|
Name |
Accession |
Description |
Interval |
E-value |
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
8-582 |
0e+00 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 1008.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 8 ASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKD-IRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLIN 86
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAERDrIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 87 GVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEIPVNF 166
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHNGVAVVTIPVDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 167 GFQEIDENSYYGSGSYERSFIAPALNEVEVDKAVEILNNAERPVIYAGYGGVKAGEVITELSRKIKAPIITTGKNFEAFE 246
Cdd:TIGR02720 161 GWQEIPDNDYYASSVSYQTPLLPAPDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 247 WNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFPFAEVYEAFKNTEKFIQVDIDPYKLGKRHALDASILGDAGQAAKA 326
Cdd:TIGR02720 241 DRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADAKKALAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 327 ILDKVNPVESTPWWRANVKNNQNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNM 406
Cdd:TIGR02720 321 ILAQVEPRESTPWWQANVANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 407 WRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIKDKYEDTNKHLF 486
Cdd:TIGR02720 401 WITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQPLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 487 GCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKlNKEGKTVVIDARISQHRPLPVEVLELDPKQHSEEAIKAFKE 566
Cdd:TIGR02720 481 GVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAKA-IKQGKPVLIDAKITGDRPLPVEKLRLDPALSSAADIEAFKE 559
|
570
....*....|....*.
gi 446113971 567 KYEAEELVPFRLFLEE 582
Cdd:TIGR02720 560 KYEAQELKPLSTYLKQ 575
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
5-545 |
3.76e-167 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 486.97 E-value: 3.76e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHL 84
Cdd:COG0028 2 KMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 85 INGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIP 163
Cdd:COG0028 82 VTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSgRPGPVVLDIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 164 VNFGFQEIDENSYygSGSYERSFIAPALNEVEVDKAVEILNNAERPVIYAGYGGVKAG--EVITELSRKIKAPIITTGKN 241
Cdd:COG0028 162 KDVQAAEAEEEPA--PPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGaaEELRALAERLGAPVVTTLMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 242 FEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFPFAE--VYEAFKNTEKFIQVDIDPYKLGKRHALDASILGD 319
Cdd:COG0028 240 KGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVtgNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 320 AGQAAKAILDKVNPVES-TPWWRANVKnnqNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQTSTRH 398
Cdd:COG0028 320 AKAVLAALLEALEPRADdRAAWLARIA---AWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 399 LHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIKDKY 478
Cdd:COG0028 397 LRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQ 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446113971 479 EDT-NKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVklnKEGKTVVIDARISQHRPLP 545
Cdd:COG0028 477 ELFyGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEAL---ASDGPALIDVRVDPEENPP 541
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
5-577 |
7.22e-165 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 482.19 E-value: 7.22e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKD-IRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATH 83
Cdd:PRK08611 3 KIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQDkIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 84 LINGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEIP 163
Cdd:PRK08611 83 LLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVLTIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 164 VNFGFQEIDENSYYGSGSYERSfiAPALNEVEVDKAVEILNNAERPVIYAGYGGVKAGEVITELSRKIKAPIITT--GKN 241
Cdd:PRK08611 163 DDLPAQKIKDTTNKTVDTFRPT--VPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTlpAKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 242 FEAFEWNYEglTGSAYRVGWKPANEVVFEADTVLFLGSNFPFAEVyeaFKNTEKFIQVDIDPYKLGKRHALDASILGDAG 321
Cdd:PRK08611 241 IIPDDHPYS--LGNLGKIGTKPAYEAMQEADLLIMVGTNYPYVDY---LPKKAKAIQIDTDPANIGKRYPVNVGLVGDAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 322 QAAKAILDKVNPVESTPWWRANVKNNQNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQTSTRHLHM 401
Cdd:PRK08611 316 KALHQLTENIKHVEDRRFLEACQENMAKWWKWMEEDENNASTPIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 402 TPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIkdKYEDT 481
Cdd:PRK08611 396 GTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFI--KYEQQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 482 NK-HL-FGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNkegKTVVIDARISQHR-PLPVEVLELDPKQHSE 558
Cdd:PRK08611 474 AAgELeYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQD---KPVIIDVYVDPNAaPLPGKIVNDEALGYSK 550
|
570
....*....|....*....
gi 446113971 559 EAIKAFKEKYEAEELVPFR 577
Cdd:PRK08611 551 WAIKSLFEDKKLDQMPPLK 569
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
7-569 |
2.02e-97 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 307.53 E-value: 2.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 7 TASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKdIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLIN 86
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSK-VKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 87 GVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEIPVNF 166
Cdd:PRK06457 82 GLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINLPVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 167 --GFQEIDENSYYGSGSYERSfiapalneVEVDKAVEILNNAERPVIYAGYGGVKAGEVITELSRKIKAPIIttgknfea 244
Cdd:PRK06457 162 lrKSSEYKGSKNTEVGKVKYS--------IDFSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPII-------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 245 FEWNYEGL--------TGSAYRVGWKPANEVVFEADTVLFLGSNFPfaevYEAFKNTE-KFIQVDIDPYKLGKRHALDAS 315
Cdd:PRK06457 226 YTLNGKGIlpdldpkvMGGIGLLGTKPSIEAMDKADLLIMLGTSFP----YVNFLNKSaKVIQVDIDNSNIGKRLDVDLS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 316 ILGDAGQaakaiLDKVNPVESTPWWRANVKNN-QNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQT 394
Cdd:PRK06457 302 YPIPVAE-----FLNIDIEEKSDKFYEELKGKkEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 395 STRHLHMTPKNMWRTSPLFATMGIALPGGIAAK-KDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAF 473
Cdd:PRK06457 377 TARHFRASGEQTFIFSAWLGSMGIGVPGSVGASfAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGM 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 474 IKDKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAvkLNKEGKTVVIDARISQHRPLPVevlELDP 553
Cdd:PRK06457 457 IKFEQEVMGYPEWGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEF--LNTKGPAVLDAIVDPNERPMPP---KLTF 531
|
570
....*....|....*.
gi 446113971 554 KQHSEEAIKAFKEKYE 569
Cdd:PRK06457 532 KQAGEYVLSIFREKLE 547
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
5-541 |
5.72e-90 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 288.81 E-value: 5.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHL 84
Cdd:PRK09124 2 KQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 85 INGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEIPV 164
Cdd:PRK09124 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVVLPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 165 NFGFQEIDENSYYGSGSYERSFIAPAlnEVEVDKAVEILNNAERPVIYAGYGGVKAGEVITELSRKIKAPIITTGKNFEA 244
Cdd:PRK09124 162 DVALKPAPERATPHWYHAPQPVVTPA--EEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRGKEH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 245 FEWN--YE-GLTGsayRVGWKPANEVVFEADTVLFLGSNFPfaevYEAFKNTE-KFIQVDIDPYKLGKRHALDASILGDA 320
Cdd:PRK09124 240 VEYDnpYDvGMTG---LIGFSSGYHAMMNCDTLLMLGTDFP----YRQFYPTDaKIIQIDINPGSLGRRSPVDLGLVGDV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 321 GQAAKAILDKVNPVESTPWWRANVKNNQNWRDYMNKLEGKTEGELQLYQVYNA--INKHADQDAIYSIDVGDTTQTSTRH 398
Cdd:PRK09124 313 KATLAALLPLLEEKTDRKFLDKALEHYRKARKGLDDLAVPSDGGKPIHPQYLArqISEFAADDAIFTCDVGTPTVWAARY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 399 LHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIKDKY 478
Cdd:PRK09124 393 LKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEM 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446113971 479 EDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAvkLNKEGKtVVIDARISQH 541
Cdd:PRK09124 473 KAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRA--FAHDGP-ALVDVVTAKQ 532
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-553 |
1.68e-79 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 261.86 E-value: 1.68e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 1 MTQGKITASAAMLNVLKTWGVDTIYGIPSgtlSSLMDA--LAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGG 78
Cdd:PRK07525 1 MGKMKMTPSEAFVETLQAHGITHAFGIIG---SAFMDAsdLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 79 PGATHLINGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPA 158
Cdd:PRK07525 78 PGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESGPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 159 VVEIPVNFGFQEIDENSYYGSgSYERsfiaPALNEVEVDKAVEILNNAERPVIYAGYGGVKAG--EVITELSRKIKAPII 236
Cdd:PRK07525 158 QINIPRDYFYGVIDVEIPQPV-RLER----GAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDaiEECKALAERLDAPVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 237 TTGKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNF-PFAEV--Y--EAFKNTEKFIQVDIDPYKLGKRHA 311
Cdd:PRK07525 233 CGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLnPFGTLpqYgiDYWPKDAKIIQVDINPDRIGLTKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 312 LDASILGDAGQAAKAILDKVNPVESTPWWRANVKNN-----QNWRDYMNKL---------------EGKTEGELQLYQVY 371
Cdd:PRK07525 313 VSVGICGDAKAVARELLARLAERLAGDAGREERKALiaaekSAWEQELSSWdhedddpgtdwneeaRARKPDYMHPRQAL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 372 NAINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDV 451
Cdd:PRK07525 393 REIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 452 ITNVQYDLPVINVVFSNGKYAFIK----DKYEDtnkHLFGCDFP-NADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLN 526
Cdd:PRK07525 473 MTAVRHNWPVTAVVFRNYQWGAEKknqvDFYNN---RFVGTELDnNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDAQ 549
|
570 580 590
....*....|....*....|....*....|....*.
gi 446113971 527 KEGKTVVIDARISQH--RP-------LPVEVLELDP 553
Cdd:PRK07525 550 NEGKTTVIEIMCNQElgEPfrrdalkKPVRVLGKYK 585
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
20-522 |
5.16e-79 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 260.31 E-value: 5.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 20 GVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYDAAMDNTPFL 99
Cdd:PRK06546 17 GVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLYDAHRSGAPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 100 AILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEIPVNFGFQEIDENSYYGS 179
Cdd:PRK06546 97 AIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGGGVSVVTLPGDIADEPAPEGFAPSV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 180 GSYERSFIAPalNEVEVDKAVEILNNAERPVIYAGYGGVKAGEVITELSRKIKAPIITT--GKNFEAFEWNYE-GLTGsa 256
Cdd:PRK06546 177 ISPRRPTVVP--DPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSlrGKEWIQYDNPFDvGMSG-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 257 yRVGWKPANEVVFEADTVLFLGSNFPfaevYEAFKNTEKFIQVDIDPYKLGKRHALDASILGDAGQAAKAILDKVNPVES 336
Cdd:PRK06546 253 -LLGYGAAHEAMHEADLLILLGTDFP----YDQFLPDVRTAQVDIDPEHLGRRTRVDLAVHGDVAETIRALLPLVKEKTD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 337 TPWWRANVKNNqnwRDYMNKLEG----KTEGELQLYQVYNA--INKHADQDAIYSIDVGDTTQTSTRHLhmTPKNMWRT- 409
Cdd:PRK06546 328 RRFLDRMLKKH---ARKLEKVVGaytrKVEKHTPIHPEYVAsiLDELAADDAVFTVDTGMCNVWAARYI--TPNGRRRVi 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 410 -SPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIK-----DKYEDtnk 483
Cdd:PRK06546 403 gSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKlemlvDGLPD--- 479
|
490 500 510
....*....|....*....|....*....|....*....
