|
Name |
Accession |
Description |
Interval |
E-value |
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
9-473 |
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: 803.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 9 FQFLDVARQDPEKKDIDVRKSEFVEIYKPFTAEVAANQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGRIFQAAELCH 88
Cdd:TIGR01318 1 FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 89 QTNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSSVKWTDKKVAIIGAGPAGLGCADIL 168
Cdd:TIGR01318 81 QTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 169 VRNGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQDYDAVFMGMGTYTYM 248
Cdd:TIGR01318 161 ARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRSM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 249 KGGFPGEELEGVYDALDFLIANVNRTQGWEQNPNE-YISVEGKKVIVLGGGDTAMDCNRTSIRQGAEQVTCAYRRDEANM 327
Cdd:TIGR01318 241 RGGLPGEDAPGVLPALPFLIANTRQLMGLPEEPEEpLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 328 PGSRREVKNAREEGVNFLFNRQPIEIV-GENGQVTGVKVVTTQLGAPDSRGRRSPEPIPGSEEVLAADAVLLAFGFRPSP 406
Cdd:TIGR01318 321 PGSRREVANAREEGVEFLFNVQPVSIEsDEDGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881045658 407 ADWFAPANIGLDGSGRVLAAEQQQYKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYLDV 473
Cdd:TIGR01318 401 MPWLAAHGITLDSWGRIITALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV 467
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
7-473 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 794.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 7 NDFQFLDVARQDPEKKDIDVRKSEFVEIYKPFTAEVAANQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGRIFQAAEL 86
Cdd:PRK12810 3 KPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 87 CHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGNAEKYINDTAFALGW-RPDmSSVKWTDKKVAIIGAGPAGLGCA 165
Cdd:PRK12810 83 LHQTNNFPEFTGRVCPAP--CEGACTLNINFGPVTIKNIERYIIDKAFEEGWvKPD-PPVKRTGKKVAVVGSGPAGLAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 166 DILVRNGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQDYDAVFMGMGTY 245
Cdd:PRK12810 160 DQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 246 TYMKGGFPGEELEGVYDALDFLIANVNRTQGWEQNPneYISVEGKKVIVLGGGDTAMDCNRTSIRQGAEQVTcayRRDEA 325
Cdd:PRK12810 240 KPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDETEP--FISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVT---QRDIM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 326 NMPGSRR-------------EVKNAREEGVNFLFNRQPIEIVGENGQVTGVKVVTTQLGAPDsrgrrsPEPIPGSEEVLA 392
Cdd:PRK12810 315 PMPPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGD------FEPVEGSEFVLP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 393 ADAVLLAFGFRPSPADWFAPANIGLDGSGRVLAAEQQqykFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYLD 472
Cdd:PRK12810 389 ADLVLLAMGFTGPEAGLLAQFGVELDERGRVAAPDNA---YQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLM 465
|
.
gi 881045658 473 V 473
Cdd:PRK12810 466 G 466
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
15-473 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 750.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 15 ARQDPEKKDIDVRKSEFVEIYKPFTAEVAANQTHRCLGCG-NPYCEWKCPVHNYIPNWLKLIAEGRIFQAAELCHQTNTL 93
Cdd:PRK12769 192 PRGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGeHSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 94 PEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSSVKWTDKKVAIIGAGPAGLGCADILVRNGV 173
Cdd:PRK12769 272 PEITGRVCPQDRLCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNGV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 174 KPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQDYDAVFMGMGTYTYMKGGFP 253
Cdd:PRK12769 352 AVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLP 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 254 GEELEGVYDALDFLIANVNRTQGWEQNPNE-YISVEGKKVIVLGGGDTAMDCNRTSIRQGAEQVTCAYRRDEANMPGSRR 332
Cdd:PRK12769 432 NEDAPGVYDALPFLIANTKQVMGLEELPEEpFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 333 EVKNAREEGVNFLFNRQPIEIV-GENGQVTGVKVVTTQLGAPDSRGRRSPEPIPGSEEVLAADAVLLAFGFRPSPADWFA 411
Cdd:PRK12769 512 EVKNAREEGANFEFNVQPVALElNEQGHVCGIRFLRTRLGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGFNPHGMPWLE 591
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881045658 412 PANIGLDGSGRVLAAEQQQYKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYLDV 473
Cdd:PRK12769 592 SHGVTVDKWGRIIADVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLGV 653
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
27-470 |
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: 653.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 27 RKSEFVEIYKPFTAEVAANQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGRIFQAAELCHQTNTLPEVCGRVCPqdRL 106
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--AP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 107 CEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSSVKWTDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGG 186
Cdd:COG0493 79 CEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 187 LLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQDYDAVFMGMGTYTYMKGGFPGEELEGVYDALDF 266
Cdd:COG0493 159 LLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 267 LIAnVNRTQGweqnpNEYISVEGKKVIVLGGGDTAMDCNRTSIRQGAEQVTCAYRRDEANMPGSRREVKNAREEGVNFLF 346
Cdd:COG0493 239 LTA-VNLGEA-----PDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 347 NRQPIEIVG-ENGQVTGVKVVTTQLGAPDSRGRRSPEPIPGSEEVLAADAVLLAFGFRPSPADWFAPANIGLDGSGRVLA 425
Cdd:COG0493 313 LVAPVEIIGdENGRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 881045658 426 AEQqqyKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDY 470
Cdd:COG0493 393 DEE---TYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
10-471 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 579.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 10 QFLDVARQDPEKKDIDVRKSEFVEIYKPFTAEVAANQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGRIFQAAELCHQ 89
Cdd:PRK11749 2 KFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 90 TNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSSVKwTDKKVAIIGAGPAGLGCADILV 169
Cdd:PRK11749 82 TNPLPAVCGRVCPQERLCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKRAPK-TGKKVAVIGAGPAGLTAAHRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 170 RNGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQDYDAVFMGMGTYTYMK 249
Cdd:PRK11749 161 RKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 250 GGFPGEELEGVYDALDFLiANVNRTQGWEQNPneyisvEGKKVIVLGGGDTAMDCNRTSIRQGAEQVTCAYRRDEANMPG 329
Cdd:PRK11749 241 LGIPGENLGGVYSAVDFL-TRVNQAVADYDLP------VGKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 330 SRREVKNAREEGVNFLFNRQPIEIVGENGQVTGVKVVTTQLGAPDSRGRRSpEPIPGSEEVLAADAVLLAFGFRPSPADW 409
Cdd:PRK11749 314 SEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMELGEPDASGRRR-VPIEGSEFTLPADLVIKAIGQTPNPLIL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881045658 410 FAPANIGLDGSGRVLAAEQQqykFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK11749 393 STTPGLELNRWGTIIADDET---GRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYL 451
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
12-472 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 573.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 12 LDV-ARQDPEKKDIDVRKSEFVEIYKPFTAEVAANQTHRCLGCGN-PYCEWKCPVHNYIPNWLKLIAEGRIFQAAELCHQ 89
