|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
2-470 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 661.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 2 LRFIDTPRQTPEKRAAELRREDFEEVYSGFKERQAEAQASRCSQCGVPFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSE 81
Cdd:PRK11749 1 LKFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 82 STSNMPEICGRICPQDRLCEGSCVIEQSGHgTVTIGAVEQYITDNAWSKGWIKPIaPARERPQSIGIIGAGPAGLSAADE 161
Cdd:PRK11749 81 ETNPLPAVCGRVCPQERLCEGACVRGKKGE-PVAIGRLERYITDWAMETGWVLFK-RAPKTGKKVAVIGAGPAGLTAAHR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 162 LRSLGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKA 241
Cdd:PRK11749 159 LARKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 242 RELSVPGVGANGVVRALDYLTASNRKGFGDEVPgfdeghmnaHGKRVVVVGGGDTAMDCVRTAIRQDAASVTCLYRRDRE 321
Cdd:PRK11749 239 RFLGIPGENLGGVYSAVDFLTRVNQAVADYDLP---------VGKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGRE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 322 NMPGSAREVVNAEEEGISFRWLSNPKLLLGDANKLDGIRVARMRLGPPDASGRQSpEEIPGEDADLAADMVIKALGFSPE 401
Cdd:PRK11749 310 EMPASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMELGEPDASGRRR-VPIEGSEFTLPADLVIKAIGQTPN 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503066337 402 dLPTAFDEPDLALTRYGTLKVDPSSYETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQYFKGQTV 470
Cdd:PRK11749 389 -PLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAAS 456
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
20-464 |
0e+00 |
|
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: 598.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 20 RREDFEEVYSGFKERQAEAQASRCSQCGVPFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSESTSNMPEICGRICPqdRL 99
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--AP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 100 CEGSCVIEQsGHGTVTIGAVEQYITDNAWSKGWIKPIAPARERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAG 179
Cdd:COG0493 79 CEGACVRGI-VDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 180 GLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKARELSVPGVGANGVVRALD 259
Cdd:COG0493 158 GLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 260 YLTASNRKGFGDEVPgfdeghmnAHGKRvvvvgggDTAMDCVRTAIRQDAASVTCLYRRDRENMPGSAREVVNAEEEGIS 339
Cdd:COG0493 238 FLTAVNLGEAPDTIL--------AVGKRvvvigggNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 340 FRWLSNPKLLLGDAN-KLDGIRVARMRLGPPDASGRQSPEEIPGEDADLAADMVIKALGFSPeDLPTAFDEPDLALTRYG 418
Cdd:COG0493 310 FLFLVAPVEIIGDENgRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTP-DPSGLEEELGLELDKRG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 503066337 419 TLKVDPSSYETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQY 464
Cdd:COG0493 389 TIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
4-470 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 576.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 4 FIDTPRQTPEKRAAELRREDFEEVYSGFKERQAEAQASRCSQCGVPFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSEST 83
Cdd:PRK12810 7 FLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 84 SNMPEICGRICPQDrlCEGSCVIEQsGHGTVTIGAVEQYITDNAWSKGWIKPIAPARERPQSIGIIGAGPAGLSAADELR 163
Cdd:PRK12810 87 NNFPEFTGRVCPAP--CEGACTLNI-NFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGSGPAGLAAADQLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 164 SLGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKARE 243
Cdd:PRK12810 164 RAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAYKPRD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 244 LSVPGVGANGVVRALDYLTASNRKGFGDEVPGFdeghMNAHGKRVVVVGGGDTAMDCVRTAIRQDAASVTclyRRDRENM 323
Cdd:PRK12810 244 LGIPGRDLDGVHFAMDFLIQNTRRVLGDETEPF----ISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVT---QRDIMPM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 324 PGSAR-------------EVVNAEEEGISFRWLSNPKLLLGDANKLDGIRVARMRLGPPDasgrqsPEEIPGEDADLAAD 390
Cdd:PRK12810 317 PPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGD------FEPVEGSEFVLPAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 391 MVIKALGFSPEDlPTAFDEPDLALTRYGTLKVDPSSYETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQYFKGQTV 470
Cdd:PRK12810 391 LVLLAMGFTGPE-AGLLAQFGVELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMGSTA 469
|
|
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
4-465 |
1.74e-164 |
|
glutamate synthase small subunit family protein, proteobacterial; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit and homologs. TIGR01317 describes the small subunit (or equivalent region from longer forms) in eukaryotes, Gram-positive bacteria, and some other lineages, both NADH and NADPH-dependent. TIGR01316 describes a protein of similar length, from Archaea and a number of bacterial lineages, that forms glutamate synthase homotetramers without a large subunit. This model describes both glutatate synthase small subunit and closely related paralogs of unknown function from a number of gamma and alpha subdivision Proteobacteria, including E. coli.
Pssm-ID: 273553 [Multi-domain] Cd Length: 467 Bit Score: 473.52 E-value: 1.74e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 4 FIDTPRQTPEKRAAELRREDFEEVYSGFKERQAEAQASRCSQCGVPFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSEST 83
Cdd:TIGR01318 3 FIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSHQT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 84 SNMPEICGRICPQDRLCEGSCVIEQSgHGTVTIGAVEQYITDNAWSKGWIKPIAPARERPQSIGIIGAGPAGLSAADELR 163
Cdd:TIGR01318 83 NTLPEICGRVCPQDRLCEGACTLNDE-GGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 164 SLGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKARE 243
Cdd:TIGR01318 162 RAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRSMR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 244 LSVPGVGANGVVRALDYLTASNRKGFG-DEVPgfDEGHMNAHGKRVVVVGGGDTAMDCVRTAIRQDAASVTCLYRRDREN 322
Cdd:TIGR01318 242 GGLPGEDAPGVLPALPFLIANTRQLMGlPEEP--EEPLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEAN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 323 MPGSAREVVNAEEEGISFRWLSNPKLLLGDAN-KLDGIRVARMRLGPPDASGRQSPEEIPGEDADLAADMVIKALGFSPE 401
Cdd:TIGR01318 320 MPGSRREVANAREEGVEFLFNVQPVSIESDEDgQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPH 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503066337 402 DLPTaFDEPDLALTRYGTLKVDPSS---YETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQYF 465