gi 446113971 484 hlFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEA 522
Cdd:PRK06546 480 --FGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREA 516
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
5-538 |
5.52e-78 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 257.01 E-value: 5.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAeDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHL 84
Cdd:PRK06048 7 KMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELY-DSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 85 INGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACR-AAVSKKGPAVVEIP 163
Cdd:PRK06048 86 VTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHiASTGRPGPVLIDLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 164 VNFGFQEIDensYYGSGSYERSFIAPAL--NEVEVDKAVEILNNAERPVIYAGyGGV---KAGEVITELSRKIKAPIITT 238
Cdd:PRK06048 166 KDVTTAEID---FDYPDKVELRGYKPTYkgNPQQIKRAAELIMKAERPIIYAG-GGVissNASEELVELAETIPAPVTTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 239 GKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFPFAEV--YEAFKNTEKFIQVDIDPYKLGKRHALDASI 316
Cdd:PRK06048 242 LMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTgkLASFAPNAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 317 LGDAGQAAKAILDKVNPVESTPWwraNVKNNQNWRDYMNKLEGKTEGELQLY---QVYNAInkhadQDAIYSIDVGDTTQ 393
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDRKEW---LDKINQWKKEYPLKYKEREDVIKPQYvieQIYELC-----PDAIIVTEVGQHQM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 394 TSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAF 473
Cdd:PRK06048 394 WAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGM 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446113971 474 IKDKYEDTNKHLFGCDF--PNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLnkeGKTVVIDARI 538
Cdd:PRK06048 474 VRQWQELFYDKRYSHTCikGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVAS---DRPVVIDFIV 537
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
6-553 |
1.13e-77 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 256.19 E-value: 1.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 6 ITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLI 85
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 86 NGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPV 164
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTgRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 165 NFGFQEIDeNSYYGSGSYeRSFiAPAL--NEVEVDKAVEILNNAERPVIYAGyGGV---KAGEVITELSRKIKAPIITTG 239
Cdd:TIGR00118 161 DVTTAEIE-YPYPEKVNL-PGY-RPTVkgHPLQIKKAAELINLAKKPVILVG-GGViiaGASEELKELAERIQIPVTTTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 240 KNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFP--FAEVYEAFKNTEKFIQVDIDPYKLGKRHALDASIL 317
Cdd:TIGR00118 237 MGLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDdrVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 318 GDAGQAAKAILDKVNPV---ESTPWWranvKNNQNWR-DYMNKLEgKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQ 393
Cdd:TIGR00118 317 GDARNVLEELLKKLFELkerKESAWL----EQINKWKkEYPLKMD-YTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 394 TSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAF 473
Cdd:TIGR00118 392 WAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGM 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 474 IKD----KYEDTNKHLFGCDFPnaDYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNkegKTVVIDARISQhrplPVEVL 549
Cdd:TIGR00118 472 VRQwqelFYEERYSHTHMGSLP--DFVKLAEAYGIKGIRIEKPEELDEKLKEALSSN---EPVLLDVVVDK----PENVL 542
|
....
gi 446113971 550 ELDP 553
Cdd:TIGR00118 543 PMVA 546
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
5-540 |
5.25e-76 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 252.48 E-value: 5.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEdKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHL 84
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPP-AGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 85 INGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEIPV 164
Cdd:TIGR03457 80 VTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREMGPAQLNIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 165 NFGFQEIDENSYYGSgSYERsfiaPALNEVEVDKAVEILNNAERPVIYAGyGGVKAGEVITE---LSRKIKAPIITTGKN 241
Cdd:TIGR03457 160 DYFYGEIDVEIPRPV-RLDR----GAGGATSLAQAARLLAEAKFPVIISG-GGVVMGDAVEEckaLAERLGAPVVNSYLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 242 FEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNF-PFAEV----YEAFKNTEKFIQVDIDPYKLGKRHALDASI 316
Cdd:TIGR03457 234 NDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLgPFGTLpqygIDYWPKNAKIIQVDANAKMIGLVKKVTVGI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 317 LGDAGQAAKAILDKVNPV--------------ESTPWWRANVKNNQNWRD----YMNKLEGKTEGE-LQLYQVYNAINKH 377
Cdd:TIGR03457 314 CGDAKAAAAEILQRLAGKagdanraerkakiqAERSAWEQELSEMTHERDpfslDMIVEQRQEEGNwLHPRQVLRELEKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 378 ADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQY 457
Cdd:TIGR03457 394 MPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 458 DLPVINVVFSNGKY-AFIKDKYEDTNKHLFGCDFPN-ADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNKEGKTVVID 535
Cdd:TIGR03457 474 DIPVTAVVFRNRQWgAEKKNQVDFYNNRFVGTELESeLSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQAEGKTTVIE 553
|
....*
gi 446113971 536 ARISQ 540
Cdd:TIGR03457 554 IVCTR 558
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
368-544 |
1.86e-75 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 237.81 E-value: 1.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 368 YQVYNAINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMC 447
Cdd:cd02014 5 ERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGFAML 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 448 YPDVITNVQYDLPVINVVFSNGKYAFIKDKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNk 527
Cdd:cd02014 85 MGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALAAD- 163
|
170
....*....|....*..
gi 446113971 528 egKTVVIDARISQHRPL 544
Cdd:cd02014 164 --GPVVIDVVTDPNEPP 178
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
16-537 |
1.73e-74 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 248.67 E-value: 1.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 16 LKTWGVDTIYGIPSGTLSSLMDAL--AEDKdIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYDAAM 93
Cdd:PRK08273 13 LREWGVRRVFGYPGDGINGLLGALgrADDK-PEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYDAKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 94 DNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIA-VYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEIPVNfgFQEID 172
Cdd:PRK08273 92 DHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAgAFVQMVTVPEQLRHLVDRAVRTALAERTVTAVILPND--VQELE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 173 EN-------SYYGSGSYERSFIAPAlnEVEVDKAVEILNNAERPVIYAGYGGVKAGEVITELSRKIKAPIITT--GKNF- 242
Cdd:PRK08273 170 YEppphahgTVHSGVGYTRPRVVPY--DEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGVAKAllGKAAl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 243 -EAFEWnyegLTGSAYRVGWKPANEVVFEADTVLFLGSNFPFAEVYEAFkNTEKFIQVDIDPYKLGKRHALDASILGDAG 321
Cdd:PRK08273 248 pDDLPW----VTGSIGLLGTKPSYELMRECDTLLMVGSSFPYSEFLPKE-GQARGVQIDIDGRMLGLRYPMEVNLVGDAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 322 QAAKAILDKVNPVESTPWWRANVKNNQNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQTSTRHLHM 401
Cdd:PRK08273 323 ETLRALLPLLERKKDRSWRERIEKWVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADSGSCANWYARDLRM 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 402 TPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMC-YPDVITNVQY-----DLPVINVVFSNGKYAFI- 474
Cdd:PRK08273 403 RRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKYwrqwsDPRLIVLVLNNRDLNQVt 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446113971 475 --------KDKYEDTNkhlfgcDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVklnKEGKTVVIDAR 537
Cdd:PRK08273 483 weqrvmegDPKFEASQ------DLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEAL---AADRPVVLEVK 544
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
7-170 |
6.75e-74 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 233.21 E-value: 6.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 7 TASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLIN 86
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 87 GVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEIPVNF 166
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKRGVAVLILPGDV 160
|
....
gi 446113971 167 GFQE 170
Cdd:cd07039 161 QDAP 164
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
11-545 |
1.38e-67 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 230.03 E-value: 1.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 11 AMLNVLKTWGVDTIYGIPSGTLSSLMDALAeDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYD 90
Cdd:PRK06276 6 AIIKALEAEGVKIIFGYPGGALLPFYDALY-DSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGIAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 91 AAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPVNFGFQ 169
Cdd:PRK06276 85 AYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTgRPGPVHIDLPKDVQEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 170 EIDENSYYGSGSYERSFIAPAL--NEVEVDKAVEILNNAERPVIYAGyGGV---KAGEVITELSRKIKAPIITT--GKNf 242
Cdd:PRK06276 165 ELDLEKYPIPAKIDLPGYKPTTfgHPLQIKKAAELIAEAERPVILAG-GGViisGASEELIELSELVKIPVCTTlmGKG- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 243 eAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFPFAEV--YEAFKNTEKFIQVDIDPYKLGKRHALDASILGDA 320
Cdd:PRK06276 243 -AFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTgdISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVGDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 321 GQAAKAILDKVNpvestpwwRANVKNNQNWRDYMNKLEGKTEGEL--------------QLYQVYNAINkhADQDAIYSI 386
Cdd:PRK06276 322 KNVLRDLLAELM--------KKEIKNKSEWLERVKKLKKESIPRMdfddkpikpqrvikELMEVLREID--PSKNTIITT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 387 DVGDtTQTSTRHLHMT--PKNMWRTSPLfATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINV 464
Cdd:PRK06276 392 DVGQ-NQMWMAHFFKTsaPRSFISSGGL-GTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVIC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 465 VFSN---GKYAFIKDKYEDtnKHLFGCDFPNA-DYAKIAEAQGAVGFTVDRIEDIDAVVAEAVklnKEGKTVVIDARISQ 540
Cdd:PRK06276 470 IFDNrtlGMVYQWQNLYYG--KRQSEVHLGETpDFVKLAESYGVKADRVEKPDEIKEALKEAI---KSGEPYLLDIIIDP 544
|
....*
gi 446113971 541 HRPLP 545
Cdd:PRK06276 545 AEALP 549
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
2-538 |
3.71e-66 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 226.86 E-value: 3.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 2 TQGKITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDAL--AE-DKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGG 78
Cdd:PRK07418 15 TPQRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELykAEaEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 79 PGATHLINGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGP 157
Cdd:PRK07418 95 PGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSgRPGP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 158 AVVEIPVNFGFQEIDensyygsgsYER----SFIAPAL------NEVEVDKAVEILNNAERPVIYAGYGGVKAG--EVIT 225
Cdd:PRK07418 175 VLIDIPKDVGQEEFD---------YVPvepgSVKPPGYrptvkgNPRQINAALKLIEEAERPLLYVGGGAISAGahAELK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 226 ELSRKIKAPIITT--GKNfeAFEWNYE------GLTGSAYrvgwkpANEVVFEADTVLFLGSNFP--FAEVYEAFKNTEK 295
Cdd:PRK07418 246 ELAERFQIPVTTTlmGKG--AFDEHHPlsvgmlGMHGTAY------ANFAVTECDLLIAVGARFDdrVTGKLDEFASRAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 296 FIQVDIDPYKLGKRHALDASILGDAGQAAKAILDKVNPVESTPWWRANVKNNQNWRDYMNKLEGKTEGELQLYQVYNAIN 375
Cdd:PRK07418 318 VIHIDIDPAEVGKNRRPDVPIVGDVRKVLVKLLERSLEPTTPPRTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 376 KHAdQDAIYSIDVGDTTQTSTRHLHMTPKNmWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNV 455
Cdd:PRK07418 398 DLA-PDAYYTTDVGQHQMWAAQFLRNGPRR-WISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 456 QYDLPVINVVFSNG--------KYAFIKDKYEDTNkhlFGCDFPnaDYAKIAEAQGAVGFTVDRIEDIDAVVAEAvkLNK 527
Cdd:PRK07418 476 QYGINVKTVIINNGwqgmvrqwQESFYGERYSASN---MEPGMP--DFVKLAEAFGVKGMVISERDQLKDAIAEA--LAH 548
|
570
....*....|.
