|
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: 551.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 532 DISVELAGLKFPNPFGLASATPTTSSSMIRRAFEAGWGFAVTKTFSLDKDIVTNVSPRIVRGITSGPmygpGQGSFLNIE 611
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGR----GQIGFNNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 612 LISEKTAAYWCKSIAELKADFPNHILLASIMCSYSREDWTELSKMAEVAGADALELNLSCPHGMGERGMGLACGQDPELV 691
Cdd:cd02940 77 LISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 692 RNICRWVRQAVQIPFFAKLTPNVTDIVNIAMAAQEGGADGVTATNTVSGLMGLKADSTPwPAVGGALRTTYGGMSGNAIR 771
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTP-PAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550010823 772 PIALRAVSAIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGL 834
Cdd:cd02940 236 PIALRAVSQIARAPePGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
532-1007 |
2.40e-129 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 398.55 E-value: 2.40e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 532 DISVELAGLKFPNPFGLASATPTTSSSMIRRAFEAGWGFAVTKTfsLDKDIVTNVSPRIvrgitsGPMYGPGQG--SFLN 609
Cdd:PRK08318 3 DLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKT--LGPPIVNVSSPRF------GALVKEDRRfiGFNN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 610 IELISEKTAAYWCKSIAELKADFPNHILLASIMCSYSREDWTELSKMAEVAGADALELNLSCPHGMGERGMGLACGQDPE 689
Cdd:PRK08318 75 IELITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 690 LVRNICRWVRQAVQIPFFAKLTPNVTDIVNIAMAAQEGGADGVTATNTVSGLMGLKADS-TPWPAVGGalRTTYGGMSGN 768
Cdd:PRK08318 155 LVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRmIPMPIVNG--KSSHGGYCGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 769 AIRPIALRAVSAIAR--ALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGlrallylksieeL 846
Cdd:PRK08318 233 AVKPIALNMVAEIARdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISG------------L 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 847 EDWngqspatmqhqkgkpvprfadlmgkklpsfgpyleqrkkiiaenkvkLKEQSMAavlpekkhfipkkpipAIKDVIG 926
Cdd:PRK08318 301 SHY-----------------------------------------------MDEKGFA----------------SLEDMVG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 927 KALQYIGTYGELCNTEQVVALIDEEMCINCGKCYMTCNDSGYQAIQFDP--KTHLPTVTDSCTGCTLCLSVCPVIDCIRM 1004
Cdd:PRK08318 318 LAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDEdgTRTPEVIEEECVGCNLCAHVCPVEGCITM 397
|
...
gi 2550010823 1005 VSR 1007
Cdd:PRK08318 398 GEV 400
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
53-509 |
2.76e-115 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 362.96 E-value: 2.76e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 53 EKLENNFDDIkHTTLSERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCPT 132
Cdd:PRK11749 17 EERAQNFDEV-APGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 133 SDLCVGGCNLYATEEgPINIGGLQQFATE-VFKAMNIPQIRNPSLPRvedmpeayhvKIALLGAGPASLSCASFLARLGY 211
Cdd:PRK11749 96 ERLCEGACVRGKKGE-PVAIGRLERYITDwAMETGWVLFKRAPKTGK----------KVAVIGAGPAGLTAAHRLARKGY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 212 SnITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEAELMKDLGVKIIFSKGLAMDgMTLRTLKeDGYEAVFIGIGLPEPNRD 291
Cdd:PRK11749 165 D-VTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRD-ITLDELR-AGYDAVFIGTGAGLPRFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 292 SIF-QGLrtdQGFYTSKDFLPLVAMASkpgmcarhSPLPSIHG-TVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTN 369
Cdd:PRK11749 242 GIPgENL---GGVYSAVDFLTRVNQAV--------ADYDLPVGkRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 370 IRAVPEEMELAKEEKCEFLPFLSPRKVVLRGGQIVAMEFVRTE---QDDNGNWKE-DEDQVVRLKADVVISAFGSiLSDS 445
Cdd:PRK11749 311 MPASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMElgePDASGRRRVpIEGSEFTLPADLVIKAIGQ-TPNP 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550010823 446 KVREAMAPIKFNRWGLPEVDPETMQTSEPWVFAGGD-VGGlANTTVESVNDGKQASWYMHRYLQS 509
Cdd:PRK11749 390 LILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDiVTG-AATVVWAVGDGKDAAEAIHEYLEG 453
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
57-506 |
1.30e-113 |
|
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: 357.52 E-value: 1.30e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 57 NNFDDIkHTTLSERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCPTsdLC 136
Cdd:COG0493 3 KDFREV-YPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--PC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 137 VGGCNLyATEEGPINIGGLQQFATEvfKAMNIPQIRNPslPRVEDMPEayhvKIALLGAGPASLSCASFLARLGYSnITI 216
Cdd:COG0493 80 EGACVR-GIVDEPVAIGALERFIAD--KAFEEGWVKPP--PPAPRTGK----KVAVVGSGPAGLAAAYQLARAGHE-VTV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 217 FEKQEYVGGLSTSEIPQFRLPYDVVNFEAELMKDLGVKIIFSKGLAMDgMTLRTLKEDgYEAVFIGIGLPEPNRDSIfQG 296
Cdd:COG0493 150 FEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKD-ITLDELLEE-FDAVFLATGAGKPRDLGI-PG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 297 lRTDQGFYTSKDFLPLVAMaskpgMCARHSPLPsIHGTVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTNIRAVPEE 376
Cdd:COG0493 227 -EDLKGVHSAMDFLTAVNL-----GEAPDTILA-VGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 377 MELAKEEKCEFLPFLSPRKVVLR-GGQIVAMEFVRTE---QDDNGNWK--EDEDQVVRLKADVVISAFGSILSDSKVREA 450
Cdd:COG0493 300 VEEALEEGVEFLFLVAPVEIIGDeNGRVTGLECVRMElgePDESGRRRpvPIEGSEFTLPADLVILAIGQTPDPSGLEEE 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2550010823 451 MApIKFNRWGLPEVDPETMQTSEPWVFAGGDVGGLANTTVESVNDGKQASWYMHRY 506
Cdd:COG0493 380 LG-LELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
535-833 |
6.85e-93 |
|
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: 297.34 E-value: 6.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 535 VELAGLKFPNPFGLASATPTTSSSMIRRAFEAGWGFAVTKTFSLDkDIVTNVSPRIVRgITSGPMYGPGQGSFLNIELIS 614
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLH-PRPGNPLPRVAR-LPPEGESYPEQLGILNSFGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 615 EKTAAYWCKSIAELKADFPNHILLASIMCSySREDWTELSKMAEVAGADALELNLSCPHGMGERGmglaCGQDPELVRNI 694
Cdd:cd02810 79 NLGLDVWLQDIAKAKKEFPGQPLIASVGGS-SKEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 695 CRWVRQAVQIPFFAKLTPNVT--DIVNIAMAAQEGGADGVTATNTVSGLMGLKadstpwPAVGGALRTTYGGMSGNAIRP 772
Cdd:cd02810 154 LKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDL------KTVGPGPKRGTGGLSGAPIRP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550010823 773 IALRAVSAIARALP-GFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTG 833
Cdd:cd02810 228 LALRWVARLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
532-838 |
2.59e-86 |
|
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: 279.65 E-value: 2.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 532 DISVELAGLKFPNPFGLASATPTTSSSMIRRAFEAGWGFAVTKTFSLDKdIVTNVSPRIVRgiTsgpmygPGQGSFLNIE 611
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEP-QPGNPRPRLFR--L------PEDSGLINRM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 612 LISEKTAAYWCKSIAELKAdfPNHILLASIMCSySREDWTELSKMAEVAGADALELNLSCPHGmgeRGMGLACGQDPELV 691
Cdd:COG0167 72 GLNNPGVDAFLERLLPAKR--YDVPVIVNIGGN-TVEDYVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 692 RNICRWVRQAVQIPFFAKLTPNVTDIVNIAMAAQEGGADGVTATNTVSGL-MGLKadsTPWPAVGGalrtTYGGMSGNAI 770
Cdd:COG0167 146 AELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRaIDLE---TRRPVLAN----EAGGLSGPAL 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550010823 771 RPIALRAVSAIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALL 838
Cdd:COG0167 219 KPIALRMVREVAQAVGGdIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYL 287
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
532-853 |
3.73e-84 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 277.49 E-value: 3.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 532 DISVELAGLKFPNPFGLASATPTTSSSMIRRAFEAGWGFAVTKTFSLDKDIVTNVSPRIVR------GITSGPMYGpgqg 605
Cdd:PLN02495 10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARlraganGSAKGRVIG---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 606 sFLNIELISEKTAAYWCKSIAELKADFPNHILLASIMCSYSREDWTELSKMAEVAGADALELNLSCPHGMGERGMGLACG 685
Cdd:PLN02495 86 -WQNIELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 686 QDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVNIAMAAQEGGADGVTATNTVSGLMGLKADS-TPWPAVGGalRTTYGG 764
Cdd:PLN02495 165 QDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLDTlRPEPCVEG--YSTPGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 765 MSGNAIRPIALRAVSAIARALPG-FP----ILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALLY 839
Cdd:PLN02495 243 YSSKAVRPIALAKVMAIAKMMKSeFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMK 322
|
330
....*....|....