Cdd:PRK12809 171 LPVnSRKGADKISASERKTHFGEIYCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 90 TNTLPEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSSVKWTDKKVAIIGAGPAGLGCADILV 169
Cdd:PRK12809 251 TSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILA 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 170 RNGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQDYDAVFMGMGTYTYMK 249
Cdd:PRK12809 331 RAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 250 GGFPGEELEGVYDALDFLIANVNRTQGWEQNpNEY--ISVEGKKVIVLGGGDTAMDCNRTSIRQGAEQVTCAYRRDEANM 327
Cdd:PRK12809 411 ADLPHEDAPGVIQALPFLTAHTRQLMGLPES-EEYplTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSM 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 328 PGSRREVKNAREEGVNFLFNRQPIEIV-GENGQVTGVKVVTTQLGAPDSRGRRSPEPIPGSEEVLAADAVLLAFGFRPSP 406
Cdd:PRK12809 490 PGSRKEVVNAREEGVEFQFNVQPQYIAcDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHA 569
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881045658 407 ADWFAPANIGLDGSGRVLAAEQQQYKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYLD 472
Cdd:PRK12809 570 MPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDMLTLFD 635
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
14-471 |
3.02e-131 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 387.84 E-value: 3.02e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 14 VARQDPEkkdidVRKSEFVEIYKPFTAEVAANQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGRIFQAAELCHQTNTL 93
Cdd:PRK12831 11 VREQDPE-----VRATNFEEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 94 PEVCGRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRPDMSSVKwTDKKVAIIGAGPAGLGCADILVRNGV 173
Cdd:PRK12831 86 PAVCGRVCPQESQCEGKCVLGIKGEPVAIGKLERFVADWARENGIDLSETEEK-KGKKVAVIGSGPAGLTCAGDLAKMGY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 174 KPVVFDKRPEIGGLLTFGIPEFKMEKD-VMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQD--YDAVFMGMGTYTYMKG 250
Cdd:PRK12831 165 DVTIFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFDAVFIGSGAGLPKFM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 251 GFPGEELEGVYDALDFLiANVNRTQGWEQNPNEYISVeGKKVIVLGGGDTAMDCNRTSIRQGAEqVTCAYRRDEANMPGS 330
Cdd:PRK12831 245 GIPGENLNGVFSANEFL-TRVNLMKAYKPEYDTPIKV-GKKVAVVGGGNVAMDAARTALRLGAE-VHIVYRRSEEELPAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 331 RREVKNAREEGVNFLFNRQPIEIVG-ENGQVTGVKVVTTQLGAPDSRGRRSPEPIPGSEEVLAADAVLLAFGFRPSPADW 409
Cdd:PRK12831 322 VEEVHHAKEEGVIFDLLTNPVEILGdENGWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLIS 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881045658 410 FAPANIGLDGSGRVLAAEQQqykFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK12831 402 STTKGLKINKRGCIVADEET---GLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYL 460
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
17-471 |
1.65e-117 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 361.75 E-value: 1.65e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 17 QDPEKKdidvRKSEFVEIYKPFTAEVAANQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGRIFQAAELCHQTNTLPEV 96
Cdd:PRK12778 302 LDPEYR----AHNRFEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAV 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 97 CGRVCPQDRLCEGACT-LNDGFGAVTIGNAEKYINDTAFALGwRPDMSSVK-WTDKKVAIIGAGPAGLGCADILVRNGVK 174
Cdd:PRK12778 378 CGRVCPQEKQCESKCIhGKMGEEAVAIGYLERFVADYERESG-NISVPEVAeKNGKKVAVIGSGPAGLSFAGDLAKRGYD 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 175 PVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLL-QDYDAVFM--GMGTYTYMkgG 251
Cdd:PRK12778 457 VTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEeEGFKGIFIasGAGLPNFM--N 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 252 FPGEELEGVYDALDFLiANVNRTQGWEQNPNEYISVeGKKVIVLGGGDTAMDCNRTSIRQGAEQVTCAYRRDEANMPGSR 331
Cdd:PRK12778 535 IPGENSNGVMSSNEYL-TRVNLMDAASPDSDTPIKF-GKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARL 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 332 REVKNAREEGVNFLFNRQPIEIVG-ENGQVTGVKVVTTQLGAPDSRGRRSPEPIPGSEEVLAADAVLLAFGFRPSPADWF 410
Cdd:PRK12778 613 EEVKHAKEEGIEFLTLHNPIEYLAdEKGWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLVPS 692
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 881045658 411 APANIGLDGSGRVLAAEQQqykfQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK12778 693 SIPGLELNRKGTIVVDEEM----QSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYL 749
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
19-471 |
1.59e-112 |
|
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: 339.15 E-value: 1.59e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 19 PEKKDIDVRKSEFveiykPFTAEVAANQTHRCLGCGNPY--CEWKCPVHNYIPNWLKLIAEGRIFQAAELCHQTNTLPEV 96
Cdd:TIGR01316 2 PEERSKLFQEAAL-----GYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 97 CGRVCPQDRLCEGACTLNDGFG----AVTIGNAEKYINDTAFALGWRPDMSSVKWTDKKVAIIGAGPAGLGCADILVRNG 172
Cdd:TIGR01316 77 CGRVCPQERQCEGQCTVGKMFKdvgkPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 173 VKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQDYDAVFMGMGTYTYMKGGF 252
Cdd:TIGR01316 157 HSVTVFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 253 PGEELEGVYDALDFLIaNVNRTQGWEqNPNEYISVE-GKKVIVLGGGDTAMDCNRTSIRQGAEqVTCAYRRDEANMPGSR 331
Cdd:TIGR01316 237 PGEELCGVYSANDFLT-RANLMKAYE-FPHADTPVYaGKSVVVIGGGNTAVDSARTALRLGAE-VHCLYRRTREDMTARV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 332 REVKNAREEGVNFLFNRQPIEIVG-ENGQVTGVKVVTTQLGAPDSRGRRSPEPIPGSEEVLAADAVLLAFGFRPSPAdWF 410
Cdd:TIGR01316 314 EEIAHAEEEGVKFHFLCQPVEIIGdEEGNVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPI-MA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 881045658 411 APANIGLDGSGRVLAAEQQqykfQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:TIGR01316 393 ETTRLKTSERGTIVVDEDQ----RTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
11-471 |
1.02e-111 |
|
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: 338.34 E-value: 1.02e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 11 FLDVARQDPEKKDIDVRKSEFVEIYKPFTAEVAANQTHRCLGCGNPYC--EWKCPVHNYIPNWLKLIAEGRIFQAAELCH 88
Cdd:TIGR01317 5 FLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFChnDSGCPLNNLIPEFNDLVFRGRWKEALDRLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 89 QTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGNAEKYINDTAFALGW-RPDMSSVKwTDKKVAIIGAGPAGLGCADI 167
Cdd:TIGR01317 85 ATNNFPEFTGRVCPAP--CEGACTLGISEDPVGIKSIERIIIDKGFQEGWvQPRPPSKR-TGKKVAVVGSGPAGLAAADQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 168 LVRNGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQDYDAVFMGMGTYTY 247
Cdd:TIGR01317 162 LNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATKP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 248 MKGGFPGEELEGVYDALDFLIANVNRTQGWEQNPNEYISVEGKKVIVLGGGDTAMDCNRTSIRQGAEQVT-------CAY 320
Cdd:TIGR01317 242 RDLPIPGRELKGIHYAMEFLPSATKALLGKDFKDIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHqfeimpkPPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 321 RRDEANM----PGSRReVKNAREEGVNfLFNRQP-------IEIVG-ENGQVTGVKVVTTQLgAPDSRGRRSPEPIPGSE 388
Cdd:TIGR01317 322 ARAKDNPwpewPRVYR-VDYAHEEAAA-HYGRDPreysiltKEFIGdDEGKVTALRTVRVEW-KKSQDGKWQFVEIPGSE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 389 EVLAADAVLLAFGFRPSPADWFAPANIGLDGSGRVLAAEQQqykFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGIL 468
Cdd:TIGR01317 399 EVFEADLVLLAMGFVGPEQILLDDFGVKKTRRGNISAGYDD---YSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVD 475
|
...
