|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-578 |
0e+00 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 1120.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGL 80
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 81 IHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVI 160
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 161 CPNDLLTEKIKDTTNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLVGVGAKQAKDELRAFIEAAKIPVVHTLPAKT 240
Cdd:PRK08611 161 IPDDLPAQKIKDTTNKTVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPAKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 241 ILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPYVDYLPKKnIKAIQIDTNPKNIGHRFNINVGIVGDSKIALH 320
Cdd:PRK08611 241 IIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYVDYLPKK-AKAIQIDTDPANIGKRYPVNVGLVGDAKKALH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 321 QLTENIKHVAERPFLNKTLERKAVWDKWMEQDKNNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNN 400
Cdd:PRK08611 320 QLTENIKHVEDRRFLEACQENMAKWWKWMEEDENNASTPIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNLGTNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 401 KFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAGELE 480
Cdd:PRK08611 400 KFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 481 YAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLPGKIVNEEAFGYGKWAFRSITED 560
Cdd:PRK08611 480 YAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAPLPGKIVNDEALGYSKWAIKSLFED 559
|
570
....*....|....*...
gi 446985388 561 KHldLDQIPPISVAAKRF 578
Cdd:PRK08611 560 KK--LDQMPPLKKALKRF 575
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
2-544 |
0e+00 |
|
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: 553.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 2 AKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLI 81
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRR-QSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 82 HLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAY-EQKGVAVVI 160
Cdd:COG0028 80 NLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATsGRPGPVVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 161 CPNDLLTEKIKDTTNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTLPA 238
Cdd:COG0028 160 IPKDVQAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGArrAGAAEELRALAERLGAPVVTTLMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 239 KTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPYVD------YLPKKNIkaIQIDTNPKNIGHRFNINVGIV 312
Cdd:COG0028 240 KGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVtgnwdeFAPDAKI--IHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 313 GDSKIALHQLTENIKhvAERPFLNKTLERKAVWDKWMEQDKNNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTR 392
Cdd:COG0028 318 GDAKAVLAALLEALE--PRADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAAR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 393 YLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYE 472
Cdd:COG0028 396 YLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQW 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446985388 473 QQAAGELEY-AVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPlPGKIVNE 544
Cdd:COG0028 476 QELFYGGRYsGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENP-PGATLDE 547
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
8-555 |
3.81e-156 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 458.52 E-value: 3.81e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLRtvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGM 87
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIR--KSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 88 YDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVICPNDLL- 166
Cdd:PRK06457 84 YDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINLPVDILr 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 167 -TEKIKDTTNKPVDtsrptvvSPKYK-DIKKAVKLINKSKKPVMLVGVGAKQAKDELRAFIEAAKIPVVHTLPAKTILPD 244
Cdd:PRK06457 164 kSSEYKGSKNTEVG-------KVKYSiDFSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKGILPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 245 DHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPYVDYLPkKNIKAIQIDTNPKNIGHRFNINVGIVGDskiALHQLTE 324
Cdd:PRK06457 237 LDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLN-KSAKVIQVDIDNSNIGKRLDVDLSYPIP---VAEFLNI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 325 NIKHVAERpFLNKTLERKAVWDKWMEQDKNNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNKFII 404
Cdd:PRK06457 313 DIEEKSDK-FYEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 405 SSWLGTMGCGLPGAMASKIAYPN-RQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAGELEYAV 483
Cdd:PRK06457 392 SAWLGSMGIGVPGSVGASFAVENkRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMGYPEWGV 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446985388 484 DFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLPGKIVNEEAFGYGKWAFR 555
Cdd:PRK06457 472 DLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMPPKLTFKQAGEYVLSIFR 543
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
6-542 |
1.46e-151 |
|
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: 447.75 E-value: 1.46e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 6 ANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLN 85
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 86 GMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVICPNDL 165
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHNGVAVVTIPVDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 166 LTEKIKDT--TNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLVGVGAKQAKDELRAFIEAAKIPVVHTLPAKTILP 243
Cdd:TIGR02720 161 GWQEIPDNdyYASSVSYQTPLLPAPDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 244 DDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPY--VDYLPKKNIKAIQIDTNPKNIGHRFNINVGIVGDSKIALHQ 321
Cdd:TIGR02720 241 DRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFaeVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADAKKALAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 322 LTENIKHVAERPFLNKTLERKAVWDKWMEQDKNNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNK 401
Cdd:TIGR02720 321 ILAQVEPRESTPWWQANVANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 402 FIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAGELEY 481
Cdd:TIGR02720 401 WITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQPLI 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446985388 482 AVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEA--LAQDVPTIVDVYVDpNAAPLPGKIV 542
Cdd:TIGR02720 481 GVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAkaIKQGKPVLIDAKIT-GDRPLPVEKL 542
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
10-546 |
1.76e-141 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 422.40 E-value: 1.76e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 10 LVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGMYD 89
Cdd:PRK08273 9 ILERLREWGVRRVFGYPGDGINGLLGALGRADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 90 AKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVA-VFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVICPNDLLTE 168
Cdd:PRK08273 89 AKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAgAFVQMVTVPEQLRHLVDRAVRTALAERTVTAVILPNDVQEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 169 KIKD------TTNKPVDTSRPTVVsPKYKDIKKAVKLINKSKKPVMLVGVGAKQAKDELRAFIEAAKIPVVHTLPAKTIL 242
Cdd:PRK08273 169 EYEPpphahgTVHSGVGYTRPRVV-PYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGVAKALLGKAAL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 243 PDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPYVDYLPKK-NIKAIQIDTNPKNIGHRFNINVGIVGDSKIALHQ 321
Cdd:PRK08273 248 PDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFPYSEFLPKEgQARGVQIDIDGRMLGLRYPMEVNLVGDAAETLRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 322 LTENIKHVAERPFLNKTLERKAVWDKWMEQDKNNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNK 401
Cdd:PRK08273 328 LLPLLERKKDRSWRERIEKWVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADSGSCANWYARDLRMRRGMM 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 402 FIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMV-MQDFATAVQY-----DLPLTVFVLNNKQLAFIKYEQQA 475
Cdd:PRK08273 408 ASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKYwrqwsDPRLIVLVLNNRDLNQVTWEQRV 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446985388 476 ---AGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLPGKIVNEEA 546
Cdd:PRK08273 488 megDPKFEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDPNVPPLPPHITLEQA 561
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
2-557 |
9.75e-137 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 409.38 E-value: 9.75e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 2 AKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLI 81
Cdd:PRK09124 1 MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRR-MGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 82 HLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVIC 161
Cdd:PRK09124 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 162 PNDLLTEKIKDTTNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLVGVGAKQAKDELRAFIEAAKIPVVHTLPAKTI 241
Cdd:PRK09124 160 PGDVALKPAPERATPHWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRGKEH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 242 LPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPYVDYLPKKnIKAIQIDTNPKNIGHRFNINVGIVGDSKIALHQ 321
Cdd:PRK09124 240 VEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQFYPTD-AKIIQIDINPGSLGRRSPVDLGLVGDVKATLAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 322 LTENIKHVAERPFLNKTLERKAVWDKWMEQ--DKNNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVN 399
Cdd:PRK09124 319 LLPLLEEKTDRKFLDKALEHYRKARKGLDDlaVPSDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 400 NKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAGEL 479
Cdd:PRK09124 399 RRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMKAGGYL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446985388 480 EYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLPGKIVNEEAFGYGKWAFRSI 557
Cdd:PRK09124 479 TDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMPPQIKLEQAKGFSLYMLRAI 556
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-555 |
1.73e-128 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 388.58 E-value: 1.73e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKAnEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDqFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGL 80
Cdd:PRK06546 1 MAKTVA-EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGG-IEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 81 IHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVI 160
Cdd:PRK06546 79 LHLINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGGGVSVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 161 CPNDLLTEKIKDTTNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLVGVGAKQAKDELRAFIEAAKIPVVHTLPAKT 240
Cdd:PRK06546 159 LPGDIADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 241 ILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPYVDYLPKKNIkaIQIDTNPKNIGHRFNINVGIVGDSKIALH 320
Cdd:PRK06546 239 WIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFPYDQFLPDVRT--AQVDIDPEHLGRRTRVDLAVHGDVAETIR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 321 QLTENIKHVAERPFLNKTLERKavwDKWMEQ------DKNNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTRYL 394
Cdd:PRK06546 317 ALLPLVKEKTDRRFLDRMLKKH---ARKLEKvvgaytRKVEKHTPIHPEYVASILDELAADDAVFTVDTGMCNVWAARYI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 395 NLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQ 474
Cdd:PRK06546 394 TPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEML 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 475 AAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLPGKIVNEEAFGYGKWAF 554
Cdd:PRK06546 474 VDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTDPNALSIPPTITGEQVKGFALAAS 553
|
.
gi 446985388 555 R 555
Cdd:PRK06546 554 K 554
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
4-538 |
1.24e-118 |
|
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: 362.50 E-value: 1.24e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 4 IKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVrDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHL 83
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYND-SGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 84 LNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVVICP 162
Cdd:TIGR00118 80 VTGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRpGPVLVDLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 163 NDLLTEKIKDttNKPVDTS----RPTVVsPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTL 236
Cdd:TIGR00118 160 KDVTTAEIEY--PYPEKVNlpgyRPTVK-GHPLQIKKAAELINLAKKPVILVGGGViiAGASEELKELAERIQIPVTTTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 237 PAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYP------YVDYLPkkNIKAIQIDTNPKNIGHRFNINVG 310
Cdd:TIGR00118 237 MGLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDdrvtgnLAKFAP--NAKIIHIDIDPAEIGKNVRVDIP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 311 IVGDSKIALHQLTENIKHVAER---PFLNKTLERKAVWDKWMEQDknnnSKPLRPERLMASINQFIKDDAVISADVGTAT 387
Cdd:TIGR00118 315 IVGDARNVLEELLKKLFELKERkesAWLEQINKWKKEYPLKMDYT----EEGIKPQQVIEELSRVTKDEAIVTTDVGQHQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 388 VWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLA 467
Cdd:TIGR00118 391 MWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLG 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446985388 468 FIKYEQQAAGELEYAVDF--SDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLP 538
Cdd:TIGR00118 471 MVRQWQELFYEERYSHTHmgSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLP 543
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
5-531 |
2.03e-109 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 338.34 E-value: 2.03e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 5 KANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRdqFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLL 84
Cdd:PRK08322 2 KAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSS--IKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 85 NGMYDAKMDNVPQLILSGQ--TNSTALGTkaFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVIC- 161
Cdd:PRK08322 80 TGVAYAQLGGMPMVAITGQkpIKRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLEl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 162 PNDLLTEkikDTTNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTLPAK 239
Cdd:PRK08322 158 PEDIAAE---ETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGAnrKTASKALTEFVDKTGIPFFTTQMGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 240 TILPDDHPYSIGNLGkigtktsyqTMQD---------ADLLIMVGtnYPYVDYLPKK-----NIKAIQIDTNPKNIGHRF 305
Cdd:PRK08322 235 GVIPETHPLSLGTAG---------LSQGdyvhcaiehADLIINVG--HDVIEKPPFFmnpngDKKVIHINFLPAEVDPVY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 306 NINVGIVGDSKIALHQLTENIKHVAERPFlNKTLERKAVWDKWMEQDKNNNSKPLRPERLMASINQFIKDDAVISADVGT 385
Cdd:PRK08322 304 FPQVEVVGDIANSLWQLKERLADQPHWDF-PRFLKIREAIEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 386 ATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQ 465
Cdd:PRK08322 383 YKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNA 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446985388 466 LAFIKYEQQAAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVD 531
Cdd:PRK08322 463 YGMIRWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVD 528
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-544 |
5.67e-106 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 329.81 E-value: 5.67e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLrtVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGL 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDEL--YDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 81 IHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKgvavvi 160
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGR------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 161 cPNDLLTEKIKDTTNKPVDTSRPTVVS-----PKYK----DIKKAVKLINKSKKPVMLVGVG--AKQAKDELRAFIEAAK 229
Cdd:PRK06048 157 -PGPVLIDLPKDVTTAEIDFDYPDKVElrgykPTYKgnpqQIKRAAELIMKAERPIIYAGGGviSSNASEELVELAETIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 230 IPVVHTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPyvDYLPKK------NIKAIQIDTNPKNIGH 303
Cdd:PRK06048 236 APVTTTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFD--DRVTGKlasfapNAKIIHIDIDPAEISK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 304 RFNINVGIVGDSKIALHQLTENIKHVAERPFLNKTLErkavWDKWMEQDKNNNSKPLRPERLMASINQFIKDdAVISADV 383
Cdd:PRK06048 314 NVKVDVPIVGDAKQVLKSLIKYVQYCDRKEWLDKINQ----WKKEYPLKYKEREDVIKPQYVIEQIYELCPD-AIIVTEV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 384 GTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNN 463
Cdd:PRK06048 389 GQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNN 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 464 KQLAFIKYEQQAAGELEYAVDF--SDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVD--PNAAPL-- 537
Cdd:PRK06048 469 GYLGMVRQWQELFYDKRYSHTCikGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVEceENVSPMvp 548
|
....*..