gi 446113971 528 EGKtVVIDARI 538
Cdd:PRK07418 549 DGP-VLIDVHV 558
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
5-540 |
7.62e-64 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 220.62 E-value: 7.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHL 84
Cdd:PRK07789 30 RMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 85 INGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACR-AAVSKKGPAVVEIP 163
Cdd:PRK07789 110 VTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHiASTGRPGPVLVDIP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 164 -------VNFGF-QEIDENSYygsgsyeRSFIAPalNEVEVDKAVEILNNAERPVIYAGyGGV---KAGEVITELSRKIK 232
Cdd:PRK07789 190 kdalqaqTTFSWpPRMDLPGY-------RPVTKP--HGKQIREAAKLIAAARRPVLYVG-GGViraEASAELRELAELTG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 233 APIITTGKNFEAFEWNYE------GLTGSAyrvgwkPANEVVFEADTVLFLGSNFP--FAEVYEAFKNTEKFIQVDIDPY 304
Cdd:PRK07789 260 IPVVTTLMARGAFPDSHPqhlgmpGMHGTV------AAVAALQRSDLLIALGARFDdrVTGKLDSFAPDAKVIHADIDPA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 305 KLGK-RHAlDASILGDAG-------QAAKAILDKVNPVESTPWWRANvknnQNWRD-YMNKLEGKTEGELQLYQVYNAIN 375
Cdd:PRK07789 334 EIGKnRHA-DVPIVGDVKeviaeliAALRAEHAAGGKPDLTAWWAYL----DGWREtYPLGYDEPSDGSLAPQYVIERLG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 376 KHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNV 455
Cdd:PRK07789 409 EIAGPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 456 QYDLPVINVVFSNGKYA--------FIKDKYEDTNKHLFGCDFPnaDYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNK 527
Cdd:PRK07789 489 IEGIPIKVALINNGNLGmvrqwqtlFYEERYSNTDLHTHSHRIP--DFVKLAEAYGCVGLRCEREEDVDAVIEKARAIND 566
|
570
....*....|...
gi 446113971 528 egKTVVIDARISQ 540
Cdd:PRK07789 567 --RPVVIDFVVGK 577
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
6-526 |
1.77e-63 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 218.94 E-value: 1.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 6 ITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAED---KDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGAT 82
Cdd:PRK06456 2 PTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFVEDlanGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 83 HLINGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACR-AAVSKKGPAVVE 161
Cdd:PRK06456 82 NLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYiATTGRPGPVVID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 162 IPVNFGFQEIDE----NSYYGSGSYERSFIapaLNEVEVDKAVEILNNAERPVIYAGYGGV--KAGEVITELSRKIKAPI 235
Cdd:PRK06456 162 IPRDIFYEKMEEikwpEKPLVKGYRDFPTR---IDRLALKKAAEILINAERPIILVGTGVVwsNATPEVLELAELLHIPI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 236 ITTGKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFP---FAEVYEAFKNTEKFIQVDIDPYKLGKRHAL 312
Cdd:PRK06456 239 VSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSdrtFTSYDEMVETRKKFIMVNIDPTDGEKAIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 313 DASILGDAG----QAAKAILDKVNPVESTPWwranVKNNQNWRDYMNKLEGKTE-GELQLYQVYNAINKHADQDAIYSID 387
Cdd:PRK06456 319 DVGIYGNAKiilrELIKAITELGQKRDRSAW----LKRVKEYKEYYSQFYYTEEnGKLKPWKIMKTIRQALPRDAIVTTG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 388 VGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFS 467
Cdd:PRK06456 395 VGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFD 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446113971 468 NGKYAFIKdKYEDT--NKHLFGCDF-PNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLN 526
Cdd:PRK06456 475 NRTLGLVR-QVQDLffGKRIVGVDYgPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKED 535
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
16-541 |
6.16e-63 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 217.30 E-value: 6.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 16 LKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYDAAMDN 95
Cdd:PRK06466 14 LRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGIATAYMDS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 96 TPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPVNFGfQEIDEN 174
Cdd:PRK06466 94 IPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSgRPGPVVVDIPKDMT-NPAEKF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 175 SY-YGSGSYERSFiAPAL--NEVEVDKAVEILNNAERPVIYAGyGGV---KAGEVITELSRKIKAPIITTGKNFEAFEWN 248
Cdd:PRK06466 173 EYeYPKKVKLRSY-SPAVrgHSGQIRKAVEMLLAAKRPVIYSG-GGVvlgNASALLTELAHLLNLPVTNTLMGLGGFPGT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 249 YEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFPfaevYEAFKNTEKF------IQVDIDPYKLGKRHALDASILGDAGQ 322
Cdd:PRK06466 251 DRQFLGMLGMHGTYEANMAMHHADVILAVGARFD----DRVTNGPAKFcpnakiIHIDIDPASISKTIKADIPIVGPVES 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 323 AAKAILDKVNPVESTP-------WWranvKNNQNWRDY--MNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQ 393
Cdd:PRK06466 327 VLTEMLAILKEIGEKPdkealaaWW----KQIDEWRGRhgLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQM 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 394 TSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAF 473
Cdd:PRK06466 403 FAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALGM 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446113971 474 IKD----KYEDTNKHLFGCDFPnaDYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNKegKTVVIDARISQH 541
Cdd:PRK06466 483 VRQwqdmQYEGRHSHSYMESLP--DFVKLAEAYGHVGIRITDLKDLKPKLEEAFAMKD--RLVFIDIYVDRS 550
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
5-557 |
1.03e-59 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 208.41 E-value: 1.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHL 84
Cdd:PRK08527 2 KLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 85 INGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIP 163
Cdd:PRK08527 82 VTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSgRPGPVHIDIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 164 VN-------FGF-QEIDENSYYGSGSYersfiapalNEVEVDKAVEILNNAERPVIYAGYGGV--KAGEVITELSRKIKA 233
Cdd:PRK08527 162 KDvtatlgeFEYpKEISLKTYKPTYKG---------NSRQIKKAAEAIKEAKKPLFYLGGGAIlsNASEEIRELVKKTGI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 234 PIITTGKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFP---FAEVYEAFKNTeKFIQVDIDPYKLGKRH 310
Cdd:PRK08527 233 PAVETLMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDdrvTGKLSEFAKHA-KIIHVDIDPSSISKIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 311 ALDASILGDAGQAAKAILDKVNPVEStpwwranvKNNQNWRDYMNK------LEGKTEGELQLYQ-VYNAINKHADQDAI 383
Cdd:PRK08527 312 NADYPIVGDLKNVLKEMLEELKEENP--------TTYKEWREILKRynelhpLSYEDSDEVLKPQwVIERVGELLGDDAI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 384 YSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVIN 463
Cdd:PRK08527 384 ISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVIN 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 464 VVFSNG--------KYAFIKDKYEDTNKHLfgcdfpNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNkegKTVVID 535
Cdd:PRK08527 464 IILNNNflgmvrqwQTFFYEERYSETDLST------QPDFVKLAESFGGIGFRVTTKEEFDKALKEALESD---KVALID 534
|
570 580
....*....|....*....|..
gi 446113971 536 ARISQHRplpvEVLELDPKQHS 557
Cdd:PRK08527 535 VKIDRFE----NVLPMVPAGGA 552
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
15-537 |
7.15e-59 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 205.50 E-value: 7.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 15 VLKTWGVDTIYGIPSGTLSSLMDALAeDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYDAAMD 94
Cdd:PRK08978 10 ALRAQGVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGLADALLD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 95 NTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPVNFGFQEide 173
Cdd:PRK08978 89 SVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSgRPGPVLVDIPKDIQLAE--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 174 nsyygsGSYERSFIA----PALNEVEVDKAVEILNNAERPVIYAGyGGVKAGEVITELSRKIKA---PIITTGKNFEAFE 246
Cdd:PRK08978 166 ------GELEPHLTTvenePAFPAAELEQARALLAQAKKPVLYVG-GGVGMAGAVPALREFLAAtgmPAVATLKGLGAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 247 WNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNF------------PFAEVyeafkntekfIQVDIDPYKLGKRHALDA 314
Cdd:PRK08978 239 ADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFddrvtgklntfaPHAKV----------IHLDIDPAEINKLRQAHV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 315 SILGDAGQAAKAIldkVNPVESTPwWRANVKNNQN---WRdYMNklegktEGELqlyqVY-----NAINKHADQDAIYSI 386
Cdd:PRK08978 309 ALQGDLNALLPAL---QQPLNIDA-WRQHCAQLRAehaWR-YDH------PGEA----IYapallKQLSDRKPADTVVTT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 387 DVGDTTQTSTRHLHMT-PKNmWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMcypdvitNVQ-------YD 458
Cdd:PRK08978 374 DVGQHQMWVAQHMRFTrPEN-FITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMM-------NVQelgtikrKQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 459 LPVINVVFSNGKYA--------FIKDKYEDTNKHlfgcDfpNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAvkLNKEGK 530
Cdd:PRK08978 446 LPVKIVLLDNQRLGmvrqwqqlFFDERYSETDLS----D--NPDFVMLASAFGIPGQTITRKDQVEAALDTL--LNSEGP 517
|
570
....*....|
gi 446113971 531 T---VVIDAR 537
Cdd:PRK08978 518 YllhVSIDEL 527
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
5-541 |
1.97e-58 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 205.71 E-value: 1.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHL 84
Cdd:PRK09107 10 QMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 85 INGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIP 163
Cdd:PRK09107 90 VTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSgRPGPVVVDIP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 164 VNFGF--------QEIDENSYYgsgsyersfiAPAL--NEVEVDKAVEILNNAERPVIYAGyGGV-----KAGEVITELS 228
Cdd:PRK09107 170 KDVQFatgtytppQKAPVHVSY----------QPKVkgDAEAITEAVELLANAKRPVIYSG-GGVinsgpEASRLLRELV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 229 RKIKAPIITTGKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFP--FAEVYEAFKNTEKFIQVDIDPYKL 306
Cdd:PRK09107 239 ELTGFPITSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDdrITGRLDAFSPNSKKIHIDIDPSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 307 GKRHALDASILGDAG-------QAAKAILDKVNPVESTPWWRANVKnnqnWRDyMNKLEGKTEGELQLYQVynAINK--- 376
Cdd:PRK09107 319 NKNVRVDVPIIGDVGhvledmlRLWKARGKKPDKEALADWWGQIAR----WRA-RNSLAYTPSDDVIMPQY--AIQRlye 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 377 -HADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNV 455
Cdd:PRK09107 392 lTKGRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 456 QYDLPVINVVFSNGKYAFIK--------DKYEdtnkHLFGCDFPnaDYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNk 527
Cdd:PRK09107 472 QYNLPVKIFILNNQYMGMVRqwqqllhgNRLS----HSYTEAMP--DFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVD- 544
|
570
....*....|....