gi 881045658 469 DYL 471
Cdd:TIGR01317 476 RYL 478
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
56-471 |
3.95e-101 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 313.74 E-value: 3.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 56 PYCEWKCPVHNYIPNWLKLIAEGRIFQAAELCHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGNAEKYINDTAFA 135
Cdd:PRK12771 47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCNRGQVDDAVGINAVERFLGDYAIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 136 LGWRPDMSSVKwTDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRrrEI--FTGMG 213
Cdd:PRK12771 125 NGWKFPAPAPD-TGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDA--EIqrILDLG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 214 VEFRLNVEIGTDITIDQLLQDYDAVFMGMGTYTYMKGGFPGEELEGVYDALDFLiANVNRtqgweqnpNEYISVeGKKVI 293
Cdd:PRK12771 202 VEVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFL-RAVGE--------GEPPFL-GKRVV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 294 VLGGGDTAMDCNRTSIRQGAEQVTCAYRRDEANMPGSRREVKNAREEGVNFLFNRQPIEIVGENGQVTGVKVVTTQLGAP 373
Cdd:PRK12771 272 VIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLRVITVEKMEL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 374 DSRGRrsPEPIPGSEEVLAADAVLLAFG----FRPspadwFAPANIGLDGSGRVLAAEQQQykfQTSNPKIFAGGDMVRG 449
Cdd:PRK12771 352 DEDGR--PSPVTGEEETLEADLVVLAIGqdidSAG-----LESVPGVEVGRGVVQVDPNFM---MTGRPGVFAGGDMVPG 421
|
410 420
....*....|....*....|..
gi 881045658 450 SDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK12771 422 PRTVTTAIGHGKKAARNIDAFL 443
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
19-471 |
9.80e-98 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 315.73 E-value: 9.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 19 PEKKDIDvRKSEFVEIYKPFTAEVAANQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEgRIFQAA-ELCHQTNTLPEVC 97
Cdd:PRK12775 303 PERDAVE-RARNFKEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVV-RDFDGAlEVIYEASIFPSIC 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 98 GRVCPQDRLCEGACTLNDGFGAVTIGNAEKYINDTAFAlgwrPDMSSVKWTDK--KVAIIGAGPAGLGCADILVRNGVKP 175
Cdd:PRK12775 381 GRVCPQETQCEAQCIIAKKHESVGIGRLERFVGDNARA----KPVKPPRFSKKlgKVAICGSGPAGLAAAADLVKYGVDV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 176 VVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQD--YDAVFMGMGTYTYMKGGFP 253
Cdd:PRK12775 457 TVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGAGAPTFLGIP 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 254 GEELEGVYDALDFLiANVNRTQG----WEQNPneyISVeGKKVIVLGGGDTAMDCNRTSIRQGAEQVTCAYRRDEANMPG 329
Cdd:PRK12775 537 GEFAGQVYSANEFL-TRVNLMGGdkfpFLDTP---ISL-GKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 330 SRREVKNAREEGVNFLFNRQPIEI-VGENGQVTGVKVVTTQLGAPDSRGRRSPEPIpGSEEVLAADAVLLAFGFRPSPAD 408
Cdd:PRK12775 612 RIEEIRHAKEEGIDFFFLHSPVEIyVDAEGSVRGMKVEEMELGEPDEKGRRKPMPT-GEFKDLECDTVIYALGTKANPII 690
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881045658 409 WFAPANIGLDGSGRVLAAEQQQYKFQTSN-PKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK12775 691 TQSTPGLALNKWGNIAADDGKLESTQSTNlPGVFAGGDIVTGGATVILAMGAGRRAARSIATYL 754
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
50-471 |
1.03e-89 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 286.62 E-value: 1.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 50 CLGCGNPyCEWKCPVHNYIPNWLKLIAEGRIFQAAELCHQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGNAEKYI 129
Cdd:PRK12814 97 CGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDEPVSICALKRYA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 130 --NDTAFALGWRPDMSsvKWTDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRRE 207
Cdd:PRK12814 174 adRDMESAERYIPERA--PKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADIA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 208 IFTGMGVEFRLNVEIGTDITIDQLLQDYDAVFMGMGTYTYMKGGFPGEELEGVYDALDFLiANVNrtQGWEQNPneyisv 287
Cdd:PRK12814 252 PLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFL-RNVA--LGTALHP------ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 288 eGKKVIVLGGGDTAMDCNRTSIRQGAEQVTCAYRRDEANMPGSRREVKNAREEGVNFLFNRQPIEIVGENGQVTgVKVVT 367
Cdd:PRK12814 323 -GKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGGLE-LTAIK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 368 TQLGAPDSRGRRSPEPIPGSEEVLAADAVLLAFGFRPSPADWFAPAnIGLDGSGRVLAAEQQQykfQTSNPKIFAGGDMV 447
Cdd:PRK12814 401 MQQGEPDESGRRRPVPVEGSEFTLQADTVISAIGQQVDPPIAEAAG-IGTSRNGTVKVDPETL---QTSVAGVFAGGDCV 476
|
410 420
....*....|....*....|....