gi 2550010823 840 LKSIEELEDWNGQS 853
Cdd:PLN02495 323 KHNFSSIEDFRGAS 336
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
58-509 |
1.02e-78 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 265.34 E-value: 1.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 58 NFDDIkHTTLSERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCPTSDLCV 137
Cdd:PRK12831 22 NFEEV-CLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQCE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 138 GGCNLYATEEgPINIGGLQQFATEVFKAMNIpqirnpslpRVEDMPEAYHVKIALLGAGPASLSCASFLARLGYsNITIF 217
Cdd:PRK12831 101 GKCVLGIKGE-PVAIGKLERFVADWARENGI---------DLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGY-DVTIF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 218 EKQEYVGGLSTSEIPQFRLPYD-VVNFEAELMKDLGVKI----IFSKGLAMDGMtlrtLKEDGYEAVFIGI--GLPEpnr 290
Cdd:PRK12831 170 EALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIetnvVVGKTVTIDEL----LEEEGFDAVFIGSgaGLPK--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 291 dsiFQGLRTDQ--GFYTSKDFLPLVAM--ASKPGMcarHSPLpSIHGTVIVLGAGDTAFDCATSALRCGArRVFVVFRKG 366
Cdd:PRK12831 243 ---FMGIPGENlnGVFSANEFLTRVNLmkAYKPEY---DTPI-KVGKKVAVVGGGNVAMDAARTALRLGA-EVHIVYRRS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 367 FTNIRAVPEEMELAKEEKCEFLPFLSP-RKVVLRGGQIVAMEFVRT---EQDDNGNWK--EDEDQVVRLKADVVISAFGS 440
Cdd:PRK12831 315 EEELPARVEEVHHAKEEGVIFDLLTNPvEILGDENGWVKGMKCIKMelgEPDASGRRRpvEIEGSEFVLEVDTVIMSLGT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550010823 441 -----ILSDSKvreamaPIKFNRWGLPEVDPETMQTSEPWVFAGGD-VGGLAnTTVESVNDGKQASWYMHRYLQS 509
Cdd:PRK12831 395 spnplISSTTK------GLKINKRGCIVADEETGLTSKEGVFAGGDaVTGAA-TVILAMGAGKKAAKAIDEYLSK 462
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
57-509 |
7.13e-75 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 262.37 E-value: 7.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 57 NNFDDIkHTTLSERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCPTSDLC 136
Cdd:PRK12778 310 NRFEEV-NLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQC 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 137 VGGCNLYATEEGPINIGGLQQFATEvFKAMNipqiRNPSLPRVEdmpEAYHVKIALLGAGPASLSCASFLARLGYsNITI 216
Cdd:PRK12778 389 ESKCIHGKMGEEAVAIGYLERFVAD-YERES----GNISVPEVA---EKNGKKVAVIGSGPAGLSFAGDLAKRGY-DVTV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 217 FEKQEYVGGLSTSEIPQFRLPYDVVNFEAELMKDLGVKIIFSKgLAMDGMTLRTLKEDGYEAVFIGIGLPEPNrdsiFQG 296
Cdd:PRK12778 460 FEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDV-IVGKTITIEELEEEGFKGIFIASGAGLPN----FMN 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 297 LRTDQ--GFYTSKDFLPLVAM--ASKPGmcarhSPLPSIHG-TVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTNIR 371
Cdd:PRK12778 535 IPGENsnGVMSSNEYLTRVNLmdAASPD-----SDTPIKFGkKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMP 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 372 AVPEEMELAKEEKCEFLPFLSPRKVV------LRGGQIVAMEFvrTEQDDNGNWK--EDEDQVVRLKADVVISAFGsILS 443
Cdd:PRK12778 610 ARLEEVKHAKEEGIEFLTLHNPIEYLadekgwVKQVVLQKMEL--GEPDASGRRRpvAIPGSTFTVDVDLVIVSVG-VSP 686
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2550010823 444 DSKVREAMAPIKFNRWGLPEVDPEtMQTSEPWVFAGGDVGGLANTTVESVNDGKQASWYMHRYLQS 509
Cdd:PRK12778 687 NPLVPSSIPGLELNRKGTIVVDEE-MQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSS 751
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
58-508 |
6.01e-64 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 224.27 E-value: 6.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 58 NFDDIkHTTLSERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCPTSdlCV 137
Cdd:PRK12810 26 DFKEF-YEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAP--CE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 138 GGCNLyATEEGPINIGGLQQFATEVFKAMNIPQIRNPSLPRVEdmpeayhvKIALLGAGPASLSCASFLARLGYSnITIF 217
Cdd:PRK12810 103 GACTL-NINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGK--------KVAVVGSGPAGLAAADQLARAGHK-VTVF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 218 EKQEYVGGLSTSEIPQFRLPYDVVNFEAELMKDLGVKIIFSKGLAMDgMTLRTLKEDgYEAVFIGIG------LPEPNRD 291
Cdd:PRK12810 173 ERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKD-ITAEELLAE-YDAVFLGTGaykprdLGIPGRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 292 SifqglrtdQGFYTSKDFLP---LVAMASKPGmcarhsplPSIHGT---VIVLGAGDTAFDCATSALRCGARRVfVVF-- 363
Cdd:PRK12810 251 L--------DGVHFAMDFLIqntRRVLGDETE--------PFISAKgkhVVVIGGGDTGMDCVGTAIRQGAKSV-TQRdi 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 364 -------RKGFTNIRAVPEEMEL--AKEEKCEFLPFLSPRKVVLRGGQIVAMEFVRTEqddngnWKEDEDQVV-----RL 429
Cdd:PRK12810 314 mpmppsrRNKNNPWPYWPMKLEVsnAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTE------LGEGDFEPVegsefVL 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550010823 430 KADVVISAFGSILSDSKVREAMApIKFNRWGLPEVDPETMQTSEPWVFAGGDVGGLANTTVESVNDGKQASWYMHRYLQ 508
Cdd:PRK12810 388 PADLVLLAMGFTGPEAGLLAQFG-VELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLM 465
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
532-846 |
1.80e-62 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 214.63 E-value: 1.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 532 DISVELAGLKFPNPFGLASATPTTSSSMIRRAFEAGWGFAVTKTFSLDKDIvTNVSPRIVRgiTSGPMY---G---PGQG 605
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPRE-GNPTPRIAE--TPGGMLnaiGlqnPGVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 606 SFLNIELISEKtaaywcksiaelKADFPnhiLLASImCSYSREDWTEL-SKMAEVAGADALELNLSCPHGMGergMGLAC 684
Cdd:PRK07259 78 AFIEEELPWLE------------EFDTP---IIANV-AGSTEEEYAEVaEKLSKAPNVDAIELNISCPNVKH---GGMAF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 685 GQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVNIAMAAQEGGADGVTATNTvsgLMGLKAD-STPWPAVGgalrTTYG 763
Cdd:PRK07259 139 GTDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAIDiKTRKPILA----NVTG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 764 GMSGNAIRPIALRAVSAIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIDDYCTGLRALLY---L 840
Cdd:PRK07259 212 GLSGPAIKPIALRMVYQVYQAV-DIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDkygI 289
|
....*.
gi 2550010823 841 KSIEEL 846
Cdd:PRK07259 290 KSIEEI 295
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
534-853 |
3.89e-60 |
|
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: 207.79 E-value: 3.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 534 SVELAGLKFPNPFGLASATPTTSSSMIRRAFEAGWGFAVTKTFSLDKDIvTNVSPRIVRgiTSGPMY------GPGQGSF 607
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPRE-GNPPPRVVE--TPGGMLnaiglqNPGVEAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 608 LNIELIsektaaywcksiAELKADFPnhiLLASIMCSySREDWTELSKMAEVAGADALELNLSCPHgmgERGMGLACGQD 687
Cdd:cd04740 78 LEELLP------------WLREFGTP---VIASIAGS-TVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 688 PELVRNICRWVRQAVQIPFFAKLTPNVTDIVNIAMAAQEGGADGVTATNTVSGlMGLKADS-TPwpavggALRTTYGGMS 766
Cdd:cd04740 139 PEAVAEIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKG-MAIDIETrKP------ILGNVTGGLS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 767 GNAIRPIALRAVSAIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQnQDFTVIDDYCTGLRALLYLKSIEEL 846
Cdd:cd04740 212 GPAIKPIALRMVYQVYKAV-EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLDEEGIKSI 289
|
....*..
gi 2550010823 847 EDWNGQS 853
Cdd:cd04740 290 EELVGLA 296
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
533-846 |
1.26e-54 |
|
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: 192.26 E-value: 1.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 533 ISVELAGLKFPNPFGLASATPTTSSSMIRRAFEAGWGFAVTKTFSLDKDIvTNVSPRIVRG----ITSGPMYGPGQGSFL 608
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRP-GYRNPTIVETpcgmLNAIGLQNPGVEAFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 609 NiELISEKTaaywcksiaelkaDFPNHILlASIMCSySREDWTELSKMAEVAG--ADALELNLSCPHGMGergMGLACGQ 686
Cdd:TIGR01037 80 E-ELKPVRE-------------EFPTPLI-ASVYGS-SVEEFAEVAEKLEKAPpyVDAYELNLSCPHVKG---GGIAIGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 687 DPELVRNICRWVRQAVQIPFFAKLTPNVTDIVNIAMAAQEGGADGVTATNTvsgLMGLKAD-STPWPavggALRTTYGGM 765
Cdd:TIGR01037 141 DPELSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKIDiKTGKP----ILANKTGGL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 766 SGNAIRPIALRAVSAIARALpGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFtVIDDYCTGLRALLY---LKS 842
Cdd:TIGR01037 214 SGPAIKPIALRMVYDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKaegFTS 291
|
....
