|
Name |
Accession |
Description |
Interval |
E-value |
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
14-477 |
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: 804.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 14 FQFIEVGRKDPKKKLLRQRKREFVEIHDLFKPQQAADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVSEGNILAAAELSH 93
Cdd:TIGR01318 1 FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 94 QTNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDLSKVKPTGRRVAVIGAGPAGLGCADVL 173
Cdd:TIGR01318 81 QTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 174 VRNGVTPVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYTYM 253
Cdd:TIGR01318 161 ARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRSM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 254 KGGFPGEDLPGVHDALDFLIANVNRNLGFEKSAED-FVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEENM 332
Cdd:TIGR01318 241 RGGLPGEDAPGVLPALPFLIANTRQLMGLPEEPEEpLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 333 PGSRKEVKNAKEEGVKFLFNRQPIAIVGED--RVEGVKVVETRLGEPDARGRRSPEPIPGSEEIIPAEAVLIAFGFRPSP 410
Cdd:TIGR01318 321 PGSRREVANAREEGVEFLFNVQPVSIESDEdgQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489186414 411 APWFERFEIATDSQGRVVAPAQAQFKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGILDYLGV 477
Cdd:TIGR01318 401 MPWLAAHGITLDSWGRIITALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV 467
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
12-477 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 801.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 12 NDFQFIEVGRKDPKKKLLRQRKREFVEIHDLFKPQQAADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVSEGNILAAAEL 91
Cdd:PRK12810 3 KPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 92 SHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDLSKVKPTGRRVAVIGAGPAGLGCAD 171
Cdd:PRK12810 83 LHQTNNFPEFTGRVCPAP--CEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGSGPAGLAAAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 172 VLVRNGVTPVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYT 251
Cdd:PRK12810 161 QLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAYK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 252 YMKGGFPGEDLPGVHDALDFLIANVNRNLGFEKsaEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTcayRRDEEN 331
Cdd:PRK12810 241 PRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDET--EPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVT---QRDIMP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 332 MPGSRK-------------EVKNAKEEGVKFLFNRQPIAIVGED-RVEGVKVVETRLGEPDargrrsPEPIPGSEEIIPA 397
Cdd:PRK12810 316 MPPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEGENgKVTGVKVVRTELGEGD------FEPVEGSEFVLPA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 398 EAVLIAFGFRPSPAPWFERFEIATDSQGRVVAPaqaQFKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGILDYLGV 477
Cdd:PRK12810 390 DLVLLAMGFTGPEAGLLAQFGVELDERGRVAAP---DNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMG 466
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
21-477 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 775.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 21 RKDPKKKLLRQRKREFVEIHDLFKPQQAADQAHRCLGCGN-PYCEWKCPVHNFIPNWLKLVSEGNILAAAELSHQTNTLP 99
Cdd:PRK12769 193 RGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 100 EVCGRVCPQDRLCEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDLSKVKPTGRRVAVIGAGPAGLGCADVLVRNGVT 179
Cdd:PRK12769 273 EITGRVCPQDRLCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNGVA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 180 PVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYTYMKGGFPG 259
Cdd:PRK12769 353 VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLPN 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 260 EDLPGVHDALDFLIANVNRNLGFEKSA-EDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEENMPGSRKE 338
Cdd:PRK12769 433 EDAPGVYDALPFLIANTKQVMGLEELPeEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 339 VKNAKEEGVKFLFNRQPIAIVGED--RVEGVKVVETRLGEPDARGRRSPEPIPGSEEIIPAEAVLIAFGFRPSPAPWFER 416
Cdd:PRK12769 513 VKNAREEGANFEFNVQPVALELNEqgHVCGIRFLRTRLGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGFNPHGMPWLES 592
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489186414 417 FEIATDSQGRVVAPAQAQFKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGILDYLGV 477
Cdd:PRK12769 593 HGVTVDKWGRIIADVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLGV 653
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
32-474 |
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: 667.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 32 RKREFVEIHDLFKPQQAADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVSEGNILAAAELSHQTNTLPEVCGRVCPqdRL 111
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--AP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 112 CEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDLSKVKPTGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGG 191
Cdd:COG0493 79 CEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 192 LLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYTYMKGGFPGEDLPGVHDALDF 271
Cdd:COG0493 159 LLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 272 LIAnVNRNLgfeksAEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEENMPGSRKEVKNAKEEGVKFLF 351
Cdd:COG0493 239 LTA-VNLGE-----APDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 352 NRQPIAIVGED--RVEGVKVVETRLGEPDARGRRSPEPIPGSEEIIPAEAVLIAFGFRPSPAPWFERFEIATDSQGRVVA 429
Cdd:COG0493 313 LVAPVEIIGDEngRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 489186414 430 PAQAQfkhQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGILDY 474
Cdd:COG0493 393 DEETY---QTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
21-472 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 593.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 21 RKDPKKKLLRQRKREFVEIHDLFKPQQAADQAHRCLGCGN-PYCEWKCPVHNFIPNWLKLVSEGNILAAAELSHQTNTLP 99
Cdd:PRK12809 176 RKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 100 EVCGRVCPQDRLCEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDLSKVKPTGRRVAVIGAGPAGLGCADVLVRNGVT 179
Cdd:PRK12809 256 EICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 180 PVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYTYMKGGFPG 259