Cdd:TIGR01318 400 LMPW-LAAHGITLDSWGRIITALSSgltYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWL 465
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
8-466 |
5.65e-145 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 430.32 E-value: 5.65e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 8 PRQTPEKRAAELRREDFEEVYSGFKERQAEAQASRCSQCGV-PFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSESTSNM 86
Cdd:PRK12769 192 PRGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 87 PEICGRICPQDRLCEGSCVIeQSGHGTVTIGAVEQYITDNAWSKGWIKPIAPARERPQSIGIIGAGPAGLSAADELRSLG 166
Cdd:PRK12769 272 PEITGRVCPQDRLCEGACTL-RDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNG 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 167 YRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKARELSV 246
Cdd:PRK12769 351 VAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 247 PGVGANGVVRALDYLTASNRKGFG-DEVPgfDEGHMNAHGKRVVVVGGGDTAMDCVRTAIRQDAASVTCLYRRDRENMPG 325
Cdd:PRK12769 431 PNEDAPGVYDALPFLIANTKQVMGlEELP--EEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 326 SAREVVNAEEEGISFRWLSNP-KLLLGDANKLDGIRVARMRLGPPDASGRQSPEEIPGEDADLAADMVIKALGFSPEDLP 404
Cdd:PRK12769 509 SKKEVKNAREEGANFEFNVQPvALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGFNPHGMP 588
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503066337 405 TaFDEPDLALTRYGTLKVDPSS---YETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQYFK 466
Cdd:PRK12769 589 W-LESHGVTVDKWGRIIADVESqyrYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLG 652
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
8-466 |
2.64e-128 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 387.07 E-value: 2.64e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 8 PRQTPEKRAAELRREDFEEVYSGFKERQAEAQASRCSQCG-VPFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSESTSNM 86
Cdd:PRK12809 175 SRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAeKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 87 PEICGRICPQDRLCEGSCVIEQSGhGTVTIGAVEQYITDNAWSKGWIKPIAPARERPQSIGIIGAGPAGLSAADELRSLG 166
Cdd:PRK12809 255 PEICGRVCPQDRLCEGACTLKDHS-GAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILARAG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 167 YRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKARELSV 246
Cdd:PRK12809 334 VQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 247 PGVGANGVVRALDYLTASNRKGFGdeVPGFDEGHMNA-HGKRVVVVGGGDTAMDCVRTAIRQDAASVTCLYRRDRENMPG 325
Cdd:PRK12809 414 PHEDAPGVIQALPFLTAHTRQLMG--LPESEEYPLTDvEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPG 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 326 SAREVVNAEEEGISFRWLSNPKLLLGDAN-KLDGIRVARMRLGPPDASGRQSPEEIPGEDADLAADMVIKALGFSPEDLP 404
Cdd:PRK12809 492 SRKEVVNAREEGVEFQFNVQPQYIACDEDgRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMP 571
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503066337 405 TaFDEPDLALTRYGTLKVDPSSY---ETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQYFK 466
Cdd:PRK12809 572 W-LQGSGIKLDKWGLIQTGDVGYlptQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFD 635
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
1-469 |
3.25e-128 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 380.90 E-value: 3.25e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 1 MLRFIDTPrqTPEkRAAELRREDFEEVYSGFKERQAEAQASRCSQCGVPFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLS 80
Cdd:PRK12831 3 KDRKKRVP--VRE-QDPEVRATNFEEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 81 ESTSNMPEICGRICPQDRLCEGSCVIEQSGHgTVTIGAVEQYITDNAWSKGwIKPIAPARERPQSIGIIGAGPAGLSAAD 160
Cdd:PRK12831 80 AKYNALPAVCGRVCPQESQCEGKCVLGIKGE-PVAIGKLERFVADWARENG-IDLSETEEKKGKKVAVIGSGPAGLTCAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 161 ELRSLGYRITVYDRYDRAGGLMTYGIPGFKLEKS-VVMRRVKRLADSGVTFVQNADIGGGVPFSDLRE--KHDAILIATG 237
Cdd:PRK12831 158 DLAKMGYDVTIFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEeeGFDAVFIGSG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 238 VYKARELSVPGVGANGVVRALDYLTASN-RKGFGDEvpgFDEGHMNahGKRVVVVGGGDTAMDCVRTAIRQdAASVTCLY 316
Cdd:PRK12831 238 AGLPKFMGIPGENLNGVFSANEFLTRVNlMKAYKPE---YDTPIKV--GKKVAVVGGGNVAMDAARTALRL-GAEVHIVY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 317 RRDRENMPGSAREVVNAEEEGISFRWLSNPKLLLGDAN-KLDGIRVARMRLGPPDASGRQSPEEIPGEDADLAADMVIKA 395
Cdd:PRK12831 312 RRSEEELPARVEEVHHAKEEGVIFDLLTNPVEILGDENgWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMS 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503066337 396 LGFSPEDLPTAfDEPDLALTRYGTLKVDPSSYETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQYFKGQT 469
Cdd:PRK12831 392 LGTSPNPLISS-TTKGLKINKRGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSKKW 464
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
4-470 |
5.97e-122 |
|
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate.
Pssm-ID: 162300 [Multi-domain] Cd Length: 485 Bit Score: 365.69 E-value: 5.97e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 4 FIDTPRQTPEKRAAELRREDFEEVYSGFKERQAEAQASRCSQCGVPFC--SSGCPLGNHIPDWLRLAAEDQLEEAWRLSE 81
Cdd:TIGR01317 5 FLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFChnDSGCPLNNLIPEFNDLVFRGRWKEALDRLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 82 STSNMPEICGRICPQDrlCEGSCVIEQSgHGTVTIGAVEQYITDNAWSKGWIKPIAPARERPQSIGIIGAGPAGLSAADE 161
Cdd:TIGR01317 85 ATNNFPEFTGRVCPAP--CEGACTLGIS-EDPVGIKSIERIIIDKGFQEGWVQPRPPSKRTGKKVAVVGSGPAGLAAADQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 162 LRSLGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKA 241
Cdd:TIGR01317 162 LNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATKP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 242 RELSVPGVGANGVVRALDYLTASNRKGFGDEVPgfDEGHMNAHGKRVVVVGGGDTAMDCVRTAIRQDAASVTCL------ 315
Cdd:TIGR01317 242 RDLPIPGRELKGIHYAMEFLPSATKALLGKDFK--DIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHQFeimpkp 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 316 -YRRDRENM----PGSAREVVNAEEEGISF-----RWLSNPKLLLGDAN-KLDGIRVARMRLgPPDASGRQSPEEIPGED 384
Cdd:TIGR01317 320 pEARAKDNPwpewPRVYRVDYAHEEAAAHYgrdprEYSILTKEFIGDDEgKVTALRTVRVEW-KKSQDGKWQFVEIPGSE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 385 ADLAADMVIKALGFSPEDLPTaFDEPDLALTRYGTLKVDPSSYETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQY 464
Cdd:TIGR01317 399 EVFEADLVLLAMGFVGPEQIL-LDDFGVKKTRRGNISAGYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVDRY 477
|
....*.