gi 2550010823 843 IEEL 846
Cdd:TIGR01037 292 IEEL 295
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
72-508 |
5.08e-53 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 201.71 E-value: 5.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 72 ALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCPTSDLCVGGCnLYATEEGPIN 151
Cdd:PRK12775 326 ALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQC-IIAKKHESVG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 152 IGGLQQFATEVFKAmniPQIRNPSLPRVEDmpeayhvKIALLGAGPASLSCASFLARLGySNITIFEKQEYVGGLSTSEI 231
Cdd:PRK12775 405 IGRLERFVGDNARA---KPVKPPRFSKKLG-------KVAICGSGPAGLAAAADLVKYG-VDVTVYEALHVVGGVLQYGI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 232 PQFRLPYDVVNFEAELMKDLGVKIIFSKGLAMDGMTLRTLKEDGYEAVFIGIGLPEPNrdsiFQGLRTDQG--FYTSKDF 309
Cdd:PRK12775 474 PSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDKGFDAVFLGVGAGAPT----FLGIPGEFAgqVYSANEF 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 310 LPLVAMASKPGMCARHSPLpSIHGTVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTNIRAVPEEMELAKEEKCEFLP 389
Cdd:PRK12775 550 LTRVNLMGGDKFPFLDTPI-SLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGIDFFF 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 390 FLSPRKV------VLRGGQIVAMEFvrTEQDDNGNWKE-DEDQVVRLKADVVISAFGSiLSDSKVREAMAPIKFNRWGLP 462
Cdd:PRK12775 629 LHSPVEIyvdaegSVRGMKVEEMEL--GEPDEKGRRKPmPTGEFKDLECDTVIYALGT-KANPIITQSTPGLALNKWGNI 705
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2550010823 463 EVD----PETMQTSEPWVFAGGDVGGLANTTVESVNDGKQASWYMHRYLQ 508
Cdd:PRK12775 706 AADdgklESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYLR 755
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
51-503 |
1.89e-51 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 192.55 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 51 SCEKLENNFDDIkHTTLSERGALREAMRCLKCAD-APCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMV 129
Cdd:PRK12809 183 SASERKTHFGEI-YCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 130 CPTSDLCVGGCNLyATEEGPINIGGLQQFATEVFKAMN-IPQIRNpSLPRVEdmpeayhvKIALLGAGPASLSCASFLAR 208
Cdd:PRK12809 262 CPQDRLCEGACTL-KDHSGAVSIGNLERYITDTALAMGwRPDVSK-VVPRSE--------KVAVIGAGPAGLGCADILAR 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 209 LGYsNITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEAELMKDLGVKIIFSKGLAMDgMTLRTLKEDgYEAVFIGIG---- 284
Cdd:PRK12809 332 AGV-QVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRD-ITFSDLTSE-YDAVFIGVGtygm 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 285 ----LPEPNRDSIFQGLrtdqgfytskdflPLVAMASKPGMCARHS---PLPSIHG-TVIVLGAGDTAFDCATSALRCGA 356
Cdd:PRK12809 409 mradLPHEDAPGVIQAL-------------PFLTAHTRQLMGLPESeeyPLTDVEGkRVVVLGGGDTTMDCLRTSIRLNA 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 357 RRVFVVFRKGFTNIRAVPEEMELAKEEKCEFLPFLSPRKVVL-RGGQIVAMEFVRTEQDDNGNWKEDEDQVV-----RLK 430
Cdd:PRK12809 476 ASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACdEDGRLTAVGLIRTAMGEPGPDGRRRPRPVagsefELP 555
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2550010823 431 ADVVISAFGSILSDSKVREAMApIKFNRWGL---PEVDPETMQTSEPWVFAGGDVGGLANTTVESVNDGKQASWYM 503
Cdd:PRK12809 556 ADVLIMAFGFQAHAMPWLQGSG-IKLDKWGLiqtGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDM 630
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
82-519 |
3.40e-51 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 191.87 E-value: 3.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 82 CAD--APCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCPTSdlCVGGCNLYATEEgPINIGGLQQFA 159
Cdd:PRK12814 97 CGDclGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDE-PVSICALKRYA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 160 TEvfKAMNIPQirnPSLPrveDMPEAYHVKIALLGAGPASLSCASFLARLGYsNITIFEKQEYVGGLSTSEIPQFRLPYD 239
Cdd:PRK12814 174 AD--RDMESAE---RYIP---ERAPKSGKKVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGMMRYGIPRFRLPES 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 240 VVNFEAELMKDLGVKIIFSKGLAMDgMTLRTLKEDgYEAVFIGIGLPEPNRDSIfQGLRTDqGFYTSKDFLPLVAM--AS 317
Cdd:PRK12814 245 VIDADIAPLRAMGAEFRFNTVFGRD-ITLEELQKE-FDAVLLAVGAQKASKMGI-PGEELP-GVISGIDFLRNVALgtAL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 318 KPGmcarhsplpsihGTVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTNIRAVPEEMELAKEEKCEFLPFLSPRKVV 397
Cdd:PRK12814 321 HPG------------KKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 398 LRGGQIV--AMEFVRTEQDDNGNWKED--EDQVVRLKADVVISAFGSILSDSKvrEAMAPIKFNRWGLPEVDPETMQTSE 473
Cdd:PRK12814 389 RSEGGLEltAIKMQQGEPDESGRRRPVpvEGSEFTLQADTVISAIGQQVDPPI--AEAAGIGTSRNGTVKVDPETLQTSV 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2550010823 474 PWVFAGGD-VGGlANTTVESVNDGKQASWYMHRYLQslrGVAVSAVP 519
Cdd:PRK12814 467 AGVFAGGDcVTG-ADIAINAVEQGKRAAHAIDLFLN---GKPVTAPV 509
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
86-507 |
7.97e-51 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 188.93 E-value: 7.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 86 PCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCPTSdlCVGGCNlYATEEGPINIGGLQQFATEVFKA 165
Cdd:PRK12771 48 PCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCN-RGQVDDAVGINAVERFLGDYAIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 166 MNIP-QIRNPSLPRvedmpeayhvKIALLGAGPASLSCASFLARLGYSnITIFEKQEYVGGLSTSEIPQFRLPYDVVNFE 244
Cdd:PRK12771 125 NGWKfPAPAPDTGK----------RVAVIGGGPAGLSAAYHLRRMGHA-VTIFEAGPKLGGMMRYGIPAYRLPREVLDAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 245 AELMKDLGVKIIFSKGLAMDgMTLRTLkEDGYEAVFIGIG------LPEPNRDSifqglrtdQGFYTSKDFLPLVAMASK 318
Cdd:PRK12771 194 IQRILDLGVEVRLGVRVGED-ITLEQL-EGEFDAVFVAIGaqlgkrLPIPGEDA--------AGVLDAVDFLRAVGEGEP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 319 pgmcarhsplPSIHGTVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTNIRAVPEEMELAKEEKCEFLPFLSPRKVVL 398
Cdd:PRK12771 264 ----------PFLGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 399 RGGQIVAM---EFVRTEQDDNGNWKEDEDQVVRLKADVVISAFG-SIlsDSKVREAMAPIKFNRwGLPEVDPETMQTSEP 474
Cdd:PRK12771 334 DENGATGLrviTVEKMELDEDGRPSPVTGEEETLEADLVVLAIGqDI--DSAGLESVPGVEVGR-GVVQVDPNFMMTGRP 410
|
410 420 430
....*....|....*....|....*....|....
gi 2550010823 475 WVFAGGD-VGGLANTTVeSVNDGKQASWYMHRYL 507
Cdd:PRK12771 411 GVFAGGDmVPGPRTVTT-AIGHGKKAARNIDAFL 443
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
68-509 |
1.14e-50 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 189.59 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 68 SERGALREAMRCLKCAdaPCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCptSDLCVGGCNLYATEE 147
Cdd:PRK13984 176 SKEQAMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVC--THKCETVCSIGHRGE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 148 gPINIGGLQQFATEvfkamNIPQIRNPSLprVEDMPEAYHVKIALLGAGPASLSCASFLARLGYsNITIFEKQEYVGGLS 227
Cdd:PRK13984 252 -PIAIRWLKRYIVD-----NVPVEKYSEI--LDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGVM 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 228 TSEIPQFRLPYDVVNFEAELMKDLGVKIIFSKGLAMDgMTLRTLKEdGYEAVFIGIGL--------PEPNRDSIFQGLrt 299
Cdd:PRK13984 323 RYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKD-IPLEELRE-KHDAVFLSTGFtlgrstriPGTDHPDVIQAL-- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 300 dqgfytskdflPLVAMASKpgMCARHSPLPSIHGTVIVLGAGDTAFDCATSALRC-----GARRVFVV-FRKGFTNIRAV 373
Cdd:PRK13984 399 -----------PLLREIRD--YLRGEGPKPKIPRSLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTsLERTFEEMPAD 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 374 PEEMELAKEEKCEFLPFLSPRKVVLRGGQIVAMEFVRTEQ--DDNG--NWKEDEDQVVRLKADVVISAFGSILSDSKVRE 449
Cdd:PRK13984 466 MEEIEEGLEEGVVIYPGWGPMEVVIENDKVKGVKFKKCVEvfDEEGrfNPKFDESDQIIVEADMVVEAIGQAPDYSYLPE 545
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550010823 450 AM-APIKFNRwGLPEVDpETMQTSEPWVFAGGD-VGGlaNTTVESVNDGKQASWYMHRYLQS 509
Cdd:PRK13984 546 ELkSKLEFVR-GRILTN-EYGQTSIPWLFAGGDiVHG--PDIIHGVADGYWAAEGIDMYLRK 603
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
30-507 |
2.01e-48 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 183.79 E-value: 2.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 30 STAAKKQVKKQWKRNSDKSCSSCEKLENNFDDIKHTtLSERGALREAMRCLKCAD-APCQKSCPTNLDIKSFITSIANKN 108
Cdd:PRK12769 179 PAMSKVEQMQATPPRGEPDKLAIEARKTGFDEIYLP-FRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 109 YYGAAKMILSDNPLGLTCGMVCPTSDLCVGGCNLyATEEGPINIGGLQQFATEVFKAMNIpqirNPSLPRVEdmPEAYHV 188
Cdd:PRK12769 258 IDAAVELSHQTNSLPEITGRVCPQDRLCEGACTL-RDEYGAVTIGNIERYISDQALAKGW----RPDLSQVT--KSDKRV 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 189 kiALLGAGPASLSCASFLARLGYSnITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEAELMKDLGVKIIFSKGLAMDgMTL 268
Cdd:PRK12769 331 --AIIGAGPAGLACADVLARNGVA-VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKD-ISL 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 269 RTLKEDgYEAVFIGIGLPE------PNRDSifqglrtdQGFYtskDFLPLVAMASKPGM---CARHSPLPSIHG-TVIVL 338
Cdd:PRK12769 407 ESLLED-YDAVFVGVGTYRsmkaglPNEDA--------PGVY---DALPFLIANTKQVMgleELPEEPFINTAGlNVVVL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 339 GAGDTAFDCATSALRCGARRVFVVFRKGFTNIRAVPEEMELAKEEKCEFLPFLSPRKVVL-RGGQIVAMEFVRT---EQD 414
Cdd:PRK12769 475 GGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELnEQGHVCGIRFLRTrlgEPD 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 415 DNGNWK----EDEDQVvrLKADVVISAFGSILSDSKVREAmAPIKFNRWGLPEVDPET---MQTSEPWVFAGGDVGGLAN 487
Cdd:PRK12769 555 AQGRRRpvpiPGSEFV--MPADAVIMAFGFNPHGMPWLES-HGVTVDKWGRIIADVESqyrYQTSNPKIFAGGDAVRGAD 631
|
490 500
....*....|....*....|
gi 2550010823 488 TTVESVNDGKQASWYMHRYL 507
Cdd:PRK12769 632 LVVTAMAEGRHAAQGIIDWL 651
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
56-168 |
1.06e-45 |
|
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.