Cdd:PRK12809 336 VDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPH 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 260 EDLPGVHDALDFLIANVNRNLGFEKSAE-DFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEENMPGSRKE 338
Cdd:PRK12809 416 EDAPGVIQALPFLTAHTRQLMGLPESEEyPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 339 VKNAKEEGVKFLFNRQPIAIVGED--RVEGVKVVETRLGEPDARGRRSPEPIPGSEEIIPAEAVLIAFGFRPSPAPWFER 416
Cdd:PRK12809 496 VVNAREEGVEFQFNVQPQYIACDEdgRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQG 575
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489186414 417 FEIATDSQGRVVAPAQAQFKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGIL 472
Cdd:PRK12809 576 SGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDML 631
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
15-475 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 583.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 15 QFIEVGRKDPKKKLLRQRKREFVEIHDLFKPQQAADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVSEGNILAAAELSHQ 94
Cdd:PRK11749 2 KFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 95 TNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRPdLSKVKPTGRRVAVIGAGPAGLGCADVLV 174
Cdd:PRK11749 82 TNPLPAVCGRVCPQERLCEGACVRGKKGEPVAIGRLERYITDWAMETGWVL-FKRAPKTGKKVAVIGAGPAGLTAAHRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 175 RNGVTPVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYTYMK 254
Cdd:PRK11749 161 RKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 255 GGFPGEDLPGVHDALDFLiANVNRnlgfekSAEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEENMPG 334
Cdd:PRK11749 241 LGIPGENLGGVYSAVDFL-TRVNQ------AVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 335 SRKEVKNAKEEGVKFLFNRQPIAIVGED-RVEGVKVVETRLGEPDARGRRSpEPIPGSEEIIPAEAVLIAFGFRPSPAPW 413
Cdd:PRK11749 314 SEEEVEHAKEEGVEFEWLAAPVEILGDEgRVTGVEFVRMELGEPDASGRRR-VPIEGSEFTLPADLVIKAIGQTPNPLIL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489186414 414 FERFEIATDSQGRVVApaqAQFKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGILDYL 475
Cdd:PRK11749 393 STTPGLELNRWGTIIA---DDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYL 451
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
21-475 |
8.03e-124 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 368.96 E-value: 8.03e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 21 RKDPKKKL------LRQRKREFVEIHDLFKPQQAADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVSEGNILAAAELSHQ 94
Cdd:PRK12831 2 MKDRKKRVpvreqdPEVRATNFEEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 95 TNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDLSKVKPtGRRVAVIGAGPAGLGCADVLV 174
Cdd:PRK12831 82 YNALPAVCGRVCPQESQCEGKCVLGIKGEPVAIGKLERFVADWARENGIDLSETEEKK-GKKVAVIGSGPAGLTCAGDLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 175 RNGVTPVVFDRNPEIGGLLTFGIPEFKLEK-HVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDE--YDAVFMGMGTYT 251
Cdd:PRK12831 161 KMGYDVTIFEALHEPGGVLVYGIPEFRLPKeTVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFDAVFIGSGAGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 252 YMKGGFPGEDLPGVHDALDFLIANvnrNLGfeKSAEDFVD---MKGKRVVVLGGGDTAMDCNRTSIRQGAKsVTCAYRRD 328
Cdd:PRK12831 241 PKFMGIPGENLNGVFSANEFLTRV---NLM--KAYKPEYDtpiKVGKKVAVVGGGNVAMDAARTALRLGAE-VHIVYRRS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 329 EENMPGSRKEVKNAKEEGVKFLFNRQPIAIVGED--RVEGVKVVETRLGEPDARGRRSPEPIPGSEEIIPAEAVLIAFGF 406
Cdd:PRK12831 315 EEELPARVEEVHHAKEEGVIFDLLTNPVEILGDEngWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489186414 407 RPSPAPWFERFEIATDSQGRVVAPAQAQfkhQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGILDYL 475
Cdd:PRK12831 395 SPNPLISSTTKGLKINKRGCIVADEETG---LTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYL 460
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
16-475 |
1.98e-120 |
|
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: 361.07 E-value: 1.98e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 16 FIEVGRKDPKKKLLRQRKREFVEIHDLFKPQQAADQAHRCLGCGNPYC--EWKCPVHNFIPNWLKLVSEGNILAAAELSH 93
Cdd:TIGR01317 5 FLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFChnDSGCPLNNLIPEFNDLVFRGRWKEALDRLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 94 QTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGSVEKYITDTAFAMGW-RPDLSKVKpTGRRVAVIGAGPAGLGCADV 172
Cdd:TIGR01317 85 ATNNFPEFTGRVCPAP--CEGACTLGISEDPVGIKSIERIIIDKGFQEGWvQPRPPSKR-TGKKVAVVGSGPAGLAAADQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 173 LVRNGVTPVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYTY 252
Cdd:TIGR01317 162 LNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATKP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 253 MKGGFPGEDLPGVHDALDFLIANVNRNLGFEKSAEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTcayrrDEENM 332
Cdd:TIGR01317 242 RDLPIPGRELKGIHYAMEFLPSATKALLGKDFKDIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVH-----QFEIM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 333 PGSRKE---------------VKNAKEEGvKFLFNRQP-------IAIVGED--RVEGVKVVETRLgEPDARGRRSPEPI 388
Cdd:TIGR01317 317 PKPPEArakdnpwpewprvyrVDYAHEEA-AAHYGRDPreysiltKEFIGDDegKVTALRTVRVEW-KKSQDGKWQFVEI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 389 PGSEEIIPAEAVLIAFGFRPSPAPWFERFEIATDSQGRVVApaqAQFKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAA 468
Cdd:TIGR01317 395 PGSEEVFEADLVLLAMGFVGPEQILLDDFGVKKTRRGNISA---GYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAA 471
|
....*..
gi 489186414 469 EGILDYL 475
Cdd:TIGR01317 472 AAVDRYL 478
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
30-475 |
2.08e-114 |
|
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: 344.16 E-value: 2.08e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 30 RQRKREFVEIHDLFKPQQAADQAHRCLGCGNPY--CEWKCPVHNFIPNWLKLVSEGNILAAAELSHQTNTLPEVCGRVCP 107
Cdd:TIGR01316 3 EERSKLFQEAALGYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVCP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 108 QDRLCEGACTLNDGFG----AVTIGSVEKYITDTAFAMGWRPDLSKVKPTGRRVAVIGAGPAGLGCADVLVRNGVTPVVF 183
Cdd:TIGR01316 83 QERQCEGQCTVGKMFKdvgkPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVTVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 184 DRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYTYMKGGFPGEDLP 263
Cdd:TIGR01316 163 EALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEELC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 264 GVHDALDFLIaNVNRNLGFEKSAEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKsVTCAYRRDEENMPGSRKEVKNAK 343