gi 446113971 528 egKTVVIDARISQH 541
Cdd:PRK09107 545 --KPVIFDCRVANL 556
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
7-538 |
1.17e-56 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 199.93 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 7 TASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLIN 86
Cdd:PRK08155 14 TGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 87 GVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPVN 165
Cdd:PRK08155 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSgRPGPVWIDIPKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 166 FGFQEIDENSYYGSGsyERSfIAPALNEVEVDKAVEILNNAERPVIYAGyGGV---KAGEVITELSRKIKAPIITTGKNF 242
Cdd:PRK08155 174 VQTAVIELEALPAPA--EKD-AAPAFDEESIRDAAAMINAAKRPVLYLG-GGVinsGAPARARELAEKAQLPTTMTLMAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 243 EAFEWNYE---GLTGSAyrvGWKPANEVVFEADTVLFLGSNFPFAEV--YEAFKNTEKFIQVDIDPYKLGKRHALDASIL 317
Cdd:PRK08155 250 GMLPKAHPlslGMLGMH---GARSTNYILQEADLLIVLGARFDDRAIgkTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 318 GDAGQAAKAILDKVNPVEstpwwranvknNQNWRDYMNKLEG-------KTEGELQLYQVYNAINKHADQDAIYSIDVGd 390
Cdd:PRK08155 327 ADVDDVLAQLLPLVEAQP-----------RAEWHQLVADLQRefpcpipKADDPLSHYGLINAVAACVDDNAIITTDVG- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 391 ttQTSTRHLHMTPKN---MWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFS 467
Cdd:PRK08155 395 --QHQMWTAQAYPLNrprQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMN 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446113971 468 NGKYAFIKDK----YEdtnKHLFGCDFPNA-DYAKIAEAQGAVGFTVDRIEDIDAVVAEAvkLNKEGKtVVIDARI 538
Cdd:PRK08155 473 NEALGLVHQQqslfYG---QRVFAATYPGKiNFMQIAAGFGLETCDLNNEADPQAALQEA--INRPGP-ALIHVRI 542
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
6-533 |
2.02e-54 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 194.03 E-value: 2.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 6 ITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEdKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLI 85
Cdd:PRK06725 15 VTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 86 NGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPV 164
Cdd:PRK06725 94 TGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESgRPGPVLIDIPK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 165 NFGFQEIdeNSYYGsgsyERSFI-----APALNEVEVDKAVEILNNAERPVIYAGYGGVKAG--EVITELSRKIKAPIIT 237
Cdd:PRK06725 174 DVQNEKV--TSFYN----EVVEIpgykpEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGgsEELIEFARENRIPVVS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 238 TGKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFP--FAEVYEAFKNTEKFIQVDIDPYKLGKRHALDAS 315
Cdd:PRK06725 248 TLMGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDdrVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 316 ILGDAGQAAKAILDKVNPVESTPWwranVKNNQNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQTS 395
Cdd:PRK06725 328 VVGDVKKALHMLLHMSIHTQTDEW----LQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 396 TRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIK 475
Cdd:PRK06725 404 AHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVR 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446113971 476 DKYED-TNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAvkLNKEGKTVV 533
Cdd:PRK06725 484 QWQEMfYENRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEA--FAHEGPVVV 540
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
20-540 |
3.88e-54 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 193.50 E-value: 3.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 20 GVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYDAAMDNTPFL 99
Cdd:PRK08979 18 GVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITGIATAYMDSIPMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 100 AILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACR-AAVSKKGPAVVEIPVNFGFQEIDENSYYG 178
Cdd:PRK08979 98 VLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYiASTGRPGPVVIDLPKDCLNPAILHPYEYP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 179 SGSYERSFiAPALN--EVEVDKAVEILNNAERPVIYAGYGGVKAG--EVITELSRKIKAPIITTGKNFEAFEWNYEGLTG 254
Cdd:PRK08979 178 ESIKMRSY-NPTTSghKGQIKRGLQALLAAKKPVLYVGGGAIISGadKQILQLAEKLNLPVVSTLMGLGAFPGTHKNSLG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 255 SAYRVGWKPANEVVFEADTVLFLGSNFPfaevYEAFKNTEKF------IQVDIDPYKLGKRHALDASILGDAGQAAKAIL 328
Cdd:PRK08979 257 MLGMHGRYEANMAMHNADLIFGIGVRFD----DRTTNNLEKYcpnatiLHIDIDPSSISKTVRVDIPIVGSADKVLDSML 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 329 DKVNPVEST-------PWWranvKNNQNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQTSTRHLHM 401
Cdd:PRK08979 333 ALLDESGETndeaaiaSWW----NEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQMFAALYYPF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 402 TPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIKD----K 477
Cdd:PRK08979 409 DKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMVKQwqdmI 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446113971 478 YEDTNKHLFGCDFPnaDYAKIAEAQGAVGFTVDRIEDIDAVVAEAvkLNKEGKTVVIDARISQ 540
Cdd:PRK08979 489 YQGRHSHSYMDSVP--DFAKIAEAYGHVGIRISDPDELESGLEKA--LAMKDRLVFVDINVDE 547
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
2-538 |
6.51e-53 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 190.30 E-value: 6.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 2 TQGKITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDAL---AEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGG 78
Cdd:CHL00099 6 TLREKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 79 PGATHLINGVYDAAMDNTPFLAILG--SRPVneLNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KK 155
Cdd:CHL00099 86 PGATNLVTGIATAQMDSVPLLVITGqvGRAF--IGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHgRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 156 GPAVVEIPVNFGFQEIDENSY-YGSGSYE----RSFIAPALNEVEvdKAVEILNNAERPVIYAGYGGV--KAGEVITELS 228
Cdd:CHL00099 164 GPVLIDIPKDVGLEKFDYYPPePGNTIIKilgcRPIYKPTIKRIE--QAAKLILQSSQPLLYVGGGAIisDAHQEITELA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 229 RKIKAPIITT--GKNfeAFEWNYE------GLTGSAYrvgwkpANEVVFEADTVLFLGSNFP--FAEVYEAFKNTEKFIQ 298
Cdd:CHL00099 242 ELYKIPVTTTlmGKG--IFDEDHPlclgmlGMHGTAY------ANFAVSECDLLIALGARFDdrVTGKLDEFACNAQVIH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 299 VDIDPYKLGKRHALDASILGDAGQAAKAIL-------DKVNPvESTPWWRANVKnnqNWRDYMNKLEGKTEGELQLYQVY 371
Cdd:CHL00099 314 IDIDPAEIGKNRIPQVAIVGDVKKVLQELLellknspNLLES-EQTQAWRERIN---RWRKEYPLLIPKPSTSLSPQEVI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 372 NAINKHAdQDAIYSIDVGDTTQTSTRHLHMTPKNmWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDV 451
Cdd:CHL00099 390 NEISQLA-PDAYFTTDVGQHQMWAAQFLKCKPRK-WLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQEL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 452 ITNVQYDLPvINVVFSNGKY---------AFIKDKYEDTNKHLFGCDFpnadyAKIAEAQGAVGFTVDRIEDIDAVVAEA 522
Cdd:CHL00099 468 GTIAQYNLP-IKIIIINNKWqgmvrqwqqAFYGERYSHSNMEEGAPDF-----VKLAEAYGIKGLRIKSRKDLKSSLKEA 541
|
570
....*....|....*.
gi 446113971 523 VKLNkegKTVVIDARI 538
Cdd:CHL00099 542 LDYD---GPVLIDCQV 554
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
9-537 |
1.28e-52 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 189.63 E-value: 1.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 9 SAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGV 88
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 89 YDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPVNFG 167
Cdd:PRK06965 104 ATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTgRPGPVVVDIPKDVS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 168 FQEIdenSYYGSGSYE-RSFiapalNEV------EVDKAVEILNNAERPVIYAGyGGVKAGEVITELSRKIKA---PIIT 237
Cdd:PRK06965 184 KTPC---EYEYPKSVEmRSY-----NPVtkghsgQIRKAVSLLLSAKRPYIYTG-GGVILANASRELRQLADLlgyPVTN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 238 TGKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFP---------FAEvyeafkNTEKFIQVDIDPYKLGK 308
Cdd:PRK06965 255 TLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDdrvignpahFAS------RPRKIIHIDIDPSSISK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 309 RHALDASILGDAGQAAKAILDKVNPVESTP-------WWranvKNNQNWRDyMNKLEGKTEGELQLYQ-VYNAINKHADQ 380
Cdd:PRK06965 329 RVKVDIPIVGDVKEVLKELIEQLQTAEHGPdadalaqWW----KQIEGWRS-RDCLKYDRESEIIKPQyVVEKLWELTDG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 381 DAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLP 460
Cdd:PRK06965 404 DAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTP 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 461 VINVVFSNGKYAFIKD----KYEDTNKHLFGCDFPnaDYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLnkEGKTVVIDA 536
Cdd:PRK06965 484 VKIISLNNRYLGMVRQwqeiEYSKRYSHSYMDALP--DFVKLAEAYGHVGMRIEKTSDVEPALREALRL--KDRTVFLDF 559
|
.
gi 446113971 537 R 537
Cdd:PRK06965 560 Q 560
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
7-540 |
1.78e-52 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 188.88 E-value: 1.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 7 TASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLIN 86
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 87 GVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPVN 165
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTgRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 166 FGFQEIDEnsYYGSG----SYERSFIApalNEVEVDKAVEILNNAERPVIYAGyGGVKAGEVITEL---SRKIKAPIITT 238
Cdd:PRK07282 171 VSALETDF--IYDPEvnlpSYQPTLEP---NDMQIKKILKQLSKAKKPVILAG-GGINYAEAATELnafAERYQIPVVTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 239 GKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFP--FAEVYEAFKNTEKFIQVDIDPYKLGKRHALDASI 316
Cdd:PRK07282 245 LLGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDdrLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 317 LGDAGQAAKAIL--DKVNpVESTPWWRANVKNNQNWRDYmnkleGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQT 394
Cdd:PRK07282 325 VGDAKKALQMLLaePTVH-NNTEKWIEKVTKDKNRVRSY-----DKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMW 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 395 STRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDV-ITNVqYDLPVINVVFSNGKYAF 473
Cdd:PRK07282 399 AAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELaILNI-YKVPIKVVMLNNHSLGM 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446113971 474 IKDKYED-----TNKHLFGcDFPNadYAKIAEAQGAVGFTVDRIEDIdavvAEAVKLNKEGKTVVIDARISQ 540
Cdd:PRK07282 478 VRQWQESfyegrTSESVFD-TLPD--FQLMAQAYGIKHYKFDNPETL----AQDLEVITEDVPMLIEVDISR 542
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
2-538 |
9.60e-51 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 183.54 E-value: 9.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 2 TQGKITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGA 81
Cdd:PRK08199 4 TPRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 82 THLINGVYDAAMDNTPFLAILG--SRPVNElnMDAFQELNQNPMYNGIAvynKRVAY---AEQLPKVIDEACRAAVS-KK 155
Cdd:PRK08199 84 TNASIGVHTAFQDSTPMILFVGqvARDFRE--REAFQEIDYRRMFGPMA---KWVAEiddAARIPELVSRAFHVATSgRP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 156 GPAVVEIPvnfgfqeidENSYYGSGS------YERSFIAPAlnEVEVDKAVEILNNAERPVIYAGYGG--VKAGEVITEL 227
Cdd:PRK08199 159 GPVVLALP---------EDVLSETAEvpdappYRRVAAAPG--AADLARLAELLARAERPLVILGGSGwtEAAVADLRAF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 228 SRKIKAPIITTGKNFEAFEW---NYEGLTGsayrVGWKPA-NEVVFEADTVLFLGSNFpfAEV----YEAF---KNTEKF 296
