|
Name |
Accession |
Description |
Interval |
E-value |
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
9-472 |
0e+00 |
|
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: 798.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 9 FQFIEVGRKDPKKKLLRQRKKEFVEIYEPFKPQHSADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVAEGNILQAAELSH 88
Cdd:TIGR01318 1 FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 89 QTNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDMSKVKPTGKRVAIIGAGPAGLGCADVL 168
Cdd:TIGR01318 81 QTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 169 VRGGVTPVVFDKNPEIGGLLTFGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTYTYM 248
Cdd:TIGR01318 161 ARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRSM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 249 KGGFAGEDLPGVHDALDFLIANVNRNLGFEKSPED-FVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEANM 327
Cdd:TIGR01318 241 RGGLPGEDAPGVLPALPFLIANTRQLMGLPEEPEEpLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 328 PGSRKEVKNAKEEGVKFLYNRQPIAIVGED--KVEGVKVVETRLGAPDARGRRSPEPIPGSEEIIPADAVVIAFGFRPSP 405
Cdd:TIGR01318 321 PGSRREVANAREEGVEFLFNVQPVSIESDEdgQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520807339 406 APWFEQFSIQTDSQGRVVAPEQGQYKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDYLGV 472
Cdd:TIGR01318 401 MPWLAAHGITLDSWGRIITALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV 467
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
7-472 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 783.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 7 NDFQFIEVGRKDPKKKLLRQRKKEFVEIYEPFKPQHSADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVAEGNILQAAEL 86
Cdd:PRK12810 3 KPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 87 SHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGSVEKYITDTAFAMGW-RPDmSKVKPTGKRVAIIGAGPAGLGCA 165
Cdd:PRK12810 83 LHQTNNFPEFTGRVCPAP--CEGACTLNINFGPVTIKNIERYIIDKAFEEGWvKPD-PPVKRTGKKVAVVGSGPAGLAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 166 DVLVRGGVTPVVFDKNPEIGGLLTFGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTY 245
Cdd:PRK12810 160 DQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 246 TYMKGGFAGEDLPGVHDALDFLIANVNRNLGFEKSPedFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTcayRRDEA 325
Cdd:PRK12810 240 KPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDETEP--FISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVT---QRDIM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 326 NMPGSRK-------------EVKNAKEEGVKFLYNRQPIAIVGED-KVEGVKVVETRLGAPDargrrsPEPIPGSEEIIP 391
Cdd:PRK12810 315 PMPPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEGENgKVTGVKVVRTELGEGD------FEPVEGSEFVLP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 392 ADAVVIAFGFRPSPAPWFEQFSIQTDSQGRVVAPEQGqykHQTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDYLG 471
Cdd:PRK12810 389 ADLVLLAMGFTGPEAGLLAQFGVELDERGRVAAPDNA---YQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLM 465
|
.
gi 520807339 472 V 472
Cdd:PRK12810 466 G 466
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
16-472 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 764.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 16 RKDPKKKLLRQRKKEFVEIYEPFKPQHSADQAHRCLGCGN-PYCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLP 94
Cdd:PRK12769 193 RGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 95 EVCGRVCPQDRLCEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDMSKVKPTGKRVAIIGAGPAGLGCADVLVRGGVT 174
Cdd:PRK12769 273 EITGRVCPQDRLCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNGVA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 175 PVVFDKNPEIGGLLTFGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTYTYMKGGFAG 254
Cdd:PRK12769 353 VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLPN 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 255 EDLPGVHDALDFLIANVNRNLGFEKSP-EDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEANMPGSRKE 333
Cdd:PRK12769 433 EDAPGVYDALPFLIANTKQVMGLEELPeEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 334 VKNAKEEGVKFLYNRQPIAIVGED--KVEGVKVVETRLGAPDARGRRSPEPIPGSEEIIPADAVVIAFGFRPSPAPWFEQ 411
Cdd:PRK12769 513 VKNAREEGANFEFNVQPVALELNEqgHVCGIRFLRTRLGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGFNPHGMPWLES 592
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520807339 412 FSIQTDSQGRVVAPEQGQYKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDYLGV 472
Cdd:PRK12769 593 HGVTVDKWGRIIADVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLGV 653
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
30-469 |
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: 656.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 30 EFVEIYEPFKPQHSADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPqdRLCEG 109
Cdd:COG0493 4 DFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--APCEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 110 ACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDMSKVKPTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLT 189
Cdd:COG0493 82 ACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 190 FGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTYTYMKGGFAGEDLPGVHDALDFLIA 269
Cdd:COG0493 162 YGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDFLTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 270 NVNRNLgfekspEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEANMPGSRKEVKNAKEEGVKFLYNRQ 349
Cdd:COG0493 242 VNLGEA------PDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLFLVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 350 PIAIVGED--KVEGVKVVETRLGAPDARGRRSPEPIPGSEEIIPADAVVIAFGFRPSPAPWFEQFSIQTDSQGRVVAPEQ 427
Cdd:COG0493 316 PVEIIGDEngRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVVDEE 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 520807339 428 gqyKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDY 469
Cdd:COG0493 396 ---TYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
31-467 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 585.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 31 FVEIYEPFKPQHSADQAHRCLGCGN-PYCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDRLCEG 109
Cdd:PRK12809 191 FGEIYCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDRLCEG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 110 ACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDMSKVKPTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLT 189