gi 881045658 448 RGSDLVVTAIWEGRQAAEGILDYL 471
Cdd:PRK12814 477 TGADIAINAVEQGKRAAHAIDLFL 500
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
148-472 |
1.52e-83 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 261.46 E-value: 1.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 148 TDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTD-- 225
Cdd:PRK12770 17 TGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTKVCCGep 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 226 -------------ITIDQLLQDYDAVFMGMGTYTYMKGGFPGEELEGVYDALDFLIanvnRTQGWEQN--PNEYI-SVEG 289
Cdd:PRK12770 97 lheeegdefveriVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLF----RIRAAKLGylPWEKVpPVEG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 290 KKVIVLGGGDTAMDCNRTSIRQGAEQVTCAYRRDEANMPGSRREVKNAREEGVNFLFNRQPIEIVGENGqVTGVKVVTTQ 369
Cdd:PRK12770 173 KKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIGEGR-VEGVELAKMR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 370 LGAPDSRGRRSPEPIPGSEEVLAADAVLLAFGFRPSPAdwFAPANIG--LDGSGRVLAAEqqqyKFQTSNPKIFAGGDMV 447
Cdd:PRK12770 252 LGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPP--FAKECLGieLNRKGEIVVDE----KHMTSREGVFAAGDVV 325
|
330 340
....*....|....*....|....*
gi 881045658 448 RGSDLVVTAIWEGRQAAEGILDYLD 472
Cdd:PRK12770 326 TGPSKIGKAIKSGLRAAQSIHEWLD 350
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
8-471 |
4.95e-81 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 262.78 E-value: 4.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 8 DFQFLDVARQDPEKKDIDVRKSEFVEIYKPFTAEVAANQTHRCLGCGnpYCEWKCPVHNYIPNWLKLIAEGRIFQAAELC 87
Cdd:PRK13984 145 NSELLDLERVEMEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 88 HQTNTLPEVCGRVCPQDrlCEGACTLNDGFGAVTIGNAEKYINDTAFALGWRP--DMSSVKwTDKKVAIIGAGPAGLGCA 165
Cdd:PRK13984 223 YKTNPLSMVCGRVCTHK--CETVCSIGHRGEPIAIRWLKRYIVDNVPVEKYSEilDDEPEK-KNKKVAIVGSGPAGLSAA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 166 DILVRNGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITIDQLLQDYDAVFMGMGTY 245
Cdd:PRK13984 300 YFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 246 TYMKGGFPGEELEGVYDALDFL--IANVNRTQGweqnPNEYISvegKKVIVLGGGDTAMDCNRTSIR-QGAE------QV 316
Cdd:PRK13984 380 LGRSTRIPGTDHPDVIQALPLLreIRDYLRGEG----PKPKIP---RSLVVIGGGNVAMDIARSMARlQKMEygevnvKV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 317 TCaYRRDEANMPGSRREVKNAREEGVNFLFNRQPIEIVGENGQVTGVKVVTTqLGAPDSRGRRSPEPIPGSEEVLAADAV 396
Cdd:PRK13984 453 TS-LERTFEEMPADMEEIEEGLEEGVVIYPGWGPMEVVIENDKVKGVKFKKC-VEVFDEEGRFNPKFDESDQIIVEADMV 530
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881045658 397 LLAFGFRPS----PADWFAPANIgldGSGRVLAAEQQqykfQTSNPKIFAGGDMVRGSDlVVTAIWEGRQAAEGILDYL 471
Cdd:PRK13984 531 VEAIGQAPDysylPEELKSKLEF---VRGRILTNEYG----QTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYL 601
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
62-472 |
2.20e-63 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 221.24 E-value: 2.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 62 CPVHNYIPNWLKLIAEGRIFQAAELCHQTNTLPEVCGRVCPQDRLCEGACTLNDgfGAVTIGNAEKYI--------NDTA 133
Cdd:PRK12779 214 CPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTK--RPIEIGQLEWYLpqheklvnPNAN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 134 FALGWRPDmSSVKWTDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGLLTFGIPEFKMEKDVMKRRREIFTGMG 213
Cdd:PRK12779 292 ERFAGRIS-PWAAAVKPPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLG 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 214 VEFRLNVEIGTDITIDQLLQD-YDAVFMGMGT--YTYMKggFPGEELEGVYDALDFLiANVNRTQGweqNPNEYIS---- 286
Cdd:PRK12779 371 GRFVKNFVVGKTATLEDLKAAgFWKIFVGTGAglPTFMN--VPGEHLLGVMSANEFL-TRVNLMRG---LDDDYETplpe 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 287 VEGKKVIVLGGGDTAMDCNRTSIRQGAeQVTCAYRRDEANMPGSRREVKNAREEGVNFLFNRQPIEIVG--ENGQVTGVK 364
Cdd:PRK12779 445 VKGKEVFVIGGGNTAMDAARTAKRLGG-NVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGddHTHFVTHAL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 365 VVTTQLGAPDSRGRRSPEPIpGSEEVLAADAVLLAFGFRPSPADWFAPANIGLDGSGRVLAAEQQQykfQTSNPKIFAGG 444
Cdd:PRK12779 524 LDVNELGEPDKSGRRSPKPT-GEIERVPVDLVIMALGNTANPIMKDAEPGLKTNKWGTIEVEKGSQ---RTSIKGVYSGG 599
|
410 420
....*....|....*....|....*...
gi 881045658 445 DMVRGSDLVVTAIWEGRQAAEGILDYLD 472
Cdd:PRK12779 600 DAARGGSTAIRAAGDGQAAAKEIVGEIP 627
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
27-138 |
1.35e-55 |
|
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: 180.43 E-value: 1.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 27 RKSEFVEIYKPFTAEVAANQTHRCLGCGNPYCEWKCPVHNYIPNWLKLIAEGRIFQAAELCHQTNTLPEVCGRVCPQDRL 106
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 881045658 107 CEGACTLN-DGFGAVTIGNAEKYINDTAFALGW 138
Cdd:pfam14691 81 CEGACVLGkKGFEPVAIGRLERFAADWARENGI 113
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
151-472 |
2.42e-35 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 133.32 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 151 KVAIIGAGPAGLGCADILVRNGVKPVVFDkRPEIGGLLT--------FGIPEFKMEKDVMKRRREIFTGMGVEFRL---- 218
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLAttkeienyPGFPEGISGPELAERLREQAERFGAEILLeevt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 219 NVEIGTD---ITIDQLLQdY--DAVFMGMGTYtYMKGGFPGEEL---EGVY-----DALDFlianvnrtqgweqnpneyi 285
Cdd:COG0492 81 SVDKDDGpfrVTTDDGTE-YeaKAVIIATGAG-PRKLGLPGEEEfegRGVSycatcDGFFF------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 286 svEGKKVIVLGGGDTAMD--CNRTSIrqgAEQVTCAYRRDEANmpGSRREVKNARE-EGVNFLFNRQPIEIVGENGqVTG 362
Cdd:COG0492 140 --RGKDVVVVGGGDSALEeaLYLTKF---ASKVTLIHRRDELR--ASKILVERLRAnPKIEVLWNTEVTEIEGDGR-VEG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 363 VKVVTTQlgapdsrgrrspepiPGSEEVLAADAVLLAFGFRPSpADWFAPANIGLDGSGRVLAAEqqqyKFQTSNPKIFA 442
Cdd:COG0492 212 VTLKNVK---------------TGEEKELEVDGVFVAIGLKPN-TELLKGLGLELDEDGYIVVDE----DMETSVPGVFA 271
|
330 340 350
....*....|....*....|....*....|.