Cdd:TIGR01316 243 GVYSANDFLT-RANLMKAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGAE-VHCLYRRTREDMTARVEEIAHAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 344 EEGVKFLFNRQPIAIVGED--RVEGVKVVETRLGEPDARGRRSPEPIPGSEEIIPAEAVLIAFGFRPSPAPwFERFEIAT 421
Cdd:TIGR01316 321 EEGVKFHFLCQPVEIIGDEegNVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPIM-AETTRLKT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 489186414 422 DSQGRVVAPAqaqfKHQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGILDYL 475
Cdd:TIGR01316 400 SERGTIVVDE----DQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
18-475 |
2.67e-114 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 353.66 E-value: 2.67e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 18 EVGRKD--PKKKLLRQRKRE------------FVEIHDLFKPQQAADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVSEG 83
Cdd:PRK12778 280 AELRKSmkPKERTAIERVPMpeldpeyrahnrFEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 84 NILAAAELSHQTNTLPEVCGRVCPQDRLCEGACT-LNDGFGAVTIGSVEKYITDTAFAMGwRPDLSKVKP-TGRRVAVIG 161
Cdd:PRK12778 360 NFLEAAKILKETSALPAVCGRVCPQEKQCESKCIhGKMGEEAVAIGYLERFVADYERESG-NISVPEVAEkNGKKVAVIG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 162 AGPAGLGCADVLVRNGVTPVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDE-Y 240
Cdd:PRK12778 439 SGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEgF 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 241 DAVFM--GMGTYTYMkgGFPGEDLPGVHDALDFLiANVNRNLGFEKSAEDFVDMkGKRVVVLGGGDTAMDCNRTSIRQGA 318
Cdd:PRK12778 519 KGIFIasGAGLPNFM--NIPGENSNGVMSSNEYL-TRVNLMDAASPDSDTPIKF-GKKVAVVGGGNTAMDSARTAKRLGA 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 319 KSVTCAYRRDEENMPGSRKEVKNAKEEGVKFLFNRQPIAIVGED--RVEGVKVVETRLGEPDARGRRSPEPIPGSEEIIP 396
Cdd:PRK12778 595 ERVTIVYRRSEEEMPARLEEVKHAKEEGIEFLTLHNPIEYLADEkgWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVD 674
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489186414 397 AEAVLIAFGFRPSPAPWFERFEIATDSQGRVVAPAQAqfkhQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGILDYL 475
Cdd:PRK12778 675 VDLVIVSVGVSPNPLVPSSIPGLELNRKGTIVVDEEM----QSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYL 749
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
61-476 |
2.52e-108 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 332.61 E-value: 2.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 61 PYCEWKCPVHNFIPNWLKLVSEGNILAAAELSHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGSVEKYITDTAFA 140
Cdd:PRK12771 47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCNRGQVDDAVGINAVERFLGDYAIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 141 MGWRPDLSKVkPTGRRVAVIGAGPAGLGCADVLVRNG--VTpvVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMG 218
Cdd:PRK12771 125 NGWKFPAPAP-DTGKRVAVIGGGPAGLSAAYHLRRMGhaVT--IFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 219 IEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYTYMKGGFPGEDLPGVHDALDFLianvnRNLGfeksaEDFVDMKGKRVV 298
Cdd:PRK12771 202 VEVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFL-----RAVG-----EGEPPFLGKRVV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 299 VLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEENMPGSRKEVKNAKEEGVKFLFNRQPIAI-VGEDRVEGVKVVETRLGEP 377
Cdd:PRK12771 272 VIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIeGDENGATGLRVITVEKMEL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 378 DARGRrsPEPIPGSEEIIPAEAVLIAFG----FRPspapwFERFEIATDSQGRVVAPAQAQFkhqTSNPKIFAGGDMVRG 453
Cdd:PRK12771 352 DEDGR--PSPVTGEEETLEADLVVLAIGqdidSAG-----LESVPGVEVGRGVVQVDPNFMM---TGRPGVFAGGDMVPG 421
|
410 420
....*....|....*....|...
gi 489186414 454 SDLVVTAIFEGRTAAEGILDYLG 476
Cdd:PRK12771 422 PRTVTTAIGHGKKAARNIDAFLG 444
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
52-476 |
5.53e-93 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 295.48 E-value: 5.53e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 52 AHRCLGCGNPyCEWKCPVHNFIPNWLKLVSEGNILAAAELSHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGSVE 131
Cdd:PRK12814 94 EQHCGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDEPVSICALK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 132 KYITDTAFAMGWRPDLSKVKPTGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRR 211
Cdd:PRK12814 171 RYAADRDMESAERYIPERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 212 EVFTGMGIEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYTYMKGGFPGEDLPGVHDALDFLianvnrnlgfEKSAEDFVD 291
Cdd:PRK12814 251 APLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFL----------RNVALGTAL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 292 MKGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEENMPGSRKEVKNAKEEGVKFLFNRQPIAI-VGEDRVEgVKVV 370
Cdd:PRK12814 321 HPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIeRSEGGLE-LTAI 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 371 ETRLGEPDARGRRSPEPIPGSEEIIPAEAVLIAFGFRPSPaPWFERFEIATDSQGRVVAPAQAQfkhQTSNPKIFAGGDM 450
Cdd:PRK12814 400 KMQQGEPDESGRRRPVPVEGSEFTLQADTVISAIGQQVDP-PIAEAAGIGTSRNGTVKVDPETL---QTSVAGVFAGGDC 475
|
410 420
....*....|....*....|....*.
gi 489186414 451 VRGSDLVVTAIFEGRTAAEGILDYLG 476
Cdd:PRK12814 476 VTGADIAINAVEQGKRAAHAIDLFLN 501
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
148-475 |
4.73e-90 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 278.41 E-value: 4.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 148 SKVKPTGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEI 227
Cdd:PRK12770 12 EKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTKV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 228 ---------------GKDVTMEQLLDEYDAVFMGMGTYTYMKGGFPGEDLPGVHDALDFLIANVNRNLGFEKSAEDFvDM 292
Cdd:PRK12770 92 ccgeplheeegdefvERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRIRAAKLGYLPWEKVP-PV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 293 KGKRVVVLGGGDTAMDCNRTSIRQGAKSVTCAYRRDEENMPGSRKEVKNAKEEGVKFLFNRQPIAIVGEDRVEGVKVVET 372
Cdd:PRK12770 171 EGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIGEGRVEGVELAKM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 373 RLGEPDARGRRSPEPIPGSEEIIPAEAVLIAFGFRPSPAPWFERFEIATDSQGRVVAPAqaqfKHQTSNPKIFAGGDMVR 452
Cdd:PRK12770 251 RLGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDE----KHMTSREGVFAAGDVVT 326
|
330 340
....*....|....*....|...