Pssm-ID: 434132 [Multi-domain] Cd Length: 113 Bit Score: 159.63 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 56 ENNFDDIkHTTLSERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCPTSDL 135
Cdd:pfam14691 2 IKNFEEV-ALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 2550010823 136 CVGGCNLYATEEGPINIGGLQQFATEVFKAMNI 168
Cdd:pfam14691 81 CEGACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
75-500 |
2.10e-40 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 161.92 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 75 EAMRCLKCADAPCQ------------KSCPTNLDIKSFITSIANKNYYGAAKMILSDNPLGLTCGMVCPTSDLCVGGCnl 142
Cdd:PRK12779 186 EVMRDKQCDDKPCElgvlvqgkaepkGGCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVC-- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 143 yATEEGPINIGGLQQFATEVFKAMNiPQIRNPSLPRVEDMPEAYHVKIALLGAGPASLSCASFLARLGYSnITIFEKQEY 222
Cdd:PRK12779 264 -THTKRPIEIGQLEWYLPQHEKLVN-PNANERFAGRISPWAAAVKPPIAVVGSGPSGLINAYLLAVEGFP-VTVFEAFHD 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 223 VGGLSTSEIPQFRLPYDVVNFEAELMKDLGVKIIfSKGLAMDGMTLRTLKEDGYEAVFIGIGLPEPNrdsiFQGLRTDQ- 301
Cdd:PRK12779 341 LGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFV-KNFVVGKTATLEDLKAAGFWKIFVGTGAGLPT----FMNVPGEHl 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 302 -GFYTSKDFLPLVAMASkpGMCARH-SPLPSIHG-TVIVLGAGDTAFDCATSALRCGARrVFVVFRKGFTNIRAVPEEME 378
Cdd:PRK12779 416 lGVMSANEFLTRVNLMR--GLDDDYeTPLPEVKGkEVFVIGGGNTAMDAARTAKRLGGN-VTIVYRRTKSEMPARVEELH 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 379 LAKEEKCEFLPFLSPRKV-------VLRGGQIVAMEFvrTEQDDNGNWK-EDEDQVVRLKADVVISAFGSIlSDSKVREA 450
Cdd:PRK12779 493 HALEEGINLAVLRAPREFigddhthFVTHALLDVNEL--GEPDKSGRRSpKPTGEIERVPVDLVIMALGNT-ANPIMKDA 569
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2550010823 451 MAPIKFNRWGLPEVDPETMQTSEPWVFAGGDVGGLANTTVESVNDGKQAS 500
Cdd:PRK12779 570 EPGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAA 619
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
534-838 |
2.40e-34 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 133.63 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 534 SVELAGLKFPNPFGLASATPTTSSSMIRRAFEAGWGFAVTKTFSLDKDiVTNVSPRIVRGitsgpmygpgQGSFLN-IEL 612
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQ-PGNPTPRVFRL----------PEGVLNrMGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 613 ISEKTAAYWCKSIAELKADFPnhILLASIMCSY--SREDWTE-LSKMAEVAgaDALELNLSCPHGMGERgmglACGQDPE 689
Cdd:pfam01180 72 NNPGLDAVLAELLKRRKEYPR--PDLGINLSKAgmTVDDYVEvARKIGPFA--DYIELNVSCPNTPGLR----ALQTDPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 690 LVRNICRWVRQAVQIPFFAKLTPNVTDIVNIAMAAQEGGADGVTATN-TVSGLMGLKADSTPWPAVggaLRTTYGGMSGN 768
Cdd:pfam01180 144 LAAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINaTNTTVRGMRIDLKTEKPI---LANGTGGLSGP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550010823 769 AIRPIALRAVSAIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALL 838
Cdd:pfam01180 221 PIKPIALKVIRELYQRTgPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
189-509 |
1.50e-31 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 127.03 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 189 KIALLGAGPASLSCASFLARLGYSnITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEAELMKDLGVKIIF-------SKGL 261
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYLACLGYE-VHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTrtkvccgEPLH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 262 AMDGMTL----RTLKE--DGYEAVFIGIGLPEPNRDSIfQGlRTDQGFYTSKDFLpLVAMASKPGMCARHSPLPSIHGTV 335
Cdd:PRK12770 99 EEEGDEFveriVSLEElvKKYDAVLIATGTWKSRKLGI-PG-EDLPGVYSALEYL-FRIRAAKLGYLPWEKVPPVEGKKV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 336 IVLGAGDTAFDCATSALRCGARRVFVVFRKGFTNIRAVPEEMELAKEEKCEFLPFLSPRKvVLRGGQIVAMEFVRT---E 412
Cdd:PRK12770 176 VVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVR-IIGEGRVEGVELAKMrlgE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 413 QDDNGNWKED--EDQVVRLKADVVISAFGSILSdSKVREAMAPIKFNRWGLPEVDpETMQTSEPWVFAGGDV--G----G 484
Cdd:PRK12770 255 PDESGRPRPVpiPGSEFVLEADTVVFAIGEIPT-PPFAKECLGIELNRKGEIVVD-EKHMTSREGVFAAGDVvtGpskiG 332
|
330 340
....*....|....*....|....*
gi 2550010823 485 LAnttvesVNDGKQASWYMHRYLQS 509
Cdd:PRK12770 333 KA------IKSGLRAAQSIHEWLDL 351
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
946-1004 |
1.76e-30 |
|
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: 114.30 E-value: 1.76e-30
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2550010823 946 ALIDEEMCINCGKCYMTCNDSGYQAIQFDPKTHLPTVTDSCTGCTLCLSVCPVIDCIRM 1004
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDDCITM 59
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
504-819 |
3.92e-24 |
|
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: 104.50 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 504 HRY-LQSLRGVAVSaVPELPLFYTPIDLvdiSVELAGLKFPNPFGLA-----SATpttsssMIRRAFEAGWGFAVTKTfs 577
Cdd:cd04738 13 HRLaIRALKLGLGP-PLLLLLVYDDPRL---EVEVFGLTFPNPVGLAagfdkNAE------AIDALLALGFGFVEVGT-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 578 ldkdiVT------NVSPR----------IVRgitsgpmYGpgqgsFLN--IELISEKTAAYWCK------SIAELKADFP 633
Cdd:cd04738 81 -----VTprpqpgNPKPRlfrlpedealINR-------MG-----FNNdgADAVAKRLKKRRPRggplgvNIGKNKDTPL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 634 NHILlasimcsysrEDWTELskMAEVAG-ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAV-----QIPFF 707
Cdd:cd04738 144 EDAV----------EDYVIG--VRKLGPyADYLVVNVSSPNTPGLRDL-----QGKEALRELLTAVKEERnklgkKVPLL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 708 AKLTPNVTD--IVNIAMAAQEGGADGVTATNTVSGLMGLKadstpwpavGGALRTTYGGMSGNAIRPIALRAVSAIARAL 785
Cdd:cd04738 207 VKIAPDLSDeeLEDIADVALEHGVDGIIATNTTISRPGLL---------RSPLANETGGLSGAPLKERSTEVLRELYKLT 277
|
330 340 350
....*....|....*....|....*....|....*
gi 2550010823 786 PG-FPILATGGIDSAESGLQFLHSGASVLQVCSAI 819
Cdd:cd04738 278 GGkIPIIGVGGISSGEDAYEKIRAGASLVQLYTGL 312
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
503-838 |
3.14e-20 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 93.30 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 503 MHRYLQSLRGVAVSAVPELPLFYTPIDLvdiSVELAGLKFPNPFGLA-----SATpttsssMIRrAFEA-GWGFA----V 572
Cdd:PRK05286 22 TIRALKRASRTPLLSLLRQRLTYTDPRL---PVTVMGLTFPNPVGLAagfdkNGE------AID-ALGAlGFGFVevgtV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 573 TKT----------FSLDKD----------------IVTNV---SPRIVRGItsgpmygpgqgsflNIelisektaaywCK 623
Cdd:PRK05286 92 TPRpqpgnpkprlFRLPEDealinrmgfnndgadaLAERLkkaYRGIPLGI--------------NI-----------GK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 624 S----IAELKADFpnhilLASimcsysredwtelskMAEVAG-ADALELNLSCPHGMGERGMglacgQDPELVRNICRWV 698
Cdd:PRK05286 147 NkdtpLEDAVDDY-----LIC---------------LEKLYPyADYFTVNISSPNTPGLRDL-----QYGEALDELLAAL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 699 RQAVQ-----IPFFAKLTPNVTD--IVNIAMAAQEGGADGVTATNTV---SGLMGLK-ADSTpwpavggalrttyGGMSG 767
Cdd:PRK05286 202 KEAQAelhgyVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIATNTTlsrDGLKGLPnADEA-------------GGLSG 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550010823 768 NAIRPIALRAVSAIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALL 838
Cdd:PRK05286 269 RPLFERSTEVIRRLYKELGGrLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIYEGPGLVKEIVRGLARLL 340
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
532-852 |
4.71e-20 |
|
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: 92.29 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 532 DISVELAGLKFPNPFGLASATPTTSSSMIRRAFEAGWGFAVTKtfSLDKDIVTNVSPRIVRGITSGPMYGPGQGSFLNIE 611
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLP--SLFEEQIEREAQELDRFLTYGSSFAEALSYFPEYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 612 LISEKTAAYwCKSIAELKA--DFPnhiLLASIMCsYSREDWTELSKMAEVAGADALELNLscphgmgergmgLACGQDPE 689
Cdd:cd04739 79 RYNLGPEEY-LELIRRAKRavSIP---VIASLNG-VSAGGWVDYARQIEEAGADALELNI------------YALPTDPD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 690 LVRN--------ICRWVRQAVQIPFFAKLTPNVTDIVNIAMAAQEGGADGVTATN----------TVSGLMGLKAdSTPw 751
Cdd:cd04739 142 ISGAeveqryldILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNrfyqpdidleTLEVVPNLLL-SSP- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 752 pavgGALRTTyggmsgnaIRPIalravsAIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIDDYC 831
Cdd:cd04739 220 ----AEIRLP--------LRWI------AILSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLL 281
|
330 340
....*....|....*....|.
