|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
1-572 |
0e+00 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 1182.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK09124 1 MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVVLP 160
Cdd:PRK09124 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVVLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 161 GDVALKAAPESASSHWYHAPLPTVTPAEEELRKLVQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPIVHALRGKEHV 240
Cdd:PRK09124 161 GDVALKPAPERATPHWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRGKEHV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 241 EYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKALL 320
Cdd:PRK09124 241 EYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKATLAALL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 321 PLLEEKTDRHFLDKALEHYRDARKGLDDLAKPSD--KAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRR 398
Cdd:PRK09124 321 PLLEEKTDRKFLDKALEHYRKARKGLDDLAVPSDggKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 399 LLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTD 478
Cdd:PRK09124 401 LLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMKAGGYLTD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 479 GTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGR 558
Cdd:PRK09124 481 GTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMPPQIKLEQAKGFSLYMLRAIISGR 560
|
570
....*....|....
gi 364517351 559 GDEVIELAKTNWLR 572
Cdd:PRK09124 561 GDEVIELAKTNWLR 574
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-572 |
0e+00 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 760.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK06546 1 MAKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVVLP 160
Cdd:PRK06546 81 LINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGGGVSVVTLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 161 GDVALKAAPESASSHWYHAPLPTVTPAEEELRKLVQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPIVHALRGKEHV 240
Cdd:PRK06546 161 GDIADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGKEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 241 EYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAFYPtDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKALL 320
Cdd:PRK06546 241 QYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFPYDQFLP-DVRTAQVDIDPEHLGRRTRVDLAVHGDVAETIRALL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 321 PLLEEKTDRHFLDKAL-EHYRDARKGLDDLAKPSDK--AIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKR 397
Cdd:PRK06546 320 PLVKEKTDRRFLDRMLkKHARKLEKVVGAYTRKVEKhtPIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 398 RLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLT 477
Cdd:PRK06546 400 RVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMLVDGLPD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 478 DGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISG 557
Cdd:PRK06546 480 FGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTDPNALSIPPTITGEQVKGFALAASKTVLNG 559
|
570
....*....|....*
gi 364517351 558 RGDEVIELAKTNwLR 572
Cdd:PRK06546 560 GVGEMVDMARSN-LR 573
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
1-539 |
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: 554.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVSVVVL 159
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRpGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 160 PGDVALKAAPESASSHWYHAPLPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALRGK 237
Cdd:COG0028 161 PKDVQAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGArrAGAAEELRALAERLGAPVVTTLMGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 238 EHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYR------AFYPtDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:COG0028 241 GAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRvtgnwdEFAP-DAKIIHIDIDPAEIGKNYPVDLPIVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 312 IKSTLKALLPLLEEKTDRHflDKALEHYRDARKGLDDLAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYL 391
Cdd:COG0028 320 AKAVLAALLEALEPRADDR--AAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 392 KMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMK 471
Cdd:COG0028 398 RFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 364517351 472 A-GGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIPPQIK 539
Cdd:COG0028 478 LfYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENPPGATLD 546
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-555 |
2.21e-164 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 480.27 E-value: 2.21e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM-GTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08611 2 AKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVVL 159
Cdd:PRK08611 82 HLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVLTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 160 PGDV---ALKAAPESASSHWyhaPLPTVTPAEEELRKLVQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPIVHALRG 236
Cdd:PRK08611 162 PDDLpaqKIKDTTNKTVDTF---RPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 237 KEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTL 316
Cdd:PRK08611 239 KGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYVDYLPKKAKAIQIDTDPANIGKRYPVNVGLVGDAKKAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 317 KALLPLLEEKTDRHFLDKALEHYRDARKGLD-DLAKPSDkAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNG 395
Cdd:PRK08611 319 HQLTENIKHVEDRRFLEACQENMAKWWKWMEeDENNAST-PIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNLGT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 396 KRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGY 475
Cdd:PRK08611 398 NQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 476 LTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAII 555
Cdd:PRK08611 478 LEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAPLPGKIVNDEALGYSKWAIKSLF 557
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-558 |
9.30e-137 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 408.45 E-value: 9.30e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLnRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAI-RKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVVLPGDV 163
Cdd:PRK06457 82 GLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINLPVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 164 aLKAAPESASSHWYHAPLPTVTPaeeELRKLVQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPIVHALRGKEHVEYD 243
Cdd:PRK06457 162 -LRKSSEYKGSKNTEVGKVKYSI---DFSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 244 NPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKallPLL 323
Cdd:PRK06457 238 DPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLN---IDI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 324 EEKTDRhFLDKALEHYRDARKGLDDLAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSF 403
Cdd:PRK06457 315 EEKSDK-FYEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 404 NHGSMANAMPQAIGAK-ATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGTEL 482
Cdd:PRK06457 394 WLGSMGIGVPGSVGASfAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMGYPEWGVDL 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 364517351 483 HDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGR 558
Cdd:PRK06457 474 YNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMPPKLTFKQAGEYVLSIFREKLEGI 549
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-570 |
6.23e-122 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 371.94 E-value: 6.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM-GTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08273 1 MSQTVADFILERLREWGVRRVFGYPGDGINGLLGALGRAdDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSH-YCELVSTPEQIPQVLAVAMRKAVINRGVSVVV 158
Cdd:PRK08273 81 HLLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAGaFVQMVTVPEQLRHLVDRAVRTALAERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 159 LPGDVALKAAPESASSHWY-----HAPLPTVTPAEEELRKLVQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPIVHA 233
Cdd:PRK08273 161 LPNDVQELEYEPPPHAHGTvhsgvGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 234 LRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAFYPT--DAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:PRK08273 241 LLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFPYSEFLPKegQARGVQIDIDGRMLGLRYPMEVNLVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 312 IKSTLKALLPLLEEKTDRHFLDKALEHYRDARKGLDDLAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYL 391
Cdd:PRK08273 321 AAETLRALLPLLERKKDRSWRERIEKWVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADSGSCANWYARDL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 392 KMngKRRLLGSFNHG--SMANAMPQAIGAKATAPERQVVAMCGDGGFSML-MGDFLSLA----QMKLPVKIV-IFNNSVL 463
Cdd:PRK08273 401 RM--RRGMMASLSGTlaTMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAkywrQWSDPRLIVlVLNNRDL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 464 GFVAMEMKA-GG--YLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIPPQIKL 540
Cdd:PRK08273 479 NQVTWEQRVmEGdpKFEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDPNVPPLPPHITL 558
|
570 580 590
....*....|....*....|....*....|...