gi 489186414 453 GSDLVVTAIFEGRTAAEGILDYL 475
Cdd:PRK12770 327 GPSKIGKAIKSGLRAAQSIHEWL 349
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
8-475 |
3.39e-89 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 293.00 E-value: 3.39e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 8 DRLNNDF--------QFIEVGRKDPKK-------------KLLRQRKREFVEIHDLFKPQQAADQAHRCLGCGNPYCEWK 66
Cdd:PRK12775 265 DRANEDYahvcnlekQLFEEGKRNYKKlktlvphqtpmpeRDAVERARNFKEVNLGYSLEDALQEAERCIQCAKPTCIAG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 67 CPVHNFIPNWLKLVSEGNILAAAELSHQTNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRP- 145
Cdd:PRK12775 345 CPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQCIIAKKHESVGIGRLERFVGDNARAKPVKPp 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 146 DLSKvkpTGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNT 225
Cdd:PRK12775 425 RFSK---KLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNK 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 226 EIGKDVTMEQLLDE--YDAVFMGMGTYTYMKGGFPGEDLPGVHDALDFLiANVNRNLGFEKSAEDFVDMKGKRVVVLGGG 303
Cdd:PRK12775 502 VIGKTFTVPQLMNDkgFDAVFLGVGAGAPTFLGIPGEFAGQVYSANEFL-TRVNLMGGDKFPFLDTPISLGKSVVVIGAG 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 304 DTAMDCNRTSIRQGAKSVTCAYRRDEENMPGSRKEVKNAKEEGVKFLFNRQPIAIV--GEDRVEGVKVVETRLGEPDARG 381
Cdd:PRK12775 581 NTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGIDFFFLHSPVEIYvdAEGSVRGMKVEEMELGEPDEKG 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 382 RRSPEPIPGSEEiIPAEAVLIAFGFRPSPAPWFERFEIATDSQGRVVAPAQAQFKHQTSN-PKIFAGGDMVRGSDLVVTA 460
Cdd:PRK12775 661 RRKPMPTGEFKD-LECDTVIYALGTKANPIITQSTPGLALNKWGNIAADDGKLESTQSTNlPGVFAGGDIVTGGATVILA 739
|
490
....*....|....*
gi 489186414 461 IFEGRTAAEGILDYL 475
Cdd:PRK12775 740 MGAGRRAARSIATYL 754
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
31-475 |
2.84e-77 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 252.77 E-value: 2.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 31 QRKREFVEIHDLFKPQQAADQAHRCLGCGnpYCEWKCPVHNFIPNWLKLVSEGNILAAAELSHQTNTLPEVCGRVCPQDr 110
Cdd:PRK13984 163 ERVKSFIEIVKGYSKEQAMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVCTHK- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 111 lCEGACTLNDGFGAVTIGSVEKYITDTAFAMGWRPDLS-KVKPTGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEI 189
Cdd:PRK13984 240 -CETVCSIGHRGEPIAIRWLKRYIVDNVPVEKYSEILDdEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKP 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 190 GGLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTMEQLLDEYDAVFMGMGTYTYMKGGFPGEDLPGVHDAL 269
Cdd:PRK13984 319 GGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGTDHPDVIQAL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 270 DFLianvnrnlgfeKSAEDFVDMKG------KRVVVLGGGDTAMDCNRTSIR-----QGAKSVTC-AYRRDEENMPGSRK 337
Cdd:PRK13984 399 PLL-----------REIRDYLRGEGpkpkipRSLVVIGGGNVAMDIARSMARlqkmeYGEVNVKVtSLERTFEEMPADME 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 338 EVKNAKEEGVKFLFNRQPIAIVGE-DRVEGVKVVETrLGEPDARGRRSPEPIPGSEEIIPAEAVLIAFGFRPS----PAP 412
Cdd:PRK13984 468 EIEEGLEEGVVIYPGWGPMEVVIEnDKVKGVKFKKC-VEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQAPDysylPEE 546
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489186414 413 W-----FERFEIATDSQGrvvapaqaqfkhQTSNPKIFAGGDMVRGSDlVVTAIFEGRTAAEGILDYL 475
Cdd:PRK13984 547 LkskleFVRGRILTNEYG------------QTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYL 601
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
67-473 |
1.24e-62 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 219.32 E-value: 1.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 67 CPVHNFIPNWLKLVSEGNILAAAELSHQTNTLPEVCGRVCPQDRLCEGACTLNDgfGAVTIGSVEKYI--------TDTA 138
Cdd:PRK12779 214 CPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTK--RPIEIGQLEWYLpqheklvnPNAN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 139 FAMGWRPD--LSKVKPTgrrVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLLTFGIPEFKLEKHVLSRRREVFTG 216
Cdd:PRK12779 292 ERFAGRISpwAAAVKPP---IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 217 MGIEFRLNTEIGKDVTMEQLLDE-YDAVFMGMGT--YTYMKggFPGEDLPGVHDALDFLiANVNRNLGFEKSAED-FVDM 292
Cdd:PRK12779 369 LGGRFVKNFVVGKTATLEDLKAAgFWKIFVGTGAglPTFMN--VPGEHLLGVMSANEFL-TRVNLMRGLDDDYETpLPEV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 293 KGKRVVVLGGGDTAMDCNRTSIRQGAkSVTCAYRRDEENMPGSRKEVKNAKEEGVKFLFNRQPIAIVGEDR---VEGVKV 369
Cdd:PRK12779 446 KGKEVFVIGGGNTAMDAARTAKRLGG-NVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGDDHthfVTHALL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 370 VETRLGEPDARGRRSPEPIpGSEEIIPAEAVLIAFGFRPSPAPWFERFEIATDSQGRVVAPAQAQfkhQTSNPKIFAGGD 449
Cdd:PRK12779 525 DVNELGEPDKSGRRSPKPT-GEIERVPVDLVIMALGNTANPIMKDAEPGLKTNKWGTIEVEKGSQ---RTSIKGVYSGGD 600
|
410 420
....*....|....*....|....
gi 489186414 450 MVRGSDLVVTAIFEGRTAAEGILD 473
Cdd:PRK12779 601 AARGGSTAIRAAGDGQAAAKEIVG 624
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
32-143 |
1.47e-59 |
|
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: 190.83 E-value: 1.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 32 RKREFVEIHDLFKPQQAADQAHRCLGCGNPYCEWKCPVHNFIPNWLKLVSEGNILAAAELSHQTNTLPEVCGRVCPQDRL 111
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 489186414 112 CEGACTLN-DGFGAVTIGSVEKYITDTAFAMGW 143
Cdd:pfam14691 81 CEGACVLGkKGFEPVAIGRLERFAADWARENGI 113
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
157-475 |
4.93e-37 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 137.94 E-value: 4.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 157 VAVIGAGPAGLGCADVLVRNGVTPVVFDRnPEIGGLLT--------FGIPEF--------KLEKHVLS-----RRREV-- 213
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPEGisgpelaeRLREQAERfgaeiLLEEVts 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 214 FTGMGIEFRLNTEIGKDVTMeqlldeyDAVFMGMGTYtYMKGGFPGEDLP---GVH-----DALDFlianvnrnlgfeks 285
Cdd:COG0492 82 VDKDDGPFRVTTDDGTEYEA-------KAVIIATGAG-PRKLGLPGEEEFegrGVSycatcDGFFF-------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 286 aedfvdmKGKRVVVLGGGDTAMD--CNRTSIrqgAKSVTCAYRRDEenMPGSRKEVKNAKE-EGVKFLFNRQPIAIVGED 362
Cdd:COG0492 140 -------RGKDVVVVGGGDSALEeaLYLTKF---ASKVTLIHRRDE--LRASKILVERLRAnPKIEVLWNTEVTEIEGDG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 363 RVEGVKVVETRLGEpdargrrspepipgsEEIIPAEAVLIAFGFRPSPApWFERFEIATDSQGRVVapaqAQFKHQTSNP 442
Cdd:COG0492 208 RVEGVTLKNVKTGE---------------EKELEVDGVFVAIGLKPNTE-LLKGLGLELDEDGYIV----VDEDMETSVP 267
|
330 340 350
....*....|....*....|....*....|....