gi 446985388 538 PGKIVNE 544
Cdd:PRK06048 549 AGAAINE 555
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
4-543 |
5.48e-94 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 299.36 E-value: 5.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 4 IKANEALVKALQAWDIDHLYGIPGDSI----DAVVDSlrtvrdQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPG 79
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALlpfyDALYDS------DLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 80 LIHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVV 159
Cdd:PRK06276 75 ATNLVTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 160 I-CPNDLLTEKI---KDTTNKPVDTS--RPTVVSPKyKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIP 231
Cdd:PRK06276 155 IdLPKDVQEGELdleKYPIPAKIDLPgyKPTTFGHP-LQIKKAAELIAEAERPVILAGGGViiSGASEELIELSELVKIP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 232 VVHTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYP------YVDYLPkkNIKAIQIDTNPKNIGHRF 305
Cdd:PRK06276 234 VCTTLMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSdrttgdISSFAP--NAKIIHIDIDPAEIGKNV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 306 NINVGIVGDSKIALHQLtenIKHVaerpfLNKTLERKAVWDKWMEQDKNN-------NSKPLRPERLMASINQFIKD--- 375
Cdd:PRK06276 312 RVDVPIVGDAKNVLRDL---LAEL-----MKKEIKNKSEWLERVKKLKKEsiprmdfDDKPIKPQRVIKELMEVLREidp 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 376 --DAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYD 453
Cdd:PRK06276 384 skNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 454 LPLTVFVLNNKQLAFIkYEQQAA--GELEYAVDFSDM-DHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYV 530
Cdd:PRK06276 464 IPVVICIFDNRTLGMV-YQWQNLyyGKRQSEVHLGETpDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIII 542
|
570
....*....|....*..
gi 446985388 531 DPNAA----PLPGKIVN 543
Cdd:PRK06276 543 DPAEAlpmvPPGGNLTN 559
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
359-536 |
7.30e-93 |
|
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: 282.50 E-value: 7.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 359 PLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGA 438
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 439 FQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEAL 518
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEAL 160
|
170
....*....|....*...
gi 446985388 519 AQDVPTIVDVYVDPNAAP 536
Cdd:cd02014 161 AADGPVVIDVVTDPNEPP 178
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
9-540 |
5.30e-91 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 291.60 E-value: 5.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 9 ALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDQ--FKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNG 86
Cdd:CHL00099 15 ALIDSLVRHGVKHIFGYPGGAILPIYDELYAWEKKglIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 87 MYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTA-YEQKGVAVVICPNDL 165
Cdd:CHL00099 95 IATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAkHGRPGPVLIDIPKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 166 LTEKIKDTTNKPVDTS------RPTVvSPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTLP 237
Cdd:CHL00099 175 GLEKFDYYPPEPGNTIikilgcRPIY-KPTIKRIEQAAKLILQSSQPLLYVGGGAiiSDAHQEITELAELYKIPVTTTLM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 238 AKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPyvDYLPKK------NIKAIQIDTNPKNIGHRFNINVGI 311
Cdd:CHL00099 254 GKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFD--DRVTGKldefacNAQVIHIDIDPAEIGKNRIPQVAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 312 VGDSKIALHQLTENIKHVAERPFLNKTLERKAVWDKWMEQ-----DKNNNSkpLRPERLMASINQfIKDDAVISADVGTA 386
Cdd:CHL00099 332 VGDVKKVLQELLELLKNSPNLLESEQTQAWRERINRWRKEyplliPKPSTS--LSPQEVINEISQ-LAPDAYFTTDVGQH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 387 TVWSTRYLNLGVNnKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQL 466
Cdd:CHL00099 409 QMWAAQFLKCKPR-KWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQ 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 467 AFIKYEQQAAGELEYAvdFSDM-----DHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYV--DPNAAPL-- 537
Cdd:CHL00099 488 GMVRQWQQAFYGERYS--HSNMeegapDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVieDENCYPMva 565
|
...
gi 446985388 538 PGK 540
Cdd:CHL00099 566 PGK 568
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
8-549 |
2.05e-90 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 290.80 E-value: 2.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLRTV--RDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLN 85
Cdd:PRK07418 23 YALMDSLKRHGVKHIFGYPGGAILPIYDELYKAeaEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNLVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 86 GMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVI-CPND 164
Cdd:PRK07418 103 GIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIdIPKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 165 LLTEKIKDTTNKPVDTS----RPTvVSPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTLPA 238
Cdd:PRK07418 183 VGQEEFDYVPVEPGSVKppgyRPT-VKGNPRQINAALKLIEEAERPLLYVGGGAisAGAHAELKELAERFQIPVTTTLMG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 239 KTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPyvDYLPKK------NIKAIQIDTNPKNIGHRFNINVGIV 312
Cdd:PRK07418 262 KGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFD--DRVTGKldefasRAKVIHIDIDPAEVGKNRRPDVPIV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 313 GDSKIALHQLTENIKhvaERPFLNKT---LERKAVWdkwmeqdKNN-------NSKPLRPERLMASINQFIKdDAVISAD 382
Cdd:PRK07418 340 GDVRKVLVKLLERSL---EPTTPPRTqawLERINRW-------KQDyplvvppYEGEIYPQEVLLAVRDLAP-DAYYTTD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 383 VGTATVWSTRYLNLGvNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLN 462
Cdd:PRK07418 409 VGQHQMWAAQFLRNG-PRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIIN 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 463 NKQLAFIKYEQQAAGELEYAVdfSDM-----DHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYV--DPNAA 535
Cdd:PRK07418 488 NGWQGMVRQWQESFYGERYSA--SNMepgmpDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVrrDENCY 565
|
570
....*....|....*.
gi 446985388 536 PL--PGKiVNEEAFGY 549
Cdd:PRK07418 566 PMvpPGK-SNAQMVGL 580
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
10-544 |
2.68e-89 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 286.66 E-value: 2.68e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 10 LVKALQAWDIDHLYGIPGDSIDAVVDSLRtvrdQFKFYHV--RHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGM 87
Cdd:PRK07710 22 LIEALEKEGVEVIFGYPGGAVLPLYDALY----DCGIPHIltRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 88 YDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVI-CPNDLL 166
Cdd:PRK07710 98 ADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIdIPKDMV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 167 TEKIKDTTNKPVDTS--RPTVvSPKYKDIKKAVKLINKSKKPVMLVGVGAKQAK--DELRAFIEAAKIPVVHTLPAKTIL 242
Cdd:PRK07710 178 VEEGEFCYDVQMDLPgyQPNY-EPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKasKELTSYAEQQEIPVVHTLLGLGGF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 243 PDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYP-----YVDYLPKKNIKAiQIDTNPKNIGHRFNINVGIVGDSKI 317
Cdd:PRK07710 257 PADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDdrvtgNLAYFAKEATVA-HIDIDPAEIGKNVPTEIPIVADAKQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 318 ALHQL-TENIKHVAERPFLNKTLERKAVWDKWMEqdknNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNL 396
Cdd:PRK07710 336 ALQVLlQQEGKKENHHEWLSLLKNWKEKYPLSYK----RNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 397 GVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAA 476
Cdd:PRK07710 412 KTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQEEF 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446985388 477 GELEYAVDF--SDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYV--DPNAAPL--PGKIVNE 544
Cdd:PRK07710 492 YNQRYSHSLlsCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVlqSEKVMPMvaPGKGLHE 565
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
3-538 |
3.84e-86 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 278.14 E-value: 3.84e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 3 KIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIH 82
Cdd:PRK08527 2 KLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYK-QNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 83 LLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYE-QKGVAVVIC 161
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSgRPGPVHIDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 162 PNDLLTEKIKDTTNKPVD--TSRPTVVSPKyKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTLP 237
Cdd:PRK08527 161 PKDVTATLGEFEYPKEISlkTYKPTYKGNS-RQIKKAAEAIKEAKKPLFYLGGGAilSNASEEIRELVKKTGIPAVETLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 238 AKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPyvDYLP------KKNIKAIQIDTNPKNIGHRFNINVGI 311
Cdd:PRK08527 240 ARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFD--DRVTgklsefAKHAKIIHVDIDPSSISKIVNADYPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 312 VGDSKIALHQLTENIKHVAERPFLN--KTLERkavWDKWMEQDKNNNSKPLRPERLMASINQFIKDDAVISADVGTATVW 389
Cdd:PRK08527 318 VGDLKNVLKEMLEELKEENPTTYKEwrEILKR---YNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 390 STRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFI 469
Cdd:PRK08527 395 VAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMV 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446985388 470 K------YEQQ-AAGELEYAVDFsdmdhAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLP 538
Cdd:PRK08527 475 RqwqtffYEERySETDLSTQPDF-----VKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLP 545
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
8-544 |
4.92e-82 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 267.60 E-value: 4.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLrtVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGM 87
Cdd:PRK06725 19 GHVIQCLKKLGVTTVFGYPGGAILPVYDAL--YESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 88 YDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVI-CPNDLL 166
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIdIPKDVQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 167 TEKIKDTTNKPVDTS--RPTVVsPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTLPAKTIL 242
Cdd:PRK06725 177 NEKVTSFYNEVVEIPgyKPEPR-PDSMKLREVAKAISKAKRPLLYIGGGVihSGGSEELIEFARENRIPVVSTLMGLGAY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 243 PDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPyvDYLPKK------NIKAIQIDTNPKNIGHRFNINVGIVGDSK 316
Cdd:PRK06725 256 PPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFD--DRVTGKlelfspHSKKVHIDIDPSEFHKNVAVEYPVVGDVK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 317 IALHQLTENIKHVAERPFLNKTLERKAVWDKWMEQDKNNnskpLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNL 396
Cdd:PRK06725 334 KALHMLLHMSIHTQTDEWLQKVKTWKEEYPLSYKQKESE----LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 397 GVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAA 476
Cdd:PRK06725 410 KNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEMF 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446985388 477 GELEYA-VDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVD--PNAAPL--PGKIVNE 544
Cdd:PRK06725 490 YENRLSeSKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEegENVFPMvpPNKGNNE 562
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
8-534 |
7.72e-82 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 268.39 E-value: 7.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLRtvrDQFKFYH--VRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLN 85
Cdd:PRK07789 35 QAVVRSLEELGVDVVFGIPGGAILPVYDPLF---DSTKVRHvlVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 86 GMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVVICPND 164
