 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 299 QDQ--GFYTSKDFLPLV--AKGSKAGMcacHSPLPSIRGV-VIVLGAGDTAFDCATSALRCGARrVFIVFRKGFVNIRAV 373
Cdd:PRK12779 412 GEHllGVMSANEFLTRVnlMRGLDDDY---ETPLPEVKGKeVFVIGGGNTAMDAARTAKRLGGN-VTIVYRRTKSEMPAR 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 374 PEEMELAKEEKCEFLPFLSPRKVI-------VKGGRIVAMQFvrTEQDETGKWN-EDEDQMVHLKADVVISAFGSVlSDP 445
Cdd:PRK12779 488 VEELHHALEEGINLAVLRAPREFIgddhthfVTHALLDVNEL--GEPDKSGRRSpKPTGEIERVPVDLVIMALGNT-ANP 564
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 578798496 446 KVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQAS 500
Cdd:PRK12779 565 IMKDAEPGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAA 619
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
534-838 |
1.42e-33 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 130.93 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 534 SVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDiVTNVSPRIIRgTTSGpmygpgqssFLN-IEL 612
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQ-PGNPTPRVFR-LPEG---------VLNrMGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 613 ISEKTAAYWCQSVTELKADFPDNI-VIASImcsyNKN---DWTELAKKSEDSgADALELNLSCPHGMGERgmglACGQDP 688
Cdd:pfam01180 72 NNPGLDAVLAELLKRRKEYPRPDLgINLSK----AGMtvdDYVEVARKIGPF-ADYIELNVSCPNTPGLR----ALQTDP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 689 ELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATN----TVSGlMGLKSDGTPwpavGIAKRTTyGG 764
Cdd:pfam01180 143 ELAAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINatntTVRG-MRIDLKTEK----PILANGT-GG 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578798496 765 VSGTAIRPIALRAVTSIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:pfam01180 217 LSGPPIKPIALKVIRELYQRTgPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
189-510 |
2.42e-33 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 132.04 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGV------KIICGKSLS 262
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYLACLGY-EVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVvfhtrtKVCCGEPLH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 263 VNE--------MTLSTLKEKgYKAAFIGIGLPEPNKDAIfQGlTQDQGFYTSKDFLpLVAKGSKAGMcACHSPLPSIRG- 333
Cdd:PRK12770 99 EEEgdefveriVSLEELVKK-YDAVLIATGTWKSRKLGI-PG-EDLPGVYSALEYL-FRIRAAKLGY-LPWEKVPPVEGk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 334 VVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIvKGGRIVAMQFVRT-- 411
Cdd:PRK12770 174 KVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRII-GEGRVEGVELAKMrl 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 412 -EQDETGKWNED--EDQMVHLKADVVISAFGSVLSDPKVKEALSpIKFNRWGLPEVDpETMQTSEAWVFAGGDVV----- 483
Cdd:PRK12770 253 gEPDESGRPRPVpiPGSEFVLEADTVVFAIGEIPTPPFAKECLG-IELNRKGEIVVD-EKHMTSREGVFAAGDVVtgpsk 330
|
330 340
....*....|....*....|....*...
gi 578798496 484 -GLAnttvesVNDGKQASWYIHKYVQSQ 510
Cdd:PRK12770 331 iGKA------IKSGLRAAQSIHEWLDLK 352
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
521-819 |
3.96e-22 |
|
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.