Cdd:PRK08199 228 AERWGLPVACAFRRQDLFDNrhpNYAGDLG----LGINPAlAARIREADLVLAVGTRL--GEVttqgYTLLdipVPRQTL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 297 IQVDIDPYKLGKRHALDASILGDAGQAAKAiLDKVNPVESTPWWRANVKNNQNWRDYMNKLegKTEGELQLYQVYNAINK 376
Cdd:PRK08199 302 VHVHPDAEELGRVYRPDLAIVADPAAFAAA-LAALEPPASPAWAEWTAAAHADYLAWSAPL--PGPGAVQLGEVMAWLRE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 377 HADQDAIYSIDVGDTTQTSTRHLHMTPknmWRTS--PLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITN 454
Cdd:PRK08199 379 RLPADAIITNGAGNYATWLHRFFRFRR---YRTQlaPTSGSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 455 VQYDLPVINVVFSNGKYAFIKDKYE-DTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVklnKEGKTVV 533
Cdd:PRK08199 456 VQYGLPIIVIVVNNGMYGTIRMHQErEYPGRVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERAL---ASGKPAL 532
|
....*
gi 446113971 534 IDARI 538
Cdd:PRK08199 533 IEIRI 537
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
20-535 |
6.06e-50 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 181.18 E-value: 6.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 20 GVDTIYGIPSGTLSSLMDALAeDKDIRFLQVRHEETgalAAVMQAKFG---GSIGVAVGSGGPGATHLINGVYDAAMDNT 96
Cdd:PRK08322 15 GVEYIFGIPGEENLDLLEALR-DSSIKLILTRHEQG---AAFMAATYGrltGKAGVCLSTLGPGATNLVTGVAYAQLGGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 97 PFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKK-GPAVVEIPVNFGFQEIDENs 175
Cdd:PRK08322 91 PMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERpGAVHLELPEDIAAEETDGK- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 176 yygsgSYERSFIAPAL-NEVEVDKAVEILNNAERPVIYAGYGGV--KAGEVITELSRKIKAPIITT--GK-----NFEAF 245
Cdd:PRK08322 170 -----PLPRSYSRRPYaSPKAIERAAEAIQAAKNPLILIGAGANrkTASKALTEFVDKTGIPFFTTqmGKgvipeTHPLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 246 EWNYeGLTGSAYrvgwkpANEVVFEADTVLFLGSNF----PFaevyeaFKNTE---KFIQVDIDPYKLGKRHALDASILG 318
Cdd:PRK08322 245 LGTA-GLSQGDY------VHCAIEHADLIINVGHDViekpPF------FMNPNgdkKVIHINFLPAEVDPVYFPQVEVVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 319 DAGQAAKAILDKVNPVESTPWwranvknnqnwrDYMNKLEGKTEGELQLYQ-----------VYNAINKHADQDAIYSID 387
Cdd:PRK08322 312 DIANSLWQLKERLADQPHWDF------------PRFLKIREAIEAHLEEGAdddrfpmkpqrIVADLRKVMPDDDIVILD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 388 VGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFS 467
Cdd:PRK08322 380 NGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILN 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446113971 468 NGKYAFIKDKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVklnKEGKTVVID 535
Cdd:PRK08322 460 DNAYGMIRWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEAL---AQPGVHVID 524
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
6-526 |
1.15e-49 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 180.17 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 6 ITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAeDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLI 85
Cdd:PRK07524 2 TTCGEALVRLLEAYGVETVFGIPGVHTVELYRGLA-GSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 86 NGVYDAAMDNTPFLAILGsrpVNE-----LNMDAFQEL-NQNPMYNGIAVYNKRVAYAEQLPKVIDEAcrAAV---SKKG 156
Cdd:PRK07524 81 TAMGQAYADSIPMLVISS---VNRraslgKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARA--FAVfdsARPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 157 PAVVEIPVNFGFQEIDENSyygSGSYERSFIAPAlNEVEVDKAVEILNNAERPVIYAGYGGVKAGEVITELSRKIKAPII 236
Cdd:PRK07524 156 PVHIEIPLDVLAAPADHLL---PAPPTRPARPGP-APAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 237 TTgknfeafeWNYEGLTGSAY--RVG----WKPANEVVFEADTVLFLGSNFpfAE----VY--EAFKNTEKFIQVDIDPY 304
Cdd:PRK07524 232 LT--------INAKGLLPAGHplLLGasqsLPAVRALIAEADVVLAVGTEL--GEtdydVYfdGGFPLPGELIRIDIDPD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 305 KLGKRHALDASILGDAGQAAKAILDKVNPVESTPWWRAnVKNNQNWRDYMNKLEGKTEGELQLYQ-VYNAInkhadQDAI 383
Cdd:PRK07524 302 QLARNYPPALALVGDARAALEALLARLPGQAAAADWGA-ARVAALRQALRAEWDPLTAAQVALLDtILAAL-----PDAI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 384 YsidVGDTTQT--STRHL--HMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDL 459
Cdd:PRK07524 376 F---VGDSTQPvyAGNLYfdADAPRRWFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADL 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446113971 460 PVINVVFSNGKYAFIKDKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLN 526
Cdd:PRK07524 453 PLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARP 519
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
16-533 |
4.52e-48 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 176.09 E-value: 4.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 16 LKTWGVDTIYGIPSGTLSSLMDALaEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYDAAMDN 95
Cdd:TIGR02418 9 LENQGVRYVFGIPGAKIDRVFDAL-EDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGLATANSEG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 96 TPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPvnfgfQEIDEN 174
Cdd:TIGR02418 88 DPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESgKPGAAFVSLP-----QDVVDS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 175 SYygSGSYERSFIAPALN---EVEVDKAVEILNNAERPVIYAGYGGVKAGEV--ITELSRKIKAPIITTGKNFEAFEWNY 249
Cdd:TIGR02418 163 PV--SVKAIPASYAPKLGaapDDAIDEVAEAIQNAKLPVLLLGLRASSPETTeaVRRLLKKTQLPVVETFQGAGAVSREL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 250 EglTGSAYRVGW---KPANEVVFEADTVLFLGSNfPFAevYEA-FKNTE---KFIQVDIDPYKLGKRHALDASILGDAGQ 322
Cdd:TIGR02418 241 E--DHFFGRVGLfrnQPGDRLLKQADLVITIGYD-PIE--YEPrNWNSEndaTIVHIDVEPAQIDNNYQPDLELVGDIAS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 323 AAKAILDKVNPVESTPWWRANVKNNQNwrdYMNKLEGKT----EGELQLYQVYNAINKHADQDAIYSIDVGDTTQTSTRH 398
Cdd:TIGR02418 316 TLDLLAERIPGYELPPDALAILEDLKQ---QREALDRVPatlkQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 399 LHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIKDKY 478
Cdd:TIGR02418 393 FRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQE 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 446113971 479 EDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAvkLNKEGKTVV 533
Cdd:TIGR02418 473 EMKYQRSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQA--MEVEGPVVV 525
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
5-538 |
1.07e-47 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 175.49 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHL 84
Cdd:PRK06882 3 KLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 85 INGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACR-AAVSKKGPAVVEIP 163
Cdd:PRK06882 83 ITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYiASTGRPGPVVIDIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 164 ---VNFGFQeideNSYYGSGSYERSFIAPALN--EVEVDKAVEILNNAERPVIYAGYGGVKA--GEVITELSRKIKAPII 236
Cdd:PRK06882 163 kdmVNPANK----FTYEYPEEVSLRSYNPTVQghKGQIKKALKALLVAKKPVLFVGGGVITAecSEQLTQFAQKLNLPVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 237 TTGKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFP--FAEVYEAFKNTEKFIQVDIDPYKLGKRHALDA 314
Cdd:PRK06882 239 SSLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDdrTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 315 SILGDAGQAAK---AILDKVNPVES----TPWWranvKNNQNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSID 387
Cdd:PRK06882 319 PIVGSAKNVLEeflSLLEEENLAKSqtdlTAWW----QQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 388 VGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFS 467
Cdd:PRK06882 395 VGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLN 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446113971 468 NGKYAFIKD----KYEDTNKHLFGCDFPnaDYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLnkEGKTVVIDARI 538
Cdd:PRK06882 475 NRFLGMVKQwqdlIYSGRHSQVYMNSLP--DFAKLAEAYGHVGIQIDTPDELEEKLTQAFSI--KDKLVFVDVNV 545
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
2-540 |
1.59e-47 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 174.95 E-value: 1.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 2 TQGKITASAAML-NVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLqVRHEETGALAAVMQAKFGGSIGVAVGSGGPG 80
Cdd:PRK07710 11 TEEKLMTGAQMLiEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHIL-TRHEQGAIHAAEGYARISGKPGVVIATSGPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 81 ATHLINGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAV 159
Cdd:PRK07710 90 ATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTgRPGPVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 160 VEIPVNFGFQEidensyyGSGSYERSFIAPAL------NEVEVDKAVEILNNAERPVIYAGYGGV--KAGEVITELSRKI 231
Cdd:PRK07710 170 IDIPKDMVVEE-------GEFCYDVQMDLPGYqpnyepNLLQIRKLVQAVSVAKKPVILAGAGVLhaKASKELTSYAEQQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 232 KAPIITTGKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFP--FAEVYEAFKNTEKFIQVDIDPYKLGKR 309
Cdd:PRK07710 243 EIPVVHTLLGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDdrVTGNLAYFAKEATVAHIDIDPAEIGKN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 310 HALDASILGDAGQAAKAILDKVNPVESTPWWRANVKnnqNW-RDYMNKLEGKTEGeLQLYQVYNAINKHADQDAIYSIDV 388
Cdd:PRK07710 323 VPTEIPIVADAKQALQVLLQQEGKKENHHEWLSLLK---NWkEKYPLSYKRNSES-IKPQKAIEMLYEITKGEAIVTTDV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 389 GDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSN 468
Cdd:PRK07710 399 GQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNN 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446113971 469 GKYAFIKDK----YEDTNKH-LFGCdfpNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNkegKTVVIDARISQ 540
Cdd:PRK07710 479 EALGMVRQWqeefYNQRYSHsLLSC---QPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQ---EPVVIDCRVLQ 549
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
5-538 |
3.09e-47 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 173.66 E-value: 3.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKD-IRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATH 83
Cdd:PRK08266 3 TMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 84 LINGVYDAAMDNTPFLAILGSRPVNELNmDAFQELNQNP----MYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPA 158
Cdd:PRK08266 83 AGAALLTAYGCNSPVLCLTGQIPSALIG-KGRGHLHEMPdqlaTLRSFTKWAERIEHPSEAPALVAEAFQQMLSgRPRPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 159 VVEIPVNFgFQEIDENSYYGSGsyeRSFIAPALNEVEVDKAVEILNNAERPVIYAGYGGVKAGEVITELSRKIKAPIITT 238
Cdd:PRK08266 162 ALEMPWDV-FGQRAPVAAAPPL---RPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 239 --GKNFEAfEWNYEGLTGSAYRVGWKpanevvfEADTVLFLGSNFPFAEVYEAFKNT-EKFIQVDIDPYKLGkRHALDAS 315
Cdd:PRK08266 238 rsGRGIVS-DRHPLGLNFAAAYELWP-------QTDVVIGIGSRLELPTFRWPWRPDgLKVIRIDIDPTEMR-RLKPDVA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 316 ILGDAGQAAKAILDKVNpvestpwwRANVKnNQNWRDYMNKLEGKTEGELQLYQ---VY-NAINKHADQDAIYsidVGDT 391
Cdd:PRK08266 309 IVADAKAGTAALLDALS--------KAGSK-RPSRRAELRELKAAARQRIQAVQpqaSYlRAIREALPDDGIF---VDEL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 392 TQ---TStrhlhmtpknmWRTSPLFA-----------TMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQY 457
Cdd:PRK08266 377 SQvgfAS-----------WFAFPVYAprtfvtcgyqgTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQH 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 458 DLPVINVVFSNGKYAFIK-DKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLnkeGKTVVIDA 536
Cdd:PRK08266 446 NIGVVTVVFNNNAYGNVRrDQKRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAH---GGPVLIEV 522
|
..