gi 503066337 465 FKGQTV 470
Cdd:TIGR01317 478 LMGSSV 483
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
5-468 |
5.04e-117 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 361.37 E-value: 5.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 5 IDTPR-QTPEKRAAELRREDFEEVYSGFKERQAEAQASRCSQCGVPFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSEST 83
Cdd:PRK12778 292 TAIERvPMPELDPEYRAHNRFEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKET 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 84 SNMPEICGRICPQDRLCEGSCVIEQSGHGTVTIGAVEQYITDNAWSKGWIKPIAPARERPQSIGIIGAGPAGLSAADELR 163
Cdd:PRK12778 372 SALPAVCGRVCPQEKQCESKCIHGKMGEEAVAIGYLERFVADYERESGNISVPEVAEKNGKKVAVIGSGPAGLSFAGDLA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 164 SLGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLR-EKHDAILIATGVYKAR 242
Cdd:PRK12778 452 KRGYDVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEeEGFKGIFIASGAGLPN 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 243 ELSVPGVGANGVVRALDYLTASNRkgfgdevpgfdeghMNAH----------GKRVVVVGGGDTAMDCVRTAIRQDAASV 312
Cdd:PRK12778 532 FMNIPGENSNGVMSSNEYLTRVNL--------------MDAAspdsdtpikfGKKVAVVGGGNTAMDSARTAKRLGAERV 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 313 TCLYRRDRENMPGSAREVVNAEEEGISFRWLSNPKLLLGDAN-KLDGIRVARMRLGPPDASGRQSPEEIPGEDADLAADM 391
Cdd:PRK12778 598 TIVYRRSEEEMPARLEEVKHAKEEGIEFLTLHNPIEYLADEKgWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDL 677
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503066337 392 VIKALGFSPEDL-PTAFdePDLALTRYGTLKVDPSSyETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQYFKGQ 468
Cdd:PRK12778 678 VIVSVGVSPNPLvPSSI--PGLELNRKGTIVVDEEM-QSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
18-464 |
1.96e-102 |
|
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130383 [Multi-domain] Cd Length: 449 Bit Score: 314.12 E-value: 1.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 18 ELRREDFEEVYSGFKERQAEAQASRCSQCGVPF--CSSGCPLGNHIPDWLRLAAEDQLEEAWRLSESTSNMPEICGRICP 95
Cdd:TIGR01316 3 EERSKLFQEAALGYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVCP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 96 QDRLCEGSCVIEQSGHGT---VTIGAVEQYITDNAWSKGWIKPIAPARERPQSIGIIGAGPAGLSAADELRSLGYRITVY 172
Cdd:TIGR01316 83 QERQCEGQCTVGKMFKDVgkpVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVTVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 173 DRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKARELSVPGVGAN 252
Cdd:TIGR01316 163 EALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEELC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 253 GVVRALDYLTASN-RKGFgdEVPGFDEGhmNAHGKRVVVVGGGDTAMDCVRTAIRQdAASVTCLYRRDRENMPGSAREVV 331
Cdd:TIGR01316 243 GVYSANDFLTRANlMKAY--EFPHADTP--VYAGKSVVVIGGGNTAVDSARTALRL-GAEVHCLYRRTREDMTARVEEIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 332 NAEEEGISFRWLSNPKLLLGDAN-KLDGIRVARMRLGPPDASGRQSPEEIPGEDADLAADMVIKALGFSPEdlPTAFDEP 410
Cdd:TIGR01316 318 HAEEEGVKFHFLCQPVEIIGDEEgNVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSN--PIMAETT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 503066337 411 DLALTRYGTLKVDpSSYETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQY 464
Cdd:TIGR01316 396 RLKTSERGTIVVD-EDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEY 448
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
49-494 |
3.58e-101 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 314.51 E-value: 3.58e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 49 PFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSESTSNMPEICGRICPQDrlCEGSC---VIEQSghgtVTIGAVEQYITD 125
Cdd:PRK12771 47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCnrgQVDDA----VGINAVERFLGD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 126 NAWSKGWiKPIAPARERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLAD 205
Cdd:PRK12771 121 YAIANGW-KFPAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 206 SGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKARELSVPGVGANGVVRALDYLTAsnrkgfgdevpgFDEGHMNAHG 285
Cdd:PRK12771 200 LGVEVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRA------------VGEGEPPFLG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 286 KRVVVVGGGDTAMDCVRTAIRQDAASVTCLYRRDRENMPGSAREVVNAEEEGISFRWLSNPKLLLGDANKLDGIRVARMR 365
Cdd:PRK12771 268 KRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVITVE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 366 LGPPDASGRQSPEEipGEDADLAADMVIKALGfspEDLPTAF--DEPDLALTRyGTLKVDPSSYETSLPGVFAAGDIVRG 443
Cdd:PRK12771 348 KMELDEDGRPSPVT--GEEETLEADLVVLAIG---QDIDSAGleSVPGVEVGR-GVVQVDPNFMMTGRPGVFAGGDMVPG 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 503066337 444 ASLVVWAIHDARRAAASIHQYFKGQtvgaipetvgeqqtDYDPRTYEPVAP 494
Cdd:PRK12771 422 PRTVTTAIGHGKKAARNIDAFLGGE--------------PYEHRPKREIVK 458
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
8-494 |
9.14e-92 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 300.32 E-value: 9.14e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 8 PRQT--PEKRAAElRREDFEEVYSGFKERQAEAQASRCSQCGVPFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSESTSN 85
Cdd:PRK12775 297 PHQTpmPERDAVE-RARNFKEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASI 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 86 MPEICGRICPQDRLCEGSCVIEQSgHGTVTIGAVEQYITDNAWSkgwiKPIAPAR--ERPQSIGIIGAGPAGLSAADELR 163
Cdd:PRK12775 376 FPSICGRVCPQETQCEAQCIIAKK-HESVGIGRLERFVGDNARA----KPVKPPRfsKKLGKVAICGSGPAGLAAAADLV 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 164 SLGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREK--HDAILIATGVYKA 241
Cdd:PRK12775 451 KYGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGAGAP 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 242 RELSVPGVGANGVVRALDYLTASNRKGfGDEVPGFDEGhmNAHGKRVVVVGGGDTAMDCVRTAIRQDAASVTCLYRRDRE 321
Cdd:PRK12775 531 TFLGIPGEFAGQVYSANEFLTRVNLMG-GDKFPFLDTP--ISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEA 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 322 NMPGSAREVVNAEEEGISFRWLSNPKLLLGDAN-KLDGIRVARMRLGPPDASGRQSPEEIpGEDADLAADMVIKALGFSP 400
Cdd:PRK12775 608 EAPARIEEIRHAKEEGIDFFFLHSPVEIYVDAEgSVRGMKVEEMELGEPDEKGRRKPMPT-GEFKDLECDTVIYALGTKA 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 401 EDLPTAfDEPDLALTRYGTLKVD----PSSYETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQYFKgqTVGAIPET 476
Cdd:PRK12775 687 NPIITQ-STPGLALNKWGNIAADdgklESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYLR--LGKKWPIT 763
|
490
....*....|....*...