Cdd:PRK07789 112 PIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRpGPVLVDIPKD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 165 LLTEKIKDTTNKPVDTS--RPtVVSPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTLPAKT 240
Cdd:PRK07789 192 ALQAQTTFSWPPRMDLPgyRP-VTKPHGKQIREAAKLIAAARRPVLYVGGGVirAEASAELRELAELTGIPVVTTLMARG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 241 ILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPyvDYLPKK------NIKAIQIDTNPKNIGHRFNINVGIVGD 314
Cdd:PRK07789 271 AFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFD--DRVTGKldsfapDAKVIHADIDPAEIGKNRHADVPIVGD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 315 SKIALHQLTENIKHVAERPFLNKTLERKAVWDKWMEQDKNNNSKP----LRPERLMASINQFIKDDAVISADVGTATVWS 390
Cdd:PRK07789 349 VKEVIAELIAALRAEHAAGGKPDLTAWWAYLDGWRETYPLGYDEPsdgsLAPQYVIERLGEIAGPDAIYVAGVGQHQMWA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 391 TRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIK 470
Cdd:PRK07789 429 AQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLGMVR 508
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446985388 471 ------YEQQ------AAGElEYAVDFsdmdhAKFAEAAGGKGYTIKSASEVDAIVEEALA-QDVPTIVDVYVDPNA 534
Cdd:PRK07789 509 qwqtlfYEERysntdlHTHS-HRIPDF-----VKLAEAYGCVGLRCEREEDVDAVIEKARAiNDRPVVIDFVVGKDA 579
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-531 |
1.16e-80 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 263.99 E-value: 1.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDqFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGL 80
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSG-IEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 81 IHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVV 159
Cdd:PRK08979 80 TNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRpGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 160 ICPNDLLTEKIKDTTNKPVDTS----RPTVVSPKYKdIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVV 233
Cdd:PRK08979 160 DLPKDCLNPAILHPYEYPESIKmrsyNPTTSGHKGQ-IKRGLQALLAAKKPVLYVGGGAiiSGADKQILQLAEKLNLPVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 234 HTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVG------TNYPYVDYLPkkNIKAIQIDTNPKNIGHRFNI 307
Cdd:PRK08979 239 STLMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGvrfddrTTNNLEKYCP--NATILHIDIDPSSISKTVRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 308 NVGIVGDSKIALHQLtenIKHVAERPFLNKTLERKAVWDK---WMEQDK---NNNSKPLRPERLMASINQFIKDDAVISA 381
Cdd:PRK08979 317 DIPIVGSADKVLDSM---LALLDESGETNDEAAIASWWNEievWRSRNClayDKSSERIKPQQVIETLYKLTNGDAYVAS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 382 DVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVL 461
Cdd:PRK08979 394 DVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINL 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446985388 462 NNKQLAFIKYEQQAAGELEYAVDFSDM--DHAKFAEAAGGKGYTIKSASEVDAIVEEALA-QDVPTIVDVYVD 531
Cdd:PRK08979 474 NNRFLGMVKQWQDMIYQGRHSHSYMDSvpDFAKIAEAYGHVGIRISDPDELESGLEKALAmKDRLVFVDINVD 546
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-528 |
1.15e-79 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 261.86 E-value: 1.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPGDsidAVVDSLrtvrDQF-----KFYHVRHEEVASLAAAGYTKLTGKIGVALSI 75
Cdd:PRK07525 3 KMKMTPSEAFVETLQAHGITHAFGIIGS---AFMDAS----DLFppagiRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 76 GGPGLIHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKG 155
Cdd:PRK07525 76 NGPGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 156 VAVVICPNDLLTEKIKDTTNKPVDTSRPtvvSPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVV 233
Cdd:PRK07525 156 PAQINIPRDYFYGVIDVEIPQPVRLERG---AGGEQSLAEAAELLSEAKFPVILSGAGVvlSDAIEECKALAERLDAPVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 234 HTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPY--------VDYLPkKNIKAIQIDTNPKNIGHRF 305
Cdd:PRK07525 233 CGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPfgtlpqygIDYWP-KDAKIIQVDINPDRIGLTK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 306 NINVGIVGDSKIA----LHQLTENIKHVAER-PFLNKTLERKAVWDK---------------WMEQDKNNNSKPLRPERL 365
Cdd:PRK07525 312 KVSVGICGDAKAVarelLARLAERLAGDAGReERKALIAAEKSAWEQelsswdhedddpgtdWNEEARARKPDYMHPRQA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 366 MASINQFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQD 445
Cdd:PRK07525 392 LREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 446 FATAVQYDLPLTVFVLNNKQLAFIKYEQQ-------AAGELEyavdfSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEAL 518
Cdd:PRK07525 472 VMTAVRHNWPVTAVVFRNYQWGAEKKNQVdfynnrfVGTELD-----NNVSYAGIAEAMGAEGVVVDTQEELGPALKRAI 546
|
570
....*....|...
gi 446985388 519 A---QDVPTIVDV 528
Cdd:PRK07525 547 DaqnEGKTTVIEI 559
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-543 |
1.69e-79 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 261.22 E-value: 1.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGL 80
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFK-QDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 81 IHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVV 159
Cdd:PRK06466 80 TNAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRpGPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 160 ICPndlltekiKDTTNkPVDT---SRPTVV-----SPKYK----DIKKAVKLINKSKKPVMLVGVGAKQ--AKDELRAFI 225
Cdd:PRK06466 160 DIP--------KDMTN-PAEKfeyEYPKKVklrsySPAVRghsgQIRKAVEMLLAAKRPVIYSGGGVVLgnASALLTELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 226 EAAKIPVVHTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYP-YVDYLPKK---NIKAIQIDTNPKNI 301
Cdd:PRK06466 231 HLLNLPVTNTLMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDdRVTNGPAKfcpNAKIIHIDIDPASI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 302 GHRFNINVGIVGDSKIALHQLTENIKHVAERPflnktlERKAVWDKWMEQDK-----------NNNSKPLRPERLMASIN 370
Cdd:PRK06466 311 SKTIKADIPIVGPVESVLTEMLAILKEIGEKP------DKEALAAWWKQIDEwrgrhglfpydKGDGGIIKPQQVVETLY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 371 QFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAV 450
Cdd:PRK06466 385 EVTNGDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 451 QYDLPLTVFVLNNKQLAFIKYEQQAAGELEYAVDFSDM--DHAKFAEAAGGKGYTIKSASEVDAIVEEALA-QDVPTIVD 527
Cdd:PRK06466 465 QYGLPVKIINLNNGALGMVRQWQDMQYEGRHSHSYMESlpDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFID 544
|
570
....*....|....*.
gi 446985388 528 VYVDPNAAPLPGKIVN 543
Cdd:PRK06466 545 IYVDRSEHVYPMQIAD 560
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
8-548 |
2.81e-79 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 260.89 E-value: 2.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGM 87
Cdd:PRK06965 25 EILMKALAAEGVEFIWGYPGGAVLYIYDELYK-QDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 88 YDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVVICPNDLL 166
Cdd:PRK06965 104 ATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRpGPVVVDIPKDVS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 167 TEKIKDTTNKPVDT-SRPTVVSPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTLPAKTILP 243
Cdd:PRK06965 184 KTPCEYEYPKSVEMrSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVilANASRELRQLADLLGYPVTNTLMGLGAYP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 244 DDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNY-------PyvDYLPKKNIKAIQIDTNPKNIGHRFNINVGIVGDSK 316
Cdd:PRK06965 264 ASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFddrvignP--AHFASRPRKIIHIDIDPSSISKRVKVDIPIVGDVK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 317 IALHQLTENIKHVAERPflnKTLERKAVWDK---WMEQD---KNNNSKPLRPERLMASINQFIKDDAVISADVGTATVWS 390
Cdd:PRK06965 342 EVLKELIEQLQTAEHGP---DADALAQWWKQiegWRSRDclkYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMWA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 391 TRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIK 470
Cdd:PRK06965 419 AQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMVR 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 471 YEQqaagELEYAVDFSD--MD----HAKFAEAAGGKGYTIKSASEVDAIVEEALA-QDVPTIVDVYVDP--NAAPL--PG 539
Cdd:PRK06965 499 QWQ----EIEYSKRYSHsyMDalpdFVKLAEAYGHVGMRIEKTSDVEPALREALRlKDRTVFLDFQTDPteNVWPMvqAG 574
|
....*....
gi 446985388 540 KIVNEEAFG 548
Cdd:PRK06965 575 KGITEMLLG 583
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
10-538 |
3.61e-79 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 260.16 E-value: 3.61e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 10 LVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDQFKFYHV--RHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGM 87
Cdd:PRK06456 8 LVDSLKREGVKVIFGIPGLSNMQIYDAFVEDLANGELRHVlmRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLVTGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 88 YDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVVICPNDLL 166
Cdd:PRK06456 88 ITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRpGPVVIDIPRDIF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 167 TEKIKDTT--NKP-VDTSR--PTVVSPKykDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTLPAK 239
Cdd:PRK06456 168 YEKMEEIKwpEKPlVKGYRdfPTRIDRL--ALKKAAEILINAERPIILVGTGVvwSNATPEVLELAELLHIPIVSTFPGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 240 TILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVG--------TNYpyvDYLPKKNIKAIQIDTNPKNIGHRFNINVGI 311
Cdd:PRK06456 246 TAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGarfsdrtfTSY---DEMVETRKKFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 312 VGDSKIALHQLTENIKHVAER----PFLNKTLERKAVWDKWMEQDKNNNskpLRPERLMASINQFIKDDAVISADVGTAT 387
Cdd:PRK06456 323 YGNAKIILRELIKAITELGQKrdrsAWLKRVKEYKEYYSQFYYTEENGK---LKPWKIMKTIRQALPRDAIVTTGVGQHQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 388 VWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLA 467
Cdd:PRK06456 400 MWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLG 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446985388 468 FIKYEQQA-AGELEYAVDF-SDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLP 538
Cdd:PRK06456 480 LVRQVQDLfFGKRIVGVDYgPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALP 552
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
8-539 |
2.67e-78 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 257.12 E-value: 2.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSI----DAVVDSlrtvrdQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHL 83
Cdd:PRK08978 5 QWVVHALRAQGVDTVFGYPGGAImpvyDALYDG------GVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 84 LNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEAnlqklceDV-----AVFNH--QIEKGDNVFEIVNEAIRTAYEQK-G 155
Cdd:PRK08978 79 ITGLADALLDSVPVVAITGQVSSPLIGTDAFQEI-------DVlglslACTKHsfLVQSLEELPEIMAEAFEIASSGRpG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 156 VAVVICPNDLLtekIKDTTNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLV--GVGAKQAKDELRAFIEAAKIPVV 233
Cdd:PRK08978 152 PVLVDIPKDIQ---LAEGELEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVggGVGMAGAVPALREFLAATGMPAV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 234 HTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPyvDYLPKK------NIKAIQIDTNPKNIGHRFNI 307
Cdd:PRK08978 229 ATLKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFD--DRVTGKlntfapHAKVIHLDIDPAEINKLRQA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 308 NVGIVGDSKIALHQLTE--NI----KHVAErpflnktLERKAVWdkwmeqDKNNNSKPLRPERLMASINQFIKDDAVISA 381
Cdd:PRK08978 307 HVALQGDLNALLPALQQplNIdawrQHCAQ-------LRAEHAW------RYDHPGEAIYAPALLKQLSDRKPADTVVTT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 382 DVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVL 461
Cdd:PRK08978 374 DVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 462 NNKQLAFIKYEQQAAGELEYA-VDFSDM-DHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDP--NAAPL 537
Cdd:PRK08978 454 DNQRLGMVRQWQQLFFDERYSeTDLSDNpDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDEleNVWPL 533
|
....