gi 446113971 537 RI 538
Cdd:PRK08266 523 PV 524
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
15-535 |
8.63e-47 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 173.07 E-value: 8.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 15 VLKTWGVDTIYGIPSgtlSSLMDAlAEDKDIRFLQVRHEETGA-LA-AVMQAKFGGSIGVAVGSGGPGATHLINGVYDAA 92
Cdd:PRK06154 29 ILKEEGVELLFGFPV---NELFDA-AAAAGIRPVIARTERVAVhMAdGYARATSGERVGVFAVQYGPGAENAFGGVAQAY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 93 MDNTPFLAILGSRPVNELNMDAFQELNQNpmYNGIAVYNKRVAYAEQLPKVIdeacRAAVSK-----KGPAVVEIPVNFG 167
Cdd:PRK06154 105 GDSVPVLFLPTGYPRGSTDVAPNFESLRN--YRHITKWCEQVTLPDEVPELM----RRAFTRlrngrPGPVVLELPVDVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 168 FQEIDENSYygsgSYERSF-IAPALNEVEVDKAVEILNNAERPVIYAGYGGVKAG--EVITELSRKIKAPIITTGKNFEA 244
Cdd:PRK06154 179 AEELDELPL----DHRPSRrSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQatPELKELAELLEIPVMTTLNGKSA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 245 FEWNYEGLTGSAYRVgwKPANEVVF--EADTVLFLGSNFPFAEVYEAFKNTEKFIQVDIDPYKLGKRHALDASILGDAGQ 322
Cdd:PRK06154 255 FPEDHPLALGSGGRA--RPATVAHFlrEADVLFGIGCSLTRSYYGLPMPEGKTIIHSTLDDADLNKDYPIDHGLVGDAAL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 323 AAKAILDKV-NPVESTPWWRANV-----KNNQNW-RDYMNKLEGKtEGELQLYQVYNAINKHAD-QDAIYSIDVGDT-TQ 393
Cdd:PRK06154 333 VLKQMIEELrRRVGPDRGRAQQVaaeieAVRAAWlAKWMPKLTSD-STPINPYRVVWELQHAVDiKTVIITHDAGSPrDQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 394 TSTRHLHMTPKNM--W-RTSPLFATMGIALpggiAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGK 470
Cdd:PRK06154 412 LSPFYVASRPGSYlgWgKTTQLGYGLGLAM----GAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNFS 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446113971 471 YAfIKDKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNKEGKTVVID 535
Cdd:PRK06154 488 MG-GYDKVMPVSTTKYRATDISGDYAAIARALGGYGERVEDPEMLVPALLRALRKVKEGTPALLE 551
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
15-515 |
3.85e-46 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 170.67 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 15 VLKTWGVDTIYGIPSGTLSSLMDAlAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYDAAMD 94
Cdd:PRK05858 14 RLKAHGVDTMFTLSGGHLFPLYDG-AREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAAQFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 95 NTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPVNFGFQEIDE 173
Cdd:PRK05858 93 QSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTpHRGPVFVDFPMDHAFSMADD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 174 NSyyGSGSYERSFIAPALNEVEVDKAVEILNNAERPVIYAG---YGGvKAGEVITELSRKIKAPIITTGKNFEAFEWNYE 250
Cdd:PRK05858 173 DG--RPGALTELPAGPTPDPDALARAAGLLAEAQRPVIMAGtdvWWG-HAEAALLRLAEELGIPVLMNGMGRGVVPADHP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 251 GLTGSAYRVGWKpanevvfEADTVLFLGSNFPFAEVYEAFKNTEKFIQVDIDPYKLGKRHALDASILGDAGQAAKAILDK 330
Cdd:PRK05858 250 LAFSRARGKALG-------EADVVLVVGVPMDFRLGFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILSALAGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 331 VN-PVESTPWWRANVKNNQNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRT 409
Cdd:PRK05858 323 GGdRTDHQGWIEELRTAETAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 410 SPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIKDKYEdtnkHLFGCD 489
Cdd:PRK05858 403 PGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKHPME----ALYGYD 478
|
490 500 510
....*....|....*....|....*....|.
gi 446113971 490 F-----PNADYAKIAEAQGAVGFTVDRIEDI 515
Cdd:PRK05858 479 VaadlrPGTRYDEVVRALGGHGELVTVPAEL 509
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
5-534 |
4.47e-46 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 171.32 E-value: 4.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAA--VMQAKfGGSIGVAVGSGGPGAT 82
Cdd:PRK11269 3 KMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAegYTRAT-AGNIGVCIGTSGPAGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 83 HLINGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVE 161
Cdd:PRK11269 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSgRPGPVLID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 162 IPVNFGFQEIDensyYGSGSYER-SFIAPALNEVEVDKAVEILNNAERPVIYAGyGGV---KAGEVITELSRKIKAPIIT 237
Cdd:PRK11269 162 LPFDVQVAEIE----FDPDTYEPlPVYKPAATRAQIEKALEMLNAAERPLIVAG-GGVinaDASDLLVEFAELTGVPVIP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 238 TGKNFEAFEWNYE---GLTG--SAYRVGwkpaNEVVFEADTVLFLGSNFP-----FAEVYEAFKnteKFIQVDIDPYKLG 307
Cdd:PRK11269 237 TLMGWGAIPDDHPlmaGMVGlqTSHRYG----NATLLASDFVLGIGNRWAnrhtgSVEVYTKGR---KFVHVDIEPTQIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 308 KRHALDASILGDAGQAAKAIldkvnpVESTPWWRA--NVKNNQNW----RDYMNKLEGKTEGE---LQLYQVYNAINKHA 378
Cdd:PRK11269 310 RVFGPDLGIVSDAKAALELL------VEVAREWKAagRLPDRSAWvadcQERKRTLLRKTHFDnvpIKPQRVYEEMNKAF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 379 DQDAIYSIDVGDTTQTSTRHLHMTPKNMW----RTSPLfatmGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITN 454
Cdd:PRK11269 384 GRDTCYVSTIGLSQIAAAQFLHVYKPRHWincgQAGPL----GWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 455 VQYDLPVINVVFSNGKYAFIKDKyedtnKHLFGCDF--------PNA--------DYAKIAEAQGAVGFTVDRIEDIDAV 518
Cdd:PRK11269 460 AQFNLPYIHVLVNNAYLGLIRQA-----QRAFDMDYcvqlafenINSpelngygvDHVKVAEGLGCKAIRVFKPEDIAPA 534
|
570
....*....|....*.
gi 446113971 519 VAEAVKLNKEGKTVVI 534
Cdd:PRK11269 535 LEQAKALMAEFRVPVV 550
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
20-541 |
1.50e-45 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 169.65 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 20 GVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYDAAMDNTPFL 99
Cdd:PRK07979 18 GVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 100 AILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACR-AAVSKKGPAVVEIPVNFGFQEIDENSYYG 178
Cdd:PRK07979 98 VLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWlAASGRPGPVVVDLPKDILNPANKLPYVWP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 179 SGSYERSFiAPAL--NEVEVDKAVEILNNAERPVIYAGYGGVKAG--EVITELSRKIKAPIITTGKNFEAFEWNYEGLTG 254
Cdd:PRK07979 178 ESVSMRSY-NPTTqgHKGQIKRALQTLVAAKKPVVYVGGGAINAAchQQLKELVEKLNLPVVSSLMGLGAFPATHRQSLG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 255 SAYRVGWKPANEVVFEADTVLFLGSNFPfaevYEAFKNTEKF------IQVDIDPYKLGKRHALDASILGDAGQAAKAIL 328
Cdd:PRK07979 257 MLGMHGTYEANMTMHNADVIFAVGVRFD----DRTTNNLAKYcpnatvLHIDIDPTSISKTVTADIPIVGDARQVLEQML 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 329 DKVNPVESTP-------WWRAnvknNQNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGDTTQTSTRHLHM 401
Cdd:PRK07979 333 ELLSQESAHQpldeirdWWQQ----IEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 402 TPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIKD----K 477
Cdd:PRK07979 409 DKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQwqdmI 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446113971 478 YEDTNKHLFGCDFPnaDYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNKEGKTVVIDARI--SQH 541
Cdd:PRK07979 489 YSGRHSQSYMQSLP--DFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNNRLVFVDVTVdgSEH 552
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
20-519 |
2.80e-44 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 166.07 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 20 GVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYDAAMDNTPFL 99
Cdd:PLN02470 27 GVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGLADALLDSVPLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 100 AILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIP--------VNFGFQE 170
Cdd:PLN02470 107 AITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSgRPGPVLVDIPkdiqqqlaVPNWNQP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 171 IDENSYYgsgsyerSFIAPALNEVEVDKAVEILNNAERPVIYAGYGGVKAGEVITELSRKIKAPIITTGKNFEAFEWNYE 250
Cdd:PLN02470 187 MKLPGYL-------SRLPKPPEKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGLGAFPASDE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 251 ------GLTGSAYrvgwkpANEVVFEADTVLFLGSNFP--FAEVYEAFKNTEKFIQVDIDPYKLGKRHALDASILGDAGQ 322
Cdd:PLN02470 260 lslqmlGMHGTVY------ANYAVDSADLLLAFGVRFDdrVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADVKL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 323 AAKAiLDKVnpVESTPWWRANVKnnqNWRDYMNklEGKTEGELQLYQVYNAI-NKHADQ--------DAIYSIDVGDTTQ 393
Cdd:PLN02470 334 ALQG-LNKL--LEERKAKRPDFS---AWRAELD--EQKEKFPLSYPTFGDAIpPQYAIQvldeltdgNAIISTGVGQHQM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 394 TSTRHL-HMTPKNmWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYA 472
Cdd:PLN02470 406 WAAQWYkYKEPRR-WLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLG 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446113971 473 FI---KDKYEDTNK-HLFGCD-------FPnaDYAKIAEAQGAVGFTVDRIEDIDAVV 519
Cdd:PLN02470 485 MVvqwEDRFYKANRaHTYLGDpdaeaeiFP--DFLKFAEGCKIPAARVTRKSDLREAI 540
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
8-173 |
1.01e-41 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 148.15 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 8 ASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLING 87
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 88 VYDAAMDNTPFLAILGSRPVNELNMDAFQ-ELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPVN 165
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSgRPGPVYLEIPLD 160
|
....*...