gi 503066337 477 VgEQQTDYDPRTYEPVAP 494
Cdd:PRK12775 764 A-EEAAAFQPGKLLPAIE 780
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
13-493 |
1.52e-87 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 281.62 E-value: 1.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 13 EKRAAEL---RREDFEEVYsgfkerqaeaqASRCSQCGVPfCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSESTSNMPEI 89
Cdd:PRK12814 75 ETENAELhamRRQSLERLI-----------EQHCGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 90 CGRICPQDrlCEGSCvieqSGHGT---VTIGAVEQYITD--NAWSKGWIKPIAPARERpqSIGIIGAGPAGLSAADELRS 164
Cdd:PRK12814 143 LGRICPAP--CEEAC----RRHGVdepVSICALKRYAADrdMESAERYIPERAPKSGK--KVAIIGAGPAGLTAAYYLLR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 165 LGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKAREL 244
Cdd:PRK12814 215 KGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 245 SVPGVGANGVVRALDYLTASNrkgfgdevpgfdEGHMNAHGKRVVVVGGGDTAMDCVRTAIRQDAASVTCLYRRDRENMP 324
Cdd:PRK12814 295 GIPGEELPGVISGIDFLRNVA------------LGTALHPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 325 GSAREVVNAEEEGISFRWLSNPKLLLGDANKLDgIRVARMRLGPPDASGRQSPEEIPGEDADLAADMVIKALGfSPEDLP 404
Cdd:PRK12814 363 ANRAEIEEALAEGVSLRELAAPVSIERSEGGLE-LTAIKMQQGEPDESGRRRPVPVEGSEFTLQADTVISAIG-QQVDPP 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 405 TAfDEPDLALTRYGTLKVDPSSYETSLPGVFAAGDIVRGASLVVWAIHDARRAAASIHQYFKGQTVGAIPETVgeqQTDY 484
Cdd:PRK12814 441 IA-EAAGIGTSRNGTVKVDPETLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGKPVTAPVQPF---NSSY 516
|
....*....
gi 503066337 485 DPRTYEPVA 493
Cdd:PRK12814 517 GPRDKAPEA 525
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
138-468 |
3.14e-79 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 251.06 E-value: 3.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 138 PARERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIG 217
Cdd:PRK12770 13 KPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTKVC 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 218 GGVP---------------FSDLREKHDAILIATGVYKARELSVPGVGANGVVRALDYL--TASNRKGFGDEVPGFDegh 280
Cdd:PRK12770 93 CGEPlheeegdefverivsLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLfrIRAAKLGYLPWEKVPP--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 281 mnAHGKRVVVVGGGDTAMDCVRTAIRQDAASVTCLYRRDRENMPGSAREVVNAEEEGISFRWLSNPKLLLGDaNKLDGIR 360
Cdd:PRK12770 170 --VEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIGE-GRVEGVE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 361 VARMRLGPPDASGRQSPEEIPGEDADLAADMVIKALGFSPEDlPTAFDEPDLALTRYGTLKVDpSSYETSLPGVFAAGDI 440
Cdd:PRK12770 247 LAKMRLGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTP-PFAKECLGIELNRKGEIVVD-EKHMTSREGVFAAGDV 324
|
330 340
....*....|....*....|....*...
gi 503066337 441 VRGASLVVWAIHDARRAAASIHQYFKGQ 468
Cdd:PRK12770 325 VTGPSKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
3-468 |
9.53e-70 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 233.51 E-value: 9.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 3 RFIDTPRQTPEKRAAELRREDFEEVYSGFKERQAEAQASRCSQCGVpfCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSES 82
Cdd:PRK13984 147 ELLDLERVEMEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECGI--CTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 83 TSNMPEICGRICPQDrlCEGSCVIEQSGHgTVTIGAVEQYITDNAWSKGWIKPIA-PARERPQSIGIIGAGPAGLSAADE 161
Cdd:PRK13984 225 TNPLSMVCGRVCTHK--CETVCSIGHRGE-PIAIRWLKRYIVDNVPVEKYSEILDdEPEKKNKKVAIVGSGPAGLSAAYF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 162 LRSLGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGVPFSDLREKHDAILIATGVYKA 241
Cdd:PRK13984 302 LATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 242 RELSVPGVGANGVVRALDYLtasnrKGFGDEVPGfdEGHMNAHGKRVVVVGGGDTAMDCVRTAIRQDAAS-------VTC 314
Cdd:PRK13984 382 RSTRIPGTDHPDVIQALPLL-----REIRDYLRG--EGPKPKIPRSLVVIGGGNVAMDIARSMARLQKMEygevnvkVTS 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 315 LyRRDRENMPGSAREVVNAEEEGISFRWLSNPKLLLGDANKLDGIRVARMrLGPPDASGRQSPEEIPGEDADLAADMVIK 394
Cdd:PRK13984 455 L-ERTFEEMPADMEEIEEGLEEGVVIYPGWGPMEVVIENDKVKGVKFKKC-VEVFDEEGRFNPKFDESDQIIVEADMVVE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 395 ALG------FSPEDLPTA--FDEPDLALTRYGtlkvdpssyETSLPGVFAAGDIVRGASlVVWAIHDARRAAASIHQYFK 466
Cdd:PRK13984 533 AIGqapdysYLPEELKSKleFVRGRILTNEYG---------QTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYLR 602
|
..
gi 503066337 467 GQ 468
Cdd:PRK13984 603 KQ 604
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
12-482 |
9.55e-69 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 236.65 E-value: 9.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 12 PEKRAAELRREDFEEVYSGF--------KERQAEA----QASRCSQC-------GVPF-----CSSGCPLGNHIPDWLRL 67
Cdd:PRK12779 147 PYIRPAEERAVDFDLVNQGYlgyqslgySVREVELfvwlEVMRDKQCddkpcelGVLVqgkaePKGGCPVKIHIPEMLDL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 68 AAEDQLEEAWRLSESTSNMPEICGRICPQDRLCEGSCVIEQSghgTVTIGAVEQYITD---------NAWSKGWIKPIAP 138
Cdd:PRK12779 227 LGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTKR---PIEIGQLEWYLPQheklvnpnaNERFAGRISPWAA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 139 ARERPqsIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADIGG 218
Cdd:PRK12779 304 AVKPP--IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFVKNFVVGK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 219 GVPFSDL-REKHDAILIATGVYKARELSVPGVGANGVVRALDYLTASN-RKGFGDEvpgFDEGHMNAHGKRVVVVGGGDT 296
Cdd:PRK12779 382 TATLEDLkAAGFWKIFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRVNlMRGLDDD---YETPLPEVKGKEVFVIGGGNT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 297 AMDCVRTAIRQdAASVTCLYRRDRENMPGSAREVVNAEEEGISFRWLSNPKLLLGDA--NKLDGIRVARMRLGPPDASGR 374
Cdd:PRK12779 459 AMDAARTAKRL-GGNVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGDDhtHFVTHALLDVNELGEPDKSGR 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 375 QSPEEIpGEDADLAADMVIKALGFSPEdlPTAFD-EPDLALTRYGTLKVDPSSYETSLPGVFAAGDIVRGASLVVWAIHD 453
Cdd:PRK12779 538 RSPKPT-GEIERVPVDLVIMALGNTAN--PIMKDaEPGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGD 614
|
490 500
....*....|....*....|....*....