Cdd:PRK12809 271 ACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLT 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 190 FGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTYTYMKGGFAGEDLPGVHDALDFLIA 269
Cdd:PRK12809 351 FGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 270 NVNRNLGFEKSPE-DFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEANMPGSRKEVKNAKEEGVKFLYNR 348
Cdd:PRK12809 431 HTRQLMGLPESEEyPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 349 QPIAIVGEDK--VEGVKVVETRLGAPDARGRRSPEPIPGSEEIIPADAVVIAFGFRPSPAPWFEQFSIQTDSQGRVVAPE 426
Cdd:PRK12809 511 QPQYIACDEDgrLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIQTGD 590
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 520807339 427 QGQYKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGIL 467
Cdd:PRK12809 591 VGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDML 631
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
30-470 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 573.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 30 EFVEIYEPFKPQHSADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDRLCEG 109
Cdd:PRK11749 22 NFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQERLCEG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 110 ACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDMsKVKPTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLT 189
Cdd:PRK11749 102 ACVRGKKGEPVAIGRLERYITDWAMETGWVLFK-RAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGLLR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 190 FGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTYTYMKGGFAGEDLPGVHDALDFLiA 269
Cdd:PRK11749 181 YGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPRFLGIPGENLGGVYSAVDFL-T 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 270 NVNRnlgfekSPEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEANMPGSRKEVKNAKEEGVKFLYNRQ 349
Cdd:PRK11749 260 RVNQ------AVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPASEEEVEHAKEEGVEFEWLAA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 350 PIAIVGEDK-VEGVKVVETRLGAPDARGRRSpEPIPGSEEIIPADAVVIAFGFRPSPAPWFEQFSIQTDSQGRVVAPEQg 428
Cdd:PRK11749 334 PVEILGDEGrVTGVEFVRMELGEPDASGRRR-VPIEGSEFTLPADLVIKAIGQTPNPLILSTTPGLELNRWGTIIADDE- 411
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 520807339 429 qyKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDYL 470
Cdd:PRK11749 412 --TGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYL 451
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
46-470 |
1.80e-121 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 362.80 E-value: 1.80e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 46 QAHRCLGCGNPYCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGSV 125
Cdd:PRK12831 38 EASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQCEGKCVLGIKGEPVAIGKL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 126 EKYITDTAFAMGWRPDMSKVKPtGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLTFGIPEFKLEK-TVLSN 204
Cdd:PRK12831 118 ERFVADWARENGIDLSETEEKK-GKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLVYGIPEFRLPKeTVVKK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 205 RREVFTGMGIEFRLNTEVGKDVTMEQLLAE--YDAVFMGMGTYTYMKGGFAGEDLPGVHDALDFLIANvnrNLGFEKSPE 282
Cdd:PRK12831 197 EIENIKKLGVKIETNVVVGKTVTIDELLEEegFDAVFIGSGAGLPKFMGIPGENLNGVFSANEFLTRV---NLMKAYKPE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 283 -DFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKsVTCAYRRDEANMPGSRKEVKNAKEEGVKFLYNRQPIAIVGEDK--V 359
Cdd:PRK12831 274 yDTPIKVGKKVAVVGGGNVAMDAARTALRLGAE-VHIVYRRSEEELPARVEEVHHAKEEGVIFDLLTNPVEILGDENgwV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 360 EGVKVVETRLGAPDARGRRSPEPIPGSEEIIPADAVVIAFGFRPSPAPWFEQFSIQTDSQGRVVAPEQGQykhQTSNPKI 439
Cdd:PRK12831 353 KGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTKGLKINKRGCIVADEETG---LTSKEGV 429
|
410 420 430
....*....|....*....|....*....|.
gi 520807339 440 FAGGDMVRGSDLVVTAIFEGRNAAEGILDYL 470
Cdd:PRK12831 430 FAGGDAVTGAATVILAMGAGKKAAKAIDEYL 460
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
11-470 |
2.33e-117 |
|
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: 352.98 E-value: 2.33e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 11 FIEVGRKDPKKKLLRQRKKEFVEIYEPFKPQHSADQAHRCLGCGNPYC--EWKCPVHNFIPNWLKLVAEGNILQAAELSH 88
Cdd:TIGR01317 5 FLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFChnDSGCPLNNLIPEFNDLVFRGRWKEALDRLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 89 QTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGSVEKYITDTAFAMGW-RPDMSKVKpTGKRVAIIGAGPAGLGCADV 167
Cdd:TIGR01317 85 ATNNFPEFTGRVCPAP--CEGACTLGISEDPVGIKSIERIIIDKGFQEGWvQPRPPSKR-TGKKVAVVGSGPAGLAAADQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 168 LVRGGVTPVVFDKNPEIGGLLTFGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTYTY 247
Cdd:TIGR01317 162 LNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATKP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 248 MKGGFAGEDLPGVHDALDFLIANVNRNLGFEKSPEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVT-------CAY 320
Cdd:TIGR01317 242 RDLPIPGRELKGIHYAMEFLPSATKALLGKDFKDIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHqfeimpkPPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 321 RRDEANM-PGSRKEVK-NAKEEGVKFLYNRQP-------IAIVGED--KVEGVKVVETRLgAPDARGRRSPEPIPGSEEI 389
Cdd:TIGR01317 322 ARAKDNPwPEWPRVYRvDYAHEEAAAHYGRDPreysiltKEFIGDDegKVTALRTVRVEW-KKSQDGKWQFVEIPGSEEV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 390 IPADAVVIAFGFRPSPAPWFEQFSIQTDSQGRVVApeqGQYKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDY 469
Cdd:TIGR01317 401 FEADLVLLAMGFVGPEQILLDDFGVKKTRRGNISA---GYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVDRY 477
|
.
gi 520807339 470 L 470
Cdd:TIGR01317 478 L 478
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
31-470 |
2.85e-111 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 345.57 E-value: 2.85e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 31 FVEIYEPFKPQHSADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDRLCEGA 110
Cdd:PRK12778 312 FEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQCESK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 111 CT-LNDGFGAVTIGSVEKYITDTAFAMGwRPDMSKVKP-TGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLL 188
Cdd:PRK12778 392 CIhGKMGEEAVAIGYLERFVADYERESG-NISVPEVAEkNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 189 TFGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAE-YDAVFM--GMGTYTYMkgGFAGEDLPGVHDALD 265
Cdd:PRK12778 471 KYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEgFKGIFIasGAGLPNFM--NIPGENSNGVMSSNE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 266 FLiANVNRNLGFEKSPEDFVDMkGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEANMPGSRKEVKNAKEEGVKFL 345