gi 489186414 443 KIFAGGDMVRGS-DLVVTAIFEGRTAAEGILDYL 475
Cdd:COG0492 268 GVFAAGDVRDYKyRQAATAAGEGAIAALSAARYL 301
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
156-464 |
5.58e-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: 110.10 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 156 RVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEI---GGLLTFGI-------PEFKLEKHVLSRRREVFTGM--GIEFRL 223
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpygGCVLSKALlgaaeapEIASLWADLYKRKEEVVKKLnnGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 224 NTEI------GKDVTMEQLLD------EYDAVFMGMGTYTYMKGgfpgedLPGVHDALDFLIANVNrnlgfekSAEDF-V 290
Cdd:pfam07992 82 GTEVvsidpgAKKVVLEELVDgdgetiTYDRLVIATGARPRLPP------IPGVELNVGFLVRTLD-------SAEALrL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 291 DMKGKRVVVLGGGDTAMDCNRTSIRQGAKsVTCAYRRDE----ENMPGSRKEVKNAKEEGVKFLFNRQPIAIVGEDrvEG 366
Cdd:pfam07992 149 KLLPKRVVVVGGGYIGVELAAALAKLGKE-VTLIEALDRllraFDEEISAALEKALEKNGVEVRLGTSVKEIIGDG--DG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 367 VKVVEtrlgepdargrrspepipGSEEIIPAEAVLIAFGFRPSPApWFERFEIATDSQGRVVAPAQaqfkHQTSNPKIFA 446
Cdd:pfam07992 226 VEVIL------------------KDGTEIDADLVVVAIGRRPNTE-LLEAAGLELDERGGIVVDEY----LRTSVPGIYA 282
|
330
....*....|....*....
gi 489186414 447 GGDM-VRGSDLVVTAIFEG 464
Cdd:pfam07992 283 AGDCrVGGPELAQNAVAQG 301
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
152-428 |
4.46e-19 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 89.76 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 152 PTGRRVAVIGAGPAGLGCADVLVR--NGVTPVVFDRNPEIGGLLTFGI-PEFKLEKHVLSRRREVFTGMGIEFRLNTEIG 228
Cdd:PLN02852 24 SEPLHVCVVGSGPAGFYTADKLLKahDGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVTLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 229 KDVTMEQLLDEYDAVFMGMGTYTYMKGGFPGEDLPGVHDALDFlIANVNRNLGFEKSAEDFVDmkGKRVVVLGGGDTAMD 308
Cdd:PLN02852 104 RDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREF-VWWYNGHPDCVHLPPDLKS--SDTAVVLGQGNVALD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 309 CNR-----------TSI---------RQGAKSVTCAYRR-----------------------------------DEENMP 333
Cdd:PLN02852 181 CARillrptdelasTDIaehalealrGSSVRKVYLVGRRgpvqaactakelrellglknvrvrikeadltlspeDEEELK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 334 GSR------KEVKNAKEEG----------VKFLFNRQPIAI----VGEDRVEGVKVVETRLgEPDARGRRSPEPIPGSEE 393
Cdd:PLN02852 261 ASRpkrrvyELLSKAAAAGkcapsggqreLHFVFFRNPTRFldsgDGNGHVAGVKLERTVL-EGAAGSGKQVAVGTGEFE 339
|
330 340 350
....*....|....*....|....*....|....*..
gi 489186414 394 IIPAEAVLIAFGFRPSPAP--WFerfeiatDSQGRVV 428
Cdd:PLN02852 340 DLPCGLVLKSIGYKSLPVDglPF-------DHKRGVV 369
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
181-472 |
2.51e-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: 76.77 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 181 VVFDRNPEIG----GLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEI------GKDVTM---EQLldEYDAVFMGM 247
Cdd:COG0446 9 TVIEKGPHHSyqpcGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVtaidpeAKTVTLrdgETL--SYDKLVLAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 248 GTyTYMKGGFPGEDLPGVHdaldflianVNRNL-GFEKSAEDFVDMKGKRVVVLGGG------DTAMdcnrtsIRQGAKs 320
Cdd:COG0446 87 GA-RPRPPPIPGLDLPGVF---------TLRTLdDADALREALKEFKGKRAVVIGGGpiglelAEAL------RKRGLK- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 321 VTCAYRRDEEnMPGSRKEV-----KNAKEEGVKFLFNRQPIAIVGEDRvegVKVVETrlgepdargrrspepipgSEEII 395
Cdd:COG0446 150 VTLVERAPRL-LGVLDPEMaalleEELREHGVELRLGETVVAIDGDDK---VAVTLT------------------DGEEI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 396 PAEAVLIAFGFRP-------SPAPWFERFEIATDSQGrvvapaqaqfkhQTSNPKIFAGGDMVRGSDLVV---------- 458
Cdd:COG0446 208 PADLVVVAPGVRPntelakdAGLALGERGWIKVDETL------------QTSDPDVYAAGDCAEVPHPVTgktvyiplas 275
|
330
....*....|....