gi 503066337 454 ARRAAASIhqyfkgqtVGAIPETVGEQQT 482
Cdd:PRK12779 615 GQAAAKEI--------VGEIPFTPAEIKD 635
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
20-132 |
6.47e-57 |
|
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: 184.66 E-value: 6.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 20 RREDFEEVYSGFKERQAEAQASRCSQCGVPFCSSGCPLGNHIPDWLRLAAEDQLEEAWRLSESTSNMPEICGRICPQDRL 99
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 503066337 100 CEGSCVIEQSGHGTVTIGAVEQYITDNAWSKGW 132
Cdd:pfam14691 81 CEGACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
148-468 |
3.67e-27 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 110.98 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDRyDRAGG-LMTY-----------GIPGFKLeksvvMRRVKRLADS-GVTF---- 210
Cdd:COG0492 5 IIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGqLATTkeienypgfpeGISGPEL-----AERLREQAERfGAEIllee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 211 VQNADIGGGvPF---SDLREKH--DAILIATGVYkARELSVP--------GVGANGVVRALDYltaSNRK----GFGDEv 273
Cdd:COG0492 79 VTSVDKDDG-PFrvtTDDGTEYeaKAVIIATGAG-PRKLGLPgeeefegrGVSYCATCDGFFF---RGKDvvvvGGGDS- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 274 pGFDEghmnahgkrvvvvgggdtAMDCVRTairqdAASVTCLYRRDRenmPGSAREVVN--AEEEGISFRWLSNPKLLLG 351
Cdd:COG0492 153 -ALEE------------------ALYLTKF-----ASKVTLIHRRDE---LRASKILVErlRANPKIEVLWNTEVTEIEG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 352 DaNKLDGIRVARMRlgppdasgrqspeeiPGEDADLAADMVIKALGFSPE-DLptaFDEPDLALTRYGTLKVDpSSYETS 430
Cdd:COG0492 206 D-GRVEGVTLKNVK---------------TGEEKELEVDGVFVAIGLKPNtEL---LKGLGLELDEDGYIVVD-EDMETS 265
|
330 340 350
....*....|....*....|....*....|....*....
gi 503066337 431 LPGVFAAGDIVRGAS-LVVWAIHDARRAAASIHQYFKGQ 468
Cdd:COG0492 266 VPGVFAAGDVRDYKYrQAATAAGEGAIAALSAARYLEPL 304
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
148-454 |
1.57e-15 |
|
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: 76.97 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDR-----YDraGGLMTYGIPGFK------LEKSVVMRRVKRLADS---GVTFVQN 213
Cdd:pfam07992 5 VIGGGPAGLAAALTLAQLGGKVTLIEDegtcpYG--GCVLSKALLGAAeapeiaSLWADLYKRKEEVVKKlnnGIEVLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 214 A-----DIGGG-------VPFSDLREKHDAILIATGVyKARELSVPGVgANGVVRALDYLTaSNRKGFGDEVP------- 274
Cdd:pfam07992 83 TevvsiDPGAKkvvleelVDGDGETITYDRLVIATGA-RPRLPPIPGV-ELNVGFLVRTLD-SAEALRLKLLPkrvvvvg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 275 -GFdeghmnahgkrvvvvgggdTAMDCVRTAIRQdAASVTCLYRRDR--ENMPGSAREVVNA--EEEGISFRWLSNPKLL 349
Cdd:pfam07992 160 gGY-------------------IGVELAAALAKL-GKEVTLIEALDRllRAFDEEISAALEKalEKNGVEVRLGTSVKEI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 350 LGDANKLDGIrvarmrlgppDASGRQspeeipgedadLAADMVIKALGFSPEDLptAFDEPDLALTRYGTLKVDPsSYET 429
Cdd:pfam07992 220 IGDGDGVEVI----------LKDGTE-----------IDADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDE-YLRT 275
|
330 340
....*....|....*....|....*.
gi 503066337 430 SLPGVFAAGDI-VRGASLVVWAIHDA 454
Cdd:pfam07992 276 SVPGIYAAGDCrVGGPELAQNAVAQG 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
148-464 |
3.86e-15 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 76.13 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLMTYGI----PGF------------------KLEKSVVMRRVKRLAD 205
Cdd:TIGR01292 4 IIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEvenyPGFpegisgpelmekmkeqavKFGAEIIYEEVIKVDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 206 SGVTFVQNADIGGGVpfsdlreKHDAILIATGVyKARELSVPGvgangvvraldyltASNRKGFGDEVPGFDEGHMnAHG 285
Cdd:TIGR01292 84 SDRPFKVYTGDGKEY-------TAKAVIIATGA-SARKLGIPG--------------EDEFWGRGVSYCATCDGPF-FKN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 286 KRVVVVGGGDTAMDcvrTAI--RQDAASVTCLYRRDRENMPGSAREVVnAEEEGISFRWLSNPKLLLGDaNKLDGIRVAr 363
Cdd:TIGR01292 141 KEVAVVGGGDSAIE---EALylTRIAKKVTLVHRRDKFRAEKILLDRL-KKNPKIEFLWNSTVEEIVGD-NKVEGVKIK- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 364 mrlgppdasgrqspEEIPGEDADLAADMVIKALGFSPedlPTAFDEPDLALTRYGTLKVDpSSYETSLPGVFAAGDiVRG 443
Cdd:TIGR01292 215 --------------NTVTGEEEELEVDGVFIAIGHEP---NTELLKGLLELDENGYIVTD-EGMRTSVPGVFAAGD-VRD 275
|
330 340
....*....|....*....|...