gi 2550010823 832 TGLRALLYLKSIEELEDWNGQ 852
Cdd:cd04739 282 AGLEAWMEEHGYESVQQLRGS 302
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
532-852 |
4.32e-19 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 89.93 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 532 DISVELAGLKFPNPFgLASATP-TTSSSMIRRAFEAGWGFAVTKtfSLDKDIVTNVSPRIVRGITSGP-------MYGPG 603
Cdd:PRK07565 2 DLSTTYLGLTLRNPL-VASASPlSESVDNVKRLEDAGAGAVVLK--SLFEEQIRHEAAELDRHLTHGTesfaealDYFPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 604 QGSF---LN--IELISEktaaywCKSIAelkaDFPnhiLLASIMCsYSREDWTELSKMAEVAGADALELNLSCPHGmger 678
Cdd:PRK07565 79 PAKFyvgPEeyLELIRR------AKEAV----DIP---VIASLNG-SSAGGWVDYARQIEQAGADALELNIYYLPT---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 679 GMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVNIAMAAQEGGADGVTATN-------------TVSGLMgLk 745
Cdd:PRK07565 141 DPDISGAEVEQRYLDILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNrfyqpdidletleVVPGLV-L- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 746 adSTPwpavgGALRTTyggmsgnaIRPIalravsAIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFT 825
Cdd:PRK07565 219 --STP-----AELRLP--------LRWI------AILSGRVGADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPD 277
|
330 340
....*....|....*....|....*..
gi 2550010823 826 VIDDYCTGLRALLYLKSIEELEDWNGQ 852
Cdd:PRK07565 278 YIGTILRGLEDWMERHGYESLQQFRGS 304
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
555-817 |
7.71e-19 |
|
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: 85.72 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 555 TSSSMIRRAFEAGWGFAVTKTFSLDKDIVTNVSPRIvrgitsgpmygpgqgsflnielisektaaywcksiAELKADFPN 634
Cdd:cd04722 13 DPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEV-----------------------------------LKEVAAETD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 635 HILLASIMCSYSREDWTELSKMAEVAGADALELNLSCPHGmgergmglacgqdPELVRNICRWVRQAV-QIPFFAKLTPN 713
Cdd:cd04722 58 LPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL-------------AREDLELIRELREAVpDVKVVVKLSPT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 714 VTDivnIAMAAQEGGADGVTATNtvsglmglkadstpwpavggalrTTYGGMSGNAIRPIALRAvsAIARALPGFPILAT 793
Cdd:cd04722 125 GEL---AAAAAEEAGVDEVGLGN-----------------------GGGGGGGRDAVPIADLLL--ILAKRGSKVPVIAG 176
|
250 260
....*....|....*....|....
gi 2550010823 794 GGIDSAESGLQFLHSGASVLQVCS 817
Cdd:cd04722 177 GGINDPEDAAEALALGADGVIVGS 200
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
661-838 |
8.63e-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: 81.99 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 661 GADALELNLSCPH--GMGERGMglacgqDPELVRNICRWVRQAVQIPFFAKLTPnVTDIVNIAMAAQ--EGGADG---VT 733
Cdd:cd04741 119 FPLAMELNLSCPNvpGKPPPAY------DFDATLEYLTAVKAAYSIPVGVKTPP-YTDPAQFDTLAEalNAFACPisfIT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 734 ATNTV-SGLMgLKADSTPwPAVGGAlrTTYGGMSGNAIRPIALRAVSAIARALPG-FPILATGGIDSAESGLQFLHSGAS 811
Cdd:cd04741 192 ATNTLgNGLV-LDPERET-VVLKPK--TGFGGLAGAYLHPLALGNVRTFRRLLPSeIQIIGVGGVLDGRGAFRMRLAGAS 267
|
170 180
....*....|....*....|....*..
gi 2550010823 812 VLQVCSAIQNQDFTVIDDYCTGLRALL 838
Cdd:cd04741 268 AVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
504-818 |
8.72e-17 |
|
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273408 Cd Length: 335 Bit Score: 82.91 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 504 HRY-LQSLRGVavSAVPELPLFYTPIDLVD-ISVELAGLKFPNPFGLAsATPTTSSSMIRRAFEAGWGFAVTKTFSlDKD 581
Cdd:TIGR01036 17 HELtFQFLRLG--TGTPFLALLRSLFGASDpLEVTVLGLKFPNPLGLA-AGFDKDGEAIDALGAMGFGFLEIGTVT-PKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 582 IVTNVSPRIVRGITSGpmygpgqgSFLNIELISEKTAAYWCKSIAELKADFPNHILLAS---IMCSYSREDWTELSKMAe 658
Cdd:TIGR01036 93 QPGNPRPRLFRLIEDE--------ALINRMGFNNHGADVLVERLKRARYKGPIGINIGKnkdTPSEDAKEDYAACLRKL- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 659 VAGADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAVQI-------PFFAKLTPNVT--DIVNIAMAAQEGGA 729
Cdd:TIGR01036 164 GPLADYLVVNVSSPNTPGLRDL-----QYKAELRDLLTAVKQEQDGlrrvhrvPVLVKIAPDLTesDLEDIADSLVELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 730 DGVTATNTV---SGLMGLKADSTPwpavggalrttyGGMSGnaiRPIALRAVSAIAR---ALPG-FPILATGGIDSAESG 802
Cdd:TIGR01036 239 DGVIATNTTvsrSLVQGPKNSDET------------GGLSG---KPLQDKSTEIIRRlyaELQGrLPIIGVGGISSAQDA 303
|
330
....*....|....*.
gi 2550010823 803 LQFLHSGASVLQVCSA 818
Cdd:TIGR01036 304 LEKIRAGASLLQIYSG 319
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
532-852 |
1.39e-13 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 72.68 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 532 DISVELAGLKFPNPFGLAS-ATPTTSSSMIR-RAFEAGwGFaVTKTFSLDKDiVTNVSPRIVR----GITSgpMYGPGQG 605
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAgVYCMTKEELEEvEASAAG-AF-VTKSATLEPR-PGNPEPRYADtplgSINS--MGLPNLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 606 sflnielisektAAYWCKSIAELKADFPNHILLASIMCSYSREDWTELSKMAEVAGADALELNLSCPHGMGERGMGLacg 685
Cdd:PRK02506 76 ------------FDYYLDYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAY--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 686 qDPELVRNICRWVRQAVQIPFFAKLTPNVtDIVNIAMAA---QEGGADGVTATNTV-SGLMGLKADSTPW--PAVGgalr 759
Cdd:PRK02506 141 -DFETTEQILEEVFTYFTKPLGVKLPPYF-DIVHFDQAAaifNKFPLAFVNCINSIgNGLVIDPEDETVVikPKNG---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 760 ttYGGMSGNAIRPIALRAVSAIARAL-PGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALL 838
Cdd:PRK02506 215 --FGGIGGDYIKPTALANVRAFYQRLnPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIM 292
|
330
....*....|....