gi 881045658 443 GGDMVRGS-DLVVTAIWEGRQAAEGILDYLD 472
Cdd:COG0492 272 AGDVRDYKyRQAATAAGEGAIAALSAARYLE 302
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-460 |
6.46e-28 |
|
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: 112.80 E-value: 6.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEI---GGLLTFGI-------PEFKMEKDVMKRRREIFTGM--GVEFR 217
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpygGCVLSKALlgaaeapEIASLWADLYKRKEEVVKKLnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 218 LNVEiGTDITID-QLLQDYDAVFMGMGTYTYMK-----GGFPGE-ELEGVYDALDFLIANVNRTQGWEQNPNEyisvegK 290
Cdd:pfam07992 81 LGTE-VVSIDPGaKKVVLEELVDGDGETITYDRlviatGARPRLpPIPGVELNVGFLVRTLDSAEALRLKLLP------K 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 291 KVIVLGGGDTAMDCNRTSIRQGAEqVTCAYRRDEANMP----GSRREVKNAREEGVNFLFNRQPIEIVGENGqvtGVKVV 366
Cdd:pfam07992 154 RVVVVGGGYIGVELAAALAKLGKE-VTLIEALDRLLRAfdeeISAALEKALEKNGVEVRLGTSVKEIIGDGD---GVEVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 367 TtqlgapdsrgrrspepipGSEEVLAADAVLLAFGFRPSPaDWFAPANIGLDGSGRVLAAEQQqykfQTSNPKIFAGGDM 446
Cdd:pfam07992 230 L------------------KDGTEIDADLVVVAIGRRPNT-ELLEAAGLELDERGGIVVDEYL----RTSVPGIYAAGDC 286
|
330
....*....|....*
gi 881045658 447 -VRGSDLVVTAIWEG 460
Cdd:pfam07992 287 rVGGPELAQNAVAQG 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
151-471 |
1.68e-20 |
|
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: 91.53 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 151 KVAIIGAGPAGLGCADILVRNGVKPVVFDkRPEIGGLLTF--------GIPEFKMEKDVMKRRREIFTGMGVEFRLNVEI 222
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIE-GMEPGGQLTTttevenypGFPEGISGPELMEKMKEQAVKFGAEIIYEEVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 223 GTD--------ITIDQLLQDYDAVFMGMGTyTYMKGGFPGEElegvydalDFLIANVNrtqgweqnpneYISV------E 288
Cdd:TIGR01292 80 KVDksdrpfkvYTGDGKEYTAKAVIIATGA-SARKLGIPGED--------EFWGRGVS-----------YCATcdgpffK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 289 GKKVIVLGGGDTAMD--CNRTSIrqgAEQVTCAYRRDeanmpGSRRE---VKNARE-EGVNFLFNRQPIEIVGENGqVTG 362
Cdd:TIGR01292 140 NKEVAVVGGGDSAIEeaLYLTRI---AKKVTLVHRRD-----KFRAEkilLDRLKKnPKIEFLWNSTVEEIVGDNK-VEG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 363 VKVVTTQlgapdsrgrrspepiPGSEEVLAADAVLLAFGFRPSPAdwFAPANIGLDGSGRVLAAEQQqykfQTSNPKIFA 442
Cdd:TIGR01292 211 VKIKNTV---------------TGEEEELEVDGVFIAIGHEPNTE--LLKGLLELDENGYIVTDEGM----RTSVPGVFA 269
|
330 340 350
....*....|....*....|....*....|.
gi 881045658 443 GGDmVRGSDL--VVTAIWEGRQAAEGILDYL 471
Cdd:TIGR01292 270 AGD-VRDKGYrqAVTAAGDGCIAALSAERYL 299
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
152-427 |
1.72e-16 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 81.67 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 152 VAIIGAGPAGLGCADILVR--NGVKPVVFDKRPEIGGLLTFGI-PEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITI 228
Cdd:PLN02852 29 VCVVGSGPAGFYTADKLLKahDGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVTLGRDVSL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 229 DQLLQDYDAVFMGMGTYTYMKGGFPGEELEGVYDALDFLianvnrtqGWEQNPNEYIS-----VEGKKVIVLGGGDTAMD 303
Cdd:PLN02852 109 SELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFV--------WWYNGHPDCVHlppdlKSSDTAVVLGQGNVALD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 304 CNR-----------TSI--------------------RQGAEQVTCA--------------YRRDEANM---PGSRREVK 335
Cdd:PLN02852 181 CARillrptdelasTDIaehalealrgssvrkvylvgRRGPVQAACTakelrellglknvrVRIKEADLtlsPEDEEELK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 336 NAR-----------------------EEGVNFLFNRQPIEIV---GENGQVTGVKVVTTQLGAPDSRGRRSPEPIpGSEE 389
Cdd:PLN02852 261 ASRpkrrvyellskaaaagkcapsggQRELHFVFFRNPTRFLdsgDGNGHVAGVKLERTVLEGAAGSGKQVAVGT-GEFE 339
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 881045658 390 VLAADAVLLAFGFRPSPAD--WFAPAN-IGLDGSGRVLAAE 427
Cdd:PLN02852 340 DLPCGLVLKSIGYKSLPVDglPFDHKRgVVPNVHGRVLSSA 380
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
173-468 |
8.69e-14 |
|
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: 72.15 E-value: 8.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 173 VKPVVFDKRPEIG----GLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNVEIgTDITIDQ---LLQD-----YDAVFM 240
Cdd:COG0446 6 AEITVIEKGPHHSyqpcGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEV-TAIDPEAktvTLRDgetlsYDKLVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 241 GMGTyTYMKGGFPGEELEGVY-----DALDFLIANVNrtqgweqnpneyiSVEGKKVIVLGGG------DTAMdcnrtsI 309
Cdd:COG0446 85 ATGA-RPRPPPIPGLDLPGVFtlrtlDDADALREALK-------------EFKGKRAVVIGGGpiglelAEAL------R 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 310 RQGAEqVTCAYRRDEAnMPGSRREV-----KNAREEGVNFLFNRQPIEIVGENGqvtgVKVVTTqlgapdsrgrrspepi 384
Cdd:COG0446 145 KRGLK-VTLVERAPRL-LGVLDPEMaalleEELREHGVELRLGETVVAIDGDDK----VAVTLT---------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 385 pgSEEVLAADAVLLAFGFRPSpADWFAPANIGLDGSGRVLAAEQQqykfQTSNPKIFAGGDMVRGSDLVV---------- 454
Cdd:COG0446 203 --DGEEIPADLVVVAPGVRPN-TELAKDAGLALGERGWIKVDETL----QTSDPDVYAAGDCAEVPHPVTgktvyiplas 275
|
330
....*....|....