gi 503066337 444 ASL--VVWAIHDARRAAASIHQY 464
Cdd:TIGR01292 276 KGYrqAVTAAGDGCIAALSAERY 298
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
139-257 |
7.64e-10 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 60.87 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 139 ARERPQSIGIIGAGPAGLSAADEL--RSLGYRITVYDRYDRAGGLMTYGI-PGFKLEKSVVMRRVKRLADSGVTFVQNAD 215
Cdd:PLN02852 22 STSEPLHVCVVGSGPAGFYTADKLlkAHDGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVT 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 503066337 216 IGGGVPFSDLREKHDAILIATGVYKARELSVPGVGANGVVRA 257
Cdd:PLN02852 102 LGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSA 143
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
148-461 |
1.05e-09 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 60.49 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDR------------------------YDRAGGLMTYGI----PGFKLEKsvVMRR 199
Cdd:COG1249 8 VIGAGPGGYVAAIRAAQLGLKVALVEKgrlggtclnvgcipskallhaaevAHEARHAAEFGIsagaPSVDWAA--LMAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 200 V------------KRLADSGVTFVQnadiGGGVpFSDlreKH------------DAILIATGvYKARELSVPGVGAngvV 255
Cdd:COG1249 86 KdkvvdrlrggveELLKKNGVDVIR----GRAR-FVD---PHtvevtggetltaDHIVIATG-SRPRVPPIPGLDE---V 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 256 RALDYLTASNRkgfgDEVP-----------GFDEGHM-NAHGkrvvvvgggdtamdcvrtairqdaASVTCLYRRDREnM 323
Cdd:COG1249 154 RVLTSDEALEL----EELPkslvvigggyiGLEFAQIfARLG------------------------SEVTLVERGDRL-L 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 324 PGSAREVVNA-----EEEGIsfrwlsnpKLLLG-DANKL----DGIRVarmrlgppDASGRQSPEEIPgedadlaADMVI 393
Cdd:COG1249 205 PGEDPEISEAlekalEKEGI--------DILTGaKVTSVektgDGVTV--------TLEDGGGEEAVE-------ADKVL 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 394 KALGFSP--EDLptAFDEPDLALTRYGTLKVDpSSYETSLPGVFAAGDIVRGASLVVWAIHDARRAAASI 461
Cdd:COG1249 262 VATGRRPntDGL--GLEAAGVELDERGGIKVD-EYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENI 328
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
146-193 |
4.24e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 58.36 E-value: 4.24e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 503066337 146 IGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLM-TYGIPGFKLEK 193
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIER 50
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
148-192 |
6.36e-09 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 52.15 E-value: 6.36e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLM-TYGIPGFKLE 192
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAySYRVPGYVFD 46
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
143-192 |
1.34e-08 |
|
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: 56.76 E-value: 1.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503066337 143 PQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLM-TYGIPGFKLE 192
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIrTVEVDGFRID 51
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
143-461 |
1.66e-08 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 56.69 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 143 PQSIGIIGAGPAGLSAADELRSLG--YRITVYDR-----YDRAggLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNAD 215
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDpdGEITVIGAephppYNRP--PLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 216 I--------------GGGVPFsdlrekhDAILIATGVYkARELSVPGVGANGV--------VRAL-DYLTASNR-----K 267
Cdd:COG1251 79 VtaidraartvtladGETLPY-------DKLVLATGSR-PRVPPIPGADLPGVftlrtlddADALrAALAPGKRvvvigG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 268 GF-GDEVpgfdeghmnAHgkrvvvvgggdtamdcvrtAIRQDAASVTCLYRRDR--ENM--PGSAREVVNA-EEEGISFR 341
Cdd:COG1251 151 GLiGLEA---------AA-------------------ALRKRGLEVTVVERAPRllPRQldEEAGALLQRLlEALGVEVR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 342 WLSNPKLLLGDAnkldgiRVARMRLgppdASGRQspeeipgedadLAADMVIKALGFSPEdlpTAF-DEPDLALTRyGtL 420
Cdd:COG1251 203 LGTGVTEIEGDD------RVTGVRL----ADGEE-----------LPADLVVVAIGVRPN---TELaRAAGLAVDR-G-I 256
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 503066337 421 KVDPSSyETSLPGVFAAGDIVR-------GASLVVW--AIHDARRAAASI 461
Cdd:COG1251 257 VVDDYL-RTSDPDIYAAGDCAEhpgpvygRRVLELVapAYEQARVAAANL 305
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
140-180 |
4.02e-08 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 55.31 E-value: 4.02e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503066337 140 RERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGG 180
Cdd:COG1231 4 RARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
141-255 |
3.44e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 52.44 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 141 ERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAgglmtygipgFKLEKSVVMRRVKR-LADSGVTFVQNADI--- 216
Cdd:PRK07251 155 TLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTI----------LPREEPSVAALAKQyMEEDGITFLLNAHTtev 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503066337 217 ---GGGV--PFSDLREKHDAILIATG------------------------VYKARELSVPGVGANGVV 255
Cdd:PRK07251 225 kndGDQVlvVTEDETYRFDALLYATGrkpnteplglentdieltergaikVDDYCQTSVPGVFAVGDV 292
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
143-181 |
3.60e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 52.58 E-value: 3.60e-07
10 20 30
....*....|....*....|....*....|....*....
gi 503066337 143 PQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGL 181
Cdd:PRK07208 4 KKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
142-182 |
7.75e-07 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 51.03 E-value: 7.75e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503066337 142 RPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLM 182
Cdd:COG3380 2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRM 42
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
144-474 |
1.94e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 50.24 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 144 QSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLM---TYGIPGFKLEKSVV---MRRVKrlADSGVTFVQNA--- 214
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAaqlHKTFPGLDCPQCILeplIAEVE--ANPNITVYTGAeve 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 215 DIGGGV----------PFSDLREKHDAILIATG--VYKARELSVPGVGAN-GVVRALDY--LTASN---RKGFGDEVP-- 274
Cdd:COG1148 219 EVSGYVgnftvtikkgPREEIEIEVGAIVLATGfkPYDPTKLGEYGYGKYpNVITNLELerLLAAGkilRPSDGKEPKsv 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 275 GF-------DEGHMNAHGKRVvvvgggdtamdCVRTAIRQdA---------ASVTCLYR--RdrenMPGSAREVVN-AEE 335
Cdd:COG1148 299 AFiqcvgsrDEENGLPYCSRV-----------CCMYALKQ-AlylkeknpdADVYIFYRdiR----TYGKYEEFYRrARE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 336 EGISF-RWlsnpklllgdanKLDGIRvarmrlgpPDASGR---QSPEEIPGEDADLAADMVIKALGFSP----EDLPTAF 407
Cdd:COG1148 363 DGVRFiRG------------RVAEIE--------EDEGGKlvvTVEDTLLGEPVEIEADLVVLATGMVPsednEELAKLL 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503066337 408 depDLALTRYGTL-----KVDPssYETSLPGVFAAGdIVRGASLVVWAIHDARRAAASIHQYFKGQTVGAIP 474
Cdd:COG1148 423 ---KLPLDQDGFFleahpKLRP--VETATDGIFLAG-AAHGPKDIPESIAQATAAAARAIQLLSKGELGVEP 488
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
148-190 |
4.04e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 49.08 E-value: 4.04e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLM-TYGIPGFK 190
Cdd:COG1233 8 VIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRArTFERPGFR 51
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
136-184 |
4.33e-06 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 49.09 E-value: 4.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503066337 136 IAPARER--PQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLMTY 184
Cdd:PLN02172 1 MAPAQNPinSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVY 51
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
111-220 |
1.04e-05 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 48.06 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 111 HGTVTIGAVEQYITDNAWS----KGWIK-----PIAPARER------PQSIGIIGAGPAGLSAADELRSLGYRITVYDRY 175
Cdd:PLN02328 191 HALESIRAEHKNLVDSAYNflleHGYINfgvapVIKEAQLRsfegvePANVVVVGAGLAGLVAARQLLSMGFKVVVLEGR 270
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 503066337 176 DRAGGlmtygipgfkleksvvmrRVKRLADSGVTFVQNADIGGGV 220
Cdd:PLN02328 271 ARPGG------------------RVKTMKMKGDGVVAAADLGGSV 297
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
133-180 |
1.24e-05 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 48.09 E-value: 1.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 503066337 133 IKPIAPARERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGG 180
Cdd:PLN03000 174 IKDKFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGG 221
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
142-180 |
1.94e-05 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 46.77 E-value: 1.94e-05
10 20 30
....*....|....*....|....*....|....*....
gi 503066337 142 RPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGG 180
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
148-179 |
2.72e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 46.20 E-value: 2.72e-05
10 20 30
....*....|....*....|....*....|..