gi 2550010823 839 YLKSIEELEDWNGQ 852
Cdd:PRK02506 293 AEKGYQSLEDFRGK 306
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
948-1008 |
6.29e-13 |
|
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: 65.07 E-value: 6.29e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550010823 948 IDEEMCINCGKCYMTCNDsgyQAIQFDPKTHLPTVTDSCTGCTLCLSVCPViDCIRMVSRT 1008
Cdd:COG1144 27 VDEDKCIGCGLCWIVCPD---GAIRVDDGKYYGIDYDYCKGCGICAEVCPV-KAIEMVPEE 83
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
189-483 |
1.01e-12 |
|
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: 70.04 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 189 KIALLGAGPASLSCASFLARLGYSnITIFEKQE---YVGGLSTSEIPQFRLPYDVVNFEAELMKDL-------------- 251
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGK-VTLIEDEGtcpYGGCVLSKALLGAAEAPEIASLWADLYKRKeevvkklnngievl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 252 ----GVKIIFSKGLamdgMTLRTLKEDG-----YEAVFIGIG-------LPEPNRDSIFqGLRTdqgfYTSKDFLplvam 315
Cdd:pfam07992 81 lgteVVSIDPGAKK----VVLEELVDGDgetitYDRLVIATGarprlppIPGVELNVGF-LVRT----LDSAEAL----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 316 askpgmcaRHSPLPsihGTVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTniRAVPEEMELAKEEKceflpfLSPRK 395
Cdd:pfam07992 147 --------RLKLLP---KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLL--RAFDEEISAALEKA------LEKNG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 396 VVLRGGQIVamefVRTEQDDNGNWKEDEDqVVRLKADVVISAFGSILSDSKVREAmaPIKFNRWGLPEVDpETMQTSEPW 475
Cdd:pfam07992 208 VEVRLGTSV----KEIIGDGDGVEVILKD-GTEIDADLVVVAIGRRPNTELLEAA--GLELDERGGIVVD-EYLRTSVPG 279
|
....*...
gi 2550010823 476 VFAGGDVG 483
Cdd:pfam07992 280 IYAAGDCR 287
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
945-1009 |
8.17e-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: 61.28 E-value: 8.17e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550010823 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPKTHLPTVTDSCTGCTLCLSVCPViDCIRMVSRTT 1009
Cdd:COG1149 5 IPVIDEEKCIGCGLCVEVCP---EGAIKLDDGGAPVVDPDLCTGCGACVGVCPT-GAITLEEREA 65
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
945-1005 |
4.99e-11 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 62.12 E-value: 4.99e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550010823 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPKTHLPTVTDSCTGCTLCLSVCPViDCIRMV 1005
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACP---VDAIVGAAKAMHTVIADECTGCDLCVEPCPT-DCIEMI 163
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
886-1007 |
1.79e-10 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 62.43 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 886 RKKIIAENKVKLKEQSMAAVLPEKKHFIPKKPIPAIKDVIGKALQYIGTYGELCNTEQVVALIDEEMCINCGKCYMTCnd 965
Cdd:COG1145 117 AVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVC-- 194
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2550010823 966 sGYQAIQFDPKTHLPTV-TDSCTGCTLCLSVCPViDCIRMVSR 1007
Cdd:COG1145 195 -PTGAIRLKDGKPQIVVdPDKCIGCGACVKVCPV-GAISLEPK 235
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
945-1005 |
3.14e-10 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 60.73 E-value: 3.14e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550010823 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPKtHLPTV-TDSCTGCTLCLSVCPViDCIRMV 1005
Cdd:PRK05113 108 VAFIDEDNCIGCTKCIQACP---VDAIVGATK-AMHTViSDLCTGCDLCVAPCPT-DCIEMI 164
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
945-1011 |
4.28e-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: 61.55 E-value: 4.28e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550010823 945 VALI-----DEEMCINCGKCYMTCNdsgYQAIQFDPKtHLPTV-TDSCTGCTLCLSVCPViDCIRMVSRTTPY 1011
Cdd:COG2878 126 AAVIggpkgCEYGCIGCGDCIKACP---FDAIVGAAK-GMHTVdEDKCTGCGLCVEACPV-DCIEMVPVSPTV 193
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
945-1008 |
5.74e-10 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 61.35 E-value: 5.74e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550010823 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPKTHLPTVTDSCTGCTLCLSVCPViDCIRMVSRT 1008
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACP---VDAIVGAPKQMHTVLADLCTGCDLCVPPCPV-DCIDMVPVT 138
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
476-818 |
8.50e-10 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 62.06 E-value: 8.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 476 VFAGGDVGGLANTTVESVNDGKQASWYMH--RYL--QSLRGVAVSA-----VPELPLFYTPIdlvdISVELAGLKFPNPF 546
Cdd:PLN02826 12 AIAGGAYVSTVDEATFCGWLFNATKLVNPlfRLLdpETAHSLAISAaarglVPREKRPDPSV----LGVEVWGRTFSNPI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 547 GLAsATPTTSSSMIRRAFEAGWGFAVTKTfsldkdiVT------NVSPRIVRGITSGPMYGPGQGSFLNIELISEKTAAY 620
Cdd:PLN02826 88 GLA-AGFDKNAEAVEGLLGLGFGFVEIGS-------VTplpqpgNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 621 WCKS-IAELKADFPNH------------ILLASIMCSYSREDwtelskMAE--VAG-------ADALELNLSCPHGMGER 678
Cdd:PLN02826 160 HGKRkLDETSSSSFSSddvkaggkagpgILGVNLGKNKTSED------AAAdyVQGvralsqyADYLVINVSSPNTPGLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 679 GMglacgQDPELVRNICRWVR---------QAVQIPFFAKLTPNVT--DIVNIAMAAQEGGADGVTATNTVSglmglkad 747
Cdd:PLN02826 234 KL-----QGRKQLKDLLKKVLaardemqwgEEGPPPLLVKIAPDLSkeDLEDIAAVALALGIDGLIISNTTI-------- 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550010823 748 STPWPAVGGALRTTYGGMSGNAIRPIALRAVSAIARALPG-FPILATGGIDSAESGLQFLHSGASVLQVCSA 818
Cdd:PLN02826 301 SRPDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGkIPLVGCGGVSSGEDAYKKIRAGASLVQLYTA 372
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
948-1007 |
1.62e-08 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 52.02 E-value: 1.62e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550010823 948 IDEEMCINCGKCYMTCndsGYQAIQFDPKTHLPTVT--DSCTGCTLCLSVCPViDCIRMVSR 1007
Cdd:COG1146 5 IDTDKCIGCGACVEVC---PVDVLELDEEGKKALVInpEECIGCGACELVCPV-GAITVEDD 62
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
193-238 |
1.86e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 51.76 E-value: 1.86e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2550010823 193 LGAGPASLSCASFLARLGYSnITIFEKQEYVGGLSTS-EIPQFRLPY 238
Cdd:pfam13450 2 VGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSyRVPGYVFDY 47
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
648-810 |
1.17e-07 |
|
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: 54.64 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 648 EDWTELSKMAEVAGADALELNLSCPHGMGERGMGLAC-GQDPELVRNICRWVRQAVQIPFFAKLT----PNVTDIVNIAM 722
Cdd:pfam01207 66 ALLAEAAKLVEDRGADGIDINMGCPSKKVTRGGGGAAlLRNPDLVAQIVKAVVKAVGIPVTVKIRigwdDSHENAVEIAK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 723 AAQEGGADGVtatnTVSGlmglkadstpwpavggalRTTYGGMSGnairPIALRAVSAIARALPgFPILATGGIDSAESG 802
Cdd:pfam01207 146 IVEDAGAQAL----TVHG------------------RTRAQNYEG----TADWDAIKQVKQAVS-IPVIANGDITDPEDA 198
|
....*....