gi 446113971 166 FGFQEIDE 173
Cdd:pfam02776 161 VLLEEVDE 168
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
5-535 |
1.61e-41 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 157.84 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 5 KITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHL 84
Cdd:PRK07064 2 KVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 85 INGVYDAAMDNTPFLAILGS--RPVNELNMDAFQEL-NQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKK-GPAVV 160
Cdd:PRK07064 82 AGALVEALTAGTPLLHITGQieTPYLDQDLGYIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPtGPVSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 161 EIPVNFGFQEIDENSYYGSGSYErsfiAPALNEVEVDKAVEILNNAERPVIYAGYGGVKAGEVITELSrKIKAPIITTgk 240
Cdd:PRK07064 162 EIPIDIQAAEIELPDDLAPVHVA----VPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLV-DLGFGVVTS-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 241 nfeafeWNYEG-------LTGSAYRVGwKPANEVVFEADTVLFLGSNFpfaEVYEAFKNTEKF----IQVDIDPYKLGKR 309
Cdd:PRK07064 235 ------TQGRGvvpedhpASLGAFNNS-AAVEALYKTCDLLLVVGSRL---RGNETLKYSLALprplIRVDADAAADGRG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 310 HALDASILGDAGQAAKAILDKvnpVESTPW----WRANVknnqnwRDYMNKLEGKTEGELQLYQVYN-AINKHADQDAIY 384
Cdd:PRK07064 305 YPNDLFVHGDAARVLARLADR---LEGRLSvdpaFAADL------RAAREAAVADLRKGLGPYAKLVdALRAALPRDGNW 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 385 SIDVgdTTQTST---RHLHMTPKNMwRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPV 461
Cdd:PRK07064 376 VRDV--TISNSTwgnRLLPIFEPRA-NVHALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANM 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446113971 462 INVVFSNGKYAFIK---DKYEDTNKHlfGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAvkLNKEGKTVV-ID 535
Cdd:PRK07064 453 VIVLMNDGGYGVIRniqDAQYGGRRY--YVELHTPDFALLAASLGLPHWRVTSADDFEAVLREA--LAKEGPVLVeVD 526
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
11-164 |
4.54e-41 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 145.75 E-value: 4.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 11 AMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDkDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYD 90
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPLLDALARS-GIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446113971 91 AAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPV 164
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSgRPGPVALDLPK 155
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
387-536 |
6.36e-40 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 142.72 E-value: 6.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 387 DVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVF 466
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446113971 467 SNGKYAFIK----DKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVklnKEGKTVVIDA 536
Cdd:pfam02775 81 NNGGYGMTRgqqtPFGGGRYSGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEAL---EHDGPALIDV 151
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
6-540 |
8.78e-40 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 153.23 E-value: 8.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 6 ITASAAMLNVLKTWGVDTIYgIPSGT-LSSLMDALAEDKDI-----RFLQVRHEETgALAAvmqakfggSIGVAVGSGGP 79
Cdd:PRK08327 7 YTAAELFLELLKELGVDYIF-INSGTdYPPIIEAKARARAAgrplpEFVICPHEIV-AISM--------AHGYALVTGKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 80 GA---------THLINGVYDAAMDNTPFLAILGSRPVNE--------LNMDAFQE-LNQNPMYNGIAVYNKRVAYAEQLP 141
Cdd:PRK08327 77 QAvmvhvdvgtANALGGVHNAARSRIPVLVFAGRSPYTEegelgsrnTRIHWTQEmRDQGGLVREYVKWDYEIRRGDQIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 142 KVIDEACRAAVSK-KGPAVVEIPVNFGFQEIDENSYYGSGSyeRSFIAPALNEVEVDKAVEILNNAERPVIYAGYGGVKA 220
Cdd:PRK08327 157 EVVARAIQIAMSEpKGPVYLTLPREVLAEEVPEVKADAGRQ--MAPAPPAPDPEDIARAAEMLAAAERPVIITWRAGRTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 221 G--EVITELSRKIKAPIIttgkNFEAFEWNYEGltGSAYRVGWKPaNEVVFEADTVLFLGSNFPFAEVYEAFKNTEKFIQ 298
Cdd:PRK08327 235 EgfASLRRLAEELAIPVV----EYAGEVVNYPS--DHPLHLGPDP-RADLAEADLVLVVDSDVPWIPKKIRPDADARVIQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 299 VDIDPYKlgKRHAL-----DASILGDAGQAAKAILDKVNPVESTP----------WWRANVKNNQNWRDYMNKL--EGKT 361
Cdd:PRK08327 308 IDVDPLK--SRIPLwgfpcDLCIQADTSTALDQLEERLKSLASAErrrarrrraaVRELRIRQEAAKRAEIERLkdRGPI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 362 EGELQLYQVYNAINKHadqDAIYSidvgdTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGD 441
Cdd:PRK08327 386 TPAYLSYCLGEVADEY---DAIVT-----EYPFVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 442 GAFNMCYPDVITNV--QYDLPVINVVFSNGKY--------AFIKDKYEDTNKHLFGCDF-PNADYAKIAEAQGAVGFTVD 510
Cdd:PRK08327 458 GSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGWlavkeavlEVYPEGYAARKGTFPGTDFdPRPDFAKIAEAFGGYGERVE 537
|
570 580 590
....*....|....*....|....*....|.
gi 446113971 511 RIEDIDAVVAEAV-KLNKEGKTVVIDARISQ 540
Cdd:PRK08327 538 DPEELKGALRRALaAVRKGRRSAVLDVIVDR 568
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
3-524 |
2.29e-39 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 152.22 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 3 QGKITASAAMLNVLKTWGVDTIYGipsGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGAT 82
Cdd:PRK06112 11 TLNGTVAHAIARALKRHGVEQIFG---QSLPSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 83 HLINGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGPAVVE 161
Cdd:PRK06112 88 LLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSgRPGPVVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 162 IPVNFGFQEID-----ENSYYGSGSYERSFIAPALneveVDKAVEILNNAERPVIYAGyGGVKAGEVITELSRKIKA--- 233
Cdd:PRK06112 168 LPADLLTAAAAapaapRSNSLGHFPLDRTVPAPQR----LAEAASLLAQAQRPVVVAG-GGVHISGASAALAALQSLagl 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 234 PIITT--GKNFEAfEWNYEGLTGSAYRVGWKPAN----EVVFEADTVLFLG--SNFPFAEVYEAFKNTEKFIQVDIDPYK 305
Cdd:PRK06112 243 PVATTnmGKGAVD-ETHPLSLGVVGSLMGPRSPGrhlrDLVREADVVLLVGtrTNQNGTDSWSLYPEQAQYIHIDVDGEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 306 LGKRH-ALdaSILGDAGQAAKAILDKVNPVESTPWW--RANV---------KNNQNWRDY-------------MNKLEGK 360
Cdd:PRK06112 322 VGRNYeAL--RLVGDARLTLAALTDALRGRDLAARAgrRAALepaiaagreAHREDSAPValsdaspirperiMAELQAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 361 TEGELQLYqvynainkhadQDAIY-SIDV-GDTTQTSTRHLHMTPKNMwrtsplfATMGIALPGGIAAKKDNPDRQVWNI 438
Cdd:PRK06112 400 LTGDTIVV-----------ADASYsSIWVaNFLTARRAGMRFLTPRGL-------AGLGWGVPMAIGAKVARPGAPVICL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 439 MGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIKDKYEDT-NKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDA 517
Cdd:PRK06112 462 VGDGGFAHVWAELETARRMGVPVTIVVLNNGILGFQKHAETVKfGTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQ 541
|
....*..
gi 446113971 518 VVAEAVK 524
Cdd:PRK06112 542 ALAAAMA 548
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
369-538 |
2.37e-38 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 138.93 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 369 QVYNAINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCY 448
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 449 PDVITNVQYDLPVINVVFSNGKYAFIKDKYED-TNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVklnK 527
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAfYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEAL---A 157
|
170
....*....|.
gi 446113971 528 EGKTVVIDARI 538
Cdd:cd00568 158 AGGPALIEVKT 168
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
2-535 |
3.31e-37 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 145.38 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 2 TQGKITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALaEDKDIRFLQVRHEetgALAAVMQAKFG---GSIGVAVGSGG 78
Cdd:PRK08617 1 TDKKKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDAL-EDSGPELIVTRHE---QNAAFMAAAIGrltGKPGVVLVTSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 79 PGATHLINGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVS-KKGP 157
Cdd:PRK08617 77 PGVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESgRPGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 158 AVVEIPVNFGFQEIDENSyYGSGSYERSFIAPalnEVEVDKAVEILNNAERPVIYAGYGG--VKAGEVITELSRKIKAPI 235
Cdd:PRK08617 157 AFVSLPQDVVDAPVTSKA-IAPLSKPKLGPAS---PEDINYLAELIKNAKLPVLLLGMRAssPEVTAAIRRLLERTNLPV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 236 ITTgknFEA-------FEWNYEGltgsayRVGW---KPANEVVFEADTVLFLGsnfpFAEV-YEA----FKNTEKFIQVD 300
Cdd:PRK08617 233 VET---FQAagvisreLEDHFFG------RVGLfrnQPGDELLKKADLVITIG----YDPIeYEPrnwnSEGDATIIHID 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 301 IDPYKLGKRHALDASILGDAGQAAKAILDKVNPVESTPWWRANVKNNQNWRDYMNKLEGKTEGE----LQLYQvynAINK 376
Cdd:PRK08617 300 VLPAEIDNYYQPERELIGDIAATLDLLAEKLDGLSLSPQSLEILEELRAQLEELAERPARLEEGavhpLRIIR---ALQD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 377 HADQDAIYSIDVGDTTQTSTRHL------HMtpknmwrtspLFA----TMGIALPGGIAAKKDNPDRQVWNIMGDGAFNM 446
Cdd:PRK08617 377 IVTDDTTVTVDVGSHYIWMARYFrsyeprHL----------LFSngmqTLGVALPWAIAAALVRPGKKVVSVSGDGGFLF 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 447 CYPDVITNVQYDLPVINVVFSNGKYAFIKDKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAvkLN 526
Cdd:PRK08617 447 SAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMKYGRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREA--LA 524
|
....*....
gi 446113971 527 KEGkTVVID 535
Cdd:PRK08617 525 TDG-PVVID 532
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
368-539 |
2.37e-32 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 122.64 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 368 YQVYNAINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMC 447
Cdd:cd02004 2 YRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 448 YPDVITNVQYDLPVINVVFSNGKYAFIKDKYEDTNKHL--FGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKL 525
Cdd:cd02004 82 GMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGlpVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALAS 161
|
170
....*....|....
gi 446113971 526 nkeGKTVVIDARIS 539
Cdd:cd02004 162 ---GKPALINVIID 172
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
10-164 |
2.76e-31 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 118.99 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 10 AAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGsIGVAVGSGGPGATHLINGVY 89
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446113971 90 DAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEIPV 164
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
196-327 |
6.97e-31 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 117.28 E-value: 6.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 196 VDKAVEILNNAERPVIYAGYGGV--KAGEVITELSRKIKAPIITTGKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADT 273
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRrsGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446113971 274 VLFLGSNFPFAEV---YEAFKNTEKFIQVDIDPYKLGKRHALDASILGDAGQAAKAI 327
Cdd:pfam00205 81 VLAVGARFDDIRTtgkLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
369-540 |
1.28e-29 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 115.69 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 369 QVYNAINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCY 448
Cdd:cd02013 8 QVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 449 PDVITNVQYDLPVINVVFSNGKY-AFIKDKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNK 527
Cdd:cd02013 88 MEIMTAVRHKLPVTAVVFRNRQWgAEKKNQVDFYNNRFVGTELESESFAKIAEACGAKGITVDKPEDVGPALQKAIAMMA 167
|
170
....*....|...
gi 446113971 528 EGKTVVIDARISQ 540
Cdd:cd02013 168 EGKTTVIEIVCDQ 180
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
368-541 |
2.76e-29 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 114.52 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 368 YQVYNAINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMC 447
Cdd:cd02015 4 QEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSFQMN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 448 YPDVITNVQYDLPVINVVFSNG--------KYAFIKDKYedtnkhlFGCDFP-NADYAKIAEAQGAVGFTVDRIEDIDAV 518
Cdd:cd02015 84 IQELATAAQYNLPVKIVILNNGslgmvrqwQELFYEGRY-------SHTTLDsNPDFVKLAEAYGIKGLRVEKPEELEAA 156
|
170 180
....*....|....*....|...
gi 446113971 519 VAEAVklnKEGKTVVIDARISQH 541
Cdd:cd02015 157 LKEAL---ASDGPVLLDVLVDPE 176
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
16-538 |
5.53e-24 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 106.22 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 16 LKTWGVDTIYGIPSGTLSSLMdALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGathLINGVYDAAMDN 95
Cdd:PRK09259 20 LKLNGIDTIYGVVGIPITDLA-RLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPG---FLNGLTALANAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 96 T---PFLAILGS--RPVNELNMDAFQELNQnpmYNGIAVYNK---RVAYAEQLPKVIDEACRAAVS-KKGPAVVEIPVNF 166
Cdd:PRK09259 96 TncfPMIMISGSseREIVDLQQGDYEELDQ---LNAAKPFCKaafRVNRAEDIGIGVARAIRTAVSgRPGGVYLDLPAKV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 167 GFQEIDensyygSGSYERSFI-----APAL--NEVEVDKAVEILNNAERPVIYAGYGGV--KAGEVITELSRKIKAPII- 236
Cdd:PRK09259 173 LAQTMD------ADEALTSLVkvvdpAPAQlpAPEAVDRALDLLKKAKRPLIILGKGAAyaQADEQIREFVEKTGIPFLp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 237 -TTGKnfeafewnyeGL--------TGSAYRVgwkpaneVVFEADTVLFLGSNFPFAEVY---EAFKNTEKFIQVDIDPY 304
Cdd:PRK09259 247 mSMAK----------GLlpdthpqsAAAARSL-------ALANADVVLLVGARLNWLLSHgkgKTWGADKKFIQIDIEPQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 305 KLGKRHALDASILGDAGQAAKAILDKV--NPVESTPWWRANV--KNNQNWRDYMNKLEgKTEGELQLYQVYNAINK---- 376
Cdd:PRK09259 310 EIDSNRPIAAPVVGDIGSVMQALLAGLkqNTFKAPAEWLDALaeRKEKNAAKMAEKLS-TDTQPMNFYNALGAIRDvlke 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 377 HADqdaIYSIDVGDTTQTSTRHL-------HMTPKNMWrtsplfATMGIALPGGIAAKKDNpDRQVWNIMGDGAFNMCYP 449
Cdd:PRK09259 389 NPD---IYLVNEGANTLDLARNIidmykprHRLDCGTW------GVMGIGMGYAIAAAVET-GKPVVAIEGDSAFGFSGM 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 450 DVITNVQYDLPVINVVFSNGKYafikdkYEDTNKHLFGCDFP-------NADYAKIAEAQGAVGFTVDRIEDIDAVVAEA 522
Cdd:PRK09259 459 EVETICRYNLPVTVVIFNNGGI------YRGDDVNLSGAGDPsptvlvhHARYDKMMEAFGGVGYNVTTPDELRHALTEA 532
|
570
....*....|....*.
gi 446113971 523 VklnKEGKTVVIDARI 538
Cdd:PRK09259 533 I---ASGKPTLINVVI 545
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
369-535 |
1.34e-23 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 98.13 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 369 QVYNAINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCY 448
Cdd:cd02010 3 RIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 449 PDVITNVQYDLPVINVVFSNGKYAFIKDKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNke 528
Cdd:cd02010 83 QELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD-- 160
|
....*..
gi 446113971 529 gKTVVID 535
Cdd:cd02010 161 -GVHVID 166
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
373-538 |
1.33e-22 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 94.97 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 373 AINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPlFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVI 452
Cdd:cd02002 9 ALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLR-GGGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 453 TNVQYDLPVINVVFSNGKYA--------FIKDKYEDTNKHLFGCDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVk 524
Cdd:cd02002 88 TAARYGLPVTVVILNNRGYGalrsflkrVGPEGPGENAPDGLDLLDPGIDFAAIAKAFGVEAERVETPEELDEALREAL- 166
|
170
....*....|....
gi 446113971 525 lnKEGKTVVIDARI 538
Cdd:cd02002 167 --AEGGPALIEVVV 178
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
399-535 |
6.87e-19 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 85.43 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 399 LHMtpknMWRTS-PL-------FATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGK 470
Cdd:cd02003 29 LHK----LWRARtPGgyhleygYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHG 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446113971 471 YAFIKDKYEDTNKHLFGCDF--------------PNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNkegKTVVID 535
Cdd:cd02003 105 FGCINNLQESTGSGSFGTEFrdrdqesgqldgalLPVDFAANARSLGARVEKVKTIEELKAALAKAKASD---RTTVIV 180
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
20-541 |
6.21e-18 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 87.14 E-value: 6.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 20 GVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGsIGVAVGSGGPGATHLINGVYDAAMDNTPFL 99
Cdd:COG3961 19 GIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAERVPVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 100 AILGSRPVNEL-------------NMDAFQElnqnpMYNGIAVYNKRVaYAEQLPKVIDEACRAAVSKKGPAVVEIPVNF 166
Cdd:COG3961 98 HIVGAPGTRAQrrgpllhhtlgdgDFDHFLR-----MFEEVTVAQAVL-TPENAAAEIDRVLAAALREKRPVYIELPRDV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 167 GFQEIdensyygSGSYERSFIAP------ALNEVeVDKAVEILNNAERPVIYAG-----YGgvkAGEVITELSRKIKAPI 235
Cdd:COG3961 172 ADAPI-------EPPEAPLPLPPpasdpaALAAA-VAAAAERLAKAKRPVILAGvevhrFG---LQEELLALAEKTGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 236 ITT--GKNF-----EAFEWNYEGLTGSayrvgwKPANEVVFEADTVLFLGSNFpfAEVYEAF----KNTEKFIQVDIDPY 304
Cdd:COG3961 241 ATTllGKSVldeshPQFIGTYAGAASS------PEVREYVENADCVLCLGVVF--TDTNTGGftaqLDPERTIDIQPDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 305 KLGKRHALDASiLGDAGQAAKAILDKVNPVESTPwwranvknnqnwRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIY 384
Cdd:COG3961 313 RVGGHIYPGVS-LADFLEALAELLKKRSAPLPAP------------APPPPPPPAAPDAPLTQDRLWQRLQAFLDPGDIV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 385 SIDVGDTTQTSTRhLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINV 464
Cdd:COG3961 380 VADTGTSLFGAAD-LRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 465 VFSNGKYA---FIKDKYEDTNkhlfgcDFPNADYAKIAEA---QGAVGFTVDRIEDIDAVVAEAVKLNKEGktVVIDARI 538
Cdd:COG3961 459 VLNNDGYTierAIHGPDGPYN------DIANWDYAKLPEAfggGNALGFRVTTEGELEEALAAAEANTDRL--TLIEVVL 530
|
...
gi 446113971 539 SQH 541
Cdd:COG3961 531 DKM 533
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
369-533 |
3.20e-13 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 72.30 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 369 QVYNAINKHADQDAIYsidVGDTTqtSTRHLhmtpknMWRTSPL-----FATM-----GIALPGGIAAKKDNPDRQVWNI 438
Cdd:PRK07092 363 FVLQTLAALRPADAIV---VEEAP--STRPA------MQEHLPMrrqgsFYTMasgglGYGLPAAVGVALAQPGRRVIGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 439 MGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIKD-----KYEDTNkhlfGCDFPNADYAKIAEAQGAVGFTVDRIE 513
Cdd:PRK07092 432 IGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALRWfapvfGVRDVP----GLDLPGLDFVALARGYGCEAVRVSDAA 507
|
170 180
....*....|....*....|
gi 446113971 514 DIDAVVAEAvkLNKEGKTVV 533
Cdd:PRK07092 508 ELADALARA--LAADGPVLV 525
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
369-534 |
1.01e-10 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 61.53 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 369 QVYNAINKHADQDAIYSIDVGDTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCY 448
Cdd:cd02006 12 RVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 449 PDVITNVQYDLPVINVVFSNGKYAFIKD-------------KYEDTNKHlfGCDFPNADYAKIAEAQGAVGFTVDRIEDI 515
Cdd:cd02006 92 EELAVGAQHRIPYIHVLVNNAYLGLIRQaqrafdmdyqvnlAFENINSS--ELGGYGVDHVKVAEGLGCKAIRVTKPEEL 169
|
170
....*....|....*....
gi 446113971 516 DAVVAEAVKLNKEGKTVVI 534
Cdd:cd02006 170 AAAFEQAKKLMAEHRVPVV 188
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
401-540 |
1.56e-08 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 54.46 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 401 MTPKNM-WRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYA---FIKD 476
Cdd:cd02005 36 KLPKGTrFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTierAIHG 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446113971 477 KYEDTNkhlfgcDFPNADYAKIAEA----QGAVGFTVDRIEDIDAVVAEAvkLNKEGKTVVIDARISQ 540
Cdd:cd02005 116 PEASYN------DIANWNYTKLPEVfgggGGGLSFRVKTEGELDEALKDA--LFNRDKLSLIEVILPK 175
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
16-164 |
1.61e-08 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 54.04 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 16 LKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGsIGVAVGSGGPGATHLINGVYDAAMDN 95
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 96 TPFLAILGSRPVNEL-------------NMDAFQElnqnpMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEI 162
Cdd:cd07038 86 VPVVHIVGAPSTKAQasglllhhtlgdgDFDVFLK-----MFEEITCAAARLTDPENAAEEIDRVLRTALRESRPVYIEI 160
|
..
gi 446113971 163 PV 164
Cdd:cd07038 161 PR 162
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
417-524 |
1.07e-04 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 45.22 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 417 GIALPGGIAAKKDNPDRQVWNIMGDGAFnMCYPDVI-TNVQYDLPVINVVFSNGKYAFIKDKYE--------DTNKHLFG 487
Cdd:PRK07586 388 GQGLPLATGAAVACPDRKVLALQGDGSA-MYTIQALwTQARENLDVTTVIFANRAYAILRGELArvgagnpgPRALDMLD 466
|
90 100 110
....*....|....*....|....*....|....*..
gi 446113971 488 CDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVK 524
Cdd:PRK07586 467 LDDPDLDWVALAEGMGVPARRVTTAEEFADALAAALA 503
|
|
| POR_N |
pfam01855 |
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ... |
24-108 |
1.48e-03 |
|
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N terminal structural domain of the pyruvate ferredoxin oxidoreductase. This domain binds thiamine diphosphate, and along with domains II and IV, is involved in inter subunit contacts. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited.
Pssm-ID: 396432 Cd Length: 230 Bit Score: 40.32 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 24 IYGI-PSGTLSSLMDALA---EDKDIRFLQVRhEETGALAAVMQAKFGGSIgVAVGSGGPGATHLINGVYDAAMDNTPFL 99
Cdd:pfam01855 12 AYPItPSSEIAEEAAEWAangEKGDVVVIQME-SEIGAISAVIGAAAAGAR-AATATSGQGLLLMIENLGKAAGERLPVV 89
|
....*....
gi 446113971 100 AILGSRPVN 108
Cdd:pfam01855 90 IHVVARAGP 98
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
415-523 |
1.78e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 41.01 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 415 TMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINVVFSNGKYAFIKDKYEDTNKHLFG------- 487
Cdd:PRK12474 390 SIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGELQRVGAQGAGrnalsml 469
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90 100 110
....*....|....*....|....*....|....*..
gi 446113971 488 -CDFPNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAV 523
Cdd:PRK12474 470 dLHNPELNWMKIAEGLGVEASRATTAEEFSAQYAAAM 506
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|
| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
20-108 |
5.19e-03 |
|
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate.
Pssm-ID: 132917 [Multi-domain] Cd Length: 160 Bit Score: 37.87 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 20 GVDTIYGIPsGT-LSSLMDALAE----DKDIRFLQVRHEEtGALAAVMQAKFGGSIgVAVGSGGPGATHLINGVYDAAMD 94
Cdd:cd07034 13 GVDVVAAYP-ITpSTEIAETLAKavlgELGGVVVQAESEH-AAAEAAIGASAAGAR-AMTATSGPGLNLMAEALYLAAGA 89
|
90
....*....|....
gi 446113971 95 NTPFLAILGSRPVN 108
Cdd:cd07034 90 ELPLVIVVAQRPGP 103
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|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
181-319 |
7.49e-03 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 38.85 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 181 SYERSFIAPALNEVEVD------KAVEILNNAERPVIYAGYGGVKAG-EVITELSRKIKAPIITT-----GKNFEAFEwn 248
Cdd:cd02761 39 RYERRITTPRIDGKPVSleeaieKAAEILKEAKRPLFYGLGTTVCEAqRAGIELAEKLGAIIDHAasvchGPNLLALQ-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446113971 249 yegltgsayRVGWKPAN--EVVFEADTVLFLGSN----FP--------FAEVYEAFKNTEKFIQVDIDPYKlgkrhaLDA 314
Cdd:cd02761 117 ---------DSGWPTTTlgEVKNRADVIVYWGTNpmhaHPrhmsrysvFPRGFFREGGREDRTLIVVDPRK------SDT 181
|
....*
gi 446113971 315 SILGD 319
Cdd:cd02761 182 AKLAD 186
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