gi 489186414 459 TAIFEGRTAAEGIL 472
Cdd:COG0446 276 AANKQGRVAAENIL 289
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
155-472 |
4.52e-12 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 67.47 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 155 RRVAVIGAGPAGLGCADVLVRNG----VTpvVFDRnpEIGG-----LLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNT 225
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDpdgeIT--VIGA--EPHPpynrpPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 226 EI------GKDVTM---EQLldEYDAVFMGMGTYTYMkGGFPGEDLPGVHdaldflianVNRNLgfeksaEDFVDMK--- 293
Cdd:COG1251 78 RVtaidraARTVTLadgETL--PYDKLVLATGSRPRV-PPIPGADLPGVF---------TLRTL------DDADALRaal 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 294 --GKRVVVLGGG----DTAMDCnrtsiRQGAKSVTCAYRR--------DEEnmpGSRKEVKNAKEEGVKFLFNRQPIAIV 359
Cdd:COG1251 140 apGKRVVVIGGGliglEAAAAL-----RKRGLEVTVVERAprllprqlDEE---AGALLQRLLEALGVEVRLGTGVTEIE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 360 GEDRVEGVkvvetRLgepdARGRRspepipgseeiIPAEAVLIAFGFRPSPApWFERFEIATDsqGRVVAPAQAQfkhqT 439
Cdd:COG1251 212 GDDRVTGV-----RL----ADGEE-----------LPADLVVVAIGVRPNTE-LARAAGLAVD--RGIVVDDYLR----T 264
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489186414 440 SNPKIFAGGD------MVRG---SDLVVTAIFEGRTAAEGIL 472
Cdd:COG1251 265 SDPDIYAAGDcaehpgPVYGrrvLELVAPAYEQARVAAANLA 306
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
156-327 |
7.56e-11 |
|
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: 63.73 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 156 RVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGL--------LTFGIP----------------------------- 198
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTwrdnrypgLRLDTPshlyslpffpnwsddpdfptgdeilayle 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 199 ----EFKLEKHVLsRRREVftgMGIE-------FRLNTEIGKDVTmeqlldeYDAVFMGMGTYTymKG---GFPGEDLPG 264
Cdd:COG2072 88 ayadKFGLRRPIR-FGTEV---TSARwdeadgrWTVTTDDGETLT-------ARFVVVATGPLS--RPkipDIPGLEDFA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489186414 265 ---VHdaldflianvnrnlgfekSAE--DFVDMKGKRVVVLGGGDTAMDCnRTSIRQGAKSVTCAYRR 327
Cdd:COG2072 155 geqLH------------------SADwrNPVDLAGKRVLVVGTGASAVQI-APELARVAAHVTVFQRT 203
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
157-472 |
1.03e-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: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 157 VAVIGAGPAGLGCADVLVRNGVTPVVFDRNPeIGG------------LL-------------TFGI----PEFKLEKhVL 207
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGGtclnvgcipskaLLhaaevahearhaaEFGIsagaPSVDWAA-LM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 208 SRRREVFTGM--GIEFRLNTEigkDVTMEQ----LLDEYDAVFMGMGTYTYMK-----GG------FPGEDLPGVHDAld 270
Cdd:COG1249 84 ARKDKVVDRLrgGVEELLKKN---GVDVIRgrarFVDPHTVEVTGGETLTADHiviatGSrprvppIPGLDEVRVLTS-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 271 flianvnrnlgfeksaEDFVDMK--GKRVVVLGGGdtamdcnrtSI---------RQGAKsVTCAYRR-------DEEnm 332
Cdd:COG1249 159 ----------------DEALELEelPKSLVVIGGG---------YIglefaqifaRLGSE-VTLVERGdrllpgeDPE-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 333 pgSRKEVKNA-KEEGVKFLFNRQPIAIvgeDRVEGVKVVETRLGepdargrrspepipGSEEIIPAEAVLIAFGFRPSPA 411
Cdd:COG1249 211 --ISEALEKAlEKEGIDILTGAKVTSV---EKTGDGVTVTLEDG--------------GGEEAVEADKVLVATGRRPNTD 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489186414 412 PW-FERFEIATDSQGRVVAPAQaqfkHQTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGIL 472
Cdd:COG1249 272 GLgLEAAGVELDERGGIKVDEY----LRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENIL 329
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
156-209 |
5.46e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 57.97 E-value: 5.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489186414 156 RVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLL-TFGIPEFKLEK--HVLSR 209
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIERfyHHIFK 57
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
155-214 |
4.01e-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: 55.22 E-value: 4.01e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489186414 155 RRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLL-TFGIPEFKLEK---HVLSRRREVF 214
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIrTVEVDGFRIDRgphSFLTRDPEVL 65
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
155-192 |
7.03e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 54.51 E-value: 7.03e-08
10 20 30
....*....|....*....|....*....|....*...
gi 489186414 155 RRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGL 192
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
155-191 |
1.08e-07 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 53.73 E-value: 1.08e-07
10 20 30
....*....|....*....|....*....|....*..
gi 489186414 155 RRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGG 191
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
296-372 |
9.62e-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: 46.43 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 296 RVVVLGGGDTAMDCNrTSIRQGAKSVTCAYRRDEEnMPGSRKEV-----KNAKEEGVKFLFNRQPIAIVGEDRVEGVKVV 370
Cdd:pfam00070 1 RVVVVGGGYIGLELA-GALARLGSKVTVVERRDRL-LPGFDPEIakilqEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
..
gi 489186414 371 ET 372
Cdd:pfam00070 79 DG 80
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
164-428 |
1.60e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 49.53 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 164 PAGLGCADVLVRNGVTPVV----------FDRNPEIGGLLT-------FGIPE-----------FKLEKHVLSRR----- 210
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDYLilekgnignsFYRYPTHMTFFSpsftsngFGIPDlnaispgtspaFTFNREHPSGNeyaey 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 211 -REVFTGMGIEFRLNTEIgKDVTMEQLL-------DEYDA--VFMGMGTYtymkgGFPgeDLPGVHDaldflIANVNRNL 280
Cdd:pfam13738 81 lRRVADHFELPINLFEEV-TSVKKEDDGfvvttskGTYQAryVIIATGEF-----DFP--NKLGVPE-----LPKHYSYV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 281 gfeksaEDFVDMKGKRVVVLGGGDTAMDCNRTSIRQGAKsVTCAYRRDEENMPGSRKE------VKNAKEEGVKflfnRQ 354
Cdd:pfam13738 148 ------KDFHPYAGQKVVVIGGYNSAVDAALELVRKGAR-VTVLYRGSEWEDRDSDPSyslspdTLNRLEELVK----NG 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489186414 355 PIAIVGEDRVEGVKVVET--RLGEPDARgrrspepipgseEIIPAEAVLIAFGFRPSPAPwFERFEIATDSQGRVV 428
Cdd:pfam13738 217 KIKAHFNAEVKEITEVDVsyKVHTEDGR------------KVTSNDDPILATGYHPDLSF-LKKGLFELDEDGRPV 279
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
152-191 |
2.38e-06 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 49.92 E-value: 2.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489186414 152 PTGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGG 191
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
149-185 |
3.15e-06 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 49.34 E-value: 3.15e-06
10 20 30
....*....|....*....|....*....|....*..