gi 2550010823 803 LQFL-HSGA 810
Cdd:pfam01207 199 QRCLaYTGA 207
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
948-1007 |
1.67e-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: 1.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550010823 948 IDEEMCINCGKCYMTCN----DSGYQAIQFDPkthlptvtDSCTGCTLCLSVCPViDCIRMVSR 1007
Cdd:COG4231 19 IDEDKCTGCGACVKVCPadaiEEGDGKAVIDP--------DLCIGCGSCVQVCPV-DAIKLEKR 73
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
931-1005 |
2.12e-07 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 50.86 E-value: 2.12e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550010823 931 YIGTYGELCNTEQVVALIDEEMCINCGKCYMTCNdsgYQAIQFDPKthLPTVTDS--CTGCTLCLSVCPViDCIRMV 1005
Cdd:cd10549 58 ELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCP---VDAITLEDE--LEIVIDKekCIGCGICAEVCPV-NAIKLV 128
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
950-1004 |
2.19e-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: 2.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550010823 950 EEMCINCGKCYMTCNdsgYQAIQFDPKTHLPTVT---DSCTGCTLCLSVCPViDCIRM 1004
Cdd:COG1143 1 EDKCIGCGLCVRVCP---VDAITIEDGEPGKVYVidpDKCIGCGLCVEVCPT-GAISM 54
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
655-810 |
3.16e-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: 52.50 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 655 KMAEVAGADALELNLSCP-----HGmgerGMGLACGQDPELVRNICRWVRQAVQIPFFAK---LTPNVTDIVNIAMAAQE 726
Cdd:cd02801 74 KIVEELGADGIDLNMGCPspkvtKG----GAGAALLKDPELVAEIVRAVREAVPIPVTVKirlGWDDEEETLELAKALED 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 727 GGADGVtatnTVSGlmglkadstpwpavggalRTTYGGMSGNAIrpiaLRAVSAIARAlPGFPILATGGIDSAESGLQFL 806
Cdd:cd02801 150 AGASAL----TVHG------------------RTREQRYSGPAD----WDYIAEIKEA-VSIPVIANGDIFSLEDALRCL 202
|
....*
gi 2550010823 807 -HSGA 810
Cdd:cd02801 203 eQTGV 207
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
189-511 |
4.60e-07 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 52.81 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 189 KIALLGAGPASLSCASFLARLGYSnITIFEKQEyVGG--LSTSEIpqfrlpYDVVNFE-----AELMKDL-------GVK 254
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLK-TLVIEGGE-PGGqlATTKEI------ENYPGFPegisgPELAERLreqaerfGAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 255 IIFSKGLAMD----GMTLRTLKEDGYEA--VFIGIG-----LPEPN-RDSIFQGLR---TDQG-FYTSKDflplvamask 318
Cdd:COG0492 74 ILLEEVTSVDkddgPFRVTTDDGTEYEAkaVIIATGagprkLGLPGeEEFEGRGVSycaTCDGfFFRGKD---------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 319 pgmcarhsplpsihgtVIVLGAGDTAFDcatSALRCG--ARRVFVVFRKGftNIRAVPEEMELAKEekceflpflSPRKV 396
Cdd:COG0492 144 ----------------VVVVGGGDSALE---EALYLTkfASKVTLIHRRD--ELRASKILVERLRA---------NPKIE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 397 VLRGGQIVAM------EFVRTEQDDNGnwkededQVVRLKADVVISAFGSILSDSKVREAMapIKFNRWGLPEVDpETMQ 470
Cdd:COG0492 194 VLWNTEVTEIegdgrvEGVTLKNVKTG-------EEKELEVDGVFVAIGLKPNTELLKGLG--LELDEDGYIVVD-EDME 263
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2550010823 471 TSEPWVFAGGDV-GGLANTTVESVNDGKQASWYMHRYLQSLR 511
Cdd:COG0492 264 TSVPGVFAAGDVrDYKYRQAATAAGEGAIAALSAARYLEPLK 305
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
953-998 |
5.73e-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: 47.14 E-value: 5.73e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2550010823 953 CINCGKCYMTCNdsgYQAIQFDPKTHLPTVT------DSCTGCTLCLSVCPV 998
Cdd:pfam12838 1 CIGCGACVAACP---VGAITLDEVGEKKGTKtvvidpERCVGCGACVAVCPT 49
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
944-1010 |
1.16e-06 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 47.03 E-value: 1.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550010823 944 VVALIDEEMCINCGKCYMTCNdsgYQAIQFDPKTHLpTVTDSCTGCTLCLSVCPViDCIRMVSRTTP 1010
Cdd:COG2768 4 GKPYVDEEKCIGCGACVKVCP---VGAISIEDGKAV-IDPEKCIGCGACIEVCPV-GAIKIEWEEDE 65
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
945-1005 |
1.36e-06 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 48.76 E-value: 1.36e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550010823 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPKtHLPTV-TDSCTGCTLCLSVCPViDCIRMV 1005
Cdd:PRK08764 79 VAWIVEADCIGCTKCIQACP---VDAIVGGAK-HMHTViAPLCTGCELCVPACPV-DCIELH 135
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
926-1004 |
1.60e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 52.17 E-value: 1.60e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550010823 926 GKALQYIGTyGELcNTEQVVALIDEEMCINCGKCYMTCNdsgYQAIQFDPKTHLPTVTDSCTGCTLCLSVCPViDCIRM 1004
Cdd:COG1148 473 ARAIQLLSK-GEL-GVEPSVAEVDPEKCTGCGRCVEVCP---YGAISIDEKGVAEVNPALCKGCGTCAAACPS-GAISL 545
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
948-997 |
1.77e-06 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 46.09 E-value: 1.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2550010823 948 IDEEMCINCGKCYMTC--NDSGYQAIQFDPKT-HLPTVTDSCTGCTLCLSVCP 997
Cdd:pfam13237 4 IDPDKCIGCGRCTAACpaGLTRVGAIVERLEGeAVRIGVWKCIGCGACVEACP 56
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
945-998 |
1.92e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 48.79 E-value: 1.92e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550010823 945 VALIDEEMCIN------CGKCYMTCNDSGYqAIQFDPKTHLPTV-TDSCTGCTLCLSVCPV 998
Cdd:cd16373 85 VAVIDKDRCLAwqggtdCGVCVEACPTEAI-AIVLEDDVLRPVVdEDKCVGCGLCEYVCPV 144
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
945-1005 |
2.64e-06 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 47.77 E-value: 2.64e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPKTHLPtvtDSCTGC---------TLCLSVCPViDCIRMV 1005
Cdd:cd04410 74 IVLIDEDKCIGCGSCVEACP---YGAIVFDPEPGKA---VKCDLCgdrldeglePACVKACPT-GALTFG 136
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
948-998 |
4.46e-06 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 45.04 E-value: 4.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2550010823 948 IDEEMCINCGKCYMTCNDsgyQAIQFDPKThLPTVTDSCTGCTLCLSVCPV 998
Cdd:COG2221 12 IDEEKCIGCGLCVAVCPT---GAISLDDGK-LVIDEEKCIGCGACIRVCPT 58
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
194-252 |
4.47e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 50.62 E-value: 4.47e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550010823 194 GAGPASLSCASFLARLGYSnITIFEKQEYVGG-LSTSEIPQFRL---PYDVVNFEA--ELMKDLG 252
Cdd:COG1233 10 GAGIGGLAAAALLARAGYR-VTVLEKNDTPGGrARTFERPGFRFdvgPSVLTMPGVleRLFRELG 73
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
187-230 |
5.21e-06 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 50.22 E-value: 5.21e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2550010823 187 HVKIALLGAGPASLSCASFLARLGYSnITIFEKQEYVGGLSTSE 230
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHE-VTVLEASDRVGGLIRTV 43
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
652-810 |
5.74e-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: 49.32 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 652 ELSKMAEVAGADALELNLSCP------HGMGergmglAC-GQDPELVRNICRWVRQAVQIPFFAK----LTPNVTDIVNI 720
Cdd:COG0042 78 EAARIAEELGADEIDINMGCPvkkvtkGGAG------AAlLRDPELVAEIVKAVVEAVDVPVTVKirlgWDDDDENALEF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 721 AMAAQEGGADGV-----TATNTVSGlmglKADstpWPAVGgalrttyggmsgnairpiALRAVSAIaralpgfPILATGG 795
Cdd:COG0042 152 ARIAEDAGAAALtvhgrTREQRYKG----PAD---WDAIA------------------RVKEAVSI-------PVIGNGD 199
|
170
....*....|....*.
gi 2550010823 796 IDSAESGLQFL-HSGA 810
Cdd:COG0042 200 IFSPEDAKRMLeETGC 215
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
948-1016 |
1.18e-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: 45.85 E-value: 1.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550010823 948 IDEEMCINCGKCYMTCNdsgYQAIQFDPKTHLPTVT----DSCTGCTLCLSVCPViDCIRMVSRTTPYEPKRG 1016
Cdd:cd10549 3 YDPEKCIGCGICVKACP---TDAIELGPNGAIARGPeideDKCVFCGACVEVCPT-GAIELTPEGKEYVPKEK 71
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
187-484 |
1.36e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 49.02 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 187 HVKIALLGAGPASLSCASFLARLGYsNITIFEKQEYvGG-------------LSTSEI-------PQFRLPYDV--VNFE 244
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGK-KVALIEKGPL-GGtclnvgcipskalIAAAEAfheakhaEEFGIHADGpkIDFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 245 A------------------ELMKDLGVKIIFSKGLAMDGMTLRtLKEDGYEA--VFIGIGLPEPNRDSIFQGLRTDqgFY 304
Cdd:PRK06292 81 KvmarvrrerdrfvggvveGLEKKPKIDKIKGTARFVDPNTVE-VNGERIEAknIVIATGSRVPPIPGVWLILGDR--LL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 305 TSKDFLPLvamaskpgmcarhSPLPSihgTVIVLGAG----DTAFdcATSALrcGARrVFVVFRKGftniRAVP-EEMEL 379
Cdd:PRK06292 158 TSDDAFEL-------------DKLPK---SLAVIGGGviglELGQ--ALSRL--GVK-VTVFERGD----RILPlEDPEV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 380 AKEekceFLPFLSPRKVVLRGGQIVAMEfvrTEQDDNGNWKEDEDQVVRLKADVVISAFGsilsdskvREAMAP------ 453
Cdd:PRK06292 213 SKQ----AQKILSKEFKIKLGAKVTSVE---KSGDEKVEELEKGGKTETIEADYVLVATG--------RRPNTDglglen 277
|
330 340 350
....*....|....*....|....*....|...
gi 2550010823 454 --IKFNRWGLPEVDPeTMQTSEPWVFAGGDVGG 484
Cdd:PRK06292 278 tgIELDERGRPVVDE-HTQTSVPGIYAAGDVNG 309
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
187-227 |
2.87e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 47.96 E-value: 2.87e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2550010823 187 HVKIALLGAGPASLSCASFLARLGYSnITIFEKQEYVGGLS 227
Cdd:PRK07208 4 KKSVVIIGAGPAGLTAAYELLKRGYP-VTVLEADPVVGGIS 43
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
917-1007 |
5.27e-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: 44.16 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 917 PIPAIKDVIGKALQYIGTYGELCNTEQVValideeMCincgkcyMTCNDS-GYQAIQFDPKTH---LPTV-TDSCTGCTL 991
Cdd:cd10564 58 PEGALDPAREAPWPLRAEIGDSCLALQGV------EC-------RSCQDAcPTQAIRFRPRLGgiaLPELdADACTGCGA 124
|
90
....*....|....*.
gi 2550010823 992 CLSVCPViDCIRMVSR 1007
Cdd:cd10564 125 CVSVCPV-GAITLTPL 139
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
189-229 |
7.85e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 46.42 E-value: 7.85e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2550010823 189 KIALLGAGPASLSCASFLARLGYSnITIFEKQEYVGGLSTS 229
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAAS 40
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
948-1011 |
8.50e-05 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 43.15 E-value: 8.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550010823 948 IDEEMCINCGKCYMTCndsGYQAIQFDPKTHLPTVT--------DSCTGCTLCLSVCPViDCIRMVSRTTPY 1011
Cdd:cd10549 37 IDEDKCVFCGACVEVC---PTGAIELTPEGKEYVPKekeaeideEKCIGCGLCVKVCPV-DAITLEDELEIV 104
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
952-1002 |
3.29e-04 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 39.46 E-value: 3.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2550010823 952 MCINCGKCYMTCNDSGYQAIQFDPKTHLPTVTDSCTGCTLCLSVCPViDCI 1002
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQTIRGDIAGLACIGCGACVDACPR-GAI 50
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
948-998 |
3.60e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 44.25 E-value: 3.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2550010823 948 IDEEMCINCGKCYMTCndsGYQAIQFDpKTHLPTVTDSCTGCTLCLSVCPV 998
Cdd:COG4624 88 RDKEKCKNCYPCVRAC---PVKAIKVD-DGKAEIDEEKCISCGQCVAVCPF 134
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
177-302 |
3.78e-04 |
|
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: 43.85 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 177 PRVEDMPEayhvKIALLGAGPASLSCASFLARLGySNITIFEkqeyvgglsTSEIPQFRLPYDVVNFEAELMKDLGVKII 256
Cdd:pfam07992 146 LRLKLLPK----RVVVVGGGYIGVELAAALAKLG-KEVTLIE---------ALDRLLRAFDEEISAALEKALEKNGVEVR 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2550010823 257 FS---KGLAMDGMTLRTLKEDG----YEAVFIGIGLpEPNRDSIFQ-GLRTDQG 302
Cdd:pfam07992 212 LGtsvKEIIGDGDGVEVILKDGteidADLVVVAIGR-RPNTELLEAaGLELDER 264
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
945-998 |
3.97e-04 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 43.14 E-value: 3.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2550010823 945 VALIDEEMCINCGKCYMTCNdsgYQAIQFDPKtHLPTVTDSCTGCTLCLSVCPV 998
Cdd:cd03110 58 KAFIDQEKCIRCGNCERVCK---FGAILEFFQ-KLIVDESLCEGCGACVIICPR 107
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
951-997 |
6.76e-04 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 40.89 E-value: 6.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2550010823 951 EMCINCGKCYMTCNDSgyqAIQFDPKTHLPTVTDSCTGCTLCLSVCP 997
Cdd:PRK09625 59 EICINCFNCWVYCPDA---AILSRDKKLKGVDYSHCKGCGVCVEVCP 102
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
949-1008 |
1.02e-03 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 39.63 E-value: 1.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 949 DEEMCINCGKCYMTCNDSgyqAIQFDPKTHLPTVTDSCTGCTLCLSVCPViDCIRMVSRT 1008
Cdd:PRK09624 49 NRDKCVRCYLCYIYCPEP---AIYLDEEGYPVFDYDYCKGCGICANECPT-KAIEMVRET 104
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
981-1005 |
1.23e-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: 41.77 E-value: 1.23e-03
10 20
....*....|....*....|....*
gi 2550010823 981 TVTDSCTGCTLCLSVCPViDCIRMV 1005
Cdd:NF038196 182 HVTDKCIGCGICAKVCPV-NNIEME 205
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
947-997 |
2.25e-03 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 40.31 E-value: 2.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 947 LIDEEMCINCGKCYMTCNdsgYQAIQFDPKTHlptVTDSCTGC---------TLCLSVCP 997
Cdd:COG0437 86 LVDYDKCIGCRYCVAACP---YGAPRFNPETG---VVEKCTFCadrldegllPACVEACP 139
|
|
| napG |
PRK09476 |
quinol dehydrogenase periplasmic component; Provisional |
947-996 |
2.45e-03 |
|
quinol dehydrogenase periplasmic component; Provisional
Pssm-ID: 236534 [Multi-domain] Cd Length: 254 Bit Score: 40.76 E-value: 2.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550010823 947 LIDEEMCIN-----CGKCYMTCN--DsgyQAI----QFDPKTH-----LPTV-TDSCTGCTLCLSVC 996
Cdd:PRK09476 133 LVDQENCLNfqglrCDVCYRVCPliD---KAItlelERNERTGkhaffLPTVhSDACTGCGKCEKAC 196
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
983-1013 |
2.66e-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: 2.66e-03
10 20 30
....*....|....*....|....*....|.
gi 2550010823 983 TDSCTGCTLCLSVCPViDCIRMVSRTTPYEP 1013
Cdd:COG1143 1 EDKCIGCGLCVRVCPV-DAITIEDGEPGKVY 30
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
428-482 |
2.93e-03 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 40.95 E-value: 2.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2550010823 428 RLKADVVISAFGsILSDSKVREAmAPIKFNRWGLPEVDpETMQTSEPWVFAGGDV 482
Cdd:COG0446 206 EIPADLVVVAPG-VRPNTELAKD-AGLALGERGWIKVD-ETLQTSDPDVYAAGDC 257
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
945-998 |
3.71e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 38.47 E-value: 3.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550010823 945 VALIDEEMCINCGKCYMTCNDSGYQ-------AIQFDPKTHLPTVTdSCTGCTLCLSVCPV 998
Cdd:cd16372 2 LLVTDPEKCIGCLQCEEACSKTFFKeedreksCIRITETEGGYAIN-VCNQCGECIDVCPT 61
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
953-997 |
3.88e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 36.67 E-value: 3.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550010823 953 CINCGKCYMTCnDSgYQAIQFDPKT-------------HLPTVTDSCTGCTLCLSVCP 997
Cdd:pfam13534 2 CIQCGCCVDEC-PR-YLLNGDEPKKlmraaylgdleelQANKVANLCSECGLCEYACP 57
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
982-1015 |
4.26e-03 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 36.61 E-value: 4.26e-03
10 20 30
....*....|....*....|....*....|....
gi 2550010823 982 VTDSCTGCTLCLSVCPViDCIRMVSRTTPYEPKR 1015
Cdd:COG1146 6 DTDKCIGCGACVEVCPV-DVLELDEEGKKALVIN 38
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
951-1020 |
4.40e-03 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 40.83 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 951 EMCINCGKCYMTC---------NDS-------------GYQAIQFDPKTHLptVTDSCTGCTLCLSVCPV-IDCIRMVSR 1007
Cdd:COG0247 78 DACVGCGFCRAMCpsykatgdeKDSprgrinllrevleGELPLDLSEEVYE--VLDLCLTCKACETACPSgVDIADLIAE 155
|
90
....*....|....
gi 2550010823 1008 TTP-YEPKRGLPLA 1020
Cdd:COG0247 156 ARAqLVERGGRPLR 169
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
948-1007 |
4.62e-03 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 40.05 E-value: 4.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550010823 948 IDEEMCINCGKCYMTCndsgyqAIQFDPKTHLPTVTDsCTGCTLCLSVCPViDCIRMVSR 1007
Cdd:COG0348 207 YDRGDCIDCGLCVKVC------PMGIDIRKGEINQSE-CINCGRCIDACPK-DAIRFSSR 258
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
180-256 |
4.81e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 40.55 E-value: 4.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550010823 180 EDMPEayhvKIALLGAGPASLSCASFLARLGySNITIFEKQEYVGGLSTSEIPQFRLPYdvvnFEAELMKDLGVKII 256
Cdd:PRK06292 166 DKLPK----SLAVIGGGVIGLELGQALSRLG-VKVTVFERGDRILPLEDPEVSKQAQKI----LSKEFKIKLGAKVT 233
|
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
945-1005 |
5.59e-03 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 37.62 E-value: 5.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550010823 945 VALIDEEMCINCGKCYMTCNDSgyqAIQFDPKTHLPTVTDSCTGCTLCLSVCPViDCIRMV 1005
Cdd:PRK09623 45 MPVVDESKCVKCYICWKFCPEP---AIYIKEDGYVAIDYDYCKGCGICANECPT-KAITMV 101
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
189-262 |
5.76e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 36.80 E-value: 5.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550010823 189 KIALLGAGPASLSCASFLARLGySNITIFEKQEYVGGLstseipqfrLPYDVVNFEAELMKDLGVKIIFSKGLA 262
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLG-SKVTVVERRDRLLPG---------FDPEIAKILQEKLEKNGIEFLLNTTVE 64
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
187-239 |
7.09e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 39.90 E-value: 7.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2550010823 187 HVKIALLGAGPASLSCASFLARLGYSnITIFEKQEYVGG-LSTSEIPQFRLPYD 239
Cdd:COG1231 7 GKDVVIVGAGLAGLAAARELRKAGLD-VTVLEARDRVGGrVWTLRFGDDGLYAE 59
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
952-1005 |
7.54e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 40.24 E-value: 7.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2550010823 952 MCINCGKCYMTCNDsgyQAIQ-FDPKTHLPTVTDSCTGCTLCLSVCPViDCIRMV 1005
Cdd:PRK12771 511 NCFECDNCYGACPQ---DAIIkLGPGRRYHFDYDKCTGCHICADVCPC-GAIEMG 561
|
|
| |