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDRYDRAG 179
Cdd:COG2081 2 VIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
148-180 |
2.76e-05 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 46.39 E-value: 2.76e-05
10 20 30
....*....|....*....|....*....|...
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDRYDRAGG 180
Cdd:COG2072 11 VIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
145-199 |
4.19e-05 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 46.00 E-value: 4.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503066337 145 SIGIIGAGPAGLSAADELRSLG--YRITVYDRYDRAGGLM-TYGIPGFKLE---KSVVMRR 199
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIqTVRKDGFPIElgpESFLARK 62
|
|
| glucose_DH |
cd08230 |
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ... |
142-255 |
4.60e-05 |
|
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176192 [Multi-domain] Cd Length: 355 Bit Score: 45.67 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 142 RPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGglmtygipgfklEKSVVMRRVkrladsGVTFVQNADigGGVP 221
Cdd:cd08230 172 NPRRALVLGAGPIGLLAALLLRLRGFEVYVLNRRDPPD------------PKADIVEEL------GATYVNSSK--TPVA 231
|
90 100 110
....*....|....*....|....*....|....
gi 503066337 222 FSDLREKHDAILIATGVYKARELSVPGVGANGVV 255
Cdd:cd08230 232 EVKLVGEFDLIIEATGVPPLAFEALPALAPNGVV 265
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
139-238 |
5.17e-05 |
|
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: 45.19 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 139 ARERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRaggLMTygipgfKLEKSVVMRRVKRLADSGVTFVQNADI-- 216
Cdd:COG0446 120 KEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR---LLG------VLDPEMAALLEEELREHGVELRLGETVva 190
|
90 100
....*....|....*....|....*...
gi 503066337 217 -----GGGVPFSDLREKH-DAILIATGV 238
Cdd:COG0446 191 idgddKVAVTLTDGEEIPaDLVVVAPGV 218
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
168-442 |
6.29e-05 |
|
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: 44.80 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 168 RITVYDRYDRAG----GLMTYGIPGFKLEKSVVMRRVKRLADSGVTFVQNADI-------------GGGvpfsdlREKHD 230
Cdd:COG0446 7 EITVIEKGPHHSyqpcGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVtaidpeaktvtlrDGE------TLSYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 231 AILIATGVyKARELSVPGVGANGV--VRALDYLTASNRK---GFGDEV----PGF-----DEgHMNAHGKRvvvvgggdt 296
Cdd:COG0446 81 KLVLATGA-RPRPPPIPGLDLPGVftLRTLDDADALREAlkeFKGKRAvvigGGPiglelAE-ALRKRGLK--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 297 amdcvrtairqdaasVTCLYRRDREnMPGSAREVVNA-----EEEGISFRWLSNPKLLLGDANKldGIRVArmrlgppda 371
Cdd:COG0446 150 ---------------VTLVERAPRL-LGVLDPEMAALleeelREHGVELRLGETVVAIDGDDKV--AVTLT--------- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503066337 372 SGrqspEEIPgedadlaADMVIKALGFSPEdlpTAF-DEPDLALTRYGTLKVDPSsYETSLPGVFAAGDIVR 442
Cdd:COG0446 203 DG----EEIP-------ADLVVVAPGVRPN---TELaKDAGLALGERGWIKVDET-LQTSDPDVYAAGDCAE 259
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
383-455 |
8.96e-05 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 44.74 E-value: 8.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503066337 383 EDADLAADMVIKALGFSPEDLPTAFDEPDLALTRYGTLKVDpSSYETSLPGVFAAGDIVRGASLVVWAIHDAR 455
Cdd:PRK07251 236 EDETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVD-DYCQTSVPGVFAVGDVNGGPQFTYISLDDFR 307
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
4-56 |
1.40e-04 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 44.48 E-value: 1.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 503066337 4 FIDTPRQTPEKRAAELRREDFEEVYSGFKERQAEAQASRCSQCGVPF----CSSGCP 56
Cdd:PRK12771 467 FTDAPRAQRPELDADERVGDFDEVLGGLTEEEARQEAARCLSCGNCFecdnCYGACP 523
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
140-237 |
1.54e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 44.01 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 140 RERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLMTYGIPGF---KLEKSVVMR---RVKRLADSGVTFVQN 213
Cdd:PRK06292 166 DKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQaqkILSKEFKIKlgaKVTSVEKSGDEKVEE 245
|
90 100
....*....|....*....|....
gi 503066337 214 ADIGGGvpfsDLREKHDAILIATG 237
Cdd:PRK06292 246 LEKGGK----TETIEADYVLVATG 265
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
146-179 |
2.51e-04 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 43.00 E-value: 2.51e-04
10 20 30
....*....|....*....|....*....|....
gi 503066337 146 IGIIGAGPAGLSAADELRSLGYRITVYDRYDRAG 179
Cdd:COG0654 6 VLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
148-446 |
2.82e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 43.24 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDR------------------------YDRAGGLMTYGI--PGFKLEKSVVMRRVK 201
Cdd:PRK06292 8 VIGAGPAGYVAARRAAKLGKKVALIEKgplggtclnvgcipskaliaaaeaFHEAKHAEEFGIhaDGPKIDFKKVMARVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 202 RLADSGVTFVQ-------NAD-IGGGVPF--------SDLREKHDAILIATGvykARELSVPGVGANGVVRALDYLTASN 265
Cdd:PRK06292 88 RERDRFVGGVVeglekkpKIDkIKGTARFvdpntvevNGERIEAKNIVIATG---SRVPPIPGVWLILGDRLLTSDDAFE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 266 RkgfgDEVP-----------GFDEGH-MNAHGKRvvvvgggdtamdcvrtairqdaasVTCLYRRDREnMPGSAREVVNA 333
Cdd:PRK06292 165 L----DKLPkslavigggviGLELGQaLSRLGVK------------------------VTVFERGDRI-LPLEDPEVSKQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 334 EEEgisfrwlsnpklLLGDANKLD-GIRVARMRlgpPDASGRQSPEEIPGEDADLAADMVIKALGFSP--EDLptAFDEP 410
Cdd:PRK06292 216 AQK------------ILSKEFKIKlGAKVTSVE---KSGDEKVEELEKGGKTETIEADYVLVATGRRPntDGL--GLENT 278
|
330 340 350
....*....|....*....|....*....|....*.