gi 446985388 538 --PG 539
Cdd:PRK08978 534 vpPG 537
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-538 |
3.28e-78 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 256.86 E-value: 3.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGL 80
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 81 IHLLNGMYDAKMDNVPQLILSGQTNSTALGtKAF--------QEANLQKLCEDVAVFNHQIEKGDnvfeIVNEAIRTAYE 152
Cdd:PRK08266 81 LNAGAALLTAYGCNSPVLCLTGQIPSALIG-KGRghlhempdQLATLRSFTKWAERIEHPSEAPA----LVAEAFQQMLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 153 --QKGVAVVIcPNDLLTEKIKDTTNKPVDTSRPTVVSPkyKDIKKAVKLINKSKKPVMLVGVGAKQAKDELRAFIEAAKI 230
Cdd:PRK08266 156 grPRPVALEM-PWDVFGQRAPVAAAPPLRPAPPPAPDP--DAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 231 PVVHTLPAKTILPDDHPYSIGNLGkigtktSYQTMQDADLLIMVGTN----YPYVDYLPkKNIKAIQIDTNPKNIGhRFN 306
Cdd:PRK08266 233 PVVAFRSGRGIVSDRHPLGLNFAA------AYELWPQTDVVIGIGSRlelpTFRWPWRP-DGLKVIRIDIDPTEMR-RLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 307 INVGIVGDSKIALHQLTENI-KHVAERPFlnKTLERKAVWDKWMEQdknnnSKPLRPER-LMASINQFIKDDAVI---SA 381
Cdd:PRK08266 305 PDVAIVADAKAGTAALLDALsKAGSKRPS--RRAELRELKAAARQR-----IQAVQPQAsYLRAIREALPDDGIFvdeLS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 382 DVGTAT-----VWSTRylnlgvnnKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPL 456
Cdd:PRK08266 378 QVGFASwfafpVYAPR--------TFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 457 TVFVLNNKQLAFIKYEQ-QAAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTI--VDVYVDPN 533
Cdd:PRK08266 450 VTVVFNNNAYGNVRRDQkRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLieVPVPRGSE 529
|
....*
gi 446985388 534 AAPLP 538
Cdd:PRK08266 530 ASPWP 534
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
3-536 |
1.35e-77 |
|
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: 256.33 E-value: 1.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 3 KIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVrdQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIH 82
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPA--GIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 83 LLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVICP 162
Cdd:TIGR03457 79 CVTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREMGPAQLNIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 163 NDLLTEKIKDTTNKPVDTSRPtvvSPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVHTLPAKT 240
Cdd:TIGR03457 159 RDYFYGEIDVEIPRPVRLDRG---AGGATSLAQAARLLAEAKFPVIISGGGVvmGDAVEECKALAERLGAPVVNSYLHND 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 241 ILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNY-PY-------VDYLPkKNIKAIQIDTNPKNIGHRFNINVGIV 312
Cdd:TIGR03457 236 SFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLgPFgtlpqygIDYWP-KNAKIIQVDANAKMIGLVKKVTVGIC 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 313 GDSKIALHQLTENIK------HVAERpfLNKTLERKAVWDK---------------WMEQDKNNNSKPLRPERLMASINQ 371
Cdd:TIGR03457 315 GDAKAAAAEILQRLAgkagdaNRAER--KAKIQAERSAWEQelsemtherdpfsldMIVEQRQEEGNWLHPRQVLRELEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 372 FIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQ 451
Cdd:TIGR03457 393 AMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 452 YDLPLTVFVLNNKQLAFIKYEQQ-------AAGELEyavdfSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEAL---AQD 521
Cdd:TIGR03457 473 HDIPVTAVVFRNRQWGAEKKNQVdfynnrfVGTELE-----SELSFAGIADAMGAKGVVVDKPEDVGPALKKAIaaqAEG 547
|
570
....*....|....*
gi 446985388 522 VPTIVDVYVDPNAAP 536
Cdd:TIGR03457 548 KTTVIEIVCTRELGD 562
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-534 |
9.23e-77 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 253.26 E-value: 9.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGL 80
Cdd:PRK08199 5 PRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHD-ETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 81 IHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVV 159
Cdd:PRK08199 84 TNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRpGPVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 160 ICPNDLLTEKIKDTTNKPVDTSRPtvvSPKYKDIKKAVKLINKSKKPVMLVGVGAK--QAKDELRAFIEAAKIPVVHTLP 237
Cdd:PRK08199 164 ALPEDVLSETAEVPDAPPYRRVAA---APGAADLARLAELLARAERPLVILGGSGWteAAVADLRAFAERWGLPVACAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 238 AKTILPDDHPYSIGNLGkIGTKTSY-QTMQDADLLIMVGT--------NYPYVDyLPKKNIKAIQIDTNPKNIGHRFNIN 308
Cdd:PRK08199 241 RQDLFDNRHPNYAGDLG-LGINPALaARIREADLVLAVGTrlgevttqGYTLLD-IPVPRQTLVHVHPDAEELGRVYRPD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 309 VGIVGDSKIALHQLtENIKHVAERPFLNKTLERKAVWDKWmeQDKNNNSKPLRPERLMASINQFIKDDAVISADVGTATV 388
Cdd:PRK08199 319 LAIVADPAAFAAAL-AALEPPASPAWAEWTAAAHADYLAW--SAPLPGPGAVQLGEVMAWLRERLPADAIITNGAGNYAT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 389 WSTRYLNLGVNNKFI--ISswlGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQL 466
Cdd:PRK08199 396 WLHRFFRFRRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMY 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446985388 467 AFIKYEQqaagELEY-----AVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNA 534
Cdd:PRK08199 473 GTIRMHQ----EREYpgrvsGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPEA 541
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
8-531 |
1.75e-76 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 252.47 E-value: 1.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLrtVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGM 87
Cdd:PRK08617 9 DLVVDSLINQGVKYVFGIPGAKIDRVFDAL--EDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLATGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 88 YDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYE-QKGVAVVICPNDLL 166
Cdd:PRK08617 87 VTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESgRPGAAFVSLPQDVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 167 TEKIKDTTNKPVDTSRPTVVSPKykDIKKAVKLINKSKKPVMLVGVGAKQAK--DELRAFIEAAKIPVVHTLPAKTILPD 244
Cdd:PRK08617 167 DAPVTSKAIAPLSKPKLGPASPE--DINYLAELIKNAKLPVLLLGMRASSPEvtAAIRRLLERTNLPVVETFQAAGVISR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 245 DH-PYSIGNLGKIGTKTSYQTMQDADLLIMVGtnYPYVDYLPK---KNIKA--IQIDTNPKNIGHRFNINVGIVGDSKIA 318
Cdd:PRK08617 245 ELeDHFFGRVGLFRNQPGDELLKKADLVITIG--YDPIEYEPRnwnSEGDAtiIHIDVLPAEIDNYYQPERELIGDIAAT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 319 LHQLTENIKHV----AERPFLNktlERKAVWDKWMEQDKNNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTRYL 394
Cdd:PRK08617 323 LDLLAEKLDGLslspQSLEILE---ELRAQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSHYIWMARYF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 395 NLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQq 474
Cdd:PRK08617 400 RSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQE- 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446985388 475 aagELEY----AVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVD 531
Cdd:PRK08617 479 ---EMKYgrssGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVD 536
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
8-544 |
1.85e-76 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 253.48 E-value: 1.85e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGM 87
Cdd:PRK09107 15 EMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQ-QDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 88 YDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVVICPNDLL 166
Cdd:PRK09107 94 QDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRpGPVVVDIPKDVQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 167 TEKIKDTTNKPVDTSRPTvvSPKYK----DIKKAVKLINKSKKPVMLVGVG----AKQAKDELRAFIEAAKIPVVHTLPA 238
Cdd:PRK09107 174 FATGTYTPPQKAPVHVSY--QPKVKgdaeAITEAVELLANAKRPVIYSGGGvinsGPEASRLLRELVELTGFPITSTLMG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 239 KTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYP------YVDYLPkkNIKAIQIDTNPKNIGHRFNINVGIV 312
Cdd:PRK09107 252 LGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDdritgrLDAFSP--NSKKIHIDIDPSSINKNVRVDVPII 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 313 GDSKIALHQLTENIKHVAERPflnktleRKAVWDKWMEQ----------DKNNNSKPLRPERLMASINQFIKD-DAVISA 381
Cdd:PRK09107 330 GDVGHVLEDMLRLWKARGKKP-------DKEALADWWGQiarwrarnslAYTPSDDVIMPQYAIQRLYELTKGrDTYITT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 382 DVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVL 461
Cdd:PRK09107 403 EVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFIL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 462 NNKQLAFIKYEQQAAGELEYAVDFSDM--DHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLP- 538
Cdd:PRK09107 483 NNQYMGMVRQWQQLLHGNRLSHSYTEAmpDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFPm 562
|
....*....
gi 446985388 539 ---GKIVNE 544
Cdd:PRK09107 563 ipsGKAHNE 571
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
1-538 |
3.70e-76 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 252.05 E-value: 3.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIK------ANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVrDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALS 74
Cdd:PRK07282 1 MEKISlespksGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNF-EGIRHILARHEQGALHEAEGYAKSTGKLGVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 75 IGGPGLIHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK 154
Cdd:PRK07282 80 TSGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 155 GVAVVI-CPND---LLTEKIKDTT-NKPvdTSRPTVVsPKYKDIKKAVKLINKSKKPVMLVGVGAK--QAKDELRAFIEA 227
Cdd:PRK07282 160 PGPVVIdLPKDvsaLETDFIYDPEvNLP--SYQPTLE-PNDMQIKKILKQLSKAKKPVILAGGGINyaEAATELNAFAER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 228 AKIPVVHTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPyvDYL---PK---KNIKAIQIDTNPKNI 301
Cdd:PRK07282 237 YQIPVVTTLLGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFD--DRLtgnPKtfaKNAKVAHIDIDPAEI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 302 GHRFNINVGIVGDSKIALHQLTEnikhvaerpfLNKTLERKAVWDKWMEQDKNN------NSKPLRPERLMASINQFIKD 375
Cdd:PRK07282 315 GKIIKTDIPVVGDAKKALQMLLA----------EPTVHNNTEKWIEKVTKDKNRvrsydkKERVVQPQAVIERIGELTNG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 376 DAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLP 455
Cdd:PRK07282 385 DAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 456 LTVFVLNNKQLAFIKYEQQA--AGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVeEALAQDVPTIVDVYVDPN 533
Cdd:PRK07282 465 IKVVMLNNHSLGMVRQWQESfyEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDL-EVITEDVPMLIEVDISRK 543
|
....*
gi 446985388 534 AAPLP 538
Cdd:PRK07282 544 EHVLP 548
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-541 |
3.15e-73 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 244.37 E-value: 3.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVrDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGL 80
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTV-GGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 81 IHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVV 159
Cdd:PRK07979 80 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 160 ICPNDLLTEKIKDTTNKPVDTS----RPTVVSPKYKdIKKAVKLINKSKKPVMLVGVGAKQA--KDELRAFIEAAKIPVV 233
Cdd:PRK07979 160 DLPKDILNPANKLPYVWPESVSmrsyNPTTQGHKGQ-IKRALQTLVAAKKPVVYVGGGAINAacHQQLKELVEKLNLPVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 234 HTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVG------TNYPYVDYLPkkNIKAIQIDTNPKNIGHRFNI 307
Cdd:PRK07979 239 SSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGvrfddrTTNNLAKYCP--NATVLHIDIDPTSISKTVTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 308 NVGIVGDSKIALHQLTENIKHvaerpfLNKTLERKAVWDKW--MEQ-------DKNNNSKPLRPERLMASINQFIKDDAV 378
Cdd:PRK07979 317 DIPIVGDARQVLEQMLELLSQ------ESAHQPLDEIRDWWqqIEQwrarqclKYDTHSEKIKPQAVIETLWRLTKGDAY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 379 ISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTV 458
Cdd:PRK07979 391 VTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 459 FVLNNKQLAFIKYEQ--QAAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQ---DVPTIVDVYVDPN 533
Cdd:PRK07979 471 LNLNNRYLGMVKQWQdmIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQvrnNRLVFVDVTVDGS 550
|
....*...
gi 446985388 534 AAPLPGKI 541
Cdd:PRK07979 551 EHVYPMQI 558
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
8-531 |
5.21e-72 |
|
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: 240.42 E-value: 5.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvrDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGM 87
Cdd:TIGR02418 3 DLVVDQLENQGVRYVFGIPGAKIDRVFDALED--KGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 88 YDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYE-QKGVAVVICPNDLL 166
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESgKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 167 TEKIKDTTNKPVdtSRPTVVSPKYKDIKKAVKLINKSKKPVMLVGVGAKQ--AKDELRAFIEAAKIPVVHTLP-AKTILP 243
Cdd:TIGR02418 161 DSPVSVKAIPAS--YAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGLRASSpeTTEAVRRLLKKTQLPVVETFQgAGAVSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 244 DDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGtnYPYVDYLPK---KNIKA--IQIDTNPKNIGHRFNINVGIVGDSKIA 318
Cdd:TIGR02418 239 ELEDHFFGRVGLFRNQPGDRLLKQADLVITIG--YDPIEYEPRnwnSENDAtiVHIDVEPAQIDNNYQPDLELVGDIAST 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 319 LHQLTENIKHVAERPFLNKTLE-RKAVWDKWMEQDKNNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLG 397
Cdd:TIGR02418 317 LDLLAERIPGYELPPDALAILEdLKQQREALDRVPATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFRSY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 398 VNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAG 477
Cdd:TIGR02418 397 RARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKY 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446985388 478 ELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVD 531
Cdd:TIGR02418 477 QRSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVD 530
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-541 |
1.44e-71 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 240.20 E-value: 1.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVrDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGL 80
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTL-GGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 81 IHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVI 160
Cdd:PRK06882 80 TNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 161 -CPNDLLTEKIKDTTNKPVDTS----RPTVVSPKYKdIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVV 233
Cdd:PRK06882 160 dIPKDMVNPANKFTYEYPEEVSlrsyNPTVQGHKGQ-IKKALKALLVAKKPVLFVGGGVitAECSEQLTQFAQKLNLPVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 234 HTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVG------TNYPYVDYLPkkNIKAIQIDTNPKNIGHRFNI 307
Cdd:PRK06882 239 SSLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGvrfddrTTNNLAKYCP--NAKVIHIDIDPTSISKNVPA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 308 NVGIVGDSKialHQLTENIKHVAERPFLNKTLERKAVW---DKWMEQ---DKNNNSKPLRPERLMASINQFIKDDAVISA 381
Cdd:PRK06882 317 YIPIVGSAK---NVLEEFLSLLEEENLAKSQTDLTAWWqqiNEWKAKkclEFDRTSDVIKPQQVVEAIYRLTNGDAYVAS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 382 DVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVL 461
Cdd:PRK06882 394 DVGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 462 NNKQLAFIKYEQqaagELEYAVDFSDM------DHAKFAEAAGGKGYTIKSASEVDAIVEEALA-QDVPTIVDVYVDPNA 534
Cdd:PRK06882 474 NNRFLGMVKQWQ----DLIYSGRHSQVymnslpDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSiKDKLVFVDVNVDETE 549
|
....*..
gi 446985388 535 APLPGKI 541
Cdd:PRK06882 550 HVYPMQI 556
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
5-165 |
4.35e-70 |
|
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: 222.81 E-value: 4.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 5 KANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLL 84
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRR-EGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 85 NGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVICPND 164
Cdd:cd07039 80 NGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKRGVAVLILPGD 159
|
.
gi 446985388 165 L 165
Cdd:cd07039 160 V 160
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
8-538 |
4.25e-68 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 230.75 E-value: 4.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSL---RTVRdqfkfyHV--RHEEVASLAAAGYTKLTGKIGVALSIGGPGLIH 82
Cdd:PRK08155 17 ELIVRLLERQGIRIVTGIPGGAILPLYDALsqsTQIR------HIlaRHEQGAGFIAQGMARTTGKPAVCMACSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 83 LLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAyeQKG----VAV 158
Cdd:PRK08155 91 LVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIA--QSGrpgpVWI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 159 VIcPNDLLTEKIkDTTNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLVGVG--AKQAKDELRAFIEAAKIPVVHTL 236
Cdd:PRK08155 169 DI-PKDVQTAVI-ELEALPAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGviNSGAPARARELAEKAQLPTTMTL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 237 PAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPyvDYLPKK------NIKAIQIDTNPKNIGHRFNINVG 310
Cdd:PRK08155 247 MALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFD--DRAIGKteqfcpNAKIIHVDIDRAELGKIKQPHVA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 311 IVGDSKIALHQLTENIKHVAERPFLNKTLERKAVWDKWMEQDKNnnskPLRPERLMASINQFIKDDAVISADVGTATVWS 390
Cdd:PRK08155 325 IQADVDDVLAQLLPLVEAQPRAEWHQLVADLQREFPCPIPKADD----PLSHYGLINAVAACVDDNAIITTDVGQHQMWT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 391 TRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIk 470
Cdd:PRK08155 401 AQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLV- 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446985388 471 YEQQAA--GELEYAVDFSDM-DHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLP 538
Cdd:PRK08155 480 HQQQSLfyGQRVFAATYPGKiNFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYP 550
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
8-536 |
2.64e-61 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 212.70 E-value: 2.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYG--IPGDSIDAVvdslrtvrDQFKFYHV--RHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHL 83
Cdd:PRK06112 18 HAIARALKRHGVEQIFGqsLPSALFLAA--------EAIGIRQIayRTENAGGAMADGYARVSGKVAVVTAQNGPAATLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 84 LNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVVICP 162
Cdd:PRK06112 90 VAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRpGPVVLLLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 163 NDLLTEK-----IKDTTNK---PVDTSRPtvvSPKykDIKKAVKLINKSKKPVMLVG--VGAKQAKDELRAFIEAAKIPV 232
Cdd:PRK06112 170 ADLLTAAaaapaAPRSNSLghfPLDRTVP---APQ--RLAEAASLLAQAQRPVVVAGggVHISGASAALAALQSLAGLPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 233 VHTLPAKTILPDDHPYSIGNLGK-IGTKT----SYQTMQDADLLIMVG--TNYPYVD--YLPKKNIKAIQIDTNPKNIGH 303
Cdd:PRK06112 245 ATTNMGKGAVDETHPLSLGVVGSlMGPRSpgrhLRDLVREADVVLLVGtrTNQNGTDswSLYPEQAQYIHIDVDGEEVGR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 304 RFNiNVGIVGDSKIALHQLTENIKHV------AERPFLNKTLERkaVWDKWmEQDK----NNNSKPLRPERLMASINQFI 373
Cdd:PRK06112 325 NYE-ALRLVGDARLTLAALTDALRGRdlaaraGRRAALEPAIAA--GREAH-REDSapvaLSDASPIRPERIMAELQAVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 374 KDDAVISADVGTATVWSTRYLN-LGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQY 452
Cdd:PRK06112 401 TGDTIVVADASYSSIWVANFLTaRRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 453 DLPLTVFVLNNKQLAFIKY-EQQAAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVD 531
Cdd:PRK06112 481 GVPVTIVVLNNGILGFQKHaETVKFGTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITD 560
|
....*
gi 446985388 532 PNAAP 536
Cdd:PRK06112 561 PSAFP 565
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-528 |
7.77e-56 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 198.28 E-value: 7.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvRDQFKFYHVRHEEVASLAAAGYTKLT-GKIGVALSIGGPG 79
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRK-HGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 80 LIHLLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVV 159
Cdd:PRK11269 80 GTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 160 I-CPNDLLTEKIK--DTTNKPVDTSRPTvvsPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVVH 234
Cdd:PRK11269 160 IdLPFDVQVAEIEfdPDTYEPLPVYKPA---ATRAQIEKALEMLNAAERPLIVAGGGVinADASDLLVEFAELTGVPVIP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 235 TLPAKTILPDDHPYsigNLGKIGTKTSY----QTMQDADLLIMVGTNYP-----YVD-YlpKKNIKAIQIDTNPKNIGHR 304
Cdd:PRK11269 237 TLMGWGAIPDDHPL---MAGMVGLQTSHrygnATLLASDFVLGIGNRWAnrhtgSVEvY--TKGRKFVHVDIEPTQIGRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 305 FNINVGIVGDSKIALHQLTENIKH-------------VAERPFLNKTLERKAVWDkwmeqdknnnSKPLRPERLMASINQ 371
Cdd:PRK11269 312 FGPDLGIVSDAKAALELLVEVAREwkaagrlpdrsawVADCQERKRTLLRKTHFD----------NVPIKPQRVYEEMNK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 372 FIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQ 451
Cdd:PRK11269 382 AFGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 452 YDLPLTVFVLNNKQLAFIKyEQQAAGELEYAVDFS------------DMDHAKFAEAAGGKGYTIKSASEVDAIVEEALA 519
Cdd:PRK11269 462 FNLPYIHVLVNNAYLGLIR-QAQRAFDMDYCVQLAfeninspelngyGVDHVKVAEGLGCKAIRVFKPEDIAPALEQAKA 540
|
570
....*....|...
gi 446985388 520 Q----DVPTIVDV 528
Cdd:PRK11269 541 LmaefRVPVVVEV 553
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
5-538 |
4.18e-55 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 196.11 E-value: 4.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 5 KANEALVKALQAWDIDHLYGIPGDSIDAVVDSLrTVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLL 84
Cdd:PLN02470 14 KGADILVEALEREGVDTVFAYPGGASMEIHQAL-TRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 85 NGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVVICPN 163
Cdd:PLN02470 93 TGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRpGPVLVDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 164 DLLTEKIKDTTNKPVdtSRPTVVS-----PKYKDIKKAVKLINKSKKPVMLVGVGAKQAKDELRAFIEAAKIPVVHTLPA 238
Cdd:PLN02470 173 DIQQQLAVPNWNQPM--KLPGYLSrlpkpPEKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 239 KTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPyvDYLPKK------NIKAIQIDTNPKNIGHRFNINVGIV 312
Cdd:PLN02470 251 LGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFD--DRVTGKleafasRASIVHIDIDPAEIGKNKQPHVSVC 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 313 GDSKIALHQLTENIKHVAErpflnKTLERKAvWDKWMEQDKNNNskPLR---------PERLMASINQFIKDDAVISADV 383
Cdd:PLN02470 329 ADVKLALQGLNKLLEERKA-----KRPDFSA-WRAELDEQKEKF--PLSyptfgdaipPQYAIQVLDELTDGNAIISTGV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 384 GTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNN 463
Cdd:PLN02470 401 GQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 464 KQLAFI-KYEQQ---AAGELEYAVD-------FSDMdhAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDP 532
Cdd:PLN02470 481 QHLGMVvQWEDRfykANRAHTYLGDpdaeaeiFPDF--LKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPH 558
|
....*.
gi 446985388 533 NAAPLP 538
Cdd:PLN02470 559 QEHVLP 564
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
8-528 |
3.55e-54 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 192.50 E-value: 3.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGdsidavVDSLRTVR--DQFKFYHV--RHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHL 83
Cdd:PRK07524 6 EALVRLLEAYGVETVFGIPG------VHTVELYRglAGSGIRHVtpRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 84 LNGMYDAKMDNVPQLILSG--QTNSTALGTKAFQE-ANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIrtAYEQKG----V 156
Cdd:PRK07524 80 ATAMGQAYADSIPMLVISSvnRRASLGKGRGKLHElPDQRAMVAGVAAFSHTLMSAEDLPEVLARAF--AVFDSArprpV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 157 AVVIcPNDLLTEKIKDTTNKPVdtSRPTVVSPKYKDIKKAVKLINKSKKPVMLVGVGAKQAKDELRAFIEAAKIPVVHTL 236
Cdd:PRK07524 158 HIEI-PLDVLAAPADHLLPAPP--TRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVALTI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 237 PAKTILPDDHPYSIGnlGKIGTKTSYQTMQDADLLIMVGTNYPYVDY---------LPKKnikAIQIDTNPKNIGHRFNI 307
Cdd:PRK07524 235 NAKGLLPAGHPLLLG--ASQSLPAVRALIAEADVVLAVGTELGETDYdvyfdggfpLPGE---LIRIDIDPDQLARNYPP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 308 NVGIVGDSKIALHQLTENIKHVAERPF--------LNKTLErkAVWDKWMeqdknnnskplrpeRLMASINQFIKD---D 376
Cdd:PRK07524 310 ALALVGDARAALEALLARLPGQAAAADwgaarvaaLRQALR--AEWDPLT--------------AAQVALLDTILAalpD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 377 AVISADvGTATVWSTrylNLGVNNK-----FIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQ 451
Cdd:PRK07524 374 AIFVGD-STQPVYAG---NLYFDADaprrwFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVE 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446985388 452 YDLPLTVFVLNNKQLAFIKYEQQAAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDV 528
Cdd:PRK07524 450 ADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
382-528 |
1.20e-50 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 171.23 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 382 DVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVL 461
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446985388 462 NNKQLAFIKYEQQAAGE----LEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDV 528
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGgrysGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
6-535 |
2.73e-50 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 181.84 E-value: 2.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 6 ANEALVKALQAWDIDHLYGIPGDSIDAVVDSlrTVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLN 85
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDG--AREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 86 GMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYE-QKGVAVVICPND 164
Cdd:PRK05858 85 AMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTpHRGPVFVDFPMD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 165 LLTEKIKDTTNKPVDTSRPTVVSPKYKDIKKAVKLINKSKKPVMLVG--VGAKQAKDELRAFIEAAKIPVVHTLPAKTIL 242
Cdd:PRK05858 165 HAFSMADDDGRPGALTELPAGPTPDPDALARAAGLLAEAQRPVIMAGtdVWWGHAEAALLRLAEELGIPVLMNGMGRGVV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 243 PDDHPYSIgnlgkigTKTSYQTMQDADLLIMVGTnyP------YVDYLPKKNIkaIQIDTNPKNIGHRFNINVGIVGDSK 316
Cdd:PRK05858 245 PADHPLAF-------SRARGKALGEADVVLVVGV--PmdfrlgFGVFGGTAQL--VHVDDAPPQRAHHRPVAAGLYGDLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 317 IALHQLTEnikHVAERPFLNKTLER-KAVWDKWMEQDK---NNNSKPLRPERLMASINQFIKDDAVISADVGTATVWSTR 392
Cdd:PRK05858 314 AILSALAG---AGGDRTDHQGWIEElRTAETAARARDAaelADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 393 YLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYE 472
Cdd:PRK05858 391 YIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKHP 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446985388 473 QQAAGELEYAVDFS-DMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAA 535
Cdd:PRK05858 471 MEALYGYDVAADLRpGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDPSVA 534
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
364-530 |
1.08e-49 |
|
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: 169.36 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 364 RLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVM 443
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 444 QDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAGEL-EYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDV 522
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGrVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 446985388 523 PTIVDVYV 530
Cdd:cd00568 161 PALIEVKT 168
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
5-518 |
6.46e-46 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 170.38 E-value: 6.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 5 KANEALVKALQAWDIDHLYGIPGDS-IDAVVDS-LRTVRdqfkfyhVRHEEVASLAAAGYTKLTG--KIGVALSIGGPGL 80
Cdd:PRK06154 21 KVAEAVAEILKEEGVELLFGFPVNElFDAAAAAgIRPVI-------ARTERVAVHMADGYARATSgeRVGVFAVQYGPGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 81 IHLLNGMYDAKMDNVPQLILSGQTN--STAL-----GTKAFQeaNLQKLCEdvavfnhQIEKGDNVFEIVNEAIRTAYEQ 153
Cdd:PRK06154 94 ENAFGGVAQAYGDSVPVLFLPTGYPrgSTDVapnfeSLRNYR--HITKWCE-------QVTLPDEVPELMRRAFTRLRNG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 154 KGVAVVI-CPNDLLTEKIKDTtnkPVDTSRP--TVVSPKYKDIKKAVKLINKSKKPVMLVGVGAKQAK--DELRAFIEAA 228
Cdd:PRK06154 165 RPGPVVLeLPVDVLAEELDEL---PLDHRPSrrSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQatPELKELAELL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 229 KIPVVHTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADLLIMVGTNYPYVDY---LPKKNiKAIQIDTNPKNIGHRF 305
Cdd:PRK06154 242 EIPVMTTLNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYglpMPEGK-TIIHSTLDDADLNKDY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 306 NINVGIVGDSKIALHQLTENIK--HVAERPFLNKTL-ERKAVWDKWMEQ--DK-NNNSKPLRPERLMASINQFI-KDDAV 378
Cdd:PRK06154 321 PIDHGLVGDAALVLKQMIEELRrrVGPDRGRAQQVAaEIEAVRAAWLAKwmPKlTSDSTPINPYRVVWELQHAVdIKTVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 379 ISADVGT-----ATVWSTR----YLNLGVNNKfiisswlgtMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATA 449
Cdd:PRK06154 401 ITHDAGSprdqlSPFYVASrpgsYLGWGKTTQ---------LGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446985388 450 VQYDLPLTVFVLNNKQLAFIKYEQQAAGELEYAVDFSDmDHAKFAEAAGGKGYTIKSASEVDAIVEEAL 518
Cdd:PRK06154 472 VRERIPILTILLNNFSMGGYDKVMPVSTTKYRATDISG-DYAAIARALGGYGERVEDPEMLVPALLRAL 539
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
3-528 |
1.21e-45 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 169.02 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 3 KIKANEALVKALQAWDIDHLYGIPgdSI------DAVvdslrTVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIG 76
Cdd:PRK07064 2 KVTVGELIAAFLEQCGVKTAFGVI--SIhnmpilDAI-----GRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 77 GPGLIHLLNGMYDAKMDNVPQLILSGQTNSTALGTKA--FQEANLQ----KLCEDVAvfnHQIEKGDNVFEIVNEAIRTA 150
Cdd:PRK07064 75 GTGAGNAAGALVEALTAGTPLLHITGQIETPYLDQDLgyIHEAPDQltmlRAVSKAA---FRVRSAETALATIREAVRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 151 YEQKG--VAVVIcPNDLLTEKIkdttNKPVDTSRPTVVSPKYKD--IKKAVKLINKSKKPVMLVGVGAKQAKDELRAFIE 226
Cdd:PRK07064 152 LTAPTgpVSVEI-PIDIQAAEI----ELPDDLAPVHVAVPEPDAaaVAELAERLAAARRPLLWLGGGARHAGAEVKRLVD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 227 AAkIPVVHTLPAKTILPDDHPYSIGNLGkiGTKTSYQTMQDADLLIMVGTNY------PYVDYLPKKnikAIQIDTNPKN 300
Cdd:PRK07064 227 LG-FGVVTSTQGRGVVPEDHPASLGAFN--NSAAVEALYKTCDLLLVVGSRLrgnetlKYSLALPRP---LIRVDADAAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 301 IGHRFNINVGIVGDSKIALHQLtenikhvAERpfLNKTLERKAVWDKWMEQDKNNNSKPLRPE-----RLMASINQFIKD 375
Cdd:PRK07064 301 DGRGYPNDLFVHGDAARVLARL-------ADR--LEGRLSVDPAFAADLRAAREAAVADLRKGlgpyaKLVDALRAALPR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 376 DAVISADVGTA-TVWSTRYLNLGVNNKFIiSSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDL 454
Cdd:PRK07064 372 DGNWVRDVTISnSTWGNRLLPIFEPRANV-HALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENA 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446985388 455 PLTVFVLNNKQLAFIKYEQQAA-GELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDV 528
Cdd:PRK07064 451 NMVIVLMNDGGYGVIRNIQDAQyGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
360-538 |
1.93e-45 |
|
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: 158.82 E-value: 1.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 360 LRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAF 439
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 440 QMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQqaagELEYAVDFS------DMDHAKFAEAAGGKGYTIKSASEVDAI 513
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQ----ELFYEGRYShttldsNPDFVKLAEAYGIKGLRVEKPEELEAA 156
|
170 180
....*....|....*....|....*
gi 446985388 514 VEEALAQDVPTIVDVYVDPNAAPLP 538
Cdd:cd02015 157 LKEALASDGPVLLDVLVDPEENVLP 181
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-519 |
3.05e-45 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 168.25 E-value: 3.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 1 MAKIKANEALVKALQAWDIDHLYGIPG-DS---IDAVVDSLRTVRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIG 76
Cdd:PRK08327 4 LTMYTAAELFLELLKELGVDYIFINSGtDYppiIEAKARARAAGRPLPEFVICPHEIVAISMAHGYALVTGKPQAVMVHV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 77 GPGLIHLLNGMYDAKMDNVPQLILSGQTNST---ALGTKA-----FQEANLQK-LCEDVAVFNHQIEKGDNVFEIVNEAI 147
Cdd:PRK08327 84 DVGTANALGGVHNAARSRIPVLVFAGRSPYTeegELGSRNtrihwTQEMRDQGgLVREYVKWDYEIRRGDQIGEVVARAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 148 RTAY-EQKGVAVVICPNDLLTEKIKDTT---NKPVDTSRPtvvSPKYKDIKKAVKLINKSKKPVMLVGVGA--KQAKDEL 221
Cdd:PRK08327 164 QIAMsEPKGPVYLTLPREVLAEEVPEVKadaGRQMAPAPP---APDPEDIARAAEMLAAAERPVIITWRAGrtAEGFASL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 222 RAFIEAAKIPVVHTLPAKTILPDDHPYSIGNLGKIgtktsyqTMQDADLLIMVGTNYPYVDYL--PKKNIKAIQIDTNP- 298
Cdd:PRK08327 241 RRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRA-------DLAEADLVLVVDSDVPWIPKKirPDADARVIQIDVDPl 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 299 -KNIGHR-FNINVGIVGDSKIALHQLTENIK--------HVAERPFLNKTLERKAVWDKWMEQDKNNNSKPLRPERLMAS 368
Cdd:PRK08327 314 kSRIPLWgFPCDLCIQADTSTALDQLEERLKslasaerrRARRRRAAVRELRIRQEAAKRAEIERLKDRGPITPAYLSYC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 369 INQFIKDDAVISADVGTatVWstRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQmvmqdFAT 448
Cdd:PRK08327 394 LGEVADEYDAIVTEYPF--VP--RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFI-----FGV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 449 -------AVQYDLPLTVFVLNNKQLAFIK------YEQQAAGELEY--AVDFS-DMDHAKFAEAAGGKGYTIKSASEVDA 512
Cdd:PRK08327 465 peaahwvAERYGLPVLVVVFNNGGWLAVKeavlevYPEGYAARKGTfpGTDFDpRPDFAKIAEAFGGYGERVEDPEELKG 544
|
....*..
gi 446985388 513 IVEEALA 519
Cdd:PRK08327 545 ALRRALA 551
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
10-543 |
1.77e-44 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 166.31 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 10 LVKALQAWDIDHLYGIPGDSIdavVDSLRTVRDQ-FKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGMY 88
Cdd:PRK09259 16 VIDALKLNGIDTIYGVVGIPI---TDLARLAQAEgIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 89 DAKMDNVPQLILSGQTNS--TALGTKAFQEA---NLQK-LCEdvAVFnhQIEKGDNVFEIVNEAIRTAYEQK--GVAVVI 160
Cdd:PRK09259 93 NATTNCFPMIMISGSSEReiVDLQQGDYEELdqlNAAKpFCK--AAF--RVNRAEDIGIGVARAIRTAVSGRpgGVYLDL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 161 cPNDLLT-----EKIKDTTNKPVDTSRPTVVSPKykDIKKAVKLINKSKKPVMLVGVGA--KQAKDELRAFIEAAKIPVV 233
Cdd:PRK09259 169 -PAKVLAqtmdaDEALTSLVKVVDPAPAQLPAPE--AVDRALDLLKKAKRPLIILGKGAayAQADEQIREFVEKTGIPFL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 234 HTLPAKTILPDDHPYSignlgkIGTKTSYqTMQDADLLIMVGTNYPYVDYLPK-----KNIKAIQIDTNPKNIGHRFNIN 308
Cdd:PRK09259 246 PMSMAKGLLPDTHPQS------AAAARSL-ALANADVVLLVGARLNWLLSHGKgktwgADKKFIQIDIEPQEIDSNRPIA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 309 VGIVGDSKIALHQLTENIKH---VAERPFLNKTLERKAVWDKWMEQDKNNNSKPLRPERLMASINQFIKDDA-VISADVG 384
Cdd:PRK09259 319 APVVGDIGSVMQALLAGLKQntfKAPAEWLDALAERKEKNAAKMAEKLSTDTQPMNFYNALGAIRDVLKENPdIYLVNEG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 385 TATvwstryLNLGVN--------NKFIISSWlGTMGCGLPGAMASKIAyPNRQAIAIAGDGAFQMVMQDFATAVQYDLPL 456
Cdd:PRK09259 399 ANT------LDLARNiidmykprHRLDCGTW-GVMGIGMGYAIAAAVE-TGKPVVAIEGDSAFGFSGMEVETICRYNLPV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 457 TVFVLNNKQLafikY---EQQAAGELEYAVDFSDMD--HAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVD 531
Cdd:PRK09259 471 TVVIFNNGGI----YrgdDVNLSGAGDPSPTVLVHHarYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLINVVID 546
|
570
....*....|..
gi 446985388 532 PNAAPLPGKIVN 543
Cdd:PRK09259 547 PAAGTESGHITN 558
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
19-536 |
2.86e-43 |
|
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: 162.25 E-value: 2.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 19 IDHLYGIPGDSI----DAVVDslrtvRDQFKFYHVRHEEVASLAAAGYTKLTGkIGVALSIGGPGLIHLLNGMYDAKMDN 94
Cdd:COG3961 20 IRHIFGVPGDYNlpflDAIEA-----HPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 95 VPQLILSGQTNSTA----------LGTKAFQeaNLQKLCEDVAVFNHQIEKGDNVFEIvNEAIRTA-YEQKGVAVVIcPn 163
Cdd:COG3961 94 VPVVHIVGAPGTRAqrrgpllhhtLGDGDFD--HFLRMFEEVTVAQAVLTPENAAAEI-DRVLAAAlREKRPVYIEL-P- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 164 dlltekiKDTTNKPVD-TSRPTVVSPKYKD-------IKKAVKLINKSKKPVMLVGVGAK--QAKDELRAFIEAAKIPVV 233
Cdd:COG3961 169 -------RDVADAPIEpPEAPLPLPPPASDpaalaaaVAAAAERLAKAKRPVILAGVEVHrfGLQEELLALAEKTGIPVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 234 HTLPAKTILPDDHPYSIGN-LGKIGTKTSYQTMQDADLLIMVGTNYpyVDY--------LPKKNIkaIQIDTNPKNIGHR 304
Cdd:COG3961 242 TTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGVVF--TDTntggftaqLDPERT--IDIQPDSVRVGGH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 305 FNINVGIvGDSKIALHQLTEniKHVAERPFLNKTlerkavwdkwMEQDKNNNSKPLRPERLMASINQFIKDDAVISADVG 384
Cdd:COG3961 318 IYPGVSL-ADFLEALAELLK--KRSAPLPAPAPP----------PPPPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 385 TATVWSTRyLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNK 464
Cdd:COG3961 385 TSLFGAAD-LRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNND 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446985388 465 qlafiKY--EQQAAGELEYAVDFSDMDHAKFAEAAGGK---GYTIKSASEVDAIVEEALA-QDVPTIVDVYVDPNAAP 536
Cdd:COG3961 464 -----GYtiERAIHGPDGPYNDIANWDYAKLPEAFGGGnalGFRVTTEGELEEALAAAEAnTDRLTLIEVVLDKMDAP 536
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
193-322 |
2.97e-42 |
|
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: 148.10 E-value: 2.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 193 IKKAVKLINKSKKPVMLVGVGAK--QAKDELRAFIEAAKIPVVHTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADL 270
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRrsGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446985388 271 LIMVGTNY-------PYVDYLPKKNIkaIQIDTNPKNIGHRFNINVGIVGDSKIALHQL 322
Cdd:pfam00205 81 VLAVGARFddirttgKLPEFAPDAKI--IHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
362-531 |
4.12e-42 |
|
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: 149.36 E-value: 4.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 362 PERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQM 441
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 442 VMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQD 521
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
170
....*....|
gi 446985388 522 VPTIVDVYVD 531
Cdd:cd02010 161 GVHVIDCPVD 170
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-162 |
2.03e-40 |
|
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: 143.83 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLRtvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGM 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALA--RSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446985388 88 YDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAY-EQKGVAVVICP 162
Cdd:cd07035 79 ANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALsGRPGPVALDLP 154
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
193-532 |
1.83e-39 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 443162 [Multi-domain] Cd Length: 622 Bit Score: 152.59 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 193 IKKAVKLINKSKKPVMLVGVGAK--QAKDELRAFIEAAKIPVVHTLPAKTILPDDHPYSIGNLGKIGTKTSYQTMQDADL 270
Cdd:COG3962 220 LARAVELIRAAKRPLIIAGGGVRysEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLGGIGVTGTLAANALAAEADL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 271 LIMVGTNYPyvdylpkknikaiqiD------TNPKNIGHRF-NINVG-----------IVGDSKIALHQLTENIK-HVAE 331
Cdd:COG3962 300 VIGVGTRLQ---------------DfttgskTLFANPDVRFvNINVArfdaykhdalpVVADAREGLEALTEALAgWRYP 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 332 RPFLNKTLERKAVWDKWME--QDKNNNSKPLRPERLMAsINQFIKDDAVIsadVGTA--------TVWSTRYLNlGVNNK 401
Cdd:COG3962 365 AAWTDEAAELKAEWDAEVDrlYAPTNGGLPTQAQVIGA-VNEAAGPDDIV---VCAAgslpgdlhKLWRTRDPG-TYHVE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 402 FIISswlgTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAG---- 477
Cdd:COG3962 440 YGYS----CMGYEIAGGLGVKLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKIIVVLLDNHGFGCINRLQMSTGsqsf 515
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 478 --ELEY-------------AVDFsdmdhAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDP 532
Cdd:COG3962 516 gtELRDrdtetgrldggllPVDF-----AANAASLGAKAYRVTTIAELRAALERAKAADRTTVIVIKTDP 580
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
8-170 |
1.72e-38 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 139.29 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLRTvRDQFKFYHVRHEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLLNGM 87
Cdd:pfam02776 3 EALADVLKALGVDTVFGVPGGHILPLLDALAK-SPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 88 YDAKMDNVPQLILSGQTNSTALGTKAFQ-EANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTA-YEQKGVAVVICPNDL 165
Cdd:pfam02776 82 ANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAAlSGRPGPVYLEIPLDV 161
|
....*
gi 446985388 166 LTEKI 170
Cdd:pfam02776 162 LLEEV 166
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
362-531 |
1.08e-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: 123.41 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 362 PERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQM 441
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 442 VMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQ--AAGELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALA 519
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQlsYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 446985388 520 QDVPTIVDVYVD 531
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
359-534 |
7.41e-26 |
|
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: 104.90 E-value: 7.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 359 PLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGA 438
Cdd:cd02013 3 PMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 439 FQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQ-------AAGELEyavdfsDMDHAKFAEAAGGKGYTIKSASEVD 511
Cdd:cd02013 83 WGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVdfynnrfVGTELE------SESFAKIAEACGAKGITVDKPEDVG 156
|
170 180
....*....|....*....|....*.
gi 446985388 512 AIVEEALA---QDVPTIVDVYVDPNA 534
Cdd:cd02013 157 PALQKAIAmmaEGKTTVIEIVCDQEL 182
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
359-536 |
1.48e-24 |
|
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: 100.69 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 359 PLRPERLMASINQFIKDDAVISADVGTATvWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGA 438
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTSW-FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 439 FQMVMQDFATAVQYDLPLTVFVLNNKqlafiKY--EQQAAGELEYAVDFSDMDHAKFAEA----AGGKGYTIKSASEVDA 512
Cdd:cd02005 80 FQMTVQELSTMIRYGLNPIIFLINND-----GYtiERAIHGPEASYNDIANWNYTKLPEVfgggGGGLSFRVKTEGELDE 154
|
170 180
....*....|....*....|....*
gi 446985388 513 IVEEALAQ-DVPTIVDVYVDPNAAP 536
Cdd:cd02005 155 ALKDALFNrDKLSLIEVILPKDDAP 179
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
9-162 |
1.51e-24 |
|
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: 99.73 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 9 ALVKALQAWDIDHLYGIPGDSIDAVVDSLRtVRDQFKFYHVRHEEVASLAAAGYTKLTGKiGVALSIGGPGLIHLLNGMY 88
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALR-EGDKRIIDTVIHELGAAGAAAGYARAGGP-PVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446985388 89 DAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKGVAVVICP 162
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLP 153
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
360-530 |
9.78e-23 |
|
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: 95.35 E-value: 9.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 360 LRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNkfiisSWLGT----MGCGLPGAMASKIAYPNRQAIAIAG 435
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPG-----SYFTLrgggLGWGLPAAVGAALANPDRKVVAIIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 436 DGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKYEQQ------AAGELEYAVDFSD--MDHAKFAEAAGGKGYTIKSA 507
Cdd:cd02002 76 DGSFMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKrvgpegPGENAPDGLDLLDpgIDFAAIAKAFGVEAERVETP 155
|
170 180
....*....|....*....|...
gi 446985388 508 SEVDAIVEEALAQDVPTIVDVYV 530
Cdd:cd02002 156 EELDEALREALAEGGPALIEVVV 178
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
203-531 |
2.20e-19 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 91.56 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 203 SKKPVMLVG--VGAKQAKDELRAFIEAAKIPV-VHTLPAKTILPDDHPYSIGNLGKIGTKTSyQTMQDADLLIMVG---- 275
Cdd:PRK07092 206 ARRPALVVGpaVDRAGAWDDAVRLAERHRAPVwVAPMSGRCSFPEDHPLFAGFLPASREKIS-ALLDGHDLVLVIGapvf 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 276 TNYPYV--DYLPKkNIKAIQIDTNPkNIGHRFNINVGIVGDSKIALHQLTENIKHVAeRPflnkTLERKAVWDKWMEQdk 353
Cdd:PRK07092 285 TYHVEGpgPHLPE-GAELVQLTDDP-GEAAWAPMGDAIVGDIRLALRDLLALLPPSA-RP----APPARPMPPPAPAP-- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 354 nnnSKPLRPERLMASINQFIKDDAVISADV-GTATVWSTRYLNLGVNNKFIISSwlGTMGCGLPGAMASKIAYPNRQAIA 432
Cdd:PRK07092 356 ---GEPLSVAFVLQTLAALRPADAIVVEEApSTRPAMQEHLPMRRQGSFYTMAS--GGLGYGLPAAVGVALAQPGRRVIG 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 433 IAGDGAFQMVMQDFATAVQYDLPLTVFVLNNKQLAFIkyeQQAAGELEYA----VDFSDMDHAKFAEAAGGKGYTIKSAS 508
Cdd:PRK07092 431 LIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGAL---RWFAPVFGVRdvpgLDLPGLDFVALARGYGCEAVRVSDAA 507
|
330 340
....*....|....*....|...
gi 446985388 509 EVDAIVEEALAQDVPTIVDVYVD 531
Cdd:PRK07092 508 ELADALARALAADGPVLVEVEVA 530
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
369-540 |
6.62e-19 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 85.43 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 369 INQFIKDDAVISADVGT-----ATVWSTRYLNlGVNNKFIISswlgTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVM 443
Cdd:cd02003 8 LNEAIGDDDVVINAAGSlpgdlHKLWRARTPG-GYHLEYGYS----CMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 444 QDFATAVQYDLPLTVFVLNNKQLAFIKYEQQAAGELEYAVDFSDMDH--------------AKFAEAAGGKGYTIKSASE 509
Cdd:cd02003 83 SEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGTEFRDRDQesgqldgallpvdfAANARSLGARVEKVKTIEE 162
|
170 180 190
....*....|....*....|....*....|.
gi 446985388 510 VDAIVEEALAQDVPTIVDVYVDPNAAPLPGK 540
Cdd:cd02003 163 LKAALAKAKASDRTTVIVIKTDPKSMTPGYG 193
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
359-531 |
3.26e-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: 80.40 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 359 PLRPERLMASINQFIKDDAVISADVGTATVWSTRYLNLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGA 438
Cdd:cd02006 7 PIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 439 FQMVMQDFATAVQYDLPLTVFVLNNKQLAFIKyEQQAAGELEYAVDFS------------DMDHAKFAEAAGGKGYTIKS 506
Cdd:cd02006 87 FQFMIEELAVGAQHRIPYIHVLVNNAYLGLIR-QAQRAFDMDYQVNLAfeninsselggyGVDHVKVAEGLGCKAIRVTK 165
|
170 180
....*....|....*....|....*....
gi 446985388 507 ASEVDAIVEEALA----QDVPTIVDVYVD 531
Cdd:cd02006 166 PEELAAAFEQAKKlmaeHRVPVVVEAILE 194
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
55-463 |
4.81e-17 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 84.37 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 55 ASLAAAGYTKLTGkIG---VALSIGGpglIHLLNGMYDAKMDNVPQLILSGQTNSTALGT-----------------KAF 114
Cdd:PLN02573 66 AGYAADGYARARG-VGacvVTFTVGG---LSVLNAIAGAYSENLPVICIVGGPNSNDYGTnrilhhtiglpdfsqelRCF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 115 QEANlqklCEDvAVFNHQiekgDNVFEIVNEAIRTAY-EQKGVAVVICPNdLLTEKIKDTTNKPVdtsrPTVVSPKYKD- 192
Cdd:PLN02573 142 QTVT----CYQ-AVINNL----EDAHELIDTAISTALkESKPVYISVSCN-LAAIPHPTFSREPV----PFFLTPRLSNk 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 193 ------IKKAVKLINKSKKPVMLVGVGAKQAKDElRAFIE---AAKIPVVHTLPAKTILPDDHPYSIGNL-GKIGTKTSY 262
Cdd:PLN02573 208 msleaaVEAAAEFLNKAVKPVLVGGPKLRVAKAC-KAFVEladASGYPVAVMPSAKGLVPEHHPHFIGTYwGAVSTPFCA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 263 QTMQDADLLIMVG---TNYPYVDY--LPKKNiKAIQIDTNPKNIGHRFNINVGIVGDskiALHQLTENIKHvaerpflNK 337
Cdd:PLN02573 287 EIVESADAYLFAGpifNDYSSVGYslLLKKE-KAIIVQPDRVTIGNGPAFGCVLMKD---FLEALAKRVKK-------NT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 338 T----LERKAVWDKwmEQDKNNNSKPLRPERLMASINQFIKDDAVISADVGTAtvW-STRYLNLGVNNKFIISSWLGTMG 412
Cdd:PLN02573 356 TayenYKRIFVPEG--EPLKSEPGEPLRVNVLFKHIQKMLSGDTAVIAETGDS--WfNCQKLKLPEGCGYEFQMQYGSIG 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446985388 413 CGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLTVFVLNN 463
Cdd:PLN02573 432 WSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINN 482
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
8-530 |
1.81e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 63.35 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDS---IDAVVDSLRTVRDQFKFYhvrhEEVASLAAAGYTKLTGKIGVALSIGGPGLIHLL 84
Cdd:PRK12474 9 DSVVDTLLNCGVEVCFANPGTSemhFVAALDRVPRMRPVLCLF----EGVVTGAADGYGRIAGKPAVTLLHLGPGLANGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 85 NGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQK-GVAVVICPN 163
Cdd:PRK12474 85 ANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPgGIATLIMPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 164 DLLTEKIKDTTNKPVDTSRPTVVSPKYKDIKKAVKliNKSKKPVMLVGVGAKQAKDELRAFIEA---------------- 227
Cdd:PRK12474 165 DVAWNEAAYAAQPLRGIGPAPVAAETVERIAALLR--NGKKSALLLRGSALRGAPLEAAGRIQAktgvrlycdtfaprie 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 228 --------AKIPVVHtlpaktilpddhpysignlgKIGTKTsyqtMQDADLLIMVGTNYP--YVDYLPKKNIKAIQidtn 297
Cdd:PRK12474 243 rgagrvpiERIPYFH--------------------EQITAF----LKDVEQLVLVGAKPPvsFFAYPGKPSWGAPP---- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 298 pkniGHRFNINVGIVGDSKIALHQLTENIKHVAErPflnKTLERKAVWDkwMEQDKNNnskplrperlMASINQFIK--- 374
Cdd:PRK12474 295 ----GCEIVYLAQPDEDLAQALQDLADAVDAPAE-P---AARTPLALPA--LPKGALN----------SLGVAQLIAhrt 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 375 -DDAVISADVGTATVWSTRYLNLGVNNKFI-ISSwlGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQY 452
Cdd:PRK12474 355 pDQAIYADEALTSGLFFDMSYDRARPHTHLpLTG--GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 453 DLPLTVFVLNNKQLAFIKYEQQAAG--------ELEYAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPT 524
Cdd:PRK12474 433 NLDVTVVIFANRSYAILNGELQRVGaqgagrnaLSMLDLHNPELNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPR 512
|
....*.
gi 446985388 525 IVDVYV 530
Cdd:PRK12474 513 LIEAMI 518
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
8-530 |
2.41e-09 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 59.86 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDSIDAVVDSLRTVRDqfkfyhVR-----HEEVASLAAAGYTKLTGKIGVALSIGGPGLIH 82
Cdd:PRK07586 5 ESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPG------MRcvlglFEGVATGAADGYARMAGKPAATLLHLGPGLAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 83 LLNGMYDAKMDNVPQLILSGQTNSTALGTKAFQEANLQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQKG-VAVVIC 161
Cdd:PRK07586 79 GLANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGqVATLIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 162 PNDLLTEKIkDTTNKPVDTSRPTVVSPKykDIKKAVKLINKSKKPVMLVGVGAKQAkDELRAfieAAKIPvvhtlpAKT- 240
Cdd:PRK07586 159 PADVAWSEG-GPPAPPPPAPAPAAVDPA--AVEAAAAALRSGEPTVLLLGGRALRE-RGLAA---AARIA------AATg 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 241 --ILPDDHPYSI---GNLGKIgTKTSY------QTMQDADLLIMVGTNYP--YVDYLPKKNIKAIQiDTNPKNIGHRFNi 307
Cdd:PRK07586 226 arLLAETFPARMergAGRPAV-ERLPYfaeqalAQLAGVRHLVLVGAKAPvaFFAYPGKPSRLVPE-GCEVHTLAGPGE- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 308 nvgivgDSKIALHQLTENIKHVAERPFLnKTLERKAVwdkwmeqdknnNSKPLRPERLMASINQFIKDDAVISADVGT-- 385
Cdd:PRK07586 303 ------DAAAALEALADALGAKPAAPPL-AAPARPPL-----------PTGALTPEAIAQVIAALLPENAIVVDESITsg 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 386 -----ATVWSTR--YLNL-GvnnkfiisswlGTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLPLT 457
Cdd:PRK07586 365 rgffpATAGAAPhdWLTLtG-----------GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVT 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 458 VFVLNNKQLAFIKYEQQAAGELE--------YAVDFSDMDHAKFAEAAGGKGYTIKSASEVDAIVEEALAQDVPTIVDVY 529
Cdd:PRK07586 434 TVIFANRAYAILRGELARVGAGNpgpraldmLDLDDPDLDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHLIEAV 513
|
.
gi 446985388 530 V 530
Cdd:PRK07586 514 V 514
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
8-154 |
2.63e-07 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 50.57 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 8 EALVKALQAWDIDHLYGIPGDS----IDAVVDSlrtvrDQFKFYHVRHEEVASLAAAGYTKLTGkIGVALSIGGPGLIHL 83
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYnlplLDAIEEN-----PGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 84 LNGMYDAKMDNVPQLILSGQTNSTA----------LGTKAFQEAnlQKLCEDVAVFNHQIEKGDNVFEIVNEAIRTAYEQ 153
Cdd:cd07038 75 LNGIAGAYAEHVPVVHIVGAPSTKAqasglllhhtLGDGDFDVF--LKMFEEITCAAARLTDPENAAEEIDRVLRTALRE 152
|
.
gi 446985388 154 K 154
Cdd:cd07038 153 S 153
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
408-531 |
1.97e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 45.98 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 408 LGTMGCGLPGAMASKIAYPNRQAIAIAGDGAfqMVMQDFATAvqydlplTVFVLNNKQLAFIKYE----QQAAGELEYAV 483
Cdd:PRK06163 56 LGSMGLAFPIALGVALAQPKRRVIALEGDGS--LLMQLGALG-------TIAALAPKNLTIIVMDngvyQITGGQPTLTS 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446985388 484 DFSDMdhAKFAEAAG-GKGYTIKSASEVDAIVEEALAQDVPTIVDVYVD 531
Cdd:PRK06163 127 QTVDV--VAIARGAGlENSHWAADEAHFEALVDQALSGPGPSFIAVRID 173
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
409-547 |
3.75e-05 |
|
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: 44.61 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 409 GTMGCGLPGAMASKIAYPNRQAIAIAGDGAFQMVMQDFATAVQYDLP-LTVFVLNNKqlafiKYE----QQAAGeleyav 483
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPAnLIHIVLNNG-----AHDsvggQPTVS------ 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 484 dfSDMDHAKFAEAAG-GKGYTIKSASEVDAIVEEALAQDVPTIVDVYVDPNAAPLPGK-----IVNEEAF 547
Cdd:cd03371 117 --FDVSLPAIAKACGyRAVYEVPSLEELVAALAKALAADGPAFIEVKVRPGSRSDLGRpttspIENKERF 184
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
359-534 |
3.16e-04 |
|
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: 43.11 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 359 PLRPERLMASINQFIKDDAVISAdvgtaTVWSTRYL-------NLGVNNKFIIsswLGTMGCGLPGAMASKIAYPNRQAI 431
Cdd:TIGR03297 172 MTREEAIAAILDHLPDNTVIVST-----TGKTSRELyelrdriGQGHARDFLT---VGSMGHASQIALGLALARPDQRVV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 432 AIAGDGAFQMVMQDFATAVQYDLP-LTVFVLNNKqlafiKYEqQAAGELEYAVDFsdmDHAKFAEAAG-GKGYTIKSASE 509
Cdd:TIGR03297 244 CLDGDGAALMHMGGLATIGTQGPAnLIHVLFNNG-----AHD-SVGGQPTVSQHL---DFAQIAKACGyAKVYEVSTLEE 314
|
170 180
....*....|....*....|....*
gi 446985388 510 VDAIVEEALAQDVPTIVDVYVDPNA 534
Cdd:TIGR03297 315 LETALTAASSANGPRLIEVKVRPGS 339
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
362-463 |
5.59e-03 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 38.03 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985388 362 PERLM-ASINQFIKDDAVISADVGTATvwstrylnLGVNNKFIISSWLGTMGCGLPGAMASKIAYPNRQAIAIAGDGAF- 439
Cdd:cd02008 11 PHRPSfYALRKAFKKDSIVSGDIGCYT--------LGALPPLNAIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTFf 82
|
90 100
....*....|....*....|....
gi 446985388 440 QMVMQDFATAVQYDLPLTVFVLNN 463
Cdd:cd02008 83 HSGILGLINAVYNKANITVVILDN 106
|
|
| |