gi 489186414 149 KVKPTGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDR 185
Cdd:COG2509 25 GIPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
156-475 |
3.35e-06 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 48.98 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 156 RVAVIGAGPAGLGCADVLVRNGVTPV---VFDRNPE----------IGGLLTFGipefklekHVLSRRREVFTGMGIEFR 222
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKKLGGDAevtLIDPNPYhlfqpllpevAAGTLSPD--------DIAIPLRELLRRAGVRFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 223 L-------------NTEIGKDVtmeqlldEYDAVFMGMGTyTYMKGGFPG--EDLPG---VHDALDFlianvnRNLgFEK 284
Cdd:COG1252 75 QgevtgidpeartvTLADGRTL-------SYDYLVIATGS-VTNFFGIPGlaEHALPlktLEDALAL------RER-LLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 285 SAEDFVDMKGKRVVVLGGGDT------AMD------CNRTSIRQGAKSVTCAYRRDE--ENMPG-SRKEVKNA-KEEGVK 348
Cdd:COG1252 140 AFERAERRRLLTIVVVGGGPTgvelagELAellrklLRYPGIDPDKVRITLVEAGPRilPGLGEkLSEAAEKElEKRGVE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 349 FLFNRqPIAIVGEDRVegvkVVEtrlgepdargrrspepipgSEEIIPAEAVLIAFGFRPSPapWFERFEIATDSQGRVV 428
Cdd:COG1252 220 VHTGT-RVTEVDADGV----TLE-------------------DGEEIPADTVIWAAGVKAPP--LLADLGLPTDRRGRVL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489186414 429 apAQAQFKHqTSNPKIFAGGDMVRGSD--------LVVTAIFEGRTAAEGILDYL 475
Cdd:COG1252 274 --VDPTLQV-PGHPNVFAIGDCAAVPDpdgkpvpkTAQAAVQQAKVLAKNIAALL 325
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
156-248 |
4.90e-06 |
|
adrenodoxin reductase; Provisional
Pssm-ID: 240308 Cd Length: 506 Bit Score: 48.73 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 156 RVAVIGAGPAGLGCADVLVRNGVTPV-VFDRNPEIGGLLTFGI-PEFKLEKHVLSRRREVFTGMGIEFRLNTEIGKDVTM 233
Cdd:PTZ00188 41 KVGIIGAGPSALYCCKHLLKHERVKVdIFEKLPNPYGLIRYGVaPDHIHVKNTYKTFDPVFLSPNYRFFGNVHVGVDLKM 120
|
90
....*....|....*
gi 489186414 234 EQLLDEYDAVFMGMG 248
Cdd:PTZ00188 121 EELRNHYNCVIFCCG 135
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
153-192 |
7.35e-06 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 48.32 E-value: 7.35e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489186414 153 TGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGL 192
Cdd:PLN02172 9 NSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGL 48
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
159-203 |
9.91e-06 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 43.29 E-value: 9.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489186414 159 VIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLL-TFGIPEFKLE 203
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAySYRVPGYVFD 46
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
153-227 |
1.26e-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: 47.11 E-value: 1.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489186414 153 TGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPeigGLLTFGIPEF--KLEKHVLSRrrevftgmGIEFRLNTEI 227
Cdd:COG0446 123 KGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAP---RLLGVLDPEMaaLLEEELREH--------GVELRLGETV 188
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
153-191 |
1.62e-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: 47.16 E-value: 1.62e-05
10 20 30
....*....|....*....|....*....|....*....
gi 489186414 153 TGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGG 191
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
151-210 |
2.13e-05 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 46.67 E-value: 2.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489186414 151 KPTGR--RVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPE----IGGlltfGIP-----EFKLEKHVLSRR 210
Cdd:PLN00093 34 KLSGRklRVAVIGGGPAGACAAETLAKGGIETFLIERKLDnakpCGG----AIPlcmvgEFDLPLDIIDRK 100
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
154-188 |
4.82e-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: 45.46 E-value: 4.82e-05
10 20 30
....*....|....*....|....*....|....*
gi 489186414 154 GRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPE 188
Cdd:COG0771 4 GKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPA 38
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
158-190 |
4.93e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 45.43 E-value: 4.93e-05
10 20 30
....*....|....*....|....*....|...
gi 489186414 158 AVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIG 190
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
157-474 |
5.57e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 45.55 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 157 VAVIGAGPAGLGCADVLVRNGVTPVVFDRNP------------------------EIGGLLTFGI----PEFKLEKhVLS 208
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPlggtclnvgcipskaliaaaeafhEAKHAEEFGIhadgPKIDFKK-VMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 209 RRREV---FTGMgiefrlnteigkdvtMEQLLDEYDAV--FMGMGTytymkggFPGEDLPGVHD----ALDFLIANVNRN 279
Cdd:PRK06292 85 RVRRErdrFVGG---------------VVEGLEKKPKIdkIKGTAR-------FVDPNTVEVNGerieAKNIVIATGSRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 280 ---LGFEKSAED-FVDMKG--------KRVVVLGGGdtamdcnrtSI---------RQGAKsVTCAYRRDEEnMPGSRKE 338
Cdd:PRK06292 143 ppiPGVWLILGDrLLTSDDafeldklpKSLAVIGGG---------VIglelgqalsRLGVK-VTVFERGDRI-LPLEDPE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 339 VKNA------KEegVKFLFNRQPIAIvgeDRVEGVKVVETRLGepdargrrspepipGSEEIIPAEAVLIAFGFRP-SPA 411
Cdd:PRK06292 212 VSKQaqkilsKE--FKIKLGAKVTSV---EKSGDEKVEELEKG--------------GKTETIEADYVLVATGRRPnTDG 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489186414 412 PWFERFEIATDSQGRVVapaqaqFKH--QTSNPKIFAGGDMVRGSDLVVTAIFEGRTAAEGILDY 474
Cdd:PRK06292 273 LGLENTGIELDERGRPV------VDEhtQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGD 331
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
155-223 |
1.25e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.46 E-value: 1.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489186414 155 RRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLL-TFGIPEFK--------LEKHVLSRrreVFTGMGIEFRL 223
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRArTFERPGFRfdvgpsvlTMPGVLER---LFRELGLEDYL 78
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
156-221 |
1.27e-04 |
|
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: 43.93 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 156 RVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIG--------GLLTFGIPE------FKLEKHVLSRRREVFTGMGIEF 221
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYlepselARLALEALDLWEELEEELGIDC 80
|
|
| FMO-like |
pfam00743 |
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ... |
154-195 |
1.86e-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: 44.00 E-value: 1.86e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489186414 154 GRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLLTF 195
Cdd:pfam00743 1 AKKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRF 42
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
155-190 |
1.87e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 43.72 E-value: 1.87e-04
10 20 30
....*....|....*....|....*....|....*.
gi 489186414 155 RRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIG 190
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| AdhP |
COG1064 |
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ... |
138-188 |
2.67e-04 |
|
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];
Pssm-ID: 440684 [Multi-domain] Cd Length: 332 Bit Score: 42.79 E-value: 2.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489186414 138 AFAMGWRP-DLSKVKPtGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPE 188
Cdd:COG1064 147 AGITAYRAlRRAGVGP-GDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPE 197
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
157-222 |
2.80e-04 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 42.98 E-value: 2.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489186414 157 VAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLLTFGI---PEfklekHVLSRRREVFTGMGIEFR 222
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSGLvgpDM-----GFYLNKEQVVGGIAREFR 65
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
155-190 |
3.20e-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: 42.62 E-value: 3.20e-04
10 20 30
....*....|....*....|....*....|....*.