gi 881045658 455 TAIWEGRQAAEGIL 468
Cdd:COG0446 276 AANKQGRVAAENIL 289
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
152-468 |
5.18e-13 |
|
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: 70.89 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 152 VAIIGAGPAGLGCADILVRNGVKPVVFDKRPeIGG------------LL-------------TFGI----PEFKMEKdVM 202
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGGtclnvgcipskaLLhaaevahearhaaEFGIsagaPSVDWAA-LM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 203 KRRREIFTGM--GVEFRL---NVEI--GTditidqllqdydAVF--------MGMGTYTYMK-----GG------FPGEE 256
Cdd:COG1249 84 ARKDKVVDRLrgGVEELLkknGVDVirGR------------ARFvdphtvevTGGETLTADHiviatGSrprvppIPGLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 257 LEGVYDALDFLianvnrtqGWEQNPneyisvegKKVIVLGGGdtamdcnrtSIrqGAE----------QVTCAYRRDEAn 326
Cdd:COG1249 152 EVRVLTSDEAL--------ELEELP--------KSLVVIGGG---------YI--GLEfaqifarlgsEVTLVERGDRL- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 327 MPGSRREV-----KNAREEGVNFLFNRQPIEIVGENGqvtGVKVVTTQlgapdsrgrrspepiPGSEEVLAADAVLLAFG 401
Cdd:COG1249 204 LPGEDPEIsealeKALEKEGIDILTGAKVTSVEKTGD---GVTVTLED---------------GGGEEAVEADKVLVATG 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881045658 402 FRPSPADwFAPANIG--LDGSGRVLAAEQqqykFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGIL 468
Cdd:COG1249 266 RRPNTDG-LGLEAAGveLDERGGIKVDEY----LRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENIL 329
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
150-468 |
4.35e-10 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 61.31 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNG--VKPVVFDK-------RPeiggLLTFGIPEFKMEKDVMKRRREIFTGMGVEFRLNV 220
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDpdGEITVIGAephppynRP----PLSKVLAGETDEEDLLLRPADFYEENGIDLRLGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 221 EIgTDI--------TIDQLLQDYDAVFMGMGTYTYMkGGFPGEELEGVY------DAlDFLIANVNRtqgweqnpneyis 286
Cdd:COG1251 78 RV-TAIdraartvtLADGETLPYDKLVLATGSRPRV-PPIPGADLPGVFtlrtldDA-DALRAALAP------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 287 veGKKVIVLGGG----DTAMDCnrtsIRQGAEqVTCAYRRD---EANMP--GSRREVKNAREEGVNFLFNRQPIEIVGEn 357
Cdd:COG1251 142 --GKRVVVIGGGliglEAAAAL----RKRGLE-VTVVERAPrllPRQLDeeAGALLQRLLEALGVEVRLGTGVTEIEGD- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 358 GQVTGVKVvttqlgapdsrgrrspepipGSEEVLAADAVLLAFGFRPspADWFApANIGLDGSGRVLAAEQqqykFQTSN 437
Cdd:COG1251 214 DRVTGVRL--------------------ADGEELPADLVVVAIGVRP--NTELA-RAAGLAVDRGIVVDDY----LRTSD 266
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 881045658 438 PKIFAGGD------MVRGSDLV--VTAIWE-GRQAAEGIL 468
Cdd:COG1251 267 PDIYAAGDcaehpgPVYGRRVLelVAPAYEqARVAAANLA 306
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
148-353 |
2.17e-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: 59.11 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 148 TDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGG---------------LLTFGIPEFKME--------KDVMKR 204
Cdd:COG2072 5 EHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpSHLYSLPFFPNWsddpdfptGDEILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 205 -----------RREIFTGMGVE----------FRLNVEIGTDITidqllqdYDAVFMGMGTYTymKG---GFPGEElegv 260
Cdd:COG2072 85 yleayadkfglRRPIRFGTEVTsarwdeadgrWTVTTDDGETLT-------ARFVVVATGPLS--RPkipDIPGLE---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 261 ydalDFLIANVnRTQGWeqnPNEYiSVEGKKVIVLGGGDTAMDCnRTSIRQGAEQVTCAYRRdeANMPGSRREVKNAREE 340
Cdd:COG2072 152 ----DFAGEQL-HSADW---RNPV-DLAGKRVLVVGTGASAVQI-APELARVAAHVTVFQRT--PPWVLPRPNYDPERGR 219
|
250
....*....|...
gi 881045658 341 GVNFLFNRQPIEI 353
Cdd:COG2072 220 PANYLGLEAPPAL 232
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
151-199 |
6.47e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 57.97 E-value: 6.47e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 881045658 151 KVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGLL-TFGIPEFKMEK 199
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIER 50
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
151-243 |
1.03e-08 |
|
adrenodoxin reductase; Provisional
Pssm-ID: 240308 Cd Length: 506 Bit Score: 57.20 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 151 KVAIIGAGPAGLGCADILVRN-GVKPVVFDKRPEIGGLLTFGI-PEFKMEKDVMKRRREIFTGMGVEFRLNVEIGTDITI 228
Cdd:PTZ00188 41 KVGIIGAGPSALYCCKHLLKHeRVKVDIFEKLPNPYGLIRYGVaPDHIHVKNTYKTFDPVFLSPNYRFFGNVHVGVDLKM 120
|
90
....*....|....*
gi 881045658 229 DQLLQDYDAVFMGMG 243
Cdd:PTZ00188 121 EELRNHYNCVIFCCG 135
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
150-187 |
3.35e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 55.67 E-value: 3.35e-08
10 20 30
....*....|....*....|....*....|....*...
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGL 187
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
150-188 |
4.89e-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: 4.89e-08
10 20 30
....*....|....*....|....*....|....*....
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGLL 188
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
150-186 |
4.92e-08 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 54.50 E-value: 4.92e-08
10 20 30
....*....|....*....|....*....|....*..
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGG 186
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
145-211 |
2.43e-07 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 52.81 E-value: 2.43e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881045658 145 VKWTDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKrpeiGglltfgipefkmeKDVMKRRREIFTG 211
Cdd:COG2509 26 IPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLER----G-------------KDVEERTCPVAEF 75
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
154-186 |
3.57e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 47.14 E-value: 3.57e-07
10 20 30
....*....|....*....|....*....|...
gi 881045658 154 IIGAGPAGLGCADILVRNGVKPVVFDKRPEIGG 186
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGG 33
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
150-471 |
1.66e-06 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 50.13 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPV---VFDKRPE----------IGGLLTFGipefkmekDVMKRRREIFTGMGVEF 216
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKLGGDAevtLIDPNPYhlfqpllpevAAGTLSPD--------DIAIPLRELLRRAGVRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 217 RL-------------NVEIGTDItidqllqDYDAVFMGMGTyTYMKGGFPG-EE----LEGVYDALDFlianvnRTQgWE 278
Cdd:COG1252 74 IQgevtgidpeartvTLADGRTL-------SYDYLVIATGS-VTNFFGIPGlAEhalpLKTLEDALAL------RER-LL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 279 QNPNEYISVEGKKVIVLGGGDT------AMD------CNRTSIRQGAEQVTCAYRRDEAnMPGSRREVKNA-----REEG 341
Cdd:COG1252 139 AAFERAERRRLLTIVVVGGGPTgvelagELAellrklLRYPGIDPDKVRITLVEAGPRI-LPGLGEKLSEAaekelEKRG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 342 VNFLFNRQPIEIVGEngqvtgvKVVTTqlgapdsrgrrspepipgSEEVLAADAVLLAFGFRPSPadWFAPANIGLDGSG 421
Cdd:COG1252 218 VEVHTGTRVTEVDAD-------GVTLE------------------DGEEIPADTVIWAAGVKAPP--LLADLGLPTDRRG 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 881045658 422 RVLAAEQQQYkfqTSNPKIFAGGDMVRGSD--------LVVTAIWEGRQAAEGILDYL 471
Cdd:COG1252 271 RVLVDPTLQV---PGHPNVFAIGDCAAVPDpdgkpvpkTAQAAVQQAKVLAKNIAALL 325
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
148-186 |
2.06e-06 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 49.92 E-value: 2.06e-06
10 20 30
....*....|....*....|....*....|....*....
gi 881045658 148 TDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGG 186
Cdd:COG1231 6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
152-470 |
2.13e-06 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 49.79 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 152 VAIIGAGPAGLGCADILVRNGVKPVVFDKRP------------------------EIGGLLTFGI--PEFKME-KDVMKR 204
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPlggtclnvgcipskaliaaaeafhEAKHAEEFGIhaDGPKIDfKKVMAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 205 RREI---FTGMGVEFRLNVEigtdiTIDqLLQDYdAVFMGMGTytyMKGGfpGEELEGVYdaldFLIANVNRT----QGW 277
Cdd:PRK06292 86 VRRErdrFVGGVVEGLEKKP-----KID-KIKGT-ARFVDPNT---VEVN--GERIEAKN----IVIATGSRVppipGVW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 278 EQNPNEYISVEG--------KKVIVLGGGdtamdcnrtSIrqGAE----------QVTCAYRRDE--ANM-PGSRREVKN 336
Cdd:PRK06292 150 LILGDRLLTSDDafeldklpKSLAVIGGG---------VI--GLElgqalsrlgvKVTVFERGDRilPLEdPEVSKQAQK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 337 AREEGVNFLFNRQPIEIVGENGQvtgvKVVTTQLGapdsrgrrspepipGSEEVLAADAVLLAFGFRP-SPADWFAPANI 415
Cdd:PRK06292 219 ILSKEFKIKLGAKVTSVEKSGDE----KVEELEKG--------------GKTETIEADYVLVATGRRPnTDGLGLENTGI 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 881045658 416 GLDGSGRVLAAEqqqyKFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILDY 470
Cdd:PRK06292 281 ELDERGRPVVDE----HTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGD 331
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
148-196 |
7.77e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 48.31 E-value: 7.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 881045658 148 TDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGLL-TFGIPEFK 196
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRArTFERPGFR 51
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
144-243 |
1.02e-05 |
|
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: 47.31 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 144 SVKWTDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGglltfgipeFKMEKDVMKRRREIFTGMGVEFRLNVE-- 221
Cdd:pfam07992 147 RLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLL---------RAFDEEISAALEKALEKNGVEVRLGTSvk 217
|
90 100
....*....|....*....|....*....
gi 881045658 222 --IGTDITIDQLLQD-----YDAVFMGMG 243
Cdd:pfam07992 218 eiIGDGDGVEVILKDgteidADLVVVAIG 246
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
150-186 |
1.17e-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: 47.54 E-value: 1.17e-05
10 20 30
....*....|....*....|....*....|....*..
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGG 186
Cdd:COG3349 4 PRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
151-222 |
1.42e-05 |
|
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: 42.96 E-value: 1.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881045658 151 KVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGlltfgipefKMEKDVMKRRREIFTGMGVEFRLNVEI 222
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP---------GFDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
147-183 |
1.46e-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: 47.38 E-value: 1.46e-05
10 20 30
....*....|....*....|....*....|....*..
gi 881045658 147 WTDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPE 183
Cdd:COG0771 2 LKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPA 38
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
291-368 |
2.96e-05 |
|
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: 42.19 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 291 KVIVLGGGDTAMDCNrTSIRQGAEQVTCAYRRDEAnMPGSRREV-----KNAREEGVNFLFNRQPIEIVGENGqvtGVKV 365
Cdd:pfam00070 1 RVVVVGGGYIGLELA-GALARLGSKVTVVERRDRL-LPGFDPEIakilqEKLEKNGIEFLLNTTVEAIEGNGD---GVVV 75
|
...
gi 881045658 366 VTT 368
Cdd:pfam00070 76 VLT 78
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
148-464 |
4.62e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 46.01 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 148 TDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGL---LTFGIPEFK--------MEKDVMKRRR-EIFTGMGVE 215
Cdd:COG1148 139 VNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDcpqcilepLIAEVEANPNiTVYTGAEVE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 216 --------FRLNVEIG--TDITIdqllqDYDAVFMGMGtYTYMKGGFPGE----ELEGVYDALDF---LIANVNRTQGWE 278
Cdd:COG1148 219 evsgyvgnFTVTIKKGprEEIEI-----EVGAIVLATG-FKPYDPTKLGEygygKYPNVITNLELerlLAAGKILRPSDG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 279 QNPNeyiSVegkkVIVL--GGGDTAMD---CNR----TSIRQGAE--------QVTCAYR--RdeanMPGsRRE--VKNA 337
Cdd:COG1148 293 KEPK---SV----AFIQcvGSRDEENGlpyCSRvccmYALKQALYlkeknpdaDVYIFYRdiR----TYG-KYEefYRRA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 338 REEGVNFLfnR-QPIEIV-GENGQVTgVKVVTTQLGapdsrgrrspEPIpgseeVLAADAVLLAFGFRPSP-ADWFA-PA 413
Cdd:COG1148 361 REDGVRFI--RgRVAEIEeDEGGKLV-VTVEDTLLG----------EPV-----EIEADLVVLATGMVPSEdNEELAkLL 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 881045658 414 NIGLDGSGRVLAAEQQQYKFQTSNPKIFAGGdMVRGSDLVVTAIWEGRQAA 464
Cdd:COG1148 423 KLPLDQDGFFLEAHPKLRPVETATDGIFLAG-AAHGPKDIPESIAQATAAA 472
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
151-237 |
7.29e-05 |
|
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: 44.70 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 151 KVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIG--------GLLTFGIPE------FKMEKDVMKRRREIF--TGMGV 214
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYlepselARLALEALDLWEELEeeLGIDC 80
|
90 100
....*....|....*....|....*
gi 881045658 215 EFRLN--VEIGTDITIDQLLQDYDA 237
Cdd:pfam01266 81 GFRRCgvLVLARDEEEEALEKLLAA 105
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
150-185 |
1.46e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 44.11 E-value: 1.46e-04
10 20 30
....*....|....*....|....*....|....*.
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIG 185
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
153-185 |
1.55e-04 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 43.89 E-value: 1.55e-04
10 20 30
....*....|....*....|....*....|...
gi 881045658 153 AIIGAGPAGLGCADILVRNGVKPVVFDKRPEIG 185
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
148-185 |
1.91e-04 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 43.39 E-value: 1.91e-04
10 20 30
....*....|....*....|....*....|....*...
gi 881045658 148 TDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIG 185
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
150-243 |
1.99e-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: 43.26 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPeigGLLTFGIPEF-KMEKDVMKRRreiftgmGVEFRLNVEI----GT 224
Cdd:COG0446 125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERAP---RLLGVLDPEMaALLEEELREH-------GVELRLGETVvaidGD 194
|
90 100
....*....|....*....|...
gi 881045658 225 D----ITIDQLLQDYDAVFMGMG 243
Cdd:COG0446 195 DkvavTLTDGEEIPADLVVVAPG 217
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
148-187 |
2.09e-04 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 43.70 E-value: 2.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 881045658 148 TDKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGL 187
Cdd:PLN02172 9 NSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGL 48
|
|
| Malic_M |
smart00919 |
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ... |
148-198 |
2.18e-04 |
|
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: 42.79 E-value: 2.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 881045658 148 TDKKVAIIGAGPAGLGCADILVRNGVKP---VVFDKRpeigGLLTFG----IPEFKME 198
Cdd:smart00919 24 EDQRIVVNGAGAAGIGIAKLLVAAGVKRkniWLVDSK----GLLTKGrednLNPYKKP 77
|
|
| PRK08243 |
PRK08243 |
4-hydroxybenzoate 3-monooxygenase; Validated |
151-181 |
2.73e-04 |
|
4-hydroxybenzoate 3-monooxygenase; Validated
Pssm-ID: 236198 [Multi-domain] Cd Length: 392 Bit Score: 43.25 E-value: 2.73e-04
10 20 30
....*....|....*....|....*....|.
gi 881045658 151 KVAIIGAGPAGLGCADILVRNGVKPVVFDKR 181
Cdd:PRK08243 4 QVAIIGAGPAGLLLGQLLHLAGIDSVVLERR 34
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
122-222 |
3.00e-04 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 43.15 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 122 IGNAEKYI--NDTAFALGWRPdmssvkwtdKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGlltfgipefKMEK 199
Cdd:COG1249 148 PGLDEVRVltSDEALELEELP---------KSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLP---------GEDP 209
|
90 100
....*....|....*....|...
gi 881045658 200 DVMKRRREIFTGMGVEFRLNVEI 222
Cdd:COG1249 210 EISEALEKALEKEGIDILTGAKV 232
|
|
| FMO-like |
pfam00743 |
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ... |
150-190 |
3.09e-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: 3.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGLLTF 190
Cdd:pfam00743 2 KKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRF 42
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
148-185 |
3.22e-04 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 43.02 E-value: 3.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 881045658 148 TDKKVAIIGAGPAGLGCADILVRNGVKP---VVFDKRPEIG 185
Cdd:COG4529 4 ARKRIAIIGGGASGTALAIHLLRRAPEPlriTLFEPRPELG 44
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
151-183 |
3.57e-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: 40.95 E-value: 3.57e-04
10 20 30
....*....|....*....|....*....|...
gi 881045658 151 KVAIIGAGPAGLGCADILVRNGVKPVVFDKRPE 183
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPA 54
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
150-186 |
5.44e-04 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 42.55 E-value: 5.44e-04
10 20 30
....*....|....*....|....*....|....*..
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGG 186
Cdd:PLN02976 694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
152-191 |
1.12e-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: 41.06 E-value: 1.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 881045658 152 VAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGLLTFG 191
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSG 41
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
153-185 |
2.43e-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: 40.27 E-value: 2.43e-03
10 20 30
....*....|....*....|....*....|...
gi 881045658 153 AIIGAGPAGLGCADILVRNGVKPVVFDKRPEIG 185
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
128-209 |
2.47e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 40.16 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 128 YINDTAFALGWRPdmssvkwtdKKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEIGGLltfgipefkMEKDVMKRRRE 207
Cdd:PRK06292 157 LTSDDAFELDKLP---------KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPL---------EDPEVSKQAQK 218
|
..
gi 881045658 208 IF 209
Cdd:PRK06292 219 IL 220
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
150-227 |
3.06e-03 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 39.72 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 150 KKVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEI--GG-LLTFGIPEFkmekDVMKRrreiftgMGVEFRLNvEIGTDI 226
Cdd:PRK07588 1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELrtGGyMVDFWGVGY----EVAKR-------MGITDQLR-EAGYQI 68
|
.
gi 881045658 227 T 227
Cdd:PRK07588 69 E 69
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
145-186 |
4.06e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 38.61 E-value: 4.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 881045658 145 VKWTDKKVAIIGAGPAGLGCADILVRN-GVKPVVFDKRPEIGG 186
Cdd:pfam01946 13 DDYAESDVVIVGAGSSGLTAAYYLAKNrGLKVAIIERSVSPGG 55
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
152-184 |
4.70e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 39.50 E-value: 4.70e-03
10 20 30
....*....|....*....|....*....|...
gi 881045658 152 VAIIGAGPAGLGCADILVRNGVKPVVFDKRPEI 184
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
282-424 |
4.83e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 38.74 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 282 NEYISVEGKKVIVLGGGDTAMDCNRTSIRQGAEqVTCAYRRDEANMPGS----------RREVKNAREEG-VNFLFNRQP 350
Cdd:pfam13738 148 KDFHPYAGQKVVVIGGYNSAVDAALELVRKGAR-VTVLYRGSEWEDRDSdpsyslspdtLNRLEELVKNGkIKAHFNAEV 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881045658 351 IEIVGENGQVtgvkVVTTQLGapdsrgrrspepipgsEEVLAADAVLLAFGFRPSpADWFAPANIGLDGSGRVL 424
Cdd:pfam13738 227 KEITEVDVSY----KVHTEDG----------------RKVTSNDDPILATGYHPD-LSFLKKGLFELDEDGRPV 279
|
|
| NAD_bind_2_malic_enz |
cd05311 |
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ... |
149-181 |
5.22e-03 |
|
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists primarily of archaeal and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133453 [Multi-domain] Cd Length: 226 Bit Score: 38.40 E-value: 5.22e-03
10 20 30
....*....|....*....|....*....|....*.
gi 881045658 149 DKKVAIIGAGPAGLGCADILVRNGVKP---VVFDKR 181
Cdd:cd05311 25 EVKIVINGAGAAGIAIARLLLAAGAKPeniVVVDSK 60
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
151-184 |
5.29e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 38.90 E-value: 5.29e-03
10 20 30
....*....|....*....|....*....|....
gi 881045658 151 KVAIIGAGPAGLGCADILVRNGVKPVVFDKRPEI 184
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
338-469 |
5.45e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 38.98 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 338 REEGVNFLFNRQPIEIVGENGQVtgvkVVTTQlgapdsrgrrspepipgSEEVLAADAVLLAFGfRPSPADWFAPANIGL 417
Cdd:PRK05249 227 RDSGVTIRHNEEVEKVEGGDDGV----IVHLK-----------------SGKKIKADCLLYANG-RTGNTDGLNLENAGL 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 881045658 418 --DGSGRVLAAEQqqykFQTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAEGILD 469
Cdd:PRK05249 285 eaDSRGQLKVNEN----YQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVG 334
|
|
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
151-205 |
6.81e-03 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 38.96 E-value: 6.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881045658 151 KVAIIGAGPAGLGCADILVRNGVKPVVFDKRPE----IGGlltfGIP-----EFKMEKDVMKRR 205
Cdd:PLN00093 41 RVAVIGGGPAGACAAETLAKGGIETFLIERKLDnakpCGG----AIPlcmvgEFDLPLDIIDRK 100
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
339-465 |
8.25e-03 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 38.60 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881045658 339 EEGVNFLFNRQPIEIV-GENGQVTgvkvVTTQLGapdsrgrrspepipgseEVLAADAVLLAFGFRPSpADWFAPANIG- 416
Cdd:PRK06116 220 KKGIRLHTNAVPKAVEkNADGSLT----LTLEDG-----------------ETLTVDCLIWAIGREPN-TDGLGLENAGv 277
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 881045658 417 -LDGSGRVLAAEQQQykfqTSNPKIFAGGDMVRGSDLVVTAIWEGRQAAE 465
Cdd:PRK06116 278 kLNEKGYIIVDEYQN----TNVPGIYAVGDVTGRVELTPVAIAAGRRLSE 323
|
|
| |