gi 503066337 411 DLALTRYGTLKVDPSsYETSLPGVFAAGDIVRGASL 446
Cdd:PRK06292 279 GIELDERGRPVVDEH-TQTSVPGIYAAGDVNGKPPL 313
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
141-238 |
5.51e-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: 41.92 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 141 ERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLMTYGIpGFKLEKSVVMRRVKRLADSGVTFVQNADIGGGV 220
Cdd:pfam07992 150 LLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEI-SAALEKALEKNGVEVRLGTSVKEIIGDGDGVEV 228
|
90
....*....|....*....
gi 503066337 221 PFSDLRE-KHDAILIATGV 238
Cdd:pfam07992 229 ILKDGTEiDADLVVVAIGR 247
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
145-216 |
5.93e-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: 425450 [Multi-domain] Cd Length: 80 Bit Score: 38.72 E-value: 5.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503066337 145 SIGIIGAGPAGLSAADELRSLGYRITVYDRYDRagglmtygiPGFKLEKSVVMRRVKRLADSGVTFVQNADI 216
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDR---------LLPGFDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
140-237 |
6.59e-04 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 42.00 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 140 RERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAgglmtygIPGFklEKSVVMRRVKRLADSGVTFVQNADI--- 216
Cdd:COG1249 165 EELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRL-------LPGE--DPEISEALEKALEKEGIDILTGAKVtsv 235
|
90 100 110
....*....|....*....|....*....|
gi 503066337 217 ---GGGVP--FSDLREKH----DAILIATG 237
Cdd:COG1249 236 ektGDGVTvtLEDGGGEEaveaDKVLVATG 265
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
378-458 |
7.09e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 42.22 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 378 EEIPGEDADLAADMVIKALGFSPEDLPTAFDEPDLALTRYGTLKVDpSSYETSLPGVFAAGDIVRGASLVVWAIHD---- 453
Cdd:PRK06327 262 TDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVD-DHCRTNVPNVYAIGDVVRGPMLAHKAEEEgvav 340
|
....*
gi 503066337 454 ARRAA 458
Cdd:PRK06327 341 AERIA 345
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
148-174 |
7.45e-04 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 42.02 E-value: 7.45e-04
10 20
....*....|....*....|....*..
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDR 174
Cdd:COG2509 35 IVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
142-180 |
9.93e-04 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 41.64 E-value: 9.93e-04
10 20 30
....*....|....*....|....*....|....*....
gi 503066337 142 RPQSIGIIGAGPAGLSAADELRSLgYRITVYDRYDRAGG 180
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
140-180 |
1.02e-03 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 41.78 E-value: 1.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503066337 140 RERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGG 180
Cdd:PLN02976 690 SVDRKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
148-212 |
1.12e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 41.04 E-value: 1.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDRYD-------RAGGLMTYGIPgfklekSVVMRRVKRLADSGVTFVQ 212
Cdd:COG0665 7 VIGGGIAGLSTAYHLARRGLDVTVLERGRpgsgasgRNAGQLRPGLA------ALADRALVRLAREALDLWR 72
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
148-181 |
1.33e-03 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 40.77 E-value: 1.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDRYD------RAGGL 181
Cdd:pfam01494 6 IVGGGPAGLMLALLLARAGVRVVLVERHAttsvlpRAHGL 45
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
138-179 |
1.51e-03 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 40.99 E-value: 1.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 503066337 138 PARERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAG 179
Cdd:PRK01747 255 PGSPKARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
148-180 |
1.84e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 40.46 E-value: 1.84e-03
10 20 30
....*....|....*....|....*....|...
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDRYDRAGG 180
Cdd:pfam01266 4 VIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| SerA |
COG0111 |
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ... |
129-187 |
2.03e-03 |
|
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439881 [Multi-domain] Cd Length: 314 Bit Score: 40.18 E-value: 2.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 129 SKGWIKPIAPARE-RPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGGLMTYGIP 187
Cdd:COG0111 125 AGRWDRSAFRGRElRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPKPEEAADLGVG 184
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|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
148-179 |
2.70e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 40.26 E-value: 2.70e-03
10 20 30
....*....|....*....|....*....|..
gi 503066337 148 IIGAGPAGLSAADELRSLGYRITVYDRYDRAG 179
Cdd:pfam03486 5 VIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| LDH |
cd12186 |
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ... |
116-175 |
2.98e-03 |
|
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.
Pssm-ID: 240662 Cd Length: 329 Bit Score: 39.83 E-value: 2.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503066337 116 IGAVEQYITDNAWSkgWIKPIApARE-RPQSIGIIGAGPAGLSAADELRSLGYRITVYDRY 175
Cdd:cd12186 120 TPEIDRRVAKGDFR--WAPGLI-GREiRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPY 177
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|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
9-46 |
3.71e-03 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 39.71 E-value: 3.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 503066337 9 RQTPEKRAA------ELRREDFEEVYSGFKERQAEAQASRCSQC 46
Cdd:PRK12814 529 RAQPAPRVAlpelplEERTGGFEEVVTGYSPEQAREEALRCLRC 572
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|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
144-178 |
3.80e-03 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 39.62 E-value: 3.80e-03
10 20 30
....*....|....*....|....*....|....*
gi 503066337 144 QSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRA 178
Cdd:PRK12409 2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDRHRYA 36
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|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
144-255 |
4.44e-03 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 39.46 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503066337 144 QSIGIIGAGPAGLSAADELRSLGYRITVYDR---------------------------YDRAG--GLMTYGIPGFKLEKS 194
Cdd:PRK07845 2 TRIVIIGGGPGGYEAALVAAQLGADVTVIERdglggaavltdcvpsktliataevrteLRRAAelGIRFIDDGEARVDLP 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503066337 195 VVMRRVKRLADSgvtfvQNADIGGGVPFSDLRekhdaILIATGvykarELSVPGVGANGVV 255
Cdd:PRK07845 82 AVNARVKALAAA-----QSADIRARLEREGVR-----VIAGRG-----RLIDPGLGPHRVK 127
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
130-180 |
4.58e-03 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 39.40 E-value: 4.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 503066337 130 KGWIKPIAPARERPQ-SIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGG 180
Cdd:PLN02487 61 KGLFPPEPEAYKGPKlKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGG 112
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
154-192 |
6.23e-03 |
|
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
Pssm-ID: 396255 [Multi-domain] Cd Length: 446 Bit Score: 39.01 E-value: 6.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 503066337 154 AGLSAADELRSLGYRITVYDRYDRAGGLM-TYGIPGFKLE 192
Cdd:pfam01593 2 AGLAAARELLRAGHDVTVLEARDRVGGRIrTVRDDGFLIE 41
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
135-180 |
6.87e-03 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 39.10 E-value: 6.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503066337 135 PIAPARERPQSIGIIGAGPAGLSAADELRSLGYRITVYDRYDRAGG 180
Cdd:PLN02529 152 SPIPEEGTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGG 197
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|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
146-174 |
8.85e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 38.52 E-value: 8.85e-03
10 20
....*....|....*....|....*....
gi 503066337 146 IGIIGAGPAGLSAADELRSLGYRITVYDR 174
Cdd:PRK06753 3 IAIIGAGIGGLTAAALLQEQGHEVKVFEK 31
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