gi 489186414 155 RRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIG 190
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
155-190 |
4.20e-04 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 42.63 E-value: 4.20e-04
10 20 30
....*....|....*....|....*....|....*....
gi 489186414 155 RRVAVIGAGPAGLGCADVLVRNGVTP---VVFDRNPEIG 190
Cdd:COG4529 6 KRIAIIGGGASGTALAIHLLRRAPEPlriTLFEPRPELG 44
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
156-227 |
4.93e-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: 4.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489186414 156 RVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIGGLLTFGIPEFKLEKhvlsrrrevFTGMGIEFRLNTEI 227
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEK---------LEKNGIEFLLNTTV 63
|
|
| Tdh |
COG1063 |
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ... |
146-188 |
5.29e-04 |
|
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: 42.05 E-value: 5.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489186414 146 DLSKVKPtGRRVAVIGAGPAGLGCADVLVRNGVTPV-VFDRNPE 188
Cdd:COG1063 155 ERAGVKP-GDTVLVIGAGPIGLLAALAARLAGAARViVVDRNPE 197
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
149-248 |
6.27e-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: 41.53 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 149 KVKPTGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIggLLTFGIpefKLEKHVlsrrREVFTGMGIEFRLNTE-- 226
Cdd:pfam07992 147 RLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL--LRAFDE---EISAAL----EKALEKNGVEVRLGTSvk 217
|
90 100
....*....|....*....|....*....
gi 489186414 227 --IGKDVTMEQLLDE-----YDAVFMGMG 248
Cdd:pfam07992 218 eiIGDGDGVEVILKDgteidADLVVVAIG 246
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
149-188 |
9.26e-04 |
|
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: 39.80 E-value: 9.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489186414 149 KVKPTgrRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPE 188
Cdd:smart01002 17 GVPPA--KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPA 54
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
153-191 |
1.49e-03 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 40.87 E-value: 1.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489186414 153 TGRRVAVIGAGPAGLGCADVLVRN-GVTpvVFDRNPEIGG 191
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAWLLSRRhDVT--LFEANDRLGG 39
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
144-190 |
2.16e-03 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 40.62 E-value: 2.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 489186414 144 RPDLSKVKPTGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIG 190
Cdd:PRK08132 13 HADQDADDPARHPVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLS 59
|
|
| Zn_ADH7 |
cd08261 |
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ... |
154-188 |
2.16e-03 |
|
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. 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 Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various 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. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
Pssm-ID: 176222 [Multi-domain] Cd Length: 337 Bit Score: 40.25 E-value: 2.16e-03
10 20 30
....*....|....*....|....*....|....*
gi 489186414 154 GRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPE 188
Cdd:cd08261 160 GDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDE 194
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
156-245 |
2.66e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 40.06 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 156 RVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPEI----GGLltfGIPE---FKLEKHVLSRrrevftgmGIEfrlntEIG 228
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESVkevgAGI---GIGDnviKKLGNHDLAK--------GIK-----NAG 65
|
90
....*....|....*..
gi 489186414 229 KDVTMEQLLDEYDAVFM 245
Cdd:PRK06753 66 QILSTMNLLDDKGTLLN 82
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
158-190 |
5.79e-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: 39.12 E-value: 5.79e-03
10 20 30
....*....|....*....|....*....|...
gi 489186414 158 AVIGAGPAGLGCADVLVRNGVTPVVFDRNPEIG 190
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
|
|
| Malic_M |
smart00919 |
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ... |
156-199 |
5.96e-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: 38.16 E-value: 5.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 489186414 156 RVAVIGAGPAGLGCADVLVRNGVTP---VVFDRNpeigGLLTFGIPE 199
Cdd:smart00919 27 RIVVNGAGAAGIGIAKLLVAAGVKRkniWLVDSK----GLLTKGRED 69
|
|
| PRK06703 |
PRK06703 |
flavodoxin; Provisional |
226-306 |
6.04e-03 |
|
flavodoxin; Provisional
Pssm-ID: 235854 [Multi-domain] Cd Length: 151 Bit Score: 37.43 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 226 EIGKDVTMEQL-------LDEYDAVFMGmgTYTYMKGgfpgeDLPgvHDALDFlianvnrnlgFEKSAEdfVDMKGKRVV 298
Cdd:PRK06703 28 AFDHEVVLQEMdgmdaeeLLAYDGIILG--SYTWGDG-----DLP--YEAEDF----------HEDLEN--IDLSGKKVA 86
|
....*...
gi 489186414 299 VLGGGDTA 306
Cdd:PRK06703 87 VFGSGDTA 94
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
156-449 |
6.10e-03 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 38.87 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 156 RVAVIGAGPAGLGCADVLVRN--GVTPVVFDRNPEIG----GLLTFGIPEFKLEKHVLSRRREVFTGMGIEFRLNTEIGK 229
Cdd:PRK09564 2 KIIIIGGTAAGMSAAAKAKRLnkELEITVYEKTDIVSfgacGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHEVVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 230 -DVTMEQLL-----------DEYDAVFMGMGTYTYMKGgFPGEDLPGVHDALDFLIANVNRNLGFEKSAedfvdmkgKRV 297
Cdd:PRK09564 82 vDAKNKTITvknlktgsifnDTYDKLMIATGARPIIPP-IKNINLENVYTLKSMEDGLALKELLKDEEI--------KNI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186414 298 VVLGGGDTAMDCNRTSIRQGaKSVTcAYRRDEENMPGS-RKEVKNAKEE-----GVKFLFNRQPIAIVGEDRVEGVKvve 371
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLG-KNVR-IIQLEDRILPDSfDKEITDVMEEelrenGVELHLNEFVKSLIGEDKVEGVV--- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489186414 372 TRLGEPDargrrspepipgseeiipAEAVLIAFGFRPSpAPWFERFEIATDSQGRVVAPAQAqfkhQTSNPKIFAGGD 449
Cdd:PRK09564 228 TDKGEYE------------------ADVVIVATGVKPN-TEFLEDTGLKTLKNGAIIVDEYG----ETSIENIYAAGD 282
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
157-188 |
6.53e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 38.77 E-value: 6.53e-03
10 20 30
....*....|....*....|....*....|..
gi 489186414 157 VAVIGAGPAGLGCADVLVRNGVTPVVFDRNPE 188
Cdd:PRK09126 6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQPL 37
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
133-188 |
8.49e-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: 8.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489186414 133 YITDTAFAMGWRPDLSKVKPTGRRVAVIGAGPAGLGCADVLVRNGVTPVVFDRNPE 188
Cdd:COG0569 74 LFGGLLEALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPE 129
|
|
| |