gi 364517351 541 EQAKGFslymLRAIISGRGDE---VIELAKTNW 570
Cdd:PRK08273 559 EQAKAF----ASALLKGDPDAggvIVQTAKQVL 587
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
6-527 |
2.40e-108 |
|
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: 336.04 E-value: 2.40e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSL-NRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLING 84
Cdd:TIGR02720 2 SAAVLKVLEAWGVDHIYGIPGGSFNSTMDALsAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 85 LFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVVLPGDVA 164
Cdd:TIGR02720 82 LYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHNGVAVVTIPVDFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 165 LKAAPE----SASSHWYHAPLPtvTPAEEELRKLVQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPIVHALRGKEHV 240
Cdd:TIGR02720 162 WQEIPDndyyASSVSYQTPLLP--APDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 241 EYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAFYPT--DAK-IIQIDINPGSIGAHSKVDMALVGDIKSTLK 317
Cdd:TIGR02720 240 EDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKAfkNTKyFIQIDIDPAKLGKRHHTDIAVLADAKKALA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 318 ALLPLLEEKTDRHFLDKALEHYRDARKGLDDLAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKR 397
Cdd:TIGR02720 320 AILAQVEPRESTPWWQANVANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 398 RLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLT 477
Cdd:TIGR02720 400 KWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQPL 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 364517351 478 DGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTA--FRTDGPVLVDVVV 527
Cdd:TIGR02720 480 IGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAkaIKQGKPVLIDAKI 531
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
3-538 |
3.49e-102 |
|
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: 319.75 E-value: 3.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 3 QTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLI 82
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 83 NGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-LPG 161
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVdLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 162 DVALKAA----PESASSHWYHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALR 235
Cdd:TIGR00118 161 DVTTAEIeypyPEKVNLPGYR---PTVKGHPLQIKKAAELINLAKKPVILVGGGViiAGASEELKELAERIQIPVTTTLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 236 GKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:TIGR00118 238 GLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRvtgnlAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 311 DIKSTLKALLPLLEEKTDRHFLD--KALEHYRdARKGLDdlAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAA 388
Cdd:TIGR00118 318 DARNVLEELLKKLFELKERKESAwlEQINKWK-KEYPLK--MDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 389 RYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVA- 467
Cdd:TIGR00118 395 QFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRq 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 364517351 468 -MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIPPQI 538
Cdd:TIGR00118 475 wQELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVA 546
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
357-533 |
1.68e-97 |
|
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: 294.05 E-value: 1.68e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 357 IHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGF 436
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 437 SMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFR 516
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALA 161
|
170
....*....|....*..
gi 364517351 517 TDGPVLVDVVVAKEELA 533
Cdd:cd02014 162 ADGPVVIDVVTDPNEPP 178
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
9-540 |
3.97e-82 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 268.16 E-value: 3.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRmGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK06276 7 IIKALEAEGVKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGIATA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-LPGDVALKA 167
Cdd:PRK06276 86 YADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIdLPKDVQEGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 168 APESASSHWYHAPLPTVTPAEE----ELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALRGKEHVE 241
Cdd:PRK06276 166 LDLEKYPIPAKIDLPGYKPTTFghplQIKKAAELIAEAERPVILAGGGViiSGASEELIELSELVKIPVCTTLMGKGAFP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 242 YDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALVGDIKST 315
Cdd:PRK06276 246 EDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTtgdissFAP-NAKIIHIDIDPAEIGKNVRVDVPIVGDAKNV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 316 LKALLPLLEEKTDRHFlDKALEHYRDARKGLDDLAKPSDKAIHPQYLAQQISHFADE-----DAIFTCDVGTPTVWAARY 390
Cdd:PRK06276 325 LRDLLAELMKKEIKNK-SEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQMWMAHF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 391 LKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAmEM 470
Cdd:PRK06276 404 FKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVY-QW 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 364517351 471 KAGGYLTDGTELH---DTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEEL--AIPPQIKL 540
Cdd:PRK06276 483 QNLYYGKRQSEVHlgeTPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAlpMVPPGGNL 557
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
2-535 |
1.96e-79 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 260.48 E-value: 1.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 2 KQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:PRK06048 7 KMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD-LRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-LP 160
Cdd:PRK06048 86 VTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIdLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 161 GDVALKAA----PESASSHWYHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHAL 234
Cdd:PRK06048 166 KDVTTAEIdfdyPDKVELRGYK---PTYKGNPQQIKRAAELIMKAERPIIYAGGGVisSNASEELVELAETIPAPVTTTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 235 RGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYR------AFYPtDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK06048 243 MGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRvtgklaSFAP-NAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 309 VGDIKSTLKALLPLLEEKTDRHFLDKALEHyrdaRKGLDDLAKPSDKAIHPQYLAQQISHFAdEDAIFTCDVGTPTVWAA 388
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDRKEWLDKINQW----KKEYPLKYKEREDVIKPQYVIEQIYELC-PDAIIVTEVGQHQMWAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 389 RYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVA- 467
Cdd:PRK06048 397 QYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRq 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 364517351 468 -MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIP 535
Cdd:PRK06048 477 wQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSP 545
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
4-166 |
6.03e-78 |
|
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: 243.23 E-value: 6.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVVLPGDV 163
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKRGVAVLILPGDV 160
|
...
gi 364517351 164 ALK 166
Cdd:cd07039 161 QDA 163
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
1-531 |
2.87e-72 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 242.65 E-value: 2.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM---GTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPG 77
Cdd:PRK07418 17 QRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAeaeGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 78 NLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVV 157
Cdd:PRK07418 97 ATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 158 V-LPGDVALK------AAPESASSHWYHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKA 228
Cdd:PRK07418 177 IdIPKDVGQEefdyvpVEPGSVKPPGYR---PTVKGNPRQINAALKLIEEAERPLLYVGGGAisAGAHAELKELAERFQI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 229 PIVHALRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRA------FYPTdAKIIQIDINPGSIGAHS 302
Cdd:PRK07418 254 PVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVtgkldeFASR-AKVIHIDIDPAEVGKNR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 303 KVDMALVGDIKSTLKALLPLLEEKTDRHFLDKALEHYRDARKGLDDLAKPSDKAIHPQYLAQQISHFAdEDAIFTCDVGT 382
Cdd:PRK07418 333 RPDVPIVGDVRKVLVKLLERSLEPTTPPRTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLA-PDAYYTTDVGQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 383 PTVWAARYLKmNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSV 462
Cdd:PRK07418 412 HQMWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGW 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 463 LGFV-------------AMEMKAGgyltdgtelhDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAK 529
Cdd:PRK07418 491 QGMVrqwqesfygerysASNMEPG----------MPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRR 560
|
..
gi 364517351 530 EE 531
Cdd:PRK07418 561 DE 562
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-535 |
1.28e-71 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 239.62 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-L 159
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIdI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 160 PGDVALKAA----PESASSHWYHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHA 233
Cdd:PRK08527 161 PKDVTATLGefeyPKEISLKTYK---PTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAilSNASEEIRELVKKTGIPAVET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 234 LRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAFYPTD-----AKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK08527 238 LMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSefakhAKIIHVDIDPSSISKIVNADYPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 309 VGDIKSTLKALLPLLEEKTDRHFlDKALEHYRDARKgLDDLA-KPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVWA 387
Cdd:PRK08527 318 VGDLKNVLKEMLEELKEENPTTY-KEWREILKRYNE-LHPLSyEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 388 ARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFV- 466
Cdd:PRK08527 396 AQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVr 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 364517351 467 ---AMEMKAGGYLTDGTELHDtnFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIP 535
Cdd:PRK08527 476 qwqTFFYEERYSETDLSTQPD--FVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLP 545
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
4-535 |
1.96e-69 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 235.26 E-value: 1.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK07789 32 TGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQE------THPqelfreCSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVV 157
Cdd:PRK07789 112 PIADANMDSVPVVAITGQVGRGLIGTDAFQEadivgiTMP------ITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 158 VlpgDVALKAAPESASSHW--------YHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIK 227
Cdd:PRK07789 186 V---DIPKDALQAQTTFSWpprmdlpgYR---PVTKPHGKQIREAAKLIAAARRPVLYVGGGVirAEASAELRELAELTG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 228 APIVHALRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYR------AFYPtDAKIIQIDINPGSIGAH 301
Cdd:PRK07789 260 IPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRvtgkldSFAP-DAKVIHADIDPAEIGKN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 302 SKVDMALVGDIKSTLKALLPLLEektdRHFLDKALEHYRDARKGLDDL--------AKPSDKAIHPQYLAQQISHFADED 373
Cdd:PRK07789 339 RHADVPIVGDVKEVIAELIAALR----AEHAAGGKPDLTAWWAYLDGWretyplgyDEPSDGSLAPQYVIERLGEIAGPD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 374 AIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPV 453
Cdd:PRK07789 415 AIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPI 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 454 KIVIFNNSVLGFVAMEMK---AGGYltDGTELHD-----TNFARIAEACGIKGIRVEKASEVDEALQTAFRT-DGPVLVD 524
Cdd:PRK07789 495 KVALINNGNLGMVRQWQTlfyEERY--SNTDLHThshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAInDRPVVID 572
|
570
....*....|.
gi 364517351 525 VVVAKEELAIP 535
Cdd:PRK07789 573 FVVGKDAMVWP 583
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-535 |
1.96e-68 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 231.14 E-value: 1.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08155 11 KRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-L 159
Cdd:PRK08155 91 LVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIdI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 160 PGDV-----ALKAAPESAsshwyhAPLPTVTPAEEELRKLVQLIRYSSNIALMCGSG--CAGAHQELVEFAAKIKAPIVH 232
Cdd:PRK08155 171 PKDVqtaviELEALPAPA------EKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGviNSGAPARARELAEKAQLPTTM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 233 ALRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDM 306
Cdd:PRK08155 245 TLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAigkteqFCP-NAKIIHVDIDRAELGKIKQPHV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 307 ALVGDIKSTLKALLPLLeEKTDRHfldKALEHYRDARKGLDDLAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVW 386
Cdd:PRK08155 324 AIQADVDDVLAQLLPLV-EAQPRA---EWHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQHQMW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 387 AARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFV 466
Cdd:PRK08155 400 TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLV 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 364517351 467 --AMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIP 535
Cdd:PRK08155 480 hqQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYP 550
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
13-535 |
4.80e-68 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 230.78 E-value: 4.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 13 LEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDCHRNH 92
Cdd:PLN02470 23 LEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGLADALLDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 93 VPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-LPGDVALK-AAP- 169
Cdd:PLN02470 103 VPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVdIPKDIQQQlAVPn 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 170 --ESASSHWYHAPLPTVtPAEEELRKLVQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPIVHALRGKEHVEYDNPYD 247
Cdd:PLN02470 183 wnQPMKLPGYLSRLPKP-PEKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGLGAFPASDELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 248 VGMTGLIGFASGFHTMMNADTLILLGTQFPYR------AFyPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKALLP 321
Cdd:PLN02470 262 LQMLGMHGTVYANYAVDSADLLLAFGVRFDDRvtgkleAF-ASRASIVHIDIDPAEIGKNKQPHVSVCADVKLALQGLNK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 322 LLEEKTDRHFLDKALEHYRDARKGLDDLAKPS-DKAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLL 400
Cdd:PLN02470 341 LLEERKAKRPDFSAWRAELDEQKEKFPLSYPTfGDAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 401 GSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAM-------EMKAG 473
Cdd:PLN02470 421 TSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQwedrfykANRAH 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 364517351 474 GYLTDGTELHDT--NFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIP 535
Cdd:PLN02470 501 TYLGDPDAEAEIfpDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLP 564
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
1-531 |
9.00e-68 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 229.97 E-value: 9.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSL---NRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPG 77
Cdd:CHL00099 8 REKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 78 NLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVV 157
Cdd:CHL00099 88 ATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 158 V-LPGDVALKAAPesasshwYHAPLP------------TVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEF 222
Cdd:CHL00099 168 IdIPKDVGLEKFD-------YYPPEPgntiikilgcrpIYKPTIKRIEQAAKLILQSSQPLLYVGGGAiiSDAHQEITEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 223 AAKIKAPIVHALRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAF-----YPTDAKIIQIDINPGS 297
Cdd:CHL00099 241 AELYKIPVTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTgkldeFACNAQVIHIDIDPAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 298 IGAHSKVDMALVGDIKSTLKALLPLLeeKTDRHFLDKalEHYRDARKGLDD-------LAKPSDKAIHPQYLAQQISHFA 370
Cdd:CHL00099 321 IGKNRIPQVAIVGDVKKVLQELLELL--KNSPNLLES--EQTQAWRERINRwrkeyplLIPKPSTSLSPQEVINEISQLA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 371 dEDAIFTCDVGTPTVWAARYLKMnGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMK 450
Cdd:CHL00099 397 -PDAYFTTDVGQHQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 451 LPVKIVIFNNSVLGFVAM-------EMKAGGYLTDGTelhdTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLV 523
Cdd:CHL00099 475 LPIKIIIINNKWQGMVRQwqqafygERYSHSNMEEGA----PDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLI 550
|
....*...
gi 364517351 524 DVVVAKEE 531
Cdd:CHL00099 551 DCQVIEDE 558
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
4-535 |
2.37e-67 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 228.70 E-value: 2.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06725 16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVSVVVLPGD 162
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRpGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 163 VALKAA----PESASSHWYHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALRG 236
Cdd:PRK06725 175 VQNEKVtsfyNEVVEIPGYK---PEPRPDSMKLREVAKAISKAKRPLLYIGGGVihSGGSEELIEFARENRIPVVSTLMG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 237 KEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK06725 252 LGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVtgklelFSP-HSKKVHIDIDPSEFHKNVAVEYPVVG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 311 DIKSTLKALLPLLEEKTDRHFLDKALEHyrDARKGLDDLAKPSDkaIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARY 390
Cdd:PRK06725 331 DVKKALHMLLHMSIHTQTDEWLQKVKTW--KEEYPLSYKQKESE--LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 391 LKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVA--M 468
Cdd:PRK06725 407 YKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRqwQ 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 364517351 469 EMKAGGYLTDgTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIP 535
Cdd:PRK06725 487 EMFYENRLSE-SKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFP 552
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
9-535 |
3.03e-67 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 228.17 E-value: 3.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK07282 16 VLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITGIADA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-LPGDVALKA 167
Cdd:PRK07282 96 MSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIdLPKDVSALE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 168 APESASSHwYHAP--LPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALRGKEHVEYD 243
Cdd:PRK07282 176 TDFIYDPE-VNLPsyQPTLEPNDMQIKKILKQLSKAKKPVILAGGGInyAEAATELNAFAERYQIPVVTTLLGQGTIATS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 244 NPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKA 318
Cdd:PRK07282 255 HPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRltgnpKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKKALQM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 319 LLPLLEEKTD-RHFLDKALEHYRDARKglddlAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKR 397
Cdd:PRK07282 335 LLAEPTVHNNtEKWIEKVTKDKNRVRS-----YDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNER 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 398 RLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKA--GGY 475
Cdd:PRK07282 410 QLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESfyEGR 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 476 LTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTaFRTDGPVLVDVVVAKEELAIP 535
Cdd:PRK07282 490 TSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLEV-ITEDVPMLIEVDISRKEHVLP 548
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-535 |
3.13e-67 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 228.11 E-value: 3.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMpTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK07710 19 AQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHIL-TRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-LPGDVA 164
Cdd:PRK07710 98 ADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIdIPKDMV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 165 LkAAPESASSHWYHAP--LPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALRGKEHV 240
Cdd:PRK07710 178 V-EEGEFCYDVQMDLPgyQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVlhAKASKELTSYAEQQEIPVVHTLLGLGGF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 241 EYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKST 315
Cdd:PRK07710 257 PADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRvtgnlAYFAKEATVAHIDIDPAEIGKNVPTEIPIVADAKQA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 316 LKALLPLLEEKTDRHFLDKALehyrDARKGLDDLA-KPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMN 394
Cdd:PRK07710 337 LQVLLQQEGKKENHHEWLSLL----KNWKEKYPLSyKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 395 GKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVA--MEMKA 472
Cdd:PRK07710 413 TPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRqwQEEFY 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 364517351 473 GGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIP 535
Cdd:PRK07710 493 NQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMP 555
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
6-525 |
2.04e-65 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 223.91 E-value: 2.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQipqvLAVAMRKAV-INR----GVSVVVLP 160
Cdd:PRK06965 104 ATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRD----LAETVKKAFyIARtgrpGPVVVDIP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 161 GDVALKAA----PESASSHWYHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHAL 234
Cdd:PRK06965 180 KDVSKTPCeyeyPKSVEMRSYN---PVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVilANASRELRQLADLLGYPVTNTL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 235 RGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRA------FYPTDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK06965 257 MGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVignpahFASRPRKIIHIDIDPSSISKRVKVDIPI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 309 VGDIKSTLKALLPLLEE---KTDRHFLDKALEHYRDARKgLDDLA-KPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPT 384
Cdd:PRK06965 337 VGDVKEVLKELIEQLQTaehGPDADALAQWWKQIEGWRS-RDCLKyDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 385 VWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLG 464
Cdd:PRK06965 416 MWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLG 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 364517351 465 FVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFR-TDGPVLVDV 525
Cdd:PRK06965 496 MVRqwQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRlKDRTVFLDF 559
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
6-539 |
4.17e-64 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 220.08 E-value: 4.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-LPGDV- 163
Cdd:PRK08979 87 ATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIdLPKDCl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 164 --ALK---AAPESASSHWYHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALRG 236
Cdd:PRK08979 167 npAILhpyEYPESIKMRSYN---PTTSGHKGQIKRGLQALLAAKKPVLYVGGGAiiSGADKQILQLAEKLNLPVVSTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 237 KEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAF-----YPTDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:PRK08979 244 LGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTnnlekYCPNATILHIDIDPSSISKTVRVDIPIVGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 312 IKSTLKALLPLLEEKTDRHflDKA--------LEHYRDaRKGLDdLAKPSDKaIHPQYLAQQISHFADEDAIFTCDVGTP 383
Cdd:PRK08979 324 ADKVLDSMLALLDESGETN--DEAaiaswwneIEVWRS-RNCLA-YDKSSER-IKPQQVIETLYKLTNGDAYVASDVGQH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 384 TVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVL 463
Cdd:PRK08979 399 QMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 364517351 464 GFVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFR-TDGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK08979 479 GMVKqwQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAmKDRLVFVDINVDETEHVYPMQIR 557
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
2-535 |
1.23e-62 |
|
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: 216.27 E-value: 1.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 2 KQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAG-IRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVVLPG 161
Cdd:TIGR03457 80 VTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREMGPAQLNIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 162 DvalkaapesassHWY---HAPLPTVTP------AEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPI 230
Cdd:TIGR03457 160 D------------YFYgeiDVEIPRPVRldrgagGATSLAQAARLLAEAKFPVIISGGGVvmGDAVEECKALAERLGAPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 231 VHALRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQF-PYRA-------FYPTDAKIIQIDINPGSIGAHS 302
Cdd:TIGR03457 228 VNSYLHNDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLgPFGTlpqygidYWPKNAKIIQVDANAKMIGLVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 303 KVDMALVGDIKSTLKALLPLLEEKT--------------DRHFLDKALE---HYRDArKGLDDLAKPSDKA---IHPQYL 362
Cdd:TIGR03457 308 KVTVGICGDAKAAAAEILQRLAGKAgdanraerkakiqaERSAWEQELSemtHERDP-FSLDMIVEQRQEEgnwLHPRQV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 363 AQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGD 442
Cdd:TIGR03457 387 LRELEKAMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 443 FLSLAQMKLPVKIVIFNNSVLGfvaMEMKAGGYLTD----GTELH-DTNFARIAEACGIKGIRVEKASEVDEALQTAF-- 515
Cdd:TIGR03457 467 IMTAVRHDIPVTAVVFRNRQWG---AEKKNQVDFYNnrfvGTELEsELSFAGIADAMGAKGVVVDKPEDVGPALKKAIaa 543
|
570 580
....*....|....*....|
gi 364517351 516 RTDGPVLVDVVVAKEELAIP 535
Cdd:TIGR03457 544 QAEGKTTVIEIVCTRELGDP 563
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
64-531 |
3.86e-61 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 211.28 E-value: 3.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 64 TGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAV 143
Cdd:PRK08978 61 TGKVGVCIATSGPGATNLITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 144 AMRKAVINRGVSVVV-LPGDVALKAAPesaSSHWYHAPLPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELV 220
Cdd:PRK08978 141 AFEIASSGRPGPVLVdIPKDIQLAEGE---LEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVgmAGAVPALR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 221 EFAAKIKAPIVHALRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRA------FYPtDAKIIQIDIN 294
Cdd:PRK08978 218 EFLAATGMPAVATLKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVtgklntFAP-HAKVIHLDID 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 295 PGSIGAHSKVDMALVGDikstLKALLPLLEEKTDrhfLDKALEHYRDARKGLDDLAKPSDKAIHPQYLAQQISHFADEDA 374
Cdd:PRK08978 297 PAEINKLRQAHVALQGD----LNALLPALQQPLN---IDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADT 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 375 IFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVK 454
Cdd:PRK08978 370 VVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVK 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 455 IVIFNNSVLGFVAMEMK---AGGYltDGTELHDT-NFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKE 530
Cdd:PRK08978 450 IVLLDNQRLGMVRQWQQlffDERY--SETDLSDNpDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDEL 527
|
.
gi 364517351 531 E 531
Cdd:PRK08978 528 E 528
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-535 |
3.27e-60 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 209.85 E-value: 3.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK07525 4 MKMTPSEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAG-IRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVVLP 160
Cdd:PRK07525 83 FVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESGPAQINIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 161 GDvalkaapesassHWYH---APLPTV------TPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAP 229
Cdd:PRK07525 163 RD------------YFYGvidVEIPQPvrlergAGGEQSLAEAAELLSEAKFPVILSGAGVvlSDAIEECKALAERLDAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 230 IVHALRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQF-PYRA-------FYPTDAKIIQIDINPGSIGAH 301
Cdd:PRK07525 231 VACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLnPFGTlpqygidYWPKDAKIIQVDINPDRIGLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 302 SKVDMALVGDIKSTLKALLPLLEEKT-------DRHFLDKA-----------LEHYRDArKGLDDLAKPSDKA---IHPQ 360
Cdd:PRK07525 311 KKVSVGICGDAKAVARELLARLAERLagdagreERKALIAAeksaweqelssWDHEDDD-PGTDWNEEARARKpdyMHPR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 361 YLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLM 440
Cdd:PRK07525 390 QALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 441 GDFLSLAQMKLPVKIVIFNNSVLG-------------FVamemkaggyltdGTEL-HDTNFARIAEACGIKGIRVEKASE 506
Cdd:PRK07525 470 NEVMTAVRHNWPVTAVVFRNYQWGaekknqvdfynnrFV------------GTELdNNVSYAGIAEAMGAEGVVVDTQEE 537
|
570 580 590
....*....|....*....|....*....|.
gi 364517351 507 VDEALQTAF--RTDGPVLVDVVVAKEELAIP 535
Cdd:PRK07525 538 LGPALKRAIdaQNEGKTTVIEIMCNQELGEP 568
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
6-539 |
1.14e-59 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 208.06 E-value: 1.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06466 7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-LPGDVA 164
Cdd:PRK06466 87 ATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVdIPKDMT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 165 LKAA------PESASSHWYHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALRG 236
Cdd:PRK06466 167 NPAEkfeyeyPKKVKLRSYS---PAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVvlGNASALLTELAHLLNLPVTNTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 237 KEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK06466 244 LGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVtngpakFCP-NAKIIHIDIDPASISKTIKADIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 311 DIKSTLKALLPLLEE---KTDRHFLD---KALEHYRdARKGLDDLAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPT 384
Cdd:PRK06466 323 PVESVLTEMLAILKEigeKPDKEALAawwKQIDEWR-GRHGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 385 VWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLG 464
Cdd:PRK06466 402 MFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALG 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 364517351 465 FVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFR-TDGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK06466 482 MVRqwQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVDRSEHVYPMQIA 559
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
6-539 |
1.58e-59 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 207.78 E-value: 1.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK07979 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVSVVVLPGDV- 163
Cdd:PRK07979 87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKDIl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 164 --ALK---AAPESASSHWYHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALRG 236
Cdd:PRK07979 167 npANKlpyVWPESVSMRSYN---PTTQGHKGQIKRALQTLVAAKKPVVYVGGGAinAACHQQLKELVEKLNLPVVSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 237 KEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:PRK07979 244 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRttnnlAKYCPNATVLHIDIDPTSISKTVTADIPIVGD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 312 IKSTLKALLPLLEEKTDRHFLD------KALEHYRdARKGLDdLAKPSDKaIHPQYLAQQISHFADEDAIFTCDVGTPTV 385
Cdd:PRK07979 324 ARQVLEQMLELLSQESAHQPLDeirdwwQQIEQWR-ARQCLK-YDTHSEK-IKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 386 WAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGF 465
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 364517351 466 VA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAF---RTDGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK07979 481 VKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALeqvRNNRLVFVDVTVDGSEHVYPMQIR 559
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
2-539 |
3.13e-59 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 206.69 E-value: 3.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 2 KQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:PRK06882 3 KLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-LP 160
Cdd:PRK06882 83 ITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIdIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 161 GDVALKAA------PESASSHWYHaplPTVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVH 232
Cdd:PRK06882 163 KDMVNPANkftyeyPEEVSLRSYN---PTVQGHKGQIKKALKALLVAKKPVLFVGGGVitAECSEQLTQFAQKLNLPVTS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 233 ALRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMA 307
Cdd:PRK06882 240 SLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRttnnlAKYCPNAKVIHIDIDPTSISKNVPAYIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 308 LVGDIKSTLKALLPLLEE------KTDRHFLDKALEHYRdARKGLDdlAKPSDKAIHPQYLAQQISHFADEDAIFTCDVG 381
Cdd:PRK06882 320 IVGSAKNVLEEFLSLLEEenlaksQTDLTAWWQQINEWK-AKKCLE--FDRTSDVIKPQQVVEAIYRLTNGDAYVASDVG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 382 TPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNS 461
Cdd:PRK06882 397 QHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 462 VLGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRT-DGPVLVDVVVAKEELAIPPQI 538
Cdd:PRK06882 477 FLGMVKqwQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIkDKLVFVDVNVDETEHVYPMQI 556
|
.
gi 364517351 539 K 539
Cdd:PRK06882 557 R 557
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
6-542 |
9.80e-59 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 205.46 E-value: 9.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLN---RMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLI 82
Cdd:PRK06456 5 ARILVDSLKREGVKVIFGIPGLSNMQIYDAFVedlANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 83 NGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVSVVVLPG 161
Cdd:PRK06456 85 TGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRpGPVVIDIPR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 162 DVALKAA-----PESASSHWYHaPLPTVTPaEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHAL 234
Cdd:PRK06456 165 DIFYEKMeeikwPEKPLVKGYR-DFPTRID-RLALKKAAEILINAERPIILVGTGVvwSNATPEVLELAELLHIPIVSTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 235 RGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAFYP------TDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK06456 243 PGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSydemveTRKKFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 309 VGDIKSTLKALLPLLEE---KTDRHFLDKALEHYRDARKGLddLAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTV 385
Cdd:PRK06456 323 YGNAKIILRELIKAITElgqKRDRSAWLKRVKEYKEYYSQF--YYTEENGKLKPWKIMKTIRQALPRDAIVTTGVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 386 WAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGF 465
Cdd:PRK06456 401 WAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 466 V--AMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELA---IPPQIKL 540
Cdd:PRK06456 481 VrqVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELAlptLPPGGRL 560
|
..
gi 364517351 541 EQ 542
Cdd:PRK06456 561 KQ 562
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
4-535 |
5.81e-58 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 203.79 E-value: 5.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK09107 12 TGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV-LPGD 162
Cdd:PRK09107 92 PLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVdIPKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 163 VALKA----APESASSHwyHAPLPTVTPAEEELRKLVQLIRYSSNIALMCGSGC----AGAHQELVEFAAKIKAPIVHAL 234
Cdd:PRK09107 172 VQFATgtytPPQKAPVH--VSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVinsgPEASRLLRELVELTGFPITSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 235 RGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYR------AFYPTdAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK09107 250 MGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRitgrldAFSPN-SKKIHIDIDPSSINKNVRVDVPI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 309 VGDIKSTLKALLPLLE---EKTDRHFLDK---ALEHYRdARKGLDdlAKPSDKAIHPQYLAQQI-SHFADEDAIFTCDVG 381
Cdd:PRK09107 329 IGDVGHVLEDMLRLWKargKKPDKEALADwwgQIARWR-ARNSLA--YTPSDDVIMPQYAIQRLyELTKGRDTYITTEVG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 382 TPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNS 461
Cdd:PRK09107 406 QHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQ 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 364517351 462 VLGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIP 535
Cdd:PRK09107 486 YMGMVRqwQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFP 561
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
4-536 |
5.83e-57 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 200.76 E-value: 5.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWmptRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFGQSLPSALFLAAEAIGIRQIAY---RTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVSVVVLPGD 162
Cdd:PRK06112 92 PLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRpGPVVLLLPAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 163 VALKAAPESA---SSHWYHAPLPTVTPAEEELRKLVQLIRYSSNIALMCGSG--CAGAHQELVEFAAKIKAPIVHALRGK 237
Cdd:PRK06112 172 LLTAAAAAPAaprSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGvhISGASAALAALQSLAGLPVATTNMGK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 238 EHVEYDNPYDVGMTG-LIG-FASGFHTM---MNADTLILLGTQFPYRA-----FYPTDAKIIQIDINPGSIGAHSKVdMA 307
Cdd:PRK06112 252 GAVDETHPLSLGVVGsLMGpRSPGRHLRdlvREADVVLLVGTRTNQNGtdswsLYPEQAQYIHIDVDGEEVGRNYEA-LR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 308 LVGDIKSTLKALLPLLE------EKTDRHFLDKALEHYRDA-RKGLDDLAKPSDKAIHPQYLAQQISHFADEDAIFTCDV 380
Cdd:PRK06112 331 LVGDARLTLAALTDALRgrdlaaRAGRRAALEPAIAAGREAhREDSAPVALSDASPIRPERIMAELQAVLTGDTIVVADA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 381 GTPTVWAARYLKMNGKR-RLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFN 459
Cdd:PRK06112 411 SYSSIWVANFLTARRAGmRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLN 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 364517351 460 NSVLGFV--AMEMKAGGYlTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVakEELAIPP 536
Cdd:PRK06112 491 NGILGFQkhAETVKFGTH-TDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVIT--DPSAFPP 566
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-535 |
9.39e-57 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 199.47 E-value: 9.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGT-IDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08266 2 TTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQ--ETHPQ-ELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSV 156
Cdd:PRK08266 82 NAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMPDQlATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 157 VV-LPGDVALKAAPESASSHWYHAPLPTVTPaeEELRKLVQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPIVHALR 235
Cdd:PRK08266 162 ALeMPWDVFGQRAPVAAAPPLRPAPPPAPDP--DAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 236 GKEHVeyDNPYDVGMTgligFASGFHTMMNADTLILLGT----QFPYRAFYPTDAKIIQIDINPGSIGAHsKVDMALVGD 311
Cdd:PRK08266 240 GRGIV--SDRHPLGLN----FAAAYELWPQTDVVIGIGSrlelPTFRWPWRPDGLKVIRIDIDPTEMRRL-KPDVAIVAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 312 IKSTLKALLPLLEEK----TDRHfldkalEHYRDARKGLDDLAkpsdKAIHPQ--YLaQQISHFADEDAIFT---CDVGt 382
Cdd:PRK08266 313 AKAGTAALLDALSKAgskrPSRR------AELRELKAAARQRI----QAVQPQasYL-RAIREALPDDGIFVdelSQVG- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 383 ptvWAARY-LKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNS 461
Cdd:PRK08266 381 ---FASWFaFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNN 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 364517351 462 VLGFVAMEMK---AGGYLtdGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEELAIP 535
Cdd:PRK08266 458 AYGNVRRDQKrrfGGRVV--ASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEASP 532
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-527 |
1.79e-56 |
|
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: 198.43 E-value: 1.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:TIGR02418 2 ADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKG-IELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVSVVVLPGDVA 164
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKpGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 165 lkAAPESASShWYHAPLPTVTPA-EEELRKLVQLIRYSSNIALMCGSGcaGAHQELVE----FAAKIKAPIVHALRGKEH 239
Cdd:TIGR02418 161 --DSPVSVKA-IPASYAPKLGAApDDAIDEVAEAIQNAKLPVLLLGLR--ASSPETTEavrrLLKKTQLPVVETFQGAGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 240 VEYDN-PYDVGMTGLIGFASGFHTMMNADTLILLG-TQFPYRAFY---PTDAKIIQIDINPGSIGAHSKVDMALVGDIKS 314
Cdd:TIGR02418 236 VSRELeDHFFGRVGLFRNQPGDRLLKQADLVITIGyDPIEYEPRNwnsENDATIVHIDVEPAQIDNNYQPDLELVGDIAS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 315 TLKALLPLLE--EKTDRHFldKALEHYRDARKGLDDL-AKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYL 391
Cdd:TIGR02418 316 TLDLLAERIPgyELPPDAL--AILEDLKQQREALDRVpATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 392 KMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAM--E 469
Cdd:TIGR02418 394 RSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFqeE 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 364517351 470 MKAGgyLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVV 527
Cdd:TIGR02418 474 MKYQ--RSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPV 529
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
357-535 |
8.13e-55 |
|
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: 183.47 E-value: 8.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 357 IHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGF 436
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 437 SMLMGDFLSLAQMKLPVKIVIFNNSVLGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTA 514
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRqwQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|.
gi 364517351 515 FRTDGPVLVDVVVAKEELAIP 535
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLP 181
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-527 |
1.15e-54 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 193.92 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTG---DSL-NGLSDSlnrmgTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGP 76
Cdd:PRK08617 3 KKKYGADLVVDSLINQGVKYVFGIPGakiDRVfDALEDS-----GPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 77 GNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVS 155
Cdd:PRK08617 78 GVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRpGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 156 VVVLPGDVALKAAPESASSHwyhAPLPTVTPA-EEELRKLVQLIRYSSNIALMCG-----SGCAGAHQELVEfaaKIKAP 229
Cdd:PRK08617 158 FVSLPQDVVDAPVTSKAIAP---LSKPKLGPAsPEDINYLAELIKNAKLPVLLLGmrassPEVTAAIRRLLE---RTNLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 230 IVHALRGKEHV--EYDNPYdVGMTGLIGFASGFHTMMNADTLILLGtqfpYRAF-Y-------PTDAKIIQIDINPGSIG 299
Cdd:PRK08617 232 VVETFQAAGVIsrELEDHF-FGRVGLFRNQPGDELLKKADLVITIG----YDPIeYeprnwnsEGDATIIHIDVLPAEID 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 300 AHSKVDMALVGDIKSTLKALLPLLeektDRHFLDKALEHY-RDARKGLDDLAKP----SDKAIHPQYLAQQISHFADEDA 374
Cdd:PRK08617 307 NYYQPERELIGDIAATLDLLAEKL----DGLSLSPQSLEIlEELRAQLEELAERparlEEGAVHPLRIIRALQDIVTDDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 375 IFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFsMLMGDFLSLA-QMKLPV 453