Cdd:PRK12778 549 YL-TRVNLMDAASPDSDTPIKF-GKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARLEEVKHAKEEGIEFL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 346 YNRQPIAIVGEDK--VEGVKVVETRLGAPDARGRRSPEPIPGSEEIIPADAVVIAFGFRPSPAPWFEQFSIQTDSQGRVV 423
Cdd:PRK12778 627 TLHNPIEYLADEKgwVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSIPGLELNRKGTIV 706
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 520807339 424 APEQgqykHQTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDYL 470
Cdd:PRK12778 707 VDEE----MQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYL 749
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
31-470 |
1.02e-110 |
|
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: 334.53 E-value: 1.02e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 31 FVEIYEPFKPQHSADQAHRCLGCGNPY--CEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDRLCE 108
Cdd:TIGR01316 9 FQEAALGYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVCPQERQCE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 109 GACTLNDGFG----AVTIGSVEKYITDTAFAMGWRPDMSKVKPTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEI 184
Cdd:TIGR01316 89 GQCTVGKMFKdvgkPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVTVFEALHKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 185 GGLLTFGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTYTYMKGGFAGEDLPGVHDAL 264
Cdd:TIGR01316 169 GGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEELCGVYSAN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 265 DFLIaNVNRNLGFEKSPEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKsVTCAYRRDEANMPGSRKEVKNAKEEGVKF 344
Cdd:TIGR01316 249 DFLT-RANLMKAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGAE-VHCLYRRTREDMTARVEEIAHAEEEGVKF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 345 LYNRQPIAIVGEDK--VEGVKVVETRLGAPDARGRRSPEPIPGSEEIIPADAVVIAFGFRPSPAPwFEQFSIQTDSQGRV 422
Cdd:TIGR01316 327 HFLCQPVEIIGDEEgnVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIM-AETTRLKTSERGTI 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 520807339 423 VAPEqgqyKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDYL 470
Cdd:TIGR01316 406 VVDE----DQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
42-471 |
4.91e-109 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 334.15 E-value: 4.91e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 42 HSADQAHRCLGCGN--PYCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGA 119
Cdd:PRK12771 31 ATGPWRHKCPVYVDqtPPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCNRGQVDDA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 120 VTIGSVEKYITDTAFAMGWRPDmSKVKPTGKRVAIIGAGPAGLGCADVLVRGG--VTpvVFDKNPEIGGLLTFGIPEFKL 197
Cdd:PRK12771 109 VGINAVERFLGDYAIANGWKFP-APAPDTGKRVAVIGGGPAGLSAAYHLRRMGhaVT--IFEAGPKLGGMMRYGIPAYRL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 198 EKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTYTYMKGGFAGEDLPGVHDALDFLianvnRNLGF 277
Cdd:PRK12771 186 PREVLDAEIQRILDLGVEVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFL-----RAVGE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 278 EKSPedfvdMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEANMPGSRKEVKNAKEEGVKFLYNRQPIAI-VGE 356
Cdd:PRK12771 261 GEPP-----FLGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIeGDE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 357 DKVEGVKVVETRLGAPDARGRrsPEPIPGSEEIIPADAVVIAFG----FRPspapwFEQFSIQTDSQGRVVAPEQGQykh 432
Cdd:PRK12771 336 NGATGLRVITVEKMELDEDGR--PSPVTGEEETLEADLVVLAIGqdidSAG-----LESVPGVEVGRGVVQVDPNFM--- 405
|
410 420 430
....*....|....*....|....*....|....*....
gi 520807339 433 QTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDYLG 471
Cdd:PRK12771 406 MTGRPGVFAGGDMVPGPRTVTTAIGHGKKAARNIDAFLG 444
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
41-471 |
1.68e-96 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 304.34 E-value: 1.68e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 41 QHSADqahrCLGcgnPyCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAV 120
Cdd:PRK12814 95 QHCGD----CLG---P-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDEPV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 121 TIGSVEKYITDTAFAMGWRPDMSKVKPTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLTFGIPEFKLEKT 200
Cdd:PRK12814 165 SICALKRYAADRDMESAERYIPERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPES 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 201 VLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTYTYMKGGFAGEDLPGVHDALDFLiANVnrNLGFEKS 280
Cdd:PRK12814 245 VIDADIAPLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFL-RNV--ALGTALH 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 281 PedfvdmkGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEANMPGSRKEVKNAKEEGVKFLYNRQPIAI-VGEDKV 359
Cdd:PRK12814 322 P-------GKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIeRSEGGL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 360 EgVKVVETRLGAPDARGRRSPEPIPGSEEIIPADAVVIAFGFRPSPaPWFEQFSIQTDSQGRVVAPEQGQykhQTSNPKI 439
Cdd:PRK12814 395 E-LTAIKMQQGEPDESGRRRPVPVEGSEFTLQADTVISAIGQQVDP-PIAEAAGIGTSRNGTVKVDPETL---QTSVAGV 469
|
410 420 430
....*....|....*....|....*....|..
gi 520807339 440 FAGGDMVRGSDLVVTAIFEGRNAAEGILDYLG 471
Cdd:PRK12814 470 FAGGDCVTGADIAINAVEQGKRAAHAIDLFLN 501
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
143-470 |
1.09e-90 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 279.95 E-value: 1.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 143 SKVKPTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLTFGIPEFKLEK-TVLSNRREVfTGMGIEFRLNTE 221
Cdd:PRK12770 12 EKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIeRVREGVKEL-EEAGVVFHTRTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 222 V---------------GKDVTMEQLLAEYDAVFMGMGTYTYMKGGFAGEDLPGVHDALDFLIANVNRNLGF---EKSPed 283
Cdd:PRK12770 91 VccgeplheeegdefvERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRIRAAKLGYlpwEKVP-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 284 fvDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEANMPGSRKEVKNAKEEGVKFLYNRQPIAIVGEDKVEGVK 363
Cdd:PRK12770 169 --PVEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIGEGRVEGVE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 364 VVETRLGAPDARGRRSPEPIPGSEEIIPADAVVIAFGFRPSPAPWFEQFSIQTDSQGRVVAPEqgqyKHQTSNPKIFAGG 443
Cdd:PRK12770 247 LAKMRLGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDE----KHMTSREGVFAAG 322
|
330 340
....*....|....*....|....*..
gi 520807339 444 DMVRGSDLVVTAIFEGRNAAEGILDYL 470
Cdd:PRK12770 323 DVVTGPSKIGKAIKSGLRAAQSIHEWL 349
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
31-470 |
2.20e-85 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 282.60 E-value: 2.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 31 FVEIYEPFKPQHSADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDRLCEGA 110
Cdd:PRK12775 314 FKEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 111 CTLNDGFGAVTIGSVEKYITDTAFAMGWRP-DMSkvKPTGKrVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLT 189
Cdd:PRK12775 394 CIIAKKHESVGIGRLERFVGDNARAKPVKPpRFS--KKLGK-VAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 190 FGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAE--YDAVFMGMG----TYTYMKGGFAGEdlpgVHDA 263
Cdd:PRK12775 471 YGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGagapTFLGIPGEFAGQ----VYSA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 264 LDFLiANVNRnLGFEKSPedFVDMK---GKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEANMPGSRKEVKNAKEE 340
Cdd:PRK12775 547 NEFL-TRVNL-MGGDKFP--FLDTPislGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 341 GVKFLYNRQPIAIV--GEDKVEGVKVVETRLGAPDARGRRSPEPIPGSEEiIPADAVVIAFGFRPSPAPWFEQFSIQTDS 418
Cdd:PRK12775 623 GIDFFFLHSPVEIYvdAEGSVRGMKVEEMELGEPDEKGRRKPMPTGEFKD-LECDTVIYALGTKANPIITQSTPGLALNK 701
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 520807339 419 QGRVVAPEQGQYKHQTSN-PKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDYL 470
Cdd:PRK12775 702 WGNIAADDGKLESTQSTNlPGVFAGGDIVTGGATVILAMGAGRRAARSIATYL 754
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
31-470 |
2.11e-76 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 250.45 E-value: 2.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 31 FVEIYEPFKPQHSADQAHRCLGCGnpYCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDrlCEGA 110
Cdd:PRK13984 168 FIEIVKGYSKEQAMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVCTHK--CETV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 111 CTLNDGFGAVTIGSVEKYITDTAFAMGWRPDMS-KVKPTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLT 189
Cdd:PRK13984 244 CSIGHRGEPIAIRWLKRYIVDNVPVEKYSEILDdEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 190 FGIPEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTMEQLLAEYDAVFMGMGTYTYMKGGFAGEDLPGVHDALDFL-- 267
Cdd:PRK13984 324 YGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGTDHPDVIQALPLLre 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 268 IANVNRNLGfeksPEDFVDmkgKRVVVLGGGDTAMDCNRTSIR-----QGAKSVTC-AYRRDEANMPGSRKEVKNAKEEG 341
Cdd:PRK13984 404 IRDYLRGEG----PKPKIP---RSLVVIGGGNVAMDIARSMARlqkmeYGEVNVKVtSLERTFEEMPADMEEIEEGLEEG 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 342 VKFLYNRQPIAIVGE-DKVEGVKVVETrLGAPDARGRRSPEPIPGSEEIIPADAVVIAFGFRPS----PAPWFEQFSIqt 416
Cdd:PRK13984 477 VVIYPGWGPMEVVIEnDKVKGVKFKKC-VEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQAPDysylPEELKSKLEF-- 553
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 520807339 417 dSQGRVVAPEQGqykhQTSNPKIFAGGDMVRGSDlVVTAIFEGRNAAEGILDYL 470
Cdd:PRK13984 554 -VRGRILTNEYG----QTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYL 601
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
62-468 |
4.25e-65 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 225.87 E-value: 4.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 62 CPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDRLCEGACTLNDGfgAVTIGSVEKYI--------TDTA 133
Cdd:PRK12779 214 CPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTKR--PIEIGQLEWYLpqheklvnPNAN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 134 FAMGWRPD--MSKVKPTgkrVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLTFGIPEFKLEKTVLSNRREVFTG 211
Cdd:PRK12779 292 ERFAGRISpwAAAVKPP---IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 212 MGIEFRLNTEVGKDVTMEQLLAE-YDAVFMGMGT--YTYMKggFAGEDLPGVHDALDFLiANVNRNLGFEKSPED-FVDM 287
Cdd:PRK12779 369 LGGRFVKNFVVGKTATLEDLKAAgFWKIFVGTGAglPTFMN--VPGEHLLGVMSANEFL-TRVNLMRGLDDDYETpLPEV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 288 KGKRVVVLGGGDTAMDCNRTSIRQGAkSVTCAYRRDEANMPGSRKEVKNAKEEGVKFLYNRQPIAIVGEDK---VEGVKV 364
Cdd:PRK12779 446 KGKEVFVIGGGNTAMDAARTAKRLGG-NVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGDDHthfVTHALL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 365 VETRLGAPDARGRRSPEPIpGSEEIIPADAVVIAFGFRPSPAPWFEQFSIQTDSQGRVVAPEQGQykhQTSNPKIFAGGD 444
Cdd:PRK12779 525 DVNELGEPDKSGRRSPKPT-GEIERVPVDLVIMALGNTANPIMKDAEPGLKTNKWGTIEVEKGSQ---RTSIKGVYSGGD 600
|
410 420
....*....|....*....|....
gi 520807339 445 MVRGSDLVVTAIFEGRNAAEGILD 468
Cdd:PRK12779 601 AARGGSTAIRAAGDGQAAAKEIVG 624
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
31-138 |
1.63e-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: 185.44 E-value: 1.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 31 FVEIYEPFKPQHSADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVAEGNILQAAELSHQTNTLPEVCGRVCPQDRLCEGA 110
Cdd:pfam14691 5 FEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQCEGA 84
|
90 100
....*....|....*....|....*....
gi 520807339 111 CTLN-DGFGAVTIGSVEKYITDTAFAMGW 138
Cdd:pfam14691 85 CVLGkKGFEPVAIGRLERFAADWARENGI 113
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
152-470 |
9.04e-37 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 137.17 E-value: 9.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 152 VAIIGAGPAGLGCADVLVRGGVTPVVFDKnPEIGGLLT--------FGIPEF--------KLEKTVLSNRREVFTGM--G 213
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPEGisgpelaeRLREQAERFGAEILLEEvtS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 214 IE-----FRLNTEVGKDVTmeqllAeyDAVFMGMGTYtYMKGGFAGEDLP---GVH-----DALDFlianvnrnlgfeks 280
Cdd:COG0492 82 VDkddgpFRVTTDDGTEYE-----A--KAVIIATGAG-PRKLGLPGEEEFegrGVSycatcDGFFF-------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 281 pedfvdmKGKRVVVLGGGDTAMD--CNRTSIrqgAKSVTCAYRRDEANmpGSRKEVKNAKE-EGVKFLYNRQPIAIVGED 357
Cdd:COG0492 140 -------RGKDVVVVGGGDSALEeaLYLTKF---ASKVTLIHRRDELR--ASKILVERLRAnPKIEVLWNTEVTEIEGDG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 358 KVEGVKVVETRlgapdargrrspepiPGSEEIIPADAVVIAFGFRPSPApWFEQFSIQTDSQGRVVAPEQGqykhQTSNP 437
Cdd:COG0492 208 RVEGVTLKNVK---------------TGEEKELEVDGVFVAIGLKPNTE-LLKGLGLELDEDGYIVVDEDM----ETSVP 267
|
330 340 350
....*....|....*....|....*....|....
gi 520807339 438 KIFAGGDMVRGS-DLVVTAIFEGRNAAEGILDYL 470
Cdd:COG0492 268 GVFAAGDVRDYKyRQAATAAGEGAIAALSAARYL 301
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-459 |
2.25e-27 |
|
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: 111.26 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 150 KRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEI---GGLLTFGI-------PEFKLEKTVLSNRREVFTGM--GIEFR 217
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpygGCVLSKALlgaaeapEIASLWADLYKRKEEVVKKLnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 218 LNTEV------GKDVTMEQLLA------EYDAVFMGMGTYTYMKGgfagedLPGVHDALDFLIANVNRNLGFEkspedfV 285
Cdd:pfam07992 81 LGTEVvsidpgAKKVVLEELVDgdgetiTYDRLVIATGARPRLPP------IPGVELNVGFLVRTLDSAEALR------L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 286 DMKGKRVVVLGGGDTAMDCNRTSIRQGAKsVTCAYRRDEAnMPGSRKEVKNA-----KEEGVKFLYNRQPIAIVGEDkvE 360
Cdd:pfam07992 149 KLLPKRVVVVGGGYIGVELAAALAKLGKE-VTLIEALDRL-LRAFDEEISAAlekalEKNGVEVRLGTSVKEIIGDG--D 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 361 GVKVVEtrlgapdargrrspepipGSEEIIPADAVVIAFGFRPSPApWFEQFSIQTDSQGRVVAPEQGqykhQTSNPKIF 440
Cdd:pfam07992 225 GVEVIL------------------KDGTEIDADLVVVAIGRRPNTE-LLEAAGLELDERGGIVVDEYL----RTSVPGIY 281
|
330 340
....*....|....*....|
gi 520807339 441 AGGDM-VRGSDLVVTAIFEG 459
Cdd:pfam07992 282 AAGDCrVGGPELAQNAVAQG 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
152-470 |
3.11e-22 |
|
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: 96.54 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 152 VAIIGAGPAGLGCADVLVRGGVTPVVFDKnPEIGGLLTF--------GIPEFKLEKTVLSNRREVFTGMGIE-------- 215
Cdd:TIGR01292 2 VIIIGAGPAGLTAAIYAARANLKPLLIEG-MEPGGQLTTttevenypGFPEGISGPELMEKMKEQAVKFGAEiiyeevik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 216 -------FRLNTEVGKDVTMeqllaeyDAVFMGMGTyTYMKGGFAGEDL---PGVH-----DALDFlianvnrnlgfeks 280
Cdd:TIGR01292 81 vdksdrpFKVYTGDGKEYTA-------KAVIIATGA-SARKLGIPGEDEfwgRGVSycatcDGPFF-------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 281 pedfvdmKGKRVVVLGGGDTAMD--CNRTSIrqgAKSVTCAYRRDE-ANMPGSRKEVKNAkeEGVKFLYNRQPIAIVGED 357
Cdd:TIGR01292 139 -------KNKEVAVVGGGDSAIEeaLYLTRI---AKKVTLVHRRDKfRAEKILLDRLKKN--PKIEFLWNSTVEEIVGDN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 358 KVEGVKVVETrlgapdargrrspepIPGSEEIIPADAVVIAFGFRPSPAPWFEQfsIQTDSQGRVVAPEQgqykHQTSNP 437
Cdd:TIGR01292 207 KVEGVKIKNT---------------VTGEEEELEVDGVFIAIGHEPNTELLKGL--LELDENGYIVTDEG----MRTSVP 265
|
330 340 350
....*....|....*....|....*....|....*
gi 520807339 438 KIFAGGDmVRGSDL--VVTAIFEGRNAAEGILDYL 470
Cdd:TIGR01292 266 GVFAAGD-VRDKGYrqAVTAAGDGCIAALSAERYL 299
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
176-467 |
1.17e-15 |
|
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: 77.54 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 176 VVFDKNPEI-----GGLLTFGIPEFKLEKTVLSNRrEVFTGMGIEFRLNTEV------GKDVTM---EQLlaEYDAVFMG 241
Cdd:COG0446 9 TVIEKGPHHsyqpcGLPYYVGGGIKDPEDLLVRTP-ESFERKGIDVRTGTEVtaidpeAKTVTLrdgETL--SYDKLVLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 242 MGTyTYMKGGFAGEDLPGVH-----DALDFLIANVNrnlgfekspedfvDMKGKRVVVLGGG------DTAMdcnrtsIR 310
Cdd:COG0446 86 TGA-RPRPPPIPGLDLPGVFtlrtlDDADALREALK-------------EFKGKRAVVIGGGpiglelAEAL------RK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 311 QGAKsVTCAYRRDEAnMPGSRKEV-----KNAKEEGVKFLYNRQPIAIVGEDKVegvKVVETrlgapdargrrspepipg 385
Cdd:COG0446 146 RGLK-VTLVERAPRL-LGVLDPEMaalleEELREHGVELRLGETVVAIDGDDKV---AVTLT------------------ 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 386 SEEIIPADAVVIAFGFRPSpAPWFEQFSIQTDSQGRVVAPEQGqykhQTSNPKIFAGGDMVRGSDLVV----------TA 455
Cdd:COG0446 203 DGEEIPADLVVVAPGVRPN-TELAKDAGLALGERGWIKVDETL----QTSDPDVYAAGDCAEVPHPVTgktvyiplasAA 277
|
330
....*....|..
gi 520807339 456 IFEGRNAAEGIL 467
Cdd:COG0446 278 NKQGRVAAENIL 289
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
147-306 |
5.02e-15 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 77.04 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 147 PTGKRVAIIGAGPAGLGCADVLVRG--GVTPVVFDKNPEIGGLLTFGI-PEFKLEKTVLSNRREVFTGMGIEFRLNTEVG 223
Cdd:PLN02852 24 SEPLHVCVVGSGPAGFYTADKLLKAhdGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVTLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 224 KDVTMEQLLAEYDAVFMGMGTYTYMKGGFAGEDLPGVHDALDFlIANVNRNLGFEKSPEDFVDmkGKRVVVLGGGDTAMD 303
Cdd:PLN02852 104 RDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREF-VWWYNGHPDCVHLPPDLKS--SDTAVVLGQGNVALD 180
|
...
gi 520807339 304 CNR 306
Cdd:PLN02852 181 CAR 183
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
150-467 |
2.55e-11 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 65.16 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 150 KRVAIIGAGPAGLGCADVLVRGG----VTpvVFDKnpEIGG-----LLTFGIPEFKLEKTVLSNRREVFTGMGIEFRLNT 220
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDpdgeIT--VIGA--EPHPpynrpPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 221 EV------GKDVTM---EQLlaEYDAVFMGMGTYTYMkGGFAGEDLPGVHdaldflianVNRNLgfekspEDFVDMK--- 288
Cdd:COG1251 78 RVtaidraARTVTLadgETL--PYDKLVLATGSRPRV-PPIPGADLPGVF---------TLRTL------DDADALRaal 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 289 --GKRVVVLGGG----DTAMDCnrtsiRQGAKSVTCAYRRD---EANMP--GSRKEVKNAKEEGVKFLYNRQPIAIVGED 357
Cdd:COG1251 140 apGKRVVVIGGGliglEAAAAL-----RKRGLEVTVVERAPrllPRQLDeeAGALLQRLLEALGVEVRLGTGVTEIEGDD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 358 KVEGVkvvetRLgapdARGRRspepipgseeiIPADAVVIAFGFRPSPApWFEQFSIQTDsqGRVVAPEQGQykhqTSNP 437
Cdd:COG1251 215 RVTGV-----RL----ADGEE-----------LPADLVVVAIGVRPNTE-LARAAGLAVD--RGIVVDDYLR----TSDP 267
|
330 340 350
....*....|....*....|....*....|....*....
gi 520807339 438 KIFAGGD------MVRG---SDLVVTAIFEGRNAAEGIL 467
Cdd:COG1251 268 DIYAAGDcaehpgPVYGrrvLELVAPAYEQARVAAANLA 306
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
152-467 |
3.64e-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: 58.56 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 152 VAIIGAGPAGLGCADVLVRGGVTPVVFDKNPeIGG------------LL-------------TFGI----PEFKLEKtVL 202
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGGtclnvgcipskaLLhaaevahearhaaEFGIsagaPSVDWAA-LM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 203 SNRREVFTGM--GIEFRLNTEvgkDVTmeqllaeydaVFMGMGTytymkggFAGEDLPGVHD-----ALDFLIA-----N 270
Cdd:COG1249 84 ARKDKVVDRLrgGVEELLKKN---GVD----------VIRGRAR-------FVDPHTVEVTGgetltADHIVIAtgsrpR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 271 VNRNLGFEKSP----EDFVDMK--GKRVVVLGGGdtamdcnrtSI---------RQGAKsVTCAYRRDEAnMPGS----R 331
Cdd:COG1249 144 VPPIPGLDEVRvltsDEALELEelPKSLVVIGGG---------YIglefaqifaRLGSE-VTLVERGDRL-LPGEdpeiS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 332 KEVKNA-KEEGVKFLYNRQPIAIvgeDKVEGVKVVETRLGapdargrrspepipGSEEIIPADAVVIAFGFRPSPAPW-F 409
Cdd:COG1249 213 EALEKAlEKEGIDILTGAKVTSV---EKTGDGVTVTLEDG--------------GGEEAVEADKVLVATGRRPNTDGLgL 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 520807339 410 EQFSIQTDSQGRVVAPEQGQykhqTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGIL 467
Cdd:COG1249 276 EAAGVELDERGGIKVDEYLR----TSVPGIYAIGDVTGGPQLAHVASAEGRVAAENIL 329
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
147-322 |
7.25e-09 |
|
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: 57.57 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 147 PTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGG---------------LLTFGIPEFKLEKT--VLSNRREVF 209
Cdd:COG2072 4 TEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpSHLYSLPFFPNWSDdpDFPTGDEIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 210 ---------TGMGIEFRLNTEV------------------GKDVTmeqllaeYDAVFMGMGTYTymKG---GFAGEDLPG 259
Cdd:COG2072 84 ayleayadkFGLRRPIRFGTEVtsarwdeadgrwtvttddGETLT-------ARFVVVATGPLS--RPkipDIPGLEDFA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520807339 260 ---VHDAlDFlianvnrnlgfeKSPEDFvdmKGKRVVVLGGGDTAMDCnRTSIRQGAKSVTCAYRR 322
Cdd:COG2072 155 geqLHSA-DW------------RNPVDL---AGKRVLVVGTGASAVQI-APELARVAAHVTVFQRT 203
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
151-199 |
1.33e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 56.82 E-value: 1.33e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 520807339 151 RVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLL-TFGIPEFKLEK 199
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIER 50
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
150-186 |
2.37e-08 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 55.65 E-value: 2.37e-08
10 20 30
....*....|....*....|....*....|....*..
gi 520807339 150 KRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGG 186
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
150-188 |
7.62e-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: 54.45 E-value: 7.62e-08
10 20 30
....*....|....*....|....*....|....*....
gi 520807339 150 KRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLL 188
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
150-187 |
8.97e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 54.51 E-value: 8.97e-08
10 20 30
....*....|....*....|....*....|....*...
gi 520807339 150 KRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGL 187
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
291-367 |
1.32e-07 |
|
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: 48.74 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 291 RVVVLGGGDTAMDCNrTSIRQGAKSVTCAYRRDEAnMPGSRKEV-----KNAKEEGVKFLYNRQPIAIVGEDKVEGVKVV 365
Cdd:pfam00070 1 RVVVVGGGYIGLELA-GALARLGSKVTVVERRDRL-LPGFDPEIakilqEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
..
gi 520807339 366 ET 367
Cdd:pfam00070 79 DG 80
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
150-470 |
6.05e-07 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 51.29 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 150 KRVAIIGAGPAGLGCADVL---VRGGVTPVVFDKNPE----------IGGLLTFGipefklekTVLSNRREVFTGMGIEF 216
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLrkkLGGDAEVTLIDPNPYhlfqpllpevAAGTLSPD--------DIAIPLRELLRRAGVRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 217 RL-------------NTEVGKDVtmeqllaEYDAVFMGMGTYTYMKG--GFAgEDLPG---VHDALDFlianvnRNLgFE 278
Cdd:COG1252 74 IQgevtgidpeartvTLADGRTL-------SYDYLVIATGSVTNFFGipGLA-EHALPlktLEDALAL------RER-LL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 279 KSPEDFVDMKGKRVVVLGGGDT------AMD------CNRTSIRQGAKSVTCAYRRDEAnMPGSRKEVKNA-----KEEG 341
Cdd:COG1252 139 AAFERAERRRLLTIVVVGGGPTgvelagELAellrklLRYPGIDPDKVRITLVEAGPRI-LPGLGEKLSEAaekelEKRG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 342 VKFLYNRqPIAIVGEDKVegvkVVEtrlgapdargrrspepipgSEEIIPADAVVIAFGFRPSpaPWFEQFSIQTDSQGR 421
Cdd:COG1252 218 VEVHTGT-RVTEVDADGV----TLE-------------------DGEEIPADTVIWAAGVKAP--PLLADLGLPTDRRGR 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 520807339 422 VVAPEQGQYkhqTSNPKIFAGGDMVRGSD--------LVVTAIFEGRNAAEGILDYL 470
Cdd:COG1252 272 VLVDPTLQV---PGHPNVFAIGDCAAVPDpdgkpvpkTAQAAVQQAKVLAKNIAALL 325
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
144-222 |
1.66e-06 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 50.11 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 144 KVKPTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDK--------------------NPE------IGG----------- 186
Cdd:COG2509 25 GIPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLERgkdveertcpvaefwrkgkcNPEsniqfgEGGagtfsdgklnt 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520807339 187 ---------------LLTFGIPE------------FKLeKTVLSNRREVFTGMGIEFRLNTEV 222
Cdd:COG2509 105 rskdpqgliryvleiFVKFGAPEeilyaakphigtDKL-PKVVKNIREYIEELGGEIRFNTRV 166
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
147-186 |
2.70e-06 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 49.53 E-value: 2.70e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 520807339 147 PTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGG 186
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
151-243 |
6.21e-06 |
|
adrenodoxin reductase; Provisional
Pssm-ID: 240308 Cd Length: 506 Bit Score: 48.73 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 151 RVAIIGAGPAGLGCADVLVRGGVTPV-VFDKNPEIGGLLTFGI-PEFKLEKTVLSNRREVFTGMGIEFRLNTEVGKDVTM 228
Cdd:PTZ00188 41 KVGIIGAGPSALYCCKHLLKHERVKVdIFEKLPNPYGLIRYGVaPDHIHVKNTYKTFDPVFLSPNYRFFGNVHVGVDLKM 120
|
90
....*....|....*
gi 520807339 229 EQLLAEYDAVFMGMG 243
Cdd:PTZ00188 121 EELRNHYNCVIFCCG 135
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
159-404 |
1.03e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 47.22 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 159 PAGLGCADVLVRGGVTPVV----------FDKNPEIGGLLT-------FGIPE-----------FKLEKTVLSNR----- 205
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDYLilekgnignsFYRYPTHMTFFSpsftsngFGIPDlnaispgtspaFTFNREHPSGNeyaey 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 206 -REVFTGMGIEFRLNTEVgKDVTMEQLL-------AEYDA--VFMGMGTYTYmkggfagEDLPGVHDaldflIANVNRNL 275
Cdd:pfam13738 81 lRRVADHFELPINLFEEV-TSVKKEDDGfvvttskGTYQAryVIIATGEFDF-------PNKLGVPE-----LPKHYSYV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 276 gfekspEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKsVTCAYRRDEANMPGSRKE--VKNAKEEGVKFLYNRQPIAI 353
Cdd:pfam13738 148 ------KDFHPYAGQKVVVIGGYNSAVDAALELVRKGAR-VTVLYRGSEWEDRDSDPSysLSPDTLNRLEELVKNGKIKA 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 520807339 354 VGEDKVEGVKVVET--RLGAPDARgrrspepipgseEIIPADAVVIAFGFRPS 404
Cdd:pfam13738 221 HFNAEVKEITEVDVsyKVHTEDGR------------KVTSNDDPILATGYHPD 261
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
147-463 |
1.41e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 47.55 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 147 PTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGL---LTFGIPEFKLEKTVLS-NRREVFTGMGIEFRLNTEV 222
Cdd:COG1148 138 PVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDCPQCILEpLIAEVEANPNITVYTGAEV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 223 GK--------DVTMEQ-------------LLA----EYDAVfmGMGTYTYmkggfaGEDlPGVHDALDF--LIANvnrnl 275
Cdd:COG1148 218 EEvsgyvgnfTVTIKKgpreeieievgaiVLAtgfkPYDPT--KLGEYGY------GKY-PNVITNLELerLLAA----- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 276 GFEKSPEDFvdMKGKRVVVL---GGGDTAMD---CNR----TSIRQ---------GAKsVTCAYR--RdeanMPGSRKE- 333
Cdd:COG1148 284 GKILRPSDG--KEPKSVAFIqcvGSRDEENGlpyCSRvccmYALKQalylkeknpDAD-VYIFYRdiR----TYGKYEEf 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 334 VKNAKEEGVKFL-YNRQPIAIVGEDKVEgVKVVETRLGapdargrrspEPIpgseeIIPADAVVIAFGFRPSPA--PWFE 410
Cdd:COG1148 357 YRRAREDGVRFIrGRVAEIEEDEGGKLV-VTVEDTLLG----------EPV-----EIEADLVVLATGMVPSEDneELAK 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 520807339 411 QFSIQTDSQGRVVAPEQGQYKHQTSNPKIFAGGdMVRGSDLVVTAIFEGRNAA 463
Cdd:COG1148 421 LLKLPLDQDGFFLEAHPKLRPVETATDGIFLAG-AAHGPKDIPESIAQATAAA 472
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
154-198 |
2.05e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 42.13 E-value: 2.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 520807339 154 IIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLL-TFGIPEFKLE 198
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAySYRVPGYVFD 46
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
149-183 |
2.51e-05 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 46.61 E-value: 2.51e-05
10 20 30
....*....|....*....|....*....|....*
gi 520807339 149 GKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPE 183
Cdd:COG0771 4 GKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPA 38
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
150-444 |
3.63e-05 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 46.19 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 150 KRVAIIGAGPAGLGCADVLVRggVTP----VVFDKNPEIG----GLLTFGIPEFKLEKTVLSNRREVFTGMGIEFRLNTE 221
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKR--LNKeleiTVYEKTDIVSfgacGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 222 VGK-DVTMEQLLAE-----------YDAVFMGMGTYTYMKGgFAGEDLPGVHDALDFLIANVNRNLgfekspedFVDMKG 289
Cdd:PRK09564 79 VVKvDAKNKTITVKnlktgsifndtYDKLMIATGARPIIPP-IKNINLENVYTLKSMEDGLALKEL--------LKDEEI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 290 KRVVVLGGGDTAMDCNRTSIRQGaKSVTcAYRRDEANMPGS-RKEVKNAKEE-----GVKFLYNRQPIAIVGEDKVEGVK 363
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLG-KNVR-IIQLEDRILPDSfDKEITDVMEEelrenGVELHLNEFVKSLIGEDKVEGVV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 364 VVETRlgapdargrrspepipgseeiIPADAVVIAFGFRPSpAPWFEQFSIQTDSQGRVVAPEQGqykhQTSNPKIFAGG 443
Cdd:PRK09564 228 TDKGE---------------------YEADVVIVATGVKPN-TEFLEDTGLKTLKNGAIIVDEYG----ETSIENIYAAG 281
|
.
gi 520807339 444 D 444
Cdd:PRK09564 282 D 282
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
153-185 |
4.11e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 45.81 E-value: 4.11e-05
10 20 30
....*....|....*....|....*....|...
gi 520807339 153 AIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIG 185
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
148-186 |
4.40e-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: 45.62 E-value: 4.40e-05
10 20 30
....*....|....*....|....*....|....*....
gi 520807339 148 TGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGG 186
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
148-187 |
4.81e-05 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 45.62 E-value: 4.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 520807339 148 TGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGL 187
Cdd:PLN02172 9 NSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGL 48
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
150-185 |
7.03e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 44.88 E-value: 7.03e-05
10 20 30
....*....|....*....|....*....|....*.
gi 520807339 150 KRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIG 185
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
150-218 |
9.95e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.84 E-value: 9.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520807339 150 KRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLL-TFGIPEFKLEK--TVLSNR---REVFTGMGIEFRL 218
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRArTFERPGFRFDVgpSVLTMPgvlERLFRELGLEDYL 78
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
150-185 |
1.18e-04 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 44.56 E-value: 1.18e-04
10 20 30
....*....|....*....|....*....|....*....
gi 520807339 150 KRVAIIGAGPAGLGCADVLVRGGVTP---VVFDKNPEIG 185
Cdd:COG4529 6 KRIAIIGGGASGTALAIHLLRRAPEPlriTLFEPRPELG 44
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
152-469 |
2.08e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 43.63 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 152 VAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLTFG-IPEfkleKTVLS-----NRREVFTGMGIEF--------- 216
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGcIPS----KALIAaaeafHEAKHAEEFGIHAdgpkidfkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 217 ---RLNTEVGKDVTM-EQLLAEYDAV--FMGMGTytymkggFAGEDLPGVHD----ALDFLIANVNRNLGFEKSPE---- 282
Cdd:PRK06292 82 vmaRVRRERDRFVGGvVEGLEKKPKIdkIKGTAR-------FVDPNTVEVNGerieAKNIVIATGSRVPPIPGVWLilgd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 283 DFVDMKG--------KRVVVLGGGdtamdcnrtSI---------RQGAKsVTCAYRRDEAnMPGSRKEVKNA------KE 339
Cdd:PRK06292 155 RLLTSDDafeldklpKSLAVIGGG---------VIglelgqalsRLGVK-VTVFERGDRI-LPLEDPEVSKQaqkilsKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 340 egVKFLYNRQPIAIvgeDKVEGVKVVETRLGapdargrrspepipGSEEIIPADAVVIAFGFRP-SPAPWFEQFSIQTDS 418
Cdd:PRK06292 224 --FKIKLGAKVTSV---EKSGDEKVEELEKG--------------GKTETIEADYVLVATGRRPnTDGLGLENTGIELDE 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 520807339 419 QGRVVAPEqgqyKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRNAAEGILDY 469
Cdd:PRK06292 285 RGRPVVDE----HTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGD 331
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
148-222 |
2.47e-04 |
|
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: 42.88 E-value: 2.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520807339 148 TGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPeigGLLTFGIPEF--KLEKtvlsnrreVFTGMGIEFRLNTEV 222
Cdd:COG0446 123 KGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAP---RLLGVLDPEMaaLLEE--------ELREHGVELRLGETV 188
|
|
| FMO-like |
pfam00743 |
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ... |
149-190 |
3.11e-04 |
|
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases.
Pssm-ID: 395602 [Multi-domain] Cd Length: 531 Bit Score: 43.23 E-value: 3.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 520807339 149 GKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLTF 190
Cdd:pfam00743 1 AKKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRF 42
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
151-185 |
4.78e-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: 42.23 E-value: 4.78e-04
10 20 30
....*....|....*....|....*....|....*
gi 520807339 151 RVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIG 185
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| Tdh |
COG1063 |
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ... |
141-183 |
1.19e-03 |
|
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440683 [Multi-domain] Cd Length: 341 Bit Score: 40.89 E-value: 1.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 520807339 141 DMSKVKPtGKRVAIIGAGPAGLGCADVLVRGGVTPV-VFDKNPE 183
Cdd:COG1063 155 ERAGVKP-GDTVLVIGAGPIGLLAALAARLAGAARViVVDRNPE 197
|
|
| AdhP |
COG1064 |
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ... |
133-183 |
1.63e-03 |
|
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];
Pssm-ID: 440684 [Multi-domain] Cd Length: 332 Bit Score: 40.48 E-value: 1.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 520807339 133 AFAMGWRP-DMSKVKPtGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPE 183
Cdd:COG1064 147 AGITAYRAlRRAGVGP-GDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPE 197
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
153-185 |
1.69e-03 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 40.66 E-value: 1.69e-03
10 20 30
....*....|....*....|....*....|...
gi 520807339 153 AIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIG 185
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
|
|
| Malic_M |
smart00919 |
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ... |
148-210 |
1.78e-03 |
|
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.
Pssm-ID: 214912 Cd Length: 231 Bit Score: 39.71 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520807339 148 TGK-----RVAIIGAGPAGLGCADVLVRGGVTP---VVFDKNpeigGLLTFG----IPEFKLEKTVLSNRREVFT 210
Cdd:smart00919 19 TGKkledqRIVVNGAGAAGIGIAKLLVAAGVKRkniWLVDSK----GLLTKGrednLNPYKKPFARKTNERETGT 89
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
151-186 |
2.06e-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: 40.07 E-value: 2.06e-03
10 20 30
....*....|....*....|....*....|....*.
gi 520807339 151 RVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGG 186
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
144-183 |
2.07e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 38.64 E-value: 2.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 520807339 144 KVKPTgkRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPE 183
Cdd:smart01002 17 GVPPA--KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPA 54
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
151-222 |
3.30e-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: 36.41 E-value: 3.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520807339 151 RVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLTFGIPEFKLEKtvlsnrrevFTGMGIEFRLNTEV 222
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEK---------LEKNGIEFLLNTTV 63
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
148-186 |
4.13e-03 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 39.33 E-value: 4.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 520807339 148 TGKRVAIIGAGPAGLGCA-------DVlvrggvtpVVFDKNPEIGG 186
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAwllsrrhDV--------TLFEANDRLGG 39
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
149-186 |
5.03e-03 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 39.47 E-value: 5.03e-03
10 20 30
....*....|....*....|....*....|....*...
gi 520807339 149 GKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGG 186
Cdd:PLN02976 693 RKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
146-183 |
5.96e-03 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 38.96 E-value: 5.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 520807339 146 KPTGK--RVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPE 183
Cdd:PLN00093 34 KLSGRklRVAVIGGGPAGACAAETLAKGGIETFLIERKLD 73
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
144-243 |
6.47e-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: 400379 [Multi-domain] Cd Length: 301 Bit Score: 38.45 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520807339 144 KVKPTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGglltfgiPEFKLEktvLSNR-REVFTGMGIEFRLNTEV 222
Cdd:pfam07992 147 RLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLL-------RAFDEE---ISAAlEKALEKNGVEVRLGTSV 216
|
90 100 110
....*....|....*....|....*....|
gi 520807339 223 ----GKDVTMEQLLAE-----YDAVFMGMG 243
Cdd:pfam07992 217 keiiGDGDGVEVILKDgteidADLVVVAIG 246
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
128-183 |
9.06e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 38.12 E-value: 9.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 520807339 128 YITDTAFAMGWRPDMSKVKPTGKRVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPE 183
Cdd:COG0569 74 LFGGLLEALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPE 129
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
151-184 |
9.08e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 38.13 E-value: 9.08e-03
10 20 30
....*....|....*....|....*....|....
gi 520807339 151 RVAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEI 184
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
152-191 |
9.53e-03 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 38.36 E-value: 9.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 520807339 152 VAIIGAGPAGLGCADVLVRGGVTPVVFDKNPEIGGLLTFG 191
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSG 41
|
|
| |