Pssm-ID: 240089 Cd Length: 327 Bit Score: 98.34 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 521 LPLFYTPIDLvdiSVEMAGLKFINPFGLA-----SATpatstsMIRRAFEAGWGFALTKTfsldkdiVT------NVSPR 589
Cdd:cd04738 30 LLLVYDDPRL---EVEVFGLTFPNPVGLAagfdkNAE------AIDALLALGFGFVEVGT-------VTprpqpgNPKPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 590 IIRGTTSGPM---YGpgqssFLN--IELISEKtaaywcqsvteLKADFPDNIVI-ASImcsyNKNDWTELAKKSED---- 659
Cdd:cd04738 94 LFRLPEDEALinrMG-----FNNdgADAVAKR-----------LKKRRPRGGPLgVNI----GKNKDTPLEDAVEDyvig 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 660 -----SGADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAV-----QIPFFAKLTPNVTD--IVSIARAAKEG 727
Cdd:cd04738 154 vrklgPYADYLVVNVSSPNTPGLRDL-----QGKEALRELLTAVKEERnklgkKVPLLVKIAPDLSDeeLEDIADVALEH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 728 GANGVTATNTVSGLMGLKSDgtpwpavgiAKRTTYGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFL 806
Cdd:cd04738 229 GVDGIIATNTTISRPGLLRS---------PLANETGGLSGAPLKERSTEVLRELYKLTGGkIPIIGVGGISSGEDAYEKI 299
|
330
....*....|...
gi 578798496 807 HSGASVLQVCSAI 819
Cdd:cd04738 300 RAGASLVQLYTGL 312
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
532-852 |
1.83e-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: 90.37 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 532 DISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGfALTkTFSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFLNIE 611
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAG-AIV-LPSLFEEQIEREAQELDRFLTYGSSFAEALSYFPEYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 612 LISEKTAAYWCQsVTELKA--DFPdniVIASIMCSYNkNDWTELAKKSEDSGADALELNLscphgmgergmgLACGQDPE 689
Cdd:cd04739 79 RYNLGPEEYLEL-IRRAKRavSIP---VIASLNGVSA-GGWVDYARQIEEAGADALELNI------------YALPTDPD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 690 LVRN--------ICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVsglmglksdgtPWPAVGIAKRTT 761
Cdd:cd04739 142 ISGAeveqryldILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRF-----------YQPDIDLETLEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 762 YGGVS-------GTAIRPIAlravtsIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGL 834
Cdd:cd04739 211 VPNLLlsspaeiRLPLRWIA------ILSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGL 284
|
330
....*....|....*...
gi 578798496 835 KALLYLKSIEELQDWDGQ 852
Cdd:cd04739 285 EAWMEEHGYESVQQLRGS 302
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
532-852 |
2.63e-19 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 90.31 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 532 DISVEMAGLKFINPFgLASATPAT-STSMIRRAFEAGWGFALTKtfSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFlni 610
Cdd:PRK07565 2 DLSTTYLGLTLRNPL-VASASPLSeSVDNVKRLEDAGAGAVVLK--SLFEEQIRHEAAELDRHLTHGTESFAEALDY--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 611 elISEKTAAYW-----CQSVTELKA--DFPdniVIASIMCSYNkNDWTELAKKSEDSGADALELNLSCPHGmgerGMGLA 683
Cdd:PRK07565 76 --FPEPAKFYVgpeeyLELIRRAKEavDIP---VIASLNGSSA-GGWVDYARQIEQAGADALELNIYYLPT----DPDIS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 684 CGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVsglmglksdgtPWPAVGIAKRTTYG 763
Cdd:PRK07565 146 GAEVEQRYLDILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRF-----------YQPDIDLETLEVVP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 764 GV--SGTAIRPIALRAVtSIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLK 841
Cdd:PRK07565 215 GLvlSTPAELRLPLRWI-AILSGRVGADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMERH 293
|
330
....*....|.
gi 578798496 842 SIEELQDWDGQ 852
Cdd:PRK07565 294 GYESLQQFRGS 304
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
559-817 |
1.11e-18 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 85.33 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 559 MIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRgttsgpmygpgqssflnielisektaaywcqsvteLKADFPDNIVI 638
Cdd:cd04722 17 LAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLK-----------------------------------EVAAETDLPLG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 639 ASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGmgergmglacgqdPELVRNICRWVRQAV-QIPFFAKLTPNVTDI 717
Cdd:cd04722 62 VQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL-------------AREDLELIRELREAVpDVKVVVKLSPTGELA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 718 vsiARAAKEGGANGVTATNtvsglmglksdgtpwpavgiakrttYGGVSGTAIRPIALRAVTSIARALPGFPILATGGID 797
Cdd:cd04722 129 ---AAAAEEAGVDEVGLGN-------------------------GGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGIN 180
|
250 260
....*....|....*....|
gi 578798496 798 SAESGLQFLHSGASVLQVCS 817
Cdd:cd04722 181 DPEDAAEALALGADGVIVGS 200
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
535-838 |
1.03e-17 |
|
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240092 Cd Length: 294 Bit Score: 84.68 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 535 VEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKdivtnvspriiRGTTSGPMYGPGQSSFLNIELIS 614
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAG-----------RPGNPEPRYYAFPLGSINSLGLP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 615 EKTAAYWCQSVTElkadfpdnivIASIMCSYNK----------NDWTELAKK---SEDSGADALELNLSCPH--GMGERG 679
Cdd:cd04741 70 NLGLDYYLEYIRT----------ISDGLPGSAKpffisvtgsaEDIAAMYKKiaaHQKQFPLAMELNLSCPNvpGKPPPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 680 MglacgqDPELVRNICRWVRQAVQIPFFAKLTPnVTDIVSIARAAK-----EGGANGVTATNTV-SGLMgLKSDGTpwpA 753
Cdd:cd04741 140 Y------DFDATLEYLTAVKAAYSIPVGVKTPP-YTDPAQFDTLAEalnafACPISFITATNTLgNGLV-LDPERE---T 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 754 VGIAKRTTYGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCT 832
Cdd:cd04741 209 VVLKPKTGFGGLAGAYLHPLALGNVRTFRRLLPSeIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEK 288
|
....*.
gi 578798496 833 GLKALL 838
Cdd:cd04741 289 ELEDIW 294
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
662-838 |
2.97e-17 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 84.06 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 662 ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAVQ-----IPFFAKLTPNVTD--IVSIARAAKEGGANGVTA 734
Cdd:PRK05286 170 ADYFTVNISSPNTPGLRDL-----QYGEALDELLAALKEAQAelhgyVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 735 TNTV---SGLMGLKsdgtpwpavgIAKRTtyGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFLHSGA 810
Cdd:PRK05286 245 TNTTlsrDGLKGLP----------NADEA--GGLSGRPLFERSTEVIRRLYKELGGrLPIIGVGGIDSAEDAYEKIRAGA 312
|
170 180
....*....|....*....|....*...
gi 578798496 811 SVLQVCSAIQNQDFTVIEDYCTGLKALL 838
Cdd:PRK05286 313 SLVQIYSGLIYEGPGLVKEIVRGLARLL 340
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
515-818 |
1.39e-15 |
|
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: 79.06 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 515 VSAKPELPLFYTPIDLVD-ISVEMAGLKFINPFGLAsATPATSTSMIRRAFEAGWGFALTKTFSlDKDIVTNVSPRIIRG 593
Cdd:TIGR01036 27 GTGTPFLALLRSLFGASDpLEVTVLGLKFPNPLGLA-AGFDKDGEAIDALGAMGFGFLEIGTVT-PKPQPGNPRPRLFRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 594 ttsgpmygPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIAsimcsynKNDWTELAKKSED---------SGADA 664
Cdd:TIGR01036 105 --------IEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIG-------KNKDTPSEDAKEDyaaclrklgPLADY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 665 LELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAVQI-------PFFAKLTPNVT--DIVSIARAAKEGGANGVTAT 735
Cdd:TIGR01036 170 LVVNVSSPNTPGLRDL-----QYKAELRDLLTAVKQEQDGlrrvhrvPVLVKIAPDLTesDLEDIADSLVELGIDGVIAT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 736 NTV---SGLMGLKSDGTPwpavgiakrttyGGVSGtaiRPIALRAVTSIAR---ALPG-FPILATGGIDSAESGLQFLHS 808
Cdd:TIGR01036 245 NTTvsrSLVQGPKNSDET------------GGLSG---KPLQDKSTEIIRRlyaELQGrLPIIGVGGISSAQDALEKIRA 309
|
330
....*....|
gi 578798496 809 GASVLQVCSA 818
Cdd:TIGR01036 310 GASLLQIYSG 319
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
620-852 |
9.14e-13 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 69.98 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 620 YWCQSVTELKADFPDNIVIASI--MCsynKNDWTELAKKSEDSG-ADALELNLSCPHGMGERGMGLacgqDPELVRNICR 696
Cdd:PRK02506 78 YYLDYVLELQKKGPNKPHFLSVvgLS---PEETHTILKKIQASDfNGLVELNLSCPNVPGKPQIAY----DFETTEQILE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 697 WVRQAVQIPFFAKLTPNVtDIVSIARAA---KEGGANGVTATNTV-SGLMGLKSDGTpwpaVGIAKRTTYGGVSGTAIRP 772
Cdd:PRK02506 151 EVFTYFTKPLGVKLPPYF-DIVHFDQAAaifNKFPLAFVNCINSIgNGLVIDPEDET----VVIKPKNGFGGIGGDYIKP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 773 IALRAVTSIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDG 851
Cdd:PRK02506 226 TALANVRAFYQRLnPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKGYQSLEDFRG 305
|
.
gi 578798496 852 Q 852
Cdd:PRK02506 306 K 306
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
189-482 |
1.42e-10 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 63.49 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 189 KIALFGAGPASISCASFLARLGYsDITIFEKQE---YVGGLSTSEIPQFRLPYDVVNFEIELMKDL---------GVKII 256
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGG-KVTLIEDEGtcpYGGCVLSKALLGAAEAPEIASLWADLYKRKeevvkklnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 257 CGKS-LSVN----EMTLSTLKEKG-----YKAAFIGIGlPEPNKDAIfQGLTQDQGF----YTSKDFLPLVAKGSKagmc 322
Cdd:pfam07992 81 LGTEvVSIDpgakKVVLEELVDGDgetitYDRLVIATG-ARPRLPPI-PGVELNVGFlvrtLDSAEALRLKLLPKR---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 323 achsplpsirgvVIVLGAGDTAFDCATSALRCGARrVFIVFRKGFVNiRAVPEEMELAKEEKceflpfLSPRKVIVKGGR 402
Cdd:pfam07992 155 ------------VVVVGGGYIGVELAAALAKLGKE-VTLIEALDRLL-RAFDEEISAALEKA------LEKNGVEVRLGT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 403 IVamqfVRTEQDETGKWNEDEDQMVhLKADVVISAFGSVLSDPKVKEAlsPIKFNRWGLPEVDpETMQTSEAWVFAGGDV 482
Cdd:pfam07992 215 SV----KEIIGDGDGVEVILKDGTE-IDADLVVVAIGRRPNTELLEAA--GLELDERGGIVVD-EYLRTSVPGIYAAGDC 286
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
651-810 |
4.66e-08 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 55.79 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 651 TELAKKSEDSGADALELNLSCPHGMGERGMGLAC-GQDPELVRNICRWVRQAVQIPFFAKLT----PNVTDIVSIARAAK 725
Cdd:pfam01207 69 AEAAKLVEDRGADGIDINMGCPSKKVTRGGGGAAlLRNPDLVAQIVKAVVKAVGIPVTVKIRigwdDSHENAVEIAKIVE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 726 EGGANGVTatntvsglmglksdgtpwpavgIAKRTTYGGVSGTAirpiALRAVTSIARALPgFPILATGGIDSAESGLQF 805
Cdd:pfam01207 149 DAGAQALT----------------------VHGRTRAQNYEGTA----DWDAIKQVKQAVS-IPVIANGDITDPEDAQRC 201
|
....*.
gi 578798496 806 L-HSGA 810
Cdd:pfam01207 202 LaYTGA 207
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
194-238 |
9.11e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 49.84 E-value: 9.11e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 578798496 194 GAGPASISCASFLARLGYsDITIFEKQEYVGGLSTS-EIPQFRLPY 238
Cdd:pfam13450 3 GAGLAGLVAAALLAKRGF-RVLVLEKRDRLGGNAYSyRVPGYVFDY 47
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
654-810 |
1.80e-07 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 52.88 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 654 AKKSEDSGADALELNLSCP-----HGmgerGMGLACGQDPELVRNICRWVRQAVQIPFFAK---LTPNVTDIVSIARAAK 725
Cdd:cd02801 73 AKIVEELGADGIDLNMGCPspkvtKG----GAGAALLKDPELVAEIVRAVREAVPIPVTVKirlGWDDEEETLELAKALE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 726 EGGANGVtatnTVSGlmglksdgtpwpavgiakRTTYGGVSGTA----IRPIalravtsiaRALPGFPILATGGIDSAES 801
Cdd:cd02801 149 DAGASAL----TVHG------------------RTREQRYSGPAdwdyIAEI---------KEAVSIPVIANGDIFSLED 197
|
170
....*....|
gi 578798496 802 GLQFL-HSGA 810
Cdd:cd02801 198 ALRCLeQTGV 207
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
533-818 |
2.27e-06 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 50.89 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 533 ISVEMAGLKFINPFGLASATPATStsmirRAFEA----GWGFALTKTfsldkdiVT------NVSPRIIRGTTSGPMYGP 602
Cdd:PLN02826 74 LGVEVWGRTFSNPIGLAAGFDKNA-----EAVEGllglGFGFVEIGS-------VTplpqpgNPKPRVFRLREEGAIINR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 603 GQSSFLNIELISEKTAAY-----------WCQSVTELKADFPDNIVIASIMCSYNKNdwtelakkSEDSG---------- 661
Cdd:PLN02826 142 YGFNSEGIVAVAKRLGAQhgkrkldetssSSFSSDDVKAGGKAGPGILGVNLGKNKT--------SEDAAadyvqgvral 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 662 ---ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVR---------QAVQIPFFAKLTPNVT--DIVSIARAAKEG 727
Cdd:PLN02826 214 sqyADYLVINVSSPNTPGLRKL-----QGRKQLKDLLKKVLaardemqwgEEGPPPLLVKIAPDLSkeDLEDIAAVALAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 728 GANGVTATNTvsglmglkSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPG-FPILATGGIDSAESGLQFL 806
Cdd:PLN02826 289 GIDGLIISNT--------TISRPDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGkIPLVGCGGVSSGEDAYKKI 360
|
330
....*....|..
gi 578798496 807 HSGASVLQVCSA 818
Cdd:PLN02826 361 RAGASLVQLYTA 372
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
652-810 |
3.42e-06 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 50.09 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 652 ELAKKSEDSGADALELNLSCP------HGMGergmglAC-GQDPELVRNICRWVRQAVQIPFFAK----LTPNVTDIVSI 720
Cdd:COG0042 78 EAARIAEELGADEIDINMGCPvkkvtkGGAG------AAlLRDPELVAEIVKAVVEAVDVPVTVKirlgWDDDDENALEF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 721 ARAAKEGGANGVtatnTVSGlmglksdgtpwpavgiakRTT---YggvSGTA----IRpiALRAVTSIaralpgfPILAT 793
Cdd:COG0042 152 ARIAEDAGAAAL----TVHG------------------RTReqrY---KGPAdwdaIA--RVKEAVSI-------PVIGN 197
|
170
....*....|....*...
gi 578798496 794 GGIDSAESGLQFL-HSGA 810
Cdd:COG0042 198 GDIFSPEDAKRMLeETGC 215
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
194-252 |
1.17e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 48.69 E-value: 1.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578798496 194 GAGPASISCASFLARLGYsDITIFEKQEYVGG-LSTSEIPQFRL---PYDVVNFEI--ELMKDLG 252
Cdd:COG1233 10 GAGIGGLAAAALLARAGY-RVTVLEKNDTPGGrARTFERPGFRFdvgPSVLTMPGVleRLFRELG 73
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
648-852 |
2.81e-05 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 47.27 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 648 NDWTELAKKSEDSGADALELNLSCPHGMGERGM-GLACGQDPELVRNICRWVRQAVQIPFFAKL----TPNVTDIVSIAR 722
Cdd:PRK10415 77 KEMADAARINVESGAQIIDINMGCPAKKVNRKLaGSALLQYPDLVKSILTEVVNAVDVPVTLKIrtgwAPEHRNCVEIAQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 723 AAKEGGANGVTatntvsglmglksdgtpwpavgIAKRTTYGGVSGTA----IRpiALRAVTSIaralpgfPILATGGIDS 798
Cdd:PRK10415 157 LAEDCGIQALT----------------------IHGRTRACLFNGEAeydsIR--AVKQKVSI-------PVIANGDITD 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578798496 799 AESGLQFL-HSGASVLQVCSAIQNQD--FTVIEDYC-TG----------LKALLyLKSIEELQDWDGQ 852
Cdd:PRK10415 206 PLKARAVLdYTGADALMIGRAAQGRPwiFREIQHYLdTGellpplplaeVKRLL-CAHVRELHDFYGP 272
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
194-510 |
6.42e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 45.88 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 194 GAGPASISCASFLARLGYSdITIFEKQEyVGGlstseipQFRLPYDVVNF-----EI---ELMKDL-------GVKIICG 258
Cdd:COG0492 7 GAGPAGLTAAIYAARAGLK-TLVIEGGE-PGG-------QLATTKEIENYpgfpeGIsgpELAERLreqaerfGAEILLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 259 KslsVNEMTLStlkekgykaafigiglpepnkDAIFQGLTQDQGFYTSKDFLplVAKGSKAGmcacHSPLPSI-----RG 333
Cdd:COG0492 78 E---VTSVDKD---------------------DGPFRVTTDDGTEYEAKAVI--IATGAGPR----KLGLPGEeefegRG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 334 V---------------VIVLGAGDTAFDcatSALRCG--ARRVFIVFRKGfvNIRAVPEEMELAKE-EKCEFLPflspRK 395
Cdd:COG0492 128 VsycatcdgfffrgkdVVVVGGGDSALE---EALYLTkfASKVTLIHRRD--ELRASKILVERLRAnPKIEVLW----NT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 396 VI--VKG-GRIVAMQFVRTEQDETgkwnededqmVHLKADVVISAFGSV-LSDPkVKEAlsPIKFNRWGLPEVDpETMQT 471
Cdd:COG0492 199 EVteIEGdGRVEGVTLKNVKTGEE----------KELEVDGVFVAIGLKpNTEL-LKGL--GLELDEDGYIVVD-EDMET 264
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 578798496 472 SEAWVFAGGDVVG----LANTtveSVNDGKQASWYIHKYVQSQ 510
Cdd:COG0492 265 SVPGVFAAGDVRDykyrQAAT---AAGEGAIAALSAARYLEPL 304
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
189-230 |
4.34e-04 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 43.67 E-value: 4.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 578798496 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSE 230
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTV 43
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
189-252 |
6.30e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 43.34 E-value: 6.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578798496 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLSTSeipqfrlpYDVVNFEIE---------------LMKDLG 252
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGH-EVTVFEADDQLGGLAAS--------FEFGGLPIErfyhhifksdealleLLDELG 70
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
407-503 |
1.92e-03 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 41.61 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798496 407 QFVRTEQDETGKW--NEDEDQMVHLKADVVISAFGSVlsdPKVK----EALSpIKFNRWGLPEVDpETMQTSEAWVFAGG 480
Cdd:COG1249 231 KVTSVEKTGDGVTvtLEDGGGEEAVEADKVLVATGRR---PNTDglglEAAG-VELDERGGIKVD-EYLRTSVPGIYAIG 305
|
90 100
....*....|....*....|...
gi 578798496 481 DVVGLANTTVESVNDGKQASWYI 503
Cdd:COG1249 306 DVTGGPQLAHVASAEGRVAAENI 328
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
189-227 |
3.27e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 41.03 E-value: 3.27e-03
10 20 30
....*....|....*....|....*....|....*....
gi 578798496 189 KIALFGAGPASISCASFLARLGYsDITIFEKQEYVGGLS 227
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGIS 43
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
189-231 |
9.30e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 39.39 E-value: 9.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 578798496 189 KIALFGAGPASISCASFLARLGySDITIFEKQEYVGGLSTSEI 231
Cdd:PRK06292 171 SLAVIGGGVIGLELGQALSRLG-VKVTVFERGDRILPLEDPEV 212
|
|
| |