Cdd:PRK08617 383 TVTVDVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGF-LFSAMELETAvRLKLNI 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 364517351 454 KIVIFNNSVLGFVAM--EMKAGGylTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVV 527
Cdd:PRK08617 462 VHIIWNDGHYNMVEFqeEMKYGR--SSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPV 535
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
379-525 |
1.14e-52 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 176.62 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 379 DVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIF 458
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 364517351 459 NNSVLGFVAMEMKAGG----YLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDV 525
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGggrySGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
11-527 |
7.09e-51 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 183.49 E-value: 7.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 11 KTLEQAGVKRIWGVTG----DSLNGLSDSlnrmgTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLF 86
Cdd:PRK08322 9 KCLENEGVEYIFGIPGeenlDLLEALRDS-----SIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 87 DCHRNHVPVLAIAAHIP--SSEIGSgyFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVSVVVLPGDV 163
Cdd:PRK08322 84 YAQLGGMPMVAITGQKPikRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERpGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 164 AlkaaPESASSHwyhaPLP-----TVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALRG 236
Cdd:PRK08322 162 A----AEETDGK----PLPrsysrRPYASPKAIERAAEAIQAAKNPLILIGAGAnrKTASKALTEFVDKTGIPFFTTQMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 237 KEHVEYDNPYDVGMTGL-----IGFAsgFHtmmNADTLILLGTQF----PYRAFYPTDAKIIQIDINPGSIGAHSKVDMA 307
Cdd:PRK08322 234 KGVIPETHPLSLGTAGLsqgdyVHCA--IE---HADLIINVGHDViekpPFFMNPNGDKKVIHINFLPAEVDPVYFPQVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 308 LVGDIKSTLKALLPLLEEKtdRHFLDKALEHYRDA-RKGLDDLAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVW 386
Cdd:PRK08322 309 VVGDIANSLWQLKERLADQ--PHWDFPRFLKIREAiEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 387 AARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFV 466
Cdd:PRK08322 387 FARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 364517351 467 AMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVV 527
Cdd:PRK08322 467 RWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPV 527
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
362-527 |
8.38e-46 |
|
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: 158.96 E-value: 8.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 362 LAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMG 441
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 442 DFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTD-GTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGP 520
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVsGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGGP 161
|
....*..
gi 364517351 521 VLVDVVV 527
Cdd:cd00568 162 ALIEVKT 168
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
1-539 |
3.92e-42 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 159.00 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTgdSLNGLS--DSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGN 78
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVI--SIHNMPilDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 79 LHLINGLFDCHRNHVPVLAIAAHIPSSEIGS--GYFQETHPQ-ELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVS 155
Cdd:PRK07064 79 GNAAGALVEALTAGTPLLHITGQIETPYLDQdlGYIHEAPDQlTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 156 VVV-LPGDVALKAAPESASSHWYHAPLPTvtPAEEELRKLVQLIRYSSNIALMCGSGCAGAHQELVEFAAkIKAPIVHAL 234
Cdd:PRK07064 159 VSVeIPIDIQAAEIELPDDLAPVHVAVPE--PDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVD-LGFGVVTST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 235 RGKEHVEYDNPYDVGMTGLIGFASGFHTmmNADTLILLGTQF------PYRAFYPTDakIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK07064 236 QGRGVVPEDHPASLGAFNNSAAVEALYK--TCDLLLVVGSRLrgnetlKYSLALPRP--LIRVDADAAADGRGYPNDLFV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 309 VGDIKSTLKALLPLLEE--KTDRHFlDKALEHYRDA-----RKGLDDLAKpsdkaihpqyLAQQISHFADEDAIFTCDVG 381
Cdd:PRK07064 312 HGDAARVLARLADRLEGrlSVDPAF-AADLRAAREAavadlRKGLGPYAK----------LVDALRAALPRDGNWVRDVT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 382 TP-TVWAARYLKMNGKRRLLGSFNhGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNN 460
Cdd:PRK07064 381 ISnSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMND 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 461 SVLGFV-AMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVA-----KEELAI 534
Cdd:PRK07064 460 GGYGVIrNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVDMLsigpfAAAFAG 539
|
....*
gi 364517351 535 PPQIK 539
Cdd:PRK07064 540 PPVKK 544
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-542 |
5.18e-42 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 158.89 E-value: 5.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08199 6 RARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVSVVVL 159
Cdd:PRK08199 86 ASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRpGPVVLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 160 PGDVaLKAAPESASSHWYHAPLPTvtPAEEELRKLVQLI-RYSSNIALMCGSG-CAGAHQELVEFAAKIKAPIVHALRGK 237
Cdd:PRK08199 166 PEDV-LSETAEVPDAPPYRRVAAA--PGAADLARLAELLaRAERPLVILGGSGwTEAAVADLRAFAERWGLPVACAFRRQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 238 EHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFP------YRAF---YPtDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK08199 243 DLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGevttqgYTLLdipVP-RQTLVHVHPDAEELGRVYRPDLAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 309 VGDIKSTLKALLPLLEEKTDRHF--LDKALEHYRDARKglddlAKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPTVW 386
Cdd:PRK08199 322 VADPAAFAAALAALEPPASPAWAewTAAAHADYLAWSA-----PLPGPGAVQLGEVMAWLRERLPADAIITNGAGNYATW 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 387 AARYLKMNGKRRLLGSFNhGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFV 466
Cdd:PRK08199 397 LHRFFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTI 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 364517351 467 AM--EMKAGGYlTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVVAKEelAIPPQIKLEQ 542
Cdd:PRK08199 476 RMhqEREYPGR-VSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPE--AITPTATLSQ 550
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
62-529 |
1.71e-41 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 157.85 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 62 QLTGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGS--------GYFQETHPQ-ELFRECSHYCELVS 132
Cdd:PRK08327 71 LVTGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrntriHWTQEMRDQgGLVREYVKWDYEIR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 133 TPEQIPQVLAVAMRKAVIN-RGVSVVVLPGDVALKAAPESASSHWYHAPLPTVTPAEEELRKLVQLIRYSSNIALMC--G 209
Cdd:PRK08327 151 RGDQIGEVVARAIQIAMSEpKGPVYLTLPREVLAEEVPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITwrA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 210 SGCAGAHQELVEFAAKIKAPIVHAlRGkEHVEY--DNPYDVGmtgligfASGFHTMMNADTLILLGTQFPY---RAFYPT 284
Cdd:PRK08327 231 GRTAEGFASLRRLAEELAIPVVEY-AG-EVVNYpsDHPLHLG-------PDPRADLAