|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-579 |
0e+00 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 914.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 1 MAQKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAI 80
Cdd:PRK08611 2 AKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 81 HILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKHGVAVLTI 160
Cdd:PRK08611 82 HLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVLTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 161 PDNLPEQRVSDHYISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFLEQNHIPFISTLPAKGI 240
Cdd:PRK08611 162 PDDLPAQKIKDTTNKTVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPAKGI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 241 IGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYPYTAYLPKpgRAKSIQINTSASAIGKRYPADVGLVADIKDVIK 320
Cdd:PRK08611 242 IPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYVDYLPK--KAKAIQIDTDPANIGKRYPVNVGLVGDAKKALH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 321 QLNssETTILHPDDGFLKACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSWSARFLNVSP 400
Cdd:PRK08611 320 QLT--ENIKHVEDRRFLEACQENMAKWWKWMEEDENNASTPIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNLGT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 401 TQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYEQQAAGQ 480
Cdd:PRK08611 398 NQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 481 LNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINAYV-SDDAPLPGKIVGQEAKGYMKFGSQYL 559
Cdd:PRK08611 478 LEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALA-QDKPVIIDVYVdPNAAPLPGKIVNDEALGYSKWAIKSL 556
|
570 580
....*....|....*....|
gi 1586112881 560 KEEKKIPELPPLKDILRQFF 579
Cdd:PRK08611 557 FEDKKLDQMPPLKKALKRFL 576
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
1-542 |
2.12e-170 |
|
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: 494.68 E-value: 2.12e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 1 MAQKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQqDQIGFVQVRHeevaslaaaaeaKLTGKLGVCLSIGGPGAI 80
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQ-SGIRHILVRHeqgaafmadgyaRATGKPGVCLVTSGPGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 81 HILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAY-EKHGVAVLT 159
Cdd:COG0028 80 NLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATsGRPGPVVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 160 IPDNLPEQRVSDHYISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFISTLPA 237
Cdd:COG0028 160 IPKDVQAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAaeELRALAERLGAPVVTTLMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 238 KGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP------YTAYLPKpgrAKSIQINTSASAIGKRYPADVGL 311
Cdd:COG0028 240 KGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDdrvtgnWDEFAPD---AKIIHIDIDPAEIGKNYPVDLPI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 312 VADIKDVIKQLNSSettiLHPDDGFLKACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSW 391
Cdd:COG0028 317 VGDAKAVLAALLEA----LEPRADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 392 SARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFI 471
Cdd:COG0028 393 AARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586112881 472 EYEQQAAGQLNY-QIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINAYVSDDAPLPGK 542
Cdd:COG0028 473 RQWQELFYGGRYsGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALA-SDGPALIDVRVDPEENPPGA 543
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
5-577 |
5.49e-170 |
|
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: 494.74 E-value: 5.49e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 5 ASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILN 84
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 85 GLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKHGVAVLTIPDNL 164
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHNGVAVVTIPVDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 165 PEQRVSDH-YISSASSFQLTS-PQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFLEQNHIPFISTLPAKGIIG 242
Cdd:TIGR02720 161 GWQEIPDNdYYASSVSYQTPLlPAPDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 243 DNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYPYTAYLPKPGRAK-SIQINTSASAIGKRYPADVGLVADIKDVIKQ 321
Cdd:TIGR02720 241 DRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKAFKNTKyFIQIDIDPAKLGKRHHTDIAVLADAKKALAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 322 LNSSETTIlhPDDGFLKACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPT 401
Cdd:TIGR02720 321 ILAQVEPR--ESTPWWQANVANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 402 QKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYEQQAAGQL 481
Cdd:TIGR02720 399 NKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 482 NYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRV-QNMPVLINAYVSDDAPLPGKIVGQEAKGYMKFGSQYLK 560
Cdd:TIGR02720 479 LIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAKAIkQGKPVLIDAKITGDRPLPVEKLRLDPALSSAADIEAFK 558
|
570
....*....|....*..
gi 1586112881 561 EEKKIPELPPLKDILRQ 577
Cdd:TIGR02720 559 EKYEAQELKPLSTYLKQ 575
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
2-552 |
1.74e-141 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 420.78 E-value: 1.74e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 2 AQKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQdqIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIH 81
Cdd:PRK06457 1 MPSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSK--VKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 82 ILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKHGVAVLTIP 161
Cdd:PRK06457 79 LLNGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 162 DNL----PEQRVSDHYISSASSFqltspQIDdnrLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFLEQNHIPFISTLPA 237
Cdd:PRK06457 159 VDIlrksSEYKGSKNTEVGKVKY-----SID---FSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 238 KGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYPYTAYLPKpgRAKSIQINTSASAIGKRYPADVGLVADIKD 317
Cdd:PRK06457 231 KGILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLNK--SAKVIQVDIDNSNIGKRLDVDLSYPIPVAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 318 VIkQLNSSETtilhpDDGFLKACQENVANWNRWMTgKRELD-SKPVAPEALFNDINETAPHNTIYSIDVGTATSWSARFL 396
Cdd:PRK06457 309 FL-NIDIEEK-----SDKFYEELKGKKEDWLDSIS-KQENSlDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 397 NVSPTQKFILSSYLGTMGCALPGAIAAKI-NYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYEQ 475
Cdd:PRK06457 382 RASGEQTFIFSAWLGSMGIGVPGSVGASFaVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQ 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586112881 476 QAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRVQNmPVLINAYV-SDDAPLPGKIVGQEAKGYM 552
Cdd:PRK06457 462 EVMGYPEWGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKG-PAVLDAIVdPNERPMPPKLTFKQAGEYV 538
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-553 |
5.19e-132 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 398.13 E-value: 5.19e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 1 MAQKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAI 80
Cdd:PRK08273 1 MSQTVADFILERLREWGVRRVFGYPGDGINGLLGALGRADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 81 HILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVA-VYNKLISATDNLAEIVDEAIRTAYEKHGVAVLT 159
Cdd:PRK08273 81 HLLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAgAFVQMVTVPEQLRHLVDRAVRTALAERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 160 IPDNLPEQRVSD--------HyissaSSFQLTSPQI--DDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFLEQNHI 229
Cdd:PRK08273 161 LPNDVQELEYEPpphahgtvH-----SGVGYTRPRVvpYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 230 PFISTLPAKGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYPYTAYLPKPGRAKSIQINTSASAIGKRYPADV 309
Cdd:PRK08273 236 GVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFPYSEFLPKEGQARGVQIDIDGRMLGLRYPMEV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 310 GLVADIKDVIKQLNssETTILHPDDGFLKACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTAT 389
Cdd:PRK08273 316 NLVGDAAETLRALL--PLLERKKDRSWRERIEKWVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADSGSCA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 390 SWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMV-MQDFITAVKY-----KLPLINIVL 463
Cdd:PRK08273 394 NWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKYwrqwsDPRLIVLVL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 464 NNSKLAFIEYEQQA---AGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRVqNMPVLINAYVSDD-APL 539
Cdd:PRK08273 474 NNRDLNQVTWEQRVmegDPKFEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAA-DRPVVLEVKTDPNvPPL 552
|
570
....*....|....
gi 1586112881 540 PGKIVGQEAKGYMK 553
Cdd:PRK08273 553 PPHITLEQAKAFAS 566
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
1-552 |
5.32e-117 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 358.92 E-value: 5.32e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 1 MAQKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRkQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAI 80
Cdd:PRK09124 1 MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLR-RMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 81 HILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKHGVAVLTI 160
Cdd:PRK09124 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 161 PDNLPEQRVSDHyiSSASSFQLTSPQI--DDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFLEQNHIPFISTLPAK 238
Cdd:PRK09124 160 PGDVALKPAPER--ATPHWYHAPQPVVtpAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 239 GIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYPYTAYLPKpgRAKSIQINTSASAIGKRYPADVGLVADIKDV 318
Cdd:PRK09124 238 EHVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQFYPT--DAKIIQIDINPGSLGRRSPVDLGLVGDVKAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 319 IKQLNSSETTilHPDDGFLKACQENVAnwnrwmTGKRELDS--------KPVAPEALFNDINETAPHNTIYSIDVGTATS 390
Cdd:PRK09124 316 LAALLPLLEE--KTDRKFLDKALEHYR------KARKGLDDlavpsdggKPIHPQYLARQISEFAADDAIFTCDVGTPTV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 391 WSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAF 470
Cdd:PRK09124 388 WAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 471 IEYEQQAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYrVQNMPVLINAYVS-DDAPLPGKIVGQEAK 549
Cdd:PRK09124 468 VAMEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAF-AHDGPALVDVVTAkQELAMPPQIKLEQAK 546
|
....*.
gi 1586112881 550 G---YM 552
Cdd:PRK09124 547 GfslYM 552
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-551 |
1.62e-103 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 323.86 E-value: 1.62e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 1 MAQKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDqIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAI 80
Cdd:PRK06546 1 MAKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGG-IEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 81 HILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKHGVAVLTI 160
Cdd:PRK06546 80 HLINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGGGVSVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 161 PDNLPEQRVSDHYISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFLEQNHIPFISTLPAKGI 240
Cdd:PRK06546 160 PGDIADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGKEW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 241 IGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYPYTAYLPKpgrAKSIQINTSASAIGKRYPADVGLVADIKDVIK 320
Cdd:PRK06546 240 IQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFPYDQFLPD---VRTAQVDIDPEHLGRRTRVDLAVHGDVAETIR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 321 QLnsseTTILHP--DDGFL-KACQENVANWNRWM---TGKRElDSKPVAPEALFNDINETAPHNTIYSIDVGTATSWSAR 394
Cdd:PRK06546 317 AL----LPLVKEktDRRFLdRMLKKHARKLEKVVgayTRKVE-KHTPIHPEYVASILDELAADDAVFTVDTGMCNVWAAR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 395 FLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYE 474
Cdd:PRK06546 392 YITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLE 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586112881 475 QQAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINAYVSDDA-PLPGKIVGQEAKGY 551
Cdd:PRK06546 472 MLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFA-HPGPALVDVVTDPNAlSIPPTITGEQVKGF 548
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
3-538 |
1.71e-86 |
|
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: 278.92 E-value: 1.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 3 QKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRkQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHI 82
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALY-NDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 83 LNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIP 161
Cdd:TIGR00118 80 VTGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTgRPGPVLVDLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 162 DNLPEQRVSDHYISSAS--SFQltsPQIDDNRL--NTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFISTL 235
Cdd:TIGR00118 160 KDVTTAEIEYPYPEKVNlpGYR---PTVKGHPLqiKKAAELINLAKKPVILVGGGVIIAGAseELKELAERIQIPVTTTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 236 PAKGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP--YTAYLPK--PgRAKSIQINTSASAIGKRYPADVGL 311
Cdd:TIGR00118 237 MGLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDdrVTGNLAKfaP-NAKIIHIDIDPAEIGKNVRVDIPI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 312 VADIKDVIKQLNSSETTILHPDDgflKACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSW 391
Cdd:TIGR00118 316 VGDARNVLEELLKKLFELKERKE---SAWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 392 SARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFI 471
Cdd:TIGR00118 393 AAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586112881 472 EYEQQA--AGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINAYVSDDAP 538
Cdd:TIGR00118 473 RQWQELfyEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALS-SNEPVLLDVVVDKPEN 540
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
4-530 |
2.51e-84 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 272.86 E-value: 2.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 4 KASEQLVDVLIDWHVKHVYGLPGD-SIDTtVDALRKQQdqIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHI 82
Cdd:PRK08322 2 KAADLFVKCLENEGVEYIFGIPGEeNLDL-LEALRDSS--IKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 83 LNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAY-EKHGVAVLTIP 161
Cdd:PRK08322 79 VTGVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEeERPGAVHLELP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 162 DNLPEQRVSDHYISsASSFQLTSPqiDDNRLNTAAKLIRDSKKPLALVGLGA--KKAGSQVAAFLEQNHIPFISTLPAKG 239
Cdd:PRK08322 159 EDIAAEETDGKPLP-RSYSRRPYA--SPKAIERAAEAIQAAKNPLILIGAGAnrKTASKALTEFVDKTGIPFFTTQMGKG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 240 IIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGtnYPYTAYLPK----PGRAKSIQINTSASAIGKRYPADVGLVADI 315
Cdd:PRK08322 236 VIPETHPLSLGTAGLSQGDYVHCAIEHADLIINVG--HDVIEKPPFfmnpNGDKKVIHINFLPAEVDPVYFPQVEVVGDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 316 KDVIKQLNSSETTILH-PDDGFLKACQENVANwnrwMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSWSAR 394
Cdd:PRK08322 314 ANSLWQLKERLADQPHwDFPRFLKIREAIEAH----LEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIWFAR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 395 FLnvsPTQK---FILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFI 471
Cdd:PRK08322 390 NY---RAYEpntCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMI 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586112881 472 EYEQQAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLIN 530
Cdd:PRK08322 467 RWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALA-QPGVHVID 524
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
361-539 |
8.14e-84 |
|
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: 259.00 E-value: 8.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 361 PVAPEALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGA 440
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 441 FAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYEQQAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAY 520
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEAL 160
|
170
....*....|....*....
gi 1586112881 521 RvQNMPVLINAYVSDDAPL 539
Cdd:cd02014 161 A-ADGPVVIDVVTDPNEPP 178
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
9-542 |
4.47e-75 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 249.62 E-value: 4.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 9 LVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDQiGFVQ---VRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:CHL00099 16 LIDSLVRHGVKHIFGYPGGAILPIYDELYAWEKK-GLIKhilVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAyeKHGV--AVLT-IPD 162
Cdd:CHL00099 95 IATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIA--KHGRpgPVLIdIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 163 NLPEQRVSDH-YISSASSFQLT----SPQIDDNRLNTAAKLIRDSKKPLALVGLGA--KKAGSQVAAFLEQNHIPFISTL 235
Cdd:CHL00099 173 DVGLEKFDYYpPEPGNTIIKILgcrpIYKPTIKRIEQAAKLILQSSQPLLYVGGGAiiSDAHQEITELAELYKIPVTTTL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 236 PAKGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP--YTAYLPK-PGRAKSIQINTSASAIGKRYPADVGLV 312
Cdd:CHL00099 253 MGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDdrVTGKLDEfACNAQVIHIDIDPAEIGKNRIPQVAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 313 ADIKDVIKQ-LNSSETTILHPDDGFLKACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPhNTIYSIDVGTATSW 391
Cdd:CHL00099 333 GDVKKVLQElLELLKNSPNLLESEQTQAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQLAP-DAYFTTDVGQHQMW 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 392 SARFLNVSPtQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFI 471
Cdd:CHL00099 412 AAQFLKCKP-RKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMV 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 472 EYEQQAAGQLNYQidLQDM-----DYAKFADAAGGVGITAKTSEEFKNALNRAYRVqNMPVLINAYVSDDA---PL--PG 541
Cdd:CHL00099 491 RQWQQAFYGERYS--HSNMeegapDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDY-DGPVLIDCQVIEDEncyPMvaPG 567
|
.
gi 1586112881 542 K 542
Cdd:CHL00099 568 K 568
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
4-167 |
2.53e-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: 233.98 E-value: 2.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 4 KASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQqDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHIL 83
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRRE-GKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 84 NGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKHGVAVLTIPDN 163
Cdd:cd07039 80 NGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKRGVAVLILPGD 159
|
....
gi 1586112881 164 LPEQ 167
Cdd:cd07039 160 VQDA 163
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
4-540 |
1.03e-73 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 246.20 E-value: 1.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 4 KASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALrkQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHIL 83
Cdd:PRK06276 2 KGAEAIIKALEAEGVKIIFGYPGGALLPFYDAL--YDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 84 NGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPD 162
Cdd:PRK06276 80 TGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTgRPGPVHIDLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 163 NLPEQRVS--DHYISSASSFQLTSPQIDDNRLNT--AAKLIRDSKKPLALVGLGAKKAGS-----QVAAFLEqnhIPFIS 233
Cdd:PRK06276 160 DVQEGELDleKYPIPAKIDLPGYKPTTFGHPLQIkkAAELIAEAERPVILAGGGVIISGAseeliELSELVK---IPVCT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 234 TLPAKGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP------YTAYLPKpgrAKSIQINTSASAIGKRYPA 307
Cdd:PRK06276 237 TLMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSdrttgdISSFAPN---AKIIHIDIDPAEIGKNVRV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 308 DVGLVADIKDVIKQLNSsettilhpddgflKACQENVANWNRWMTGKREL----------DSKPVAPEALFNDINE---- 373
Cdd:PRK06276 314 DVPIVGDAKNVLRDLLA-------------ELMKKEIKNKSEWLERVKKLkkesiprmdfDDKPIKPQRVIKELMEvlre 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 374 -TAPHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAV 452
Cdd:PRK06276 381 iDPSKNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 453 KYKLPLINIVLNNSKLAFI-EYEQQAAGQLNYQIDLQDM-DYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLIN 530
Cdd:PRK06276 461 EYDIPVVICIFDNRTLGMVyQWQNLYYGKRQSEVHLGETpDFVKLAESYGVKADRVEKPDEIKEALKEAIK-SGEPYLLD 539
|
570
....*....|
gi 1586112881 531 AYVSDDAPLP 540
Cdd:PRK06276 540 IIIDPAEALP 549
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-533 |
1.11e-70 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 237.30 E-value: 1.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 1 MAQKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQqDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAI 80
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQ-NYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 81 HILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLT 159
Cdd:PRK08527 80 NAVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSgRPGPVHID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 160 IPDNLPEQrVSDHYISSASSFQLTSPQIDDN--RLNTAAKLIRDSKKPLALVGLGA--KKAGSQVAAFLEQNHIPFISTL 235
Cdd:PRK08527 160 IPKDVTAT-LGEFEYPKEISLKTYKPTYKGNsrQIKKAAEAIKEAKKPLFYLGGGAilSNASEEIRELVKKTGIPAVETL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 236 PAKGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP--YTAYLPKPGR-AKSIQINTSASAIGKRYPADVGLV 312
Cdd:PRK08527 239 MARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDdrVTGKLSEFAKhAKIIHVDIDPSSISKIVNADYPIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 313 ADIKDVIKQLNSsETTILHPDDgfLKACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSWS 392
Cdd:PRK08527 319 GDLKNVLKEMLE-ELKEENPTT--YKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 393 ARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIE 472
Cdd:PRK08527 396 AQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVR 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586112881 473 ------YEQQAAgqlNYQIDLQDmDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINAYV 533
Cdd:PRK08527 476 qwqtffYEERYS---ETDLSTQP-DFVKLAESFGGIGFRVTTKEEFDKALKEALE-SDKVALIDVKI 537
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
5-537 |
1.02e-69 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 234.67 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 5 ASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQdqIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILN 84
Cdd:PRK06048 10 GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD--LRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 85 GLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDN 163
Cdd:PRK06048 88 GIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTgRPGPVLIDLPKD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 164 LPEQRVSDHYISSASsFQLTSPQIDDN--RLNTAAKLIRDSKKPLALVGLG--AKKAGSQVAAFLEQNHIPFISTLPAKG 239
Cdd:PRK06048 168 VTTAEIDFDYPDKVE-LRGYKPTYKGNpqQIKRAAELIMKAERPIIYAGGGviSSNASEELVELAETIPAPVTTTLMGIG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 240 IIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNY------PYTAYLPKpgrAKSIQINTSASAIGKRYPADVGLVA 313
Cdd:PRK06048 247 AIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFddrvtgKLASFAPN---AKIIHIDIDPAEISKNVKVDVPIVG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 314 DIKDVIKQLNSsettilhpddgFLKACQ-----ENVANWNRWMTGKRELDSKPVAPEALFNDINETAPhNTIYSIDVGTA 388
Cdd:PRK06048 324 DAKQVLKSLIK-----------YVQYCDrkewlDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 389 TSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKL 468
Cdd:PRK06048 392 QMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYL 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586112881 469 AFIEYEQQAAGQLNY-QIDLQD-MDYAKFADAAGGVGITAKTSEEFKNALNRAYRVqNMPVLINAYVSDDA 537
Cdd:PRK06048 472 GMVRQWQELFYDKRYsHTCIKGsVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVAS-DRPVVIDFIVECEE 541
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-529 |
3.31e-69 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 233.23 E-value: 3.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 1 MAQKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDqIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAI 80
Cdd:PRK08199 6 RARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETD-IRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 81 HILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLT 159
Cdd:PRK08199 85 NASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSgRPGPVVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 160 IPDNLPEQRVSdhyISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAK--KAGSQVAAFLEQNHIPFISTLPA 237
Cdd:PRK08199 165 LPEDVLSETAE---VPDAPPYRRVAAAPGAADLARLAELLARAERPLVILGGSGWteAAVADLRAFAERWGLPVACAFRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 238 KGIIGDNHPNSLGNVGkLGTKPAY-EAMQNTDLLLMFGTNY---PYTAY----LPKPgRAKSIQINTSASAIGKRYPADV 309
Cdd:PRK08199 242 QDLFDNRHPNYAGDLG-LGINPALaARIREADLVLAVGTRLgevTTQGYtlldIPVP-RQTLVHVHPDAEELGRVYRPDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 310 GLVADIKDVIKQLNSsettiLHPDDgflkacqenVANWNRWMTGKRE--LDSKPVAP-------EALFNDINETAPHNTI 380
Cdd:PRK08199 320 AIVADPAAFAAALAA-----LEPPA---------SPAWAEWTAAAHAdyLAWSAPLPgpgavqlGEVMAWLRERLPADAI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 381 YSIDVGTATSWSARF--LNVSPTQkfiLSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPL 458
Cdd:PRK08199 386 ITNGAGNYATWLHRFfrFRRYRTQ---LAPTSGSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPI 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586112881 459 INIVLNNSKLAFI------EYEQQAAGqlnyqIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAyRVQNMPVLI 529
Cdd:PRK08199 463 IVIVVNNGMYGTIrmhqerEYPGRVSG-----TDLTNPDFAALARAYGGHGETVERTEDFAPAFERA-LASGKPALI 533
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
9-518 |
2.05e-68 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 230.92 E-value: 2.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 9 LVDVLIDWHVKHVYGLPGDSIDTTVDALrkQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNGLYD 88
Cdd:PRK08978 7 VVHALRAQGVDTVFGYPGGAIMPVYDAL--YDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 89 AKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDN--LP 165
Cdd:PRK08978 85 ALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSgRPGPVLVDIPKDiqLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 166 EQRVSDHYISSASSfqltsPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFISTLPAKGIIGD 243
Cdd:PRK08978 165 EGELEPHLTTVENE-----PAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAvpALREFLAATGMPAVATLKGLGAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 244 NHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNY------PYTAYLPKpgrAKSIQINTSASAIGKRYPADVGLVADIKD 317
Cdd:PRK08978 240 DHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFddrvtgKLNTFAPH---AKVIHLDIDPAEINKLRQAHVALQGDLNA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 318 VIKQLnsseTTILHPDdgflkACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSWSARFLN 397
Cdd:PRK08978 317 LLPAL----QQPLNID-----AWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 398 VSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYEQQA 477
Cdd:PRK08978 388 FTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1586112881 478 AGQLNY-QIDLQDM-DYAKFADAAGGVGITAKTSEEFKNALNR 518
Cdd:PRK08978 468 FFDERYsETDLSDNpDFVMLASAFGIPGQTITRKDQVEAALDT 510
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
6-537 |
2.34e-65 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 224.48 E-value: 2.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 6 SEQLVDVLIDWHVKHVYGLPGDSIDTTVDALrKQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK07789 34 AQAVVRSLEELGVDVVFGIPGGAILPVYDPL-FDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKHGVAVLT-IP-DN 163
Cdd:PRK07789 113 IADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVdIPkDA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 164 LPEQRvsdhYISSASSFQL------TSP---QIDDnrlntAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFI 232
Cdd:PRK07789 193 LQAQT----TFSWPPRMDLpgyrpvTKPhgkQIRE-----AAKLIAAARRPVLYVGGGVIRAEAsaELRELAELTGIPVV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 233 STLPAKGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP--YTAYLPK--PGrAKSIQINTSASAIGKRYPAD 308
Cdd:PRK07789 264 TTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDdrVTGKLDSfaPD-AKVIHADIDPAEIGKNRHAD 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 309 VGLVADIKDVIKQLNS---SETTILHPDDgflkacqenVANWNRWMTGKREL--------DSKPVAPEALFNDINETAPH 377
Cdd:PRK07789 343 VPIVGDVKEVIAELIAalrAEHAAGGKPD---------LTAWWAYLDGWRETyplgydepSDGSLAPQYVIERLGEIAGP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 378 NTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLP 457
Cdd:PRK07789 414 DAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIP 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 458 LINIVLNNSKLAFIE------YEQQAAgqlnyQIDLQDM-----DYAKFADAAGGVGITAKTSEEFKNALNRAYRVQNMP 526
Cdd:PRK07789 494 IKVALINNGNLGMVRqwqtlfYEERYS-----NTDLHTHshripDFVKLAEAYGCVGLRCEREEDVDAVIEKARAINDRP 568
|
570
....*....|.
gi 1586112881 527 VLINAYVSDDA 537
Cdd:PRK07789 569 VVIDFVVGKDA 579
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
7-536 |
4.05e-65 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 222.19 E-value: 4.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 7 EQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNGL 86
Cdd:PRK08266 8 EAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGAAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 87 YDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNK---LISATDNLAEIVDEAIRTAYEKH-GVAVLTIPD 162
Cdd:PRK08266 88 LTAYGCNSPVLCLTGQIPSALIGKGRGHLHEMPDQLATLRSFTKwaeRIEHPSEAPALVAEAFQQMLSGRpRPVALEMPW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 163 NLPEQRVSDHYISSASsfQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFLEQNHIPFISTLPAKGIIG 242
Cdd:PRK08266 168 DVFGQRAPVAAAPPLR--PAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRSGRGIVS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 243 DNHPNSLGNVGklgtkpAYEAMQNTDLLLMFGTNY--PYTAYLPKPGRAKSIQINTSASAIGkRYPADVGLVADIKDVik 320
Cdd:PRK08266 246 DRHPLGLNFAA------AYELWPQTDVVIGIGSRLelPTFRWPWRPDGLKVIRIDIDPTEMR-RLKPDVAIVADAKAG-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 321 qlnssettilhpddgfLKACQENVANWNRWMTGKRE----------LDSKPVAPEALF-NDINETAPHNTIY---SIDVG 386
Cdd:PRK08266 317 ----------------TAALLDALSKAGSKRPSRRAelrelkaaarQRIQAVQPQASYlRAIREALPDDGIFvdeLSQVG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 387 TAtSWSArFLNVSPTQkFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNS 466
Cdd:PRK08266 381 FA-SWFA-FPVYAPRT-FVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNN 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586112881 467 KLAFIEYEQ-QAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINAYVSDD 536
Cdd:PRK08266 458 AYGNVRRDQkRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALA-HGGPVLIEVPVPRG 527
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
5-529 |
2.25e-64 |
|
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: 220.01 E-value: 2.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 5 ASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALrkQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILN 84
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDAL--EDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 85 GLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDN 163
Cdd:TIGR02418 79 GLATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESgKPGAAFVSLPQD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 164 LPEQRVSDHYISSASSFQLTSPQIDDnrLNTAAKLIRDSKKPLALVGLGAKKAGSQVA--AFLEQNHIPFISTLPAKGII 241
Cdd:TIGR02418 159 VVDSPVSVKAIPASYAPKLGAAPDDA--IDEVAEAIQNAKLPVLLLGLRASSPETTEAvrRLLKKTQLPVVETFQGAGAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 242 G-DNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGtnYPYTAYLP----KPGRAKSIQINTSASAIGKRYPADVGLVADIK 316
Cdd:TIGR02418 237 SrELEDHFFGRVGLFRNQPGDRLLKQADLVITIG--YDPIEYEPrnwnSENDATIVHIDVEPAQIDNNYQPDLELVGDIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 317 DVIKQLNSS-ETTILHPDD-GFLKACQENVANWNRWmtgKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSWSAR 394
Cdd:TIGR02418 315 STLDLLAERiPGYELPPDAlAILEDLKQQREALDRV---PATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMAR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 395 FLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYE 474
Cdd:TIGR02418 392 YFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQ 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1586112881 475 QQAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRVqNMPVLI 529
Cdd:TIGR02418 472 EEMKYQRSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEV-EGPVVV 525
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
9-542 |
4.81e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 221.08 E-value: 4.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 9 LVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDQiGFVQ---VRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK07418 25 LMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAE-GWLKhilVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNLVTG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDNL 164
Cdd:PRK07418 104 IATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSgRPGPVLIDIPKDV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 165 pEQRVSDHYISSASSFQLT----SPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFISTLPAK 238
Cdd:PRK07418 184 -GQEEFDYVPVEPGSVKPPgyrpTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAhaELKELAERFQIPVTTTLMGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 239 GIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP--YTAYLPK-PGRAKSIQINTSASAIGKRYPADVGLVADI 315
Cdd:PRK07418 263 GAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDdrVTGKLDEfASRAKVIHIDIDPAEVGKNRRPDVPIVGDV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 316 KDVIKQLN--SSEttilhpddgflKACQENVANW----NRWmtgKREL------DSKPVAPEALFNDINETAPHnTIYSI 383
Cdd:PRK07418 343 RKVLVKLLerSLE-----------PTTPPRTQAWleriNRW---KQDYplvvppYEGEIYPQEVLLAVRDLAPD-AYYTT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 384 DVGTATSWSARFLNVSPTQkFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVL 463
Cdd:PRK07418 408 DVGQHQMWAAQFLRNGPRR-WISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVII 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 464 NNSKLAFIEYEQQAAGQLNYQIdlQDM-----DYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINAYVSDDA- 537
Cdd:PRK07418 487 NNGWQGMVRQWQESFYGERYSA--SNMepgmpDFVKLAEAFGVKGMVISERDQLKDAIAEALA-HDGPVLIDVHVRRDEn 563
|
....*....
gi 1586112881 538 --PL--PGK 542
Cdd:PRK07418 564 cyPMvpPGK 572
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
9-570 |
1.83e-62 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 215.86 E-value: 1.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 9 LVDVLIDWHVKHVYGLPGDSIDTTVDALRK--QQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNGL 86
Cdd:PRK06456 8 LVDSLKREGVKVIFGIPGLSNMQIYDAFVEdlANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLVTGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 87 YDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDNLP 165
Cdd:PRK06456 88 ITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTgRPGPVVIDIPRDIF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 166 EQRVSD------HYISSASSFQLTspqIDDNRLNTAAKLIRDSKKPLALVGLGA--KKAGSQVAAFLEQNHIPFISTLPA 237
Cdd:PRK06456 168 YEKMEEikwpekPLVKGYRDFPTR---IDRLALKKAAEILINAERPIILVGTGVvwSNATPEVLELAELLHIPIVSTFPG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 238 KGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFG---TNYPYTAYLP-KPGRAKSIQINTSASAIGKRYPADVGLVA 313
Cdd:PRK06456 245 KTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGarfSDRTFTSYDEmVETRKKFIMVNIDPTDGEKAIKVDVGIYG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 314 DIKDVIKQL--NSSETTILHPDDGFLKACQENVANWNRWMTGKrelDSKPVAPEALFNDINETAPHNTIYSIDVGTATSW 391
Cdd:PRK06456 325 NAKIILRELikAITELGQKRDRSAWLKRVKEYKEYYSQFYYTE---ENGKLKPWKIMKTIRQALPRDAIVTTGVGQHQMW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 392 SARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFI 471
Cdd:PRK06456 402 AEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 472 EYEQQAAgqLNYQIDLQDM----DYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINAYVSddaplpgkivgqe 547
Cdd:PRK06456 482 RQVQDLF--FGKRIVGVDYgpspDFVKLAEAFGALGFNVTTYEDIEKSLKSAIK-EDIPAVIRVPVD------------- 545
|
570 580
....*....|....*....|...
gi 1586112881 548 akgymkfgsqylKEEKKIPELPP 570
Cdd:PRK06456 546 ------------KEELALPTLPP 556
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
3-530 |
2.70e-60 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 209.33 E-value: 2.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 3 QKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALrkQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHI 82
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDAL--EDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 83 LNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIP 161
Cdd:PRK08617 83 ATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESgRPGAAFVSLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 162 DNLPEQRVSDHYISSASSFQLTSPQIDDnrLNTAAKLIRDSKKPLALVGLGA--KKAGSQVAAFLEQNHIPFISTLPAKG 239
Cdd:PRK08617 163 QDVVDAPVTSKAIAPLSKPKLGPASPED--INYLAELIKNAKLPVLLLGMRAssPEVTAAIRRLLERTNLPVVETFQAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 240 IIGDNH-PNSLGNVGKLGTKPAYEAMQNTDLLLMFGtnYPYTAYLP----KPGRAKSIQINTSASAIGKRYPADVGLVAD 314
Cdd:PRK08617 241 VISRELeDHFFGRVGLFRNQPGDELLKKADLVITIG--YDPIEYEPrnwnSEGDATIIHIDVLPAEIDNYYQPERELIGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 315 IKDVIKQLNSSETTILHPDDG--FLKACQENVanwNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSWS 392
Cdd:PRK08617 319 IAATLDLLAEKLDGLSLSPQSleILEELRAQL---EELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSHYIWM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 393 ARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIE 472
Cdd:PRK08617 396 ARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVE 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586112881 473 YEQqaagQLNYQ----IDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRVQNmPVLIN 530
Cdd:PRK08617 476 FQE----EMKYGrssgVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDG-PVVID 532
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
6-533 |
6.84e-58 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 203.79 E-value: 6.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 6 SEQLVDVLIDWHVKHVYGLPGDSIDTTVDALrKQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK09107 14 AEMVVQALKDQGVEHIFGYPGGAVLPIYDEI-FQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDNL 164
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSgRPGPVVVDIPKDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 165 peQRVSDHYISSASSFQLTS--PQI--DDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFL----EQNHIPFISTL- 235
Cdd:PRK09107 173 --QFATGTYTPPQKAPVHVSyqPKVkgDAEAITEAVELLANAKRPVIYSGGGVINSGPEASRLLrelvELTGFPITSTLm 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 236 -----PAKGiigdnhPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP------YTAYLPKpgrAKSIQINTSASAIGKR 304
Cdd:PRK09107 251 glgayPASG------KNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDdritgrLDAFSPN---SKKIHIDIDPSSINKN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 305 YPADVGLVADI----KDVIKQLNSSETTilhPDDGFLKACQENVANWNrwmtGKRELDSKP----VAPEALFNDINE-TA 375
Cdd:PRK09107 322 VRVDVPIIGDVghvlEDMLRLWKARGKK---PDKEALADWWGQIARWR----ARNSLAYTPsddvIMPQYAIQRLYElTK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 376 PHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYK 455
Cdd:PRK09107 395 GRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 456 LPLINIVLNNSKLAFIEYEQQAAGQLNYQIDLQDM--DYAKFADAAGGVGITAKTSEEFKNALNRAYRVqNMPVLINAYV 533
Cdd:PRK09107 475 LPVKIFILNNQYMGMVRQWQQLLHGNRLSHSYTEAmpDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDV-DKPVIFDCRV 553
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
6-530 |
8.93e-57 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 200.80 E-value: 8.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 6 SEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQqDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQ-DKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDNL 164
Cdd:PRK06965 103 IATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTgRPGPVVVDIPKDV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 165 PEQRVSDHYISSAsSFQLTSP--QIDDNRLNTAAKLIRDSKKPLALVGLGA--KKAGSQVAAFLEQNHIPFISTLPAKGI 240
Cdd:PRK06965 183 SKTPCEYEYPKSV-EMRSYNPvtKGHSGQIRKAVSLLLSAKRPYIYTGGGVilANASRELRQLADLLGYPVTNTLMGLGA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 241 IGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGT--------NYPYTAYLPKpgraKSIQINTSASAIGKRYPADVGLV 312
Cdd:PRK06965 262 YPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGArfddrvigNPAHFASRPR----KIIHIDIDPSSISKRVKVDIPIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 313 ADIKDVIKQLNSS-ETTILHPDDGFLKACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSW 391
Cdd:PRK06965 338 GDVKEVLKELIEQlQTAEHGPDADALAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMW 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 392 SARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFI 471
Cdd:PRK06965 418 AAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMV 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586112881 472 EYEQQAAGQLNYQIDLQDM--DYAKFADAAGGVGITAKTSEEFKNALNRAYRVQNMPVLIN 530
Cdd:PRK06965 498 RQWQEIEYSKRYSHSYMDAlpDFVKLAEAYGHVGMRIEKTSDVEPALREALRLKDRTVFLD 558
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
6-535 |
1.07e-56 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 200.05 E-value: 1.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 6 SEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDqIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSG-IEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIP-DN 163
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTgRPGPVVIDLPkDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 164 LPEQRVSDHYISSASSFQLTSPQIDDNR--LNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFISTLPAKG 239
Cdd:PRK08979 166 LNPAILHPYEYPESIKMRSYNPTTSGHKgqIKRGLQALLAAKKPVLYVGGGAIISGAdkQILQLAEKLNLPVVSTLMGLG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 240 IIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFG------TNYPYTAYLPKpgrAKSIQINTSASAIGKRYPADVGLV- 312
Cdd:PRK08979 246 AFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGvrfddrTTNNLEKYCPN---ATILHIDIDPSSISKTVRVDIPIVg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 313 -ADI--KDVIKQLNSSETTilhPDDGFLKACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTAT 389
Cdd:PRK08979 323 sADKvlDSMLALLDESGET---NDEAAIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 390 SWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLA 469
Cdd:PRK08979 400 MFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLG 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586112881 470 FIEYEQQAAGQLNYQIDLQDM--DYAKFADAAGGVGITAKTSEEFKNALNRAYRVQNMPVLINAYVSD 535
Cdd:PRK08979 480 MVKQWQDMIYQGRHSHSYMDSvpDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRLVFVDINVDE 547
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
6-477 |
4.12e-56 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 198.51 E-value: 4.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 6 SEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQqDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK07282 13 SDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNF-EGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDNL 164
Cdd:PRK07282 92 IADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTgRPGPVVIDLPKDV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 165 PEQRVSDHYISSAS--SFQLTSpQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFISTLPAKGI 240
Cdd:PRK07282 172 SALETDFIYDPEVNlpSYQPTL-EPNDMQIKKILKQLSKAKKPVILAGGGINYAEAatELNAFAERYQIPVVTTLLGQGT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 241 IGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNY-------PYTaYLPKpgrAKSIQINTSASAIGKRYPADVGLVA 313
Cdd:PRK07282 251 IATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFddrltgnPKT-FAKN---AKVAHIDIDPAEIGKIIKTDIPVVG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 314 DIKDVIKQLNSSETTilhpDDGFLKACQENVANWNRWMTgkRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATSWSA 393
Cdd:PRK07282 327 DAKKALQMLLAEPTV----HNNTEKWIEKVTKDKNRVRS--YDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 394 RFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEY 473
Cdd:PRK07282 401 QYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQ 480
|
....
gi 1586112881 474 EQQA 477
Cdd:PRK07282 481 WQES 484
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
6-533 |
6.52e-55 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 195.13 E-value: 6.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 6 SEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQqDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK06882 7 AEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTL-GGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDNL 164
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTgRPGPVVIDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 165 --PEQRVSDHYISSASsFQLTSPQIDDNR--LNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFISTLPAK 238
Cdd:PRK06882 166 vnPANKFTYEYPEEVS-LRSYNPTVQGHKgqIKKALKALLVAKKPVLFVGGGVITAECseQLTQFAQKLNLPVTSSLMGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 239 GIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFG------TNYPYTAYLPkpgRAKSIQINTSASAIGKRYPADVGLV 312
Cdd:PRK06882 245 GAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGvrfddrTTNNLAKYCP---NAKVIHIDIDPTSISKNVPAYIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 313 ADIKDVIKQLNSsettiLHPDDGFLKAcQENVANW----NRWMTGK---RELDSKPVAPEALFNDINETAPHNTIYSIDV 385
Cdd:PRK06882 322 GSAKNVLEEFLS-----LLEEENLAKS-QTDLTAWwqqiNEWKAKKcleFDRTSDVIKPQQVVEAIYRLTNGDAYVASDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 386 GTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNN 465
Cdd:PRK06882 396 GQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586112881 466 SKLAFIEYEQQA--AGQlNYQIDLQDM-DYAKFADAAGGVGITAKTSEEFKNALNRAYRVQNMPVLINAYV 533
Cdd:PRK06882 476 RFLGMVKQWQDLiySGR-HSQVYMNSLpDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKLVFVDVNV 545
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
6-535 |
1.20e-54 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 194.42 E-value: 1.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 6 SEQLVDVLIDWHVKHVYGLPGDSIDTTVDALrkQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK06725 18 AGHVIQCLKKLGVTTVFGYPGGAILPVYDAL--YESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDNL 164
Cdd:PRK06725 96 LADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESgRPGPVLIDIPKDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 165 PEQRVSDHY--ISSASSFQLTsPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFISTLPAKGI 240
Cdd:PRK06725 176 QNEKVTSFYneVVEIPGYKPE-PRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGseELIEFARENRIPVVSTLMGLGA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 241 IGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP--YTAYLPK-PGRAKSIQINTSASAIGKRYPADVGLVADIKD 317
Cdd:PRK06725 255 YPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDdrVTGKLELfSPHSKKVHIDIDPSEFHKNVAVEYPVVGDVKK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 318 VIKQLnsSETTILHPDDGFLkacqENVANWN-RWMTGKRELDSKpVAPEALFNDINETAPHNTIYSIDVGTATSWSARFL 396
Cdd:PRK06725 335 ALHML--LHMSIHTQTDEWL----QKVKTWKeEYPLSYKQKESE-LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 397 NVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYEQq 476
Cdd:PRK06725 408 KAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQ- 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586112881 477 aagQLNYQIDLQDM-----DYAKFADAAGGVGITAKTSEEFKNALNRAYrVQNMPVLINAYVSD 535
Cdd:PRK06725 487 ---EMFYENRLSESkigspDFVKVAEAYGVKGLRATNSTEAKQVMLEAF-AHEGPVVVDFCVEE 546
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
18-533 |
5.41e-54 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 192.62 E-value: 5.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 18 VKHVYGLPGDSIDTTVDALrKQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNGLYDAKMDHVPVL 97
Cdd:PRK08155 28 IRIVTGIPGGAILPLYDAL-SQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTAIADARLDSIPLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 98 ALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIP----------DNLPE 166
Cdd:PRK08155 107 CITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSgRPGPVWIDIPkdvqtavielEALPA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 167 QRVSDhyissassfqlTSPQIDDNRLNTAAKLIRDSKKPLALVGLG--AKKAGSQVAAFLEQNHIPFISTLPAKGIIGDN 244
Cdd:PRK08155 187 PAEKD-----------AAPAFDEESIRDAAAMINAAKRPVLYLGGGviNSGAPARARELAEKAQLPTTMTLMALGMLPKA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 245 HPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYPYTA------YLPkpgRAKSIQINTSASAIGKRYPADVGLVADIKDV 318
Cdd:PRK08155 256 HPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAigkteqFCP---NAKIIHVDIDRAELGKIKQPHVAIQADVDDV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 319 IKQLNSsettilhpddgFLKACQEnvanwNRWMTGKRELDSK----------PVAPEALFNDINETAPHNTIYSIDVGTA 388
Cdd:PRK08155 333 LAQLLP-----------LVEAQPR-----AEWHQLVADLQREfpcpipkaddPLSHYGLINAVAACVDDNAIITTDVGQH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 389 TSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKL 468
Cdd:PRK08155 397 QMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEAL 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586112881 469 AFIeYEQQA--------AGQLNYQIDlqdmdyakFADAAGGVGITA---KTSEEFKNALNRAYRvQNMPVLINAYV 533
Cdd:PRK08155 477 GLV-HQQQSlfygqrvfAATYPGKIN--------FMQIAAGFGLETcdlNNEADPQAALQEAIN-RPGPALIHVRI 542
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
6-519 |
1.50e-53 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 191.60 E-value: 1.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 6 SEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDqIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK07979 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGG-IDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDNL 164
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASgRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 165 PEQRVSDHYISSAS-SFQLTSPQIDDNR--LNTAAKLIRDSKKPLALVGLGAKKAG--SQVAAFLEQNHIPFISTLPAKG 239
Cdd:PRK07979 166 LNPANKLPYVWPESvSMRSYNPTTQGHKgqIKRALQTLVAAKKPVVYVGGGAINAAchQQLKELVEKLNLPVVSSLMGLG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 240 IIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFG------TNYPYTAYLPKpgrAKSIQINTSASAIGKRYPADVGLVA 313
Cdd:PRK07979 246 AFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGvrfddrTTNNLAKYCPN---ATVLHIDIDPTSISKTVTADIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 314 DIKDVIKQ---LNSSETTILHPDDgfLKACQENVANWNRWMTGKRELDSKPVAPEALFNDINETAPHNTIYSIDVGTATS 390
Cdd:PRK07979 323 DARQVLEQmleLLSQESAHQPLDE--IRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 391 WSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAF 470
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1586112881 471 IEYEQ--QAAGQlNYQIDLQDM-DYAKFADAAGGVGITAKTSEEFKNALNRA 519
Cdd:PRK07979 481 VKQWQdmIYSGR-HSQSYMQSLpDFVRLAEAYGHVGIQISHPDELESKLSEA 531
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
6-524 |
3.87e-52 |
|
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: 187.76 E-value: 3.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 6 SEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQdqIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:TIGR03457 5 SEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAG--IRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKHGVAVLTIPDNLP 165
Cdd:TIGR03457 83 IAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREMGPAQLNIPRDYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 166 EQRVsdhYISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLG-------------AKKAGSQVAAFLEQNhipfi 232
Cdd:TIGR03457 163 YGEI---DVEIPRPVRLDRGAGGATSLAQAARLLAEAKFPVIISGGGvvmgdaveeckalAERLGAPVVNSYLHN----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 233 STLPAkgiigdNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYPYTAYLPK------PGRAKSIQINTSASAIGKRYP 306
Cdd:TIGR03457 235 DSFPA------SHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLGPFGTLPQygidywPKNAKIIQVDANAKMIGLVKK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 307 ADVGLVADIKDVIKQLnsseTTILHPDDGFLK------ACQENVANWNR---------------WMTGKRELDSKPVAPE 365
Cdd:TIGR03457 309 VTVGICGDAKAAAAEI----LQRLAGKAGDANraerkaKIQAERSAWEQelsemtherdpfsldMIVEQRQEEGNWLHPR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 366 ALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVM 445
Cdd:TIGR03457 385 QVLRELEKAMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSM 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 446 QDFITAVKYKLPLINIVLNNsklafieyEQQAAGQLNyQIDLQD-----------MDYAKFADAAGGVGITAKTSEEFKN 514
Cdd:TIGR03457 465 NEIMTAVRHDIPVTAVVFRN--------RQWGAEKKN-QVDFYNnrfvgteleseLSFAGIADAMGAKGVVVDKPEDVGP 535
|
570
....*....|
gi 1586112881 515 ALNRAYRVQN 524
Cdd:TIGR03457 536 ALKKAIAAQA 545
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-524 |
6.70e-51 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 184.43 E-value: 6.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 1 MAQKASEQLVDVLIDWHVKHVYGLPG----DSIDTTVDAlrkqqdQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGG 76
Cdd:PRK07525 4 MKMTPSEAFVETLQAHGITHAFGIIGsafmDASDLFPPA------GIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 77 PGAIHILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKHGVA 156
Cdd:PRK07525 78 PGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESGPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 157 VLTIPDNLPEQRVSdhyISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFIST 234
Cdd:PRK07525 158 QINIPRDYFYGVID---VEIPQPVRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAieECKALAERLDAPVACG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 235 ------LPAkgiigdNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYPYTAYLPK------PGRAKSIQINTSASAIG 302
Cdd:PRK07525 235 ylhndaFPG------SHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPFGTLPQygidywPKDAKIIQVDINPDRIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 303 KRYPADVGLVADIKDVIKQLNS--SETTilhPDDGFLKACQENVAN----WNR---------------WMTGKRELDSKP 361
Cdd:PRK07525 309 LTKKVSVGICGDAKAVARELLArlAERL---AGDAGREERKALIAAeksaWEQelsswdhedddpgtdWNEEARARKPDY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 362 VAPEALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAF 441
Cdd:PRK07525 386 MHPRQALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 442 AMVMQDFITAVKYKLPLINIVLNNSklafieyeQQAAGQLNyQIDL-----------QDMDYAKFADAAGGVGITAKTSE 510
Cdd:PRK07525 466 GISMNEVMTAVRHNWPVTAVVFRNY--------QWGAEKKN-QVDFynnrfvgteldNNVSYAGIAEAMGAEGVVVDTQE 536
|
570
....*....|....
gi 1586112881 511 EFKNALNRAYRVQN 524
Cdd:PRK07525 537 ELGPALKRAIDAQN 550
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-542 |
2.44e-50 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 182.65 E-value: 2.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 6 SEQLVDVLIDWHVKHVYGLPGDSIDTTVDALrkQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK07710 19 AQMLIEALEKEGVEVIFGYPGGAVLPLYDAL--YDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDNL 164
Cdd:PRK07710 97 LADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTgRPGPVLIDIPKDM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 165 PE---QRVSDHYISSASSFQLTSP---QIddNRLNTAaklIRDSKKPLALVGLGA--KKAGSQVAAFLEQNHIPFISTLP 236
Cdd:PRK07710 177 VVeegEFCYDVQMDLPGYQPNYEPnllQI--RKLVQA---VSVAKKPVILAGAGVlhAKASKELTSYAEQQEIPVVHTLL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 237 AKGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP-----YTAYLPKpgRAKSIQINTSASAIGKRYPADVGL 311
Cdd:PRK07710 252 GLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDdrvtgNLAYFAK--EATVAHIDIDPAEIGKNVPTEIPI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 312 VADIKDVIKQLnssettiLHPDDGflkacQENVANW----NRWmtgKREL------DSKPVAPEALFNDINETAPHNTIY 381
Cdd:PRK07710 330 VADAKQALQVL-------LQQEGK-----KENHHEWlsllKNW---KEKYplsykrNSESIKPQKAIEMLYEITKGEAIV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 382 SIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINI 461
Cdd:PRK07710 395 TTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 462 VLNNSKLAFIEYEQQAAGQLNYQIDL--QDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRVQNmPVLINAYVSDDA-- 537
Cdd:PRK07710 475 ILNNEALGMVRQWQEEFYNQRYSHSLlsCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQE-PVVIDCRVLQSEkv 553
|
....*...
gi 1586112881 538 -PL--PGK 542
Cdd:PRK07710 554 mPMvaPGK 561
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
3-471 |
1.37e-49 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 180.70 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 3 QKASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQqDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHI 82
Cdd:PLN02470 13 RKGADILVEALEREGVDTVFAYPGGASMEIHQALTRS-NCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 83 LNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIP 161
Cdd:PLN02470 92 VTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSgRPGPVLVDIP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 162 DNLPEQRVSDHY---ISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFLEQNHIPFISTLPAK 238
Cdd:PLN02470 172 KDIQQQLAVPNWnqpMKLPGYLSRLPKPPEKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 239 GIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFGTNYP--YTAYLPK-PGRAKSIQINTSASAIGKRYPADVGLVADI 315
Cdd:PLN02470 252 GAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDdrVTGKLEAfASRASIVHIDIDPAEIGKNKQPHVSVCADV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 316 KDVIKQLNSsettILHPDdgflKACQENVANWNRWMTGKRE-------LDSKPVAPEALFNDINETAPHNTIYSIDVGTA 388
Cdd:PLN02470 332 KLALQGLNK----LLEER----KAKRPDFSAWRAELDEQKEkfplsypTFGDAIPPQYAIQVLDELTDGNAIISTGVGQH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 389 TSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKL 468
Cdd:PLN02470 404 QMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHL 483
|
...
gi 1586112881 469 AFI 471
Cdd:PLN02470 484 GMV 486
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
7-533 |
1.41e-49 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 180.71 E-value: 1.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 7 EQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQqDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNGL 86
Cdd:PRK06466 8 EMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQ-DKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 87 YDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAVLTIPDNL- 164
Cdd:PRK06466 87 ATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSgRPGPVVVDIPKDMt 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 165 -PEQRVSDHYISSAS--SFQLT----SPQIddnrlNTAAKLIRDSKKPLALVGLGA--KKAGSQVAAFLEQNHIPFISTL 235
Cdd:PRK06466 167 nPAEKFEYEYPKKVKlrSYSPAvrghSGQI-----RKAVEMLLAAKRPVIYSGGGVvlGNASALLTELAHLLNLPVTNTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 236 PAKGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDLLLMFG-------TNYPyTAYLPKpgrAKSIQINTSASAIGKRYPAD 308
Cdd:PRK06466 242 MGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGarfddrvTNGP-AKFCPN---AKIIHIDIDPASISKTIKAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 309 VGLVADIKDVIKQLnsseTTILHPDDGflKACQENVANW----NRW-----MTGKRELDSKPVAPEALFNDINETAPHNT 379
Cdd:PRK06466 318 IPIVGPVESVLTEM----LAILKEIGE--KPDKEALAAWwkqiDEWrgrhgLFPYDKGDGGIIKPQQVVETLYEVTNGDA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 380 IYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLI 459
Cdd:PRK06466 392 YVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVK 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586112881 460 NIVLNNSKLAFIEYEQQAAGQLNYQIDLQDM--DYAKFADAAGGVGITAKTSEEFKNALNRAYRVQNMPVLINAYV 533
Cdd:PRK06466 472 IINLNNGALGMVRQWQDMQYEGRHSHSYMESlpDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAMKDRLVFIDIYV 547
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
63-537 |
1.01e-47 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 175.33 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 63 KLTGKLGVCLSIGGPGAIHILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIV 142
Cdd:PRK06112 70 RVSGKVAVVTAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 143 DEAIRTAYE-KHGVAVLTIPDNL---PEQRVSDHYISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLG--AKKA 216
Cdd:PRK06112 150 DQAFTAATSgRPGPVVLLLPADLltaAAAAPAAPRSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGvhISGA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 217 GSQVAAFLEQNHIPFISTLPAKGIIGDNHPNSLGNVGKL-----GTKPAYEAMQNTDLLLMFG--TNYPYTA-YLPKPGR 288
Cdd:PRK06112 230 SAALAALQSLAGLPVATTNMGKGAVDETHPLSLGVVGSLmgprsPGRHLRDLVREADVVLLVGtrTNQNGTDsWSLYPEQ 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 289 AKSIQINTSASAIGKRYPAdVGLVADIKDVIKQLNSSET----TILHPDDGFLKACQEnvANWNRW---MTGKRELDSKP 361
Cdd:PRK06112 310 AQYIHIDVDGEEVGRNYEA-LRLVGDARLTLAALTDALRgrdlAARAGRRAALEPAIA--AGREAHredSAPVALSDASP 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 362 VAPEALFNDINETAPHNTIYSIDVGTATSWSARFLNV-SPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGA 440
Cdd:PRK06112 387 IRPERIMAELQAVLTGDTIVVADASYSSIWVANFLTArRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGG 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 441 FAMVMQDFITAVKYKLPLINIVLNNSKLAF-IEYEQQAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRA 519
Cdd:PRK06112 467 FAHVWAELETARRMGVPVTIVVLNNGILGFqKHAETVKFGTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAA 546
|
490
....*....|....*...
gi 1586112881 520 YRVQnMPVLINAYVSDDA 537
Cdd:PRK06112 547 MAAP-GPTLIEVITDPSA 563
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
384-531 |
1.05e-43 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 152.74 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 384 DVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVL 463
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586112881 464 NNSKLAFIEYEQQAAGQLNY----QIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINA 531
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYsgpsGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALE-HDGPALIDV 151
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
76-538 |
1.81e-39 |
|
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: 151.46 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 76 GPGAIHILNGLYDAKMDHVPVLALLG------QV----------DTQFlneEYFQEVntpqlFADVAVYNKLISATDNLA 139
Cdd:COG3961 76 GVGELSAINGIAGAYAERVPVVHIVGapgtraQRrgpllhhtlgDGDF---DHFLRM-----FEEVTVAQAVLTPENAAA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 140 EIvDEAIRTAYEKHGVAVLTIPDNLPEQRVSdhyiSSASSFQLTSPQIDDNRLNTA----AKLIRDSKKPLALVGLGAKK 215
Cdd:COG3961 148 EI-DRVLAAALREKRPVYIELPRDVADAPIE----PPEAPLPLPPPASDPAALAAAvaaaAERLAKAKRPVILAGVEVHR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 216 AG--SQVAAFLEQNHIPFISTLPAKGIIGDNHPNSLGN-VGKLGTKPAYEAMQNTDLLLMFGTNYP------YTAYLPkp 286
Cdd:COG3961 223 FGlqEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGVVFTdtntggFTAQLD-- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 287 gRAKSIQINTSASAIGKRYPADVGLvadiKDVIKQLNssettilhpddgflkacqENVANWNRWMTGKRELDSKPVAP-- 364
Cdd:COG3961 301 -PERTIDIQPDSVRVGGHIYPGVSL----ADFLEALA------------------ELLKKRSAPLPAPAPPPPPPPAApd 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 365 -----EALFNDINETAPHNTIYSIDVGTAtSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDG 439
Cdd:COG3961 358 apltqDRLWQRLQAFLDPGDIVVADTGTS-LFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 440 AFAMVMQDFITAVKYKLPLINIVLNNSKLA---FIEYEQQAagqlnYQiDLQDMDYAKFADAAGG---VGITAKTSEEFK 513
Cdd:COG3961 437 AFQLTAQELSTMLRYGLKPIIFVLNNDGYTierAIHGPDGP-----YN-DIANWDYAKLPEAFGGgnaLGFRVTTEGELE 510
|
490 500
....*....|....*....|....*.
gi 1586112881 514 NALNRAYRVQNMPVLINAYVS-DDAP 538
Cdd:COG3961 511 EALAAAEANTDRLTLIEVVLDkMDAP 536
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-529 |
2.04e-39 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 152.06 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 1 MAQ-KASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQdQIGFVQVRHEEVASLAAAAEAKLT-GKLGVCLSIGGPG 78
Cdd:PRK11269 1 MAKmRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHG-GIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 79 AIHILNGLYDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYE-KHGVAV 157
Cdd:PRK11269 80 GTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSgRPGPVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 158 LTIPDNLPEQRVsDHYISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFISTL 235
Cdd:PRK11269 160 IDLPFDVQVAEI-EFDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADAsdLLVEFAELTGVPVIPTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 236 PAKGIIGDNHPNSLGNVGkLGTKPAY--EAMQNTDLLLMFGTNYP---------YTAylpkpGRaKSIQINTSASAIGKR 304
Cdd:PRK11269 239 MGWGAIPDDHPLMAGMVG-LQTSHRYgnATLLASDFVLGIGNRWAnrhtgsvevYTK-----GR-KFVHVDIEPTQIGRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 305 YPADVGLVADIK-------DVIKQLNSSETtiLHPDDGFLKACQENvanwNRWMTGKRELDSKPVAPEALFNDINETAPH 377
Cdd:PRK11269 312 FGPDLGIVSDAKaalellvEVAREWKAAGR--LPDRSAWVADCQER----KRTLLRKTHFDNVPIKPQRVYEEMNKAFGR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 378 NTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLP 457
Cdd:PRK11269 386 DTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 458 LINIVLNNSKLAFIEyEQQAAGQLNYQIDLQ------------DMDYAKFADAAGGVGITAKTSEEFKNALNRA------ 519
Cdd:PRK11269 466 YIHVLVNNAYLGLIR-QAQRAFDMDYCVQLAfeninspelngyGVDHVKVAEGLGCKAIRVFKPEDIAPALEQAkalmae 544
|
570
....*....|
gi 1586112881 520 YRVqnmPVLI 529
Cdd:PRK11269 545 FRV---PVVV 551
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
7-529 |
2.66e-39 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 151.30 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 7 EQLVDVLIDWHVKHVYG------LPgdsidtTVDALrKQQDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAI 80
Cdd:PRK07064 7 ELIAAFLEQCGVKTAFGvisihnMP------ILDAI-GRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 81 HILNGLYDAKMDHVPVLALLGQVDTQFLNEE--YFQEV-NTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEK-HGVA 156
Cdd:PRK07064 80 NAAGALVEALTAGTPLLHITGQIETPYLDQDlgYIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTApTGPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 157 VLTIPDNLpeQRVSDHYISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFLEQNhIPFISTLP 236
Cdd:PRK07064 160 SVEIPIDI--QAAEIELPDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVDLG-FGVVTSTQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 237 AKGIIGDNHPNSLGNVGklGTKPAYEAMQNTDLLLMFGTNY------PYTAYLPKPgrakSIQINTSASAIGKRYPADVG 310
Cdd:PRK07064 237 GRGVVPEDHPASLGAFN--NSAAVEALYKTCDLLLVVGSRLrgnetlKYSLALPRP----LIRVDADAAADGRGYPNDLF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 311 LVADIKDVIKQLNSSETTILHPDDGFLKACQENVANWNRWMTgkreldsKPVAPEALFND-INETAPHNTIYSIDVGTAT 389
Cdd:PRK07064 311 VHGDAARVLARLADRLEGRLSVDPAFAADLRAAREAAVADLR-------KGLGPYAKLVDaLRAALPRDGNWVRDVTISN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 390 S-WSARFLNV-SPTQKfiLSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSK 467
Cdd:PRK07064 384 StWGNRLLPIfEPRAN--VHALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGG 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586112881 468 LAFIEYEQQAA-GQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRVQNmPVLI 529
Cdd:PRK07064 462 YGVIRNIQDAQyGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEG-PVLV 523
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
362-537 |
4.89e-39 |
|
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: 141.10 E-value: 4.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 362 VAPEALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAF 441
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 442 AMVMQDFITAVKYKLPLINIVLNNSKLAFIEYEQQAAGQLNYQIDLQDM--DYAKFADAAGGVGITAKTSEEFKNALNRA 519
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSnpDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170
....*....|....*...
gi 1586112881 520 YRVQNmPVLINAYVSDDA 537
Cdd:cd02015 161 LASDG-PVLLDVLVDPEE 177
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
192-322 |
5.34e-39 |
|
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: 139.62 E-value: 5.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 192 LNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQNHIPFISTLPAKGIIGDNHPNSLGNVGKLGTKPAYEAMQNTDL 269
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGAseELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586112881 270 LLMFGTNYP----YTAYLPKPGRAKSIQINTSASAIGKRYPADVGLVADIKDVIKQL 322
Cdd:pfam00205 81 VLAVGARFDdirtTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
366-533 |
1.18e-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: 139.70 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 366 ALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVM 445
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 446 QDFITAVKYKLPLINIVLNNSKLAFIEYEQQAAGQLNYQ-IDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAyRVQN 524
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSgTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEA-LAAG 159
|
....*....
gi 1586112881 525 MPVLINAYV 533
Cdd:cd00568 160 GPALIEVKT 168
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
4-529 |
1.64e-38 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 149.19 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 4 KASEQLVDVLIDWHVKHVYGLPGDS-IDTTVDAlrkqqdQIGFVQVRHEEVASLAAAAEAKLTG--KLGVCLSIGGPGAI 80
Cdd:PRK06154 21 KVAEAVAEILKEEGVELLFGFPVNElFDAAAAA------GIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 81 HILNGLYDAKMDHVPVLAL-------LGQVDTQFLNEEYFQEVNTPqlfadvavynkliSATDNLAEIVDEAIRTAYEK- 152
Cdd:PRK06154 95 NAFGGVAQAYGDSVPVLFLptgyprgSTDVAPNFESLRNYRHITKW-------------CEQVTLPDEVPELMRRAFTRl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 153 ----HGVAVLTIPDNLPEQRVSDHYISSASSfQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGS--QVAAFLEQ 226
Cdd:PRK06154 162 rngrPGPVVLELPVDVLAEELDELPLDHRPS-RRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQAtpELKELAEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 227 NHIPFISTLPAKGIIGDNHPNSLGNVGKlgTKPAYEA--MQNTDLLLMFGTNYPYTAY-LPKPGRAKSIQINTSASAIGK 303
Cdd:PRK06154 241 LEIPVMTTLNGKSAFPEDHPLALGSGGR--ARPATVAhfLREADVLFGIGCSLTRSYYgLPMPEGKTIIHSTLDDADLNK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 304 RYPADVGLVADIKDVIKQLNSSETTILHPDDGFLKACQENVA----NW-NRWMTgKRELDSKPVAPEALFNDINET-APH 377
Cdd:PRK06154 319 DYPIDHGLVGDAALVLKQMIEELRRRVGPDRGRAQQVAAEIEavraAWlAKWMP-KLTSDSTPINPYRVVWELQHAvDIK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 378 NTIYSIDVGTATSWSARFLNVSPTqkfilSSYLG-----TMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAV 452
Cdd:PRK06154 398 TVIITHDAGSPRDQLSPFYVASRP-----GSYLGwgkttQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586112881 453 KYKLPLINIVLNNSKLAfIEYEQQAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRV--QNMPVLI 529
Cdd:PRK06154 473 RERIPILTILLNNFSMG-GYDKVMPVSTTKYRATDISGDYAAIARALGGYGERVEDPEMLVPALLRALRKvkEGTPALL 550
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
7-529 |
1.91e-37 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 145.89 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 7 EQLVDVLIDWHVKHVYGLPGDSidtTVDALRKQQDQ-IGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNG 85
Cdd:PRK07524 6 EALVRLLEAYGVETVFGIPGVH---TVELYRGLAGSgIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 86 LYDAKMDHVPVLALLG--QVDTQFLNEEYFQEVNTPQ-LFADVAVYNKLISATDNLAEIVDEAIrtayekhgvAVLT--- 159
Cdd:PRK07524 83 MGQAYADSIPMLVISSvnRRASLGKGRGKLHELPDQRaMVAGVAAFSHTLMSAEDLPEVLARAF---------AVFDsar 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 160 -------IPDNLPEQRVSDhyISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAAFLEQNHIPFI 232
Cdd:PRK07524 154 prpvhieIPLDVLAAPADH--LLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 233 STLPAKGIIGDNHPNSLGNVGKLgtKPAYEAMQNTDLLLMFGTNYPYTAY-------LPKPGRAksIQINTSASAIGKRY 305
Cdd:PRK07524 232 LTINAKGLLPAGHPLLLGASQSL--PAVRALIAEADVVLAVGTELGETDYdvyfdggFPLPGEL--IRIDIDPDQLARNY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 306 PADVGLVADIKDVIKQL-NSSETTILHPDDGFLKAC---QENVANWNRWMTGKReldskpvapeALFNDINETAPHNTIy 381
Cdd:PRK07524 308 PPALALVGDARAALEALlARLPGQAAAADWGAARVAalrQALRAEWDPLTAAQV----------ALLDTILAALPDAIF- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 382 sidVG--TATSWSARFLNVSPTQK--FILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLP 457
Cdd:PRK07524 377 ---VGdsTQPVYAGNLYFDADAPRrwFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLP 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586112881 458 LINIVLNNSKLAFIEYEQQAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAyRVQNMPVLI 529
Cdd:PRK07524 454 LIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAA-FARPGPTLI 524
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
5-171 |
1.36e-34 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 128.51 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 5 ASEQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKQqDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILN 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKS-PGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 85 GLYDAKMDHVPVLALLGQVDTQFLNEEYFQ-EVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTA-YEKHGVAVLTIPD 162
Cdd:pfam02776 80 GLANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAAlSGRPGPVYLEIPL 159
|
....*....
gi 1586112881 163 NLPEQRVSD 171
Cdd:pfam02776 160 DVLLEEVDE 168
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
364-530 |
9.53e-34 |
|
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: 126.63 E-value: 9.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 364 PEALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAM 443
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 444 VMQDFITAVKYKLPLINIVLNNSKLAFIEYEQQAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQ 523
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALA-A 159
|
....*..
gi 1586112881 524 NMPVLIN 530
Cdd:cd02010 160 DGVHVID 166
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
364-534 |
2.95e-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: 122.26 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 364 PEALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAM 443
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 444 VMQDFITAVKYKLPLINIVLNNSKLAFIEYEQQ--AAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYR 521
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQlsYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|...
gi 1586112881 522 vQNMPVLINAYVS 534
Cdd:cd02004 161 -SGKPALINVIID 172
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
9-537 |
4.75e-31 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 127.41 E-value: 4.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 9 LVDVLIDWHVKHVYGLPGdsIDTTvDALRKQQDQ-IGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNGLY 87
Cdd:PRK09259 16 VIDALKLNGIDTIYGVVG--IPIT-DLARLAQAEgIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 88 DAKMDHVPVLALLGQ-----VDTQFLNEEYFQEVNTPQLFADVAVYnklISATDNLAEIVDEAIRTAYE-KHGVAVLTIP 161
Cdd:PRK09259 93 NATTNCFPMIMISGSsereiVDLQQGDYEELDQLNAAKPFCKAAFR---VNRAEDIGIGVARAIRTAVSgRPGGVYLDLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 162 DNLPEQrVSDHYISSASSFQLTSP---QI-DDNRLNTAAKLIRDSKKPLALVGLGA--KKAGSQVAAFLEQNHIPFISTL 235
Cdd:PRK09259 170 AKVLAQ-TMDADEALTSLVKVVDPapaQLpAPEAVDRALDLLKKAKRPLIILGKGAayAQADEQIREFVEKTGIPFLPMS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 236 PAKGIIGDNHPNSLGNVGKLgtkpayeAMQNTDLLLMFGTNYPYTAYLPKP----GRAKSIQINTSASAIGKRYPADVGL 311
Cdd:PRK09259 249 MAKGLLPDTHPQSAAAARSL-------ALANADVVLLVGARLNWLLSHGKGktwgADKKFIQIDIEPQEIDSNRPIAAPV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 312 VADIKDVIKQLNSS-ETTILHPDDGFLKACQENVANWNRWMTGKRELDSKPV----APEALFNDINEtapHNTIYSIDVG 386
Cdd:PRK09259 322 VGDIGSVMQALLAGlKQNTFKAPAEWLDALAERKEKNAAKMAEKLSTDTQPMnfynALGAIRDVLKE---NPDIYLVNEG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 387 TATSWSAR-FLNVSPTQKFILSSYLGTMGCALPGAIAAKINyPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNN 465
Cdd:PRK09259 399 ANTLDLARnIIDMYKPRHRLDCGTWGVMGIGMGYAIAAAVE-TGKPVVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNN 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586112881 466 SKL-AFIEYEQQAAGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINAyVSDDA 537
Cdd:PRK09259 478 GGIyRGDDVNLSGAGDPSPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIA-SGKPTLINV-VIDPA 548
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
7-161 |
7.33e-29 |
|
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: 112.24 E-value: 7.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 7 EQLVDVLIDWHVKHVYGLPGDSIDTTVDALRKqqDQIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNGL 86
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALAR--SGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586112881 87 YDAKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAY-EKHGVAVLTIP 161
Cdd:cd07035 79 ANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALsGRPGPVALDLP 154
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
18-530 |
6.87e-28 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 117.90 E-value: 6.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 18 VKHVYGLPGDSIDTTVDALRKQQdqIGFVQVRHEEVASLAAAAEAKLTGKLGVCLSIGGPGAIHILNGLYDAKMDHVPVL 97
Cdd:PRK05858 20 VDTMFTLSGGHLFPLYDGAREEG--IRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAAQFNQSPLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 98 ALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKH-GVAVLTIPdnlpeqrvSDHYISS 176
Cdd:PRK05858 98 VLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHrGPVFVDFP--------MDHAFSM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 177 ASSFQLTSPQI--------DDNRLNTAAKLIRDSKKPLALVG--LGAKKAGSQVAAFLEQNHIPFISTLPAKGIIGDNHP 246
Cdd:PRK05858 170 ADDDGRPGALTelpagptpDPDALARAAGLLAEAQRPVIMAGtdVWWGHAEAALLRLAEELGIPVLMNGMGRGVVPADHP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 247 nslgnvgKLGTKPAYEAMQNTDLLLMFGTNYPYT-AYLPKPGRAKSIQINTSASAIGKRYPADVGLVADIkdvikqlnss 325
Cdd:PRK05858 250 -------LAFSRARGKALGEADVVLVVGVPMDFRlGFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDL---------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 326 eTTILhpdDGFLKACQENVAnWNRWMTGKREL--------------DSKPVAPEALFNDINETAPHNTIYSIDVGTATSW 391
Cdd:PRK05858 313 -SAIL---SALAGAGGDRTD-HQGWIEELRTAetaarardaaeladDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 392 SARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFI 471
Cdd:PRK05858 388 AGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLE 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 472 EYEQQAAGQLNYQIDLQ-DMDYAKFADAAGGVGITAKTSEEFKNALNRAYrVQNMPVLIN 530
Cdd:PRK05858 468 KHPMEALYGYDVAADLRpGTRYDEVVRALGGHGELVTVPAELGPALERAF-ASGVPYLVN 526
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
364-533 |
1.21e-25 |
|
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: 103.83 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 364 PEALFNDINETAPHNTIYSIDvgtATSWSARFLNVSPTQKFilSSYLGT----MGCALPGAIAAKINYPDRPVISVNGDG 439
Cdd:cd02002 3 PEYLAAALAAALPEDAIIVDE---AVTNGLPLRDQLPLTRP--GSYFTLrgggLGWGLPAAVGAALANPDRKVVAIIGDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 440 AFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYEQQAAGQLN------YQIDLQD--MDYAKFADAAGGVGITAKTSEE 511
Cdd:cd02002 78 SFMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGpgenapDGLDLLDpgIDFAAIAKAFGVEAERVETPEE 157
|
170 180
....*....|....*....|..
gi 1586112881 512 FKNALNRAYRVQNmPVLINAYV 533
Cdd:cd02002 158 LDEALREALAEGG-PALIEVVV 178
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
65-522 |
1.72e-24 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 107.78 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 65 TGKLGVCLSIGGPGAIHILNGLYDAKMDHVPVLALLGQvdTQFLNE----------EYFQEV-NTPQLFADVAVYNKLIS 133
Cdd:PRK08327 73 TGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGR--SPYTEEgelgsrntriHWTQEMrDQGGLVREYVKWDYEIR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 134 ATDNLAEIVDEAIRTAY-EKHGVAVLTIPDNLPEQRVSDHYISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLALVG-L 211
Cdd:PRK08327 151 RGDQIGEVVARAIQIAMsEPKGPVYLTLPREVLAEEVPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITWrA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 212 GAKKAGSQVAAFLEQNH-IPFISTLPAKGIIGDNHPNSLGNVGKlgtkpayEAMQNTDLLLMFGTNYPYT-AYLPKPGRA 289
Cdd:PRK08327 231 GRTAEGFASLRRLAEELaIPVVEYAGEVVNYPSDHPLHLGPDPR-------ADLAEADLVLVVDSDVPWIpKKIRPDADA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 290 KSIQINT--SASAIGKR-YPADVGLVADIKDVIKQLNSSETTILHPDDGFLKACQENVA-NWNRWMTGKREL-----DSK 360
Cdd:PRK08327 304 RVIQIDVdpLKSRIPLWgFPCDLCIQADTSTALDQLEERLKSLASAERRRARRRRAAVReLRIRQEAAKRAEierlkDRG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 361 PVAPEALFNDINETAP-HNTIYSiDVGTaTSWSARFlnVSPTQKFILSSYlGTMGCALPGAIAAKINYPDRPVISVNGDG 439
Cdd:PRK08327 384 PITPAYLSYCLGEVADeYDAIVT-EYPF-VPRQARL--NKPGSYFGDGSA-GGLGWALGAALGAKLATPDRLVIATVGDG 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 440 AFA--------MVMQdfitavKYKLPLINIVLNN-----SKLAFIE-YEQQAAGQLNY--QIDLQ-DMDYAKFADAAGGV 502
Cdd:PRK08327 459 SFIfgvpeaahWVAE------RYGLPVLVVVFNNggwlaVKEAVLEvYPEGYAARKGTfpGTDFDpRPDFAKIAEAFGGY 532
|
490 500
....*....|....*....|
gi 1586112881 503 GITAKTSEEFKNALNRAYRV 522
Cdd:PRK08327 533 GERVEDPEELKGALRRALAA 552
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
361-524 |
7.01e-24 |
|
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: 99.51 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 361 PVAPEALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGA 440
Cdd:cd02013 3 PMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 441 FAMVMQDFITAVKYKLPLINIVLNNsklafieyeQQAAGQLNYQID----------LQDMDYAKFADAAGGVGITAKTSE 510
Cdd:cd02013 83 WGMSMMEIMTAVRHKLPVTAVVFRN---------RQWGAEKKNQVDfynnrfvgteLESESFAKIAEACGAKGITVDKPE 153
|
170
....*....|....
gi 1586112881 511 EFKNALNRAYRVQN 524
Cdd:cd02013 154 DVGPALQKAIAMMA 167
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
9-161 |
2.16e-22 |
|
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: 93.56 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 9 LVDVLIDWHVKHVYGLPGDSIDTTVDALRKQQDQIgFVQVRHEEVASLAAAAEAKLTGKlGVCLSIGGPGAIHILNGLYD 88
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRI-IDTVIHELGAAGAAAGYARAGGP-PVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586112881 89 AKMDHVPVLALLGQVDTQFLNEEYFQEVNTPQLFADVAVYNKLISATDNLAEIVDEAIRTAYEKHGVAVLTIP 161
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLP 153
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
385-538 |
5.10e-20 |
|
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: 87.97 E-value: 5.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 385 VGTATSWSARFLNVSPTQ-KFILSSYLGTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVL 463
Cdd:cd02005 23 AETGTSWFGALDLKLPKGtRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 464 NNSK---LAFIEYEQQAagqlnYQiDLQDMDYAK----FADAAGGVGITAKTSEEFKNALNRAYRVQNMPVLINAYVS-D 535
Cdd:cd02005 103 NNDGytiERAIHGPEAS-----YN-DIANWNYTKlpevFGGGGGGLSFRVKTEGELDEALKDALFNRDKLSLIEVILPkD 176
|
...
gi 1586112881 536 DAP 538
Cdd:cd02005 177 DAP 179
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
357-531 |
2.45e-17 |
|
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: 80.79 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 357 LDSKPVAPEALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPTQKFILSSYLGTMGCALPGAIAAKINYPDRPVISVN 436
Cdd:cd02006 3 FDDVPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 437 GDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEyEQQAAGQLNYQIDLQ------------DMDYAKFADAAGGVGI 504
Cdd:cd02006 83 GDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIR-QAQRAFDMDYQVNLAfeninsselggyGVDHVKVAEGLGCKAI 161
|
170 180 190
....*....|....*....|....*....|
gi 1586112881 505 TAKTSEEFKNALNRAYRV---QNMPVLINA 531
Cdd:cd02006 162 RVTKPEELAAAFEQAKKLmaeHRVPVVVEA 191
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
412-529 |
2.85e-16 |
|
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: 77.73 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 412 TMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFI--------------EYEQQA 477
Cdd:cd02003 49 CMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCInnlqestgsgsfgtEFRDRD 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1586112881 478 AGQLNYQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAyRVQNMPVLI 529
Cdd:cd02003 129 QESGQLDGALLPVDFAANARSLGARVEKVKTIEELKAALAKA-KASDRTTVI 179
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
262-533 |
4.46e-14 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 74.99 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 262 EAMQNTDLLLMFGTN-YPYTAYLPK---PGRAKSIQInTSASAIGKRYPADVGLVADIKDVIKQLNSSETTILHPDdgfL 337
Cdd:PRK07092 268 ALLDGHDLVLVIGAPvFTYHVEGPGphlPEGAELVQL-TDDPGEAAWAPMGDAIVGDIRLALRDLLALLPPSARPA---P 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 338 KAcqenvanwnRWMTGKRELDSKPVAPEALFNDINETAPHNTIYsidVGTATSWSA---RFLNVS-PTQKFILSSylGTM 413
Cdd:PRK07092 344 PA---------RPMPPPAPAPGEPLSVAFVLQTLAALRPADAIV---VEEAPSTRPamqEHLPMRrQGSFYTMAS--GGL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 414 GCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIeyeQQAAGQLNYQ----IDLQD 489
Cdd:PRK07092 410 GYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGAL---RWFAPVFGVRdvpgLDLPG 486
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1586112881 490 MDYAKFADAAGGVGITAKTSEEFKNALNRAYRvQNMPVLINAYV 533
Cdd:PRK07092 487 LDFVALARGYGCEAVRVSDAAELADALARALA-ADGPVLVEVEV 529
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
76-533 |
1.77e-11 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 66.79 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 76 GPGAIHILNGLYDAKMDHVPVLALLGQVDTqflneeYFQEVNTPqLFAD-------VAVYNKLISATDNLAEIVDEAIRT 148
Cdd:PRK07586 73 GPGLANGLANLHNARRARTPIVNIVGDHAT------YHRKYDAP-LTSDiealarpVSGWVRRSESAADVAADAAAAVAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 149 AYEKHG-VAVLTIPdnlpeqrvSDHYISSASSF-----QLTSPQIDDNRLNTAAKLIRDSKKPLALVGLGAKKAGSQVAA 222
Cdd:PRK07586 146 ARGAPGqVATLILP--------ADVAWSEGGPPappppAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 223 -----------FLEqnhipfisTLPAKGIIGDNHPNslgnVGKLG--TKPAYEAMQNTDLLLMFGTNYP--YTAYLPKPG 287
Cdd:PRK07586 218 ariaaatgarlLAE--------TFPARMERGAGRPA----VERLPyfAEQALAQLAGVRHLVLVGAKAPvaFFAYPGKPS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 288 RaksiqintsasaigkrypadvgLVADIKDVIkqlnssetTILHPDD----------GFLKACQEN--VANWNRWMTGKR 355
Cdd:PRK07586 286 R----------------------LVPEGCEVH--------TLAGPGEdaaaalealaDALGAKPAAppLAAPARPPLPTG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 356 ELDskpvaPEALFNDINETAPHNTIYSIDVGTATSWSARFLNVSPTQKFiLSSYLGTMGCALPGAIAAKINYPDRPVISV 435
Cdd:PRK07586 336 ALT-----PEAIAQVIAALLPENAIVVDESITSGRGFFPATAGAAPHDW-LTLTGGAIGQGLPLATGAAVACPDRKVLAL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 436 NGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYEQQAAGQLNY------QIDLQD--MDYAKFADAAGGVGITAK 507
Cdd:PRK07586 410 QGDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGELARVGAGNPgpraldMLDLDDpdLDWVALAEGMGVPARRVT 489
|
490 500
....*....|....*....|....*.
gi 1586112881 508 TSEEFKNALNRAYRVQNmPVLINAYV 533
Cdd:PRK07586 490 TAEEFADALAAALAEPG-PHLIEAVV 514
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
411-533 |
1.91e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 63.35 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 411 GTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAFIEYEQQAAG--------QLN 482
Cdd:PRK12474 389 GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGELQRVGaqgagrnaLSM 468
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1586112881 483 YQIDLQDMDYAKFADAAGGVGITAKTSEEFKNALNRAYrVQNMPVLINAYV 533
Cdd:PRK12474 469 LDLHNPELNWMKIAEGLGVEASRATTAEEFSAQYAAAM-AQRGPRLIEAMI 518
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
411-538 |
4.89e-07 |
|
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP).
Pssm-ID: 274508 [Multi-domain] Cd Length: 361 Bit Score: 51.97 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 411 GTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLP-LINIVLNNsklafiEYEQQAAGQLNYQidlQD 489
Cdd:TIGR03297 221 GSMGHASQIALGLALARPDQRVVCLDGDGAALMHMGGLATIGTQGPAnLIHVLFNN------GAHDSVGGQPTVS---QH 291
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1586112881 490 MDYAKFADAAG-GVGITAKTSEEFKNALNRAYRVQNmPVLINAYVSDDAP 538
Cdd:TIGR03297 292 LDFAQIAKACGyAKVYEVSTLEELETALTAASSANG-PRLIEVKVRPGSR 340
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
411-465 |
1.80e-06 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 48.46 E-value: 1.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586112881 411 GTMGCALPGAIAAKINYPDRPVISVNGDGAFAMVMQDFITAVKYKLP-LINIVLNN 465
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPAnLIHIVLNN 103
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
66-519 |
1.03e-04 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 45.08 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 66 GKLGVCLSIGGpgaIHILNGLYDAKMDHVPVLALLGQVDTQ------FLNE-----EYFQEVntpQLFADVAVYNKLISA 134
Cdd:PLN02573 80 GACVVTFTVGG---LSVLNAIAGAYSENLPVICIVGGPNSNdygtnrILHHtiglpDFSQEL---RCFQTVTCYQAVINN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 135 TDNLAEIVDEAIRTAYEKHGVAVLTIPDNL---PEQRVSDHYISSASSFQLTSPQIDDNRLNTAAKLIRDSKKPLaLVG- 210
Cdd:PLN02573 154 LEDAHELIDTAISTALKESKPVYISVSCNLaaiPHPTFSREPVPFFLTPRLSNKMSLEAAVEAAAEFLNKAVKPV-LVGg 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 211 --LGAKKAGSQVAAFLEQNHIPFISTLPAKGIIGDNHPNSLGNV-GKLGTKPAYEAMQNTDLLLMFG---TNYPYTAY-- 282
Cdd:PLN02573 233 pkLRVAKACKAFVELADASGYPVAVMPSAKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGpifNDYSSVGYsl 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 283 LPKPgrAKSIQINTSASAIGKRyPAdVGLVAdIKDVIKQLNSSettilhpddgfLKACQENVANWNRWMTGKRE-LDSKP 361
Cdd:PLN02573 313 LLKK--EKAIIVQPDRVTIGNG-PA-FGCVL-MKDFLEALAKR-----------VKKNTTAYENYKRIFVPEGEpLKSEP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 362 VAP---EALFNDINETAPHNTiySIDVGTATSWsarfLNvspTQKFILSSylgtmGCALP-----GAI----AAKINY-- 427
Cdd:PLN02573 377 GEPlrvNVLFKHIQKMLSGDT--AVIAETGDSW----FN---CQKLKLPE-----GCGYEfqmqyGSIgwsvGATLGYaq 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 428 --PDRPVISVNGDGAFAMVMQDFITAVKYKLPLINIVLNNSKLAfIEYEQQaAGQLNYqidLQDMDYAKFADA-AGGVG- 503
Cdd:PLN02573 443 aaPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGYT-IEVEIH-DGPYNV---IKNWNYTGLVDAiHNGEGk 517
|
490
....*....|....*....
gi 1586112881 504 -ITAK--TSEEFKNALNRA 519
Cdd:PLN02573 518 cWTAKvrTEEELIEAIATA 536
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
410-519 |
1.82e-03 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 39.39 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586112881 410 LGTMGCALPGAIAAKINYPdRPVISVNGDGAFAMVMQDFITAVKYK-LPLINIVLNNSKLAfieyeqQAAGQLNYQIdlq 488
Cdd:cd02001 41 LGSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNRAYG------STGGQPTPSS--- 110
|
90 100 110
....*....|....*....|....*....|.
gi 1586112881 489 DMDYAKFADAAGGVGITAKTSEEFKNALNRA 519
Cdd:cd02001 111 NVNLEAWAAACGYLVLSAPLLGGLGSEFAGL 141
|
|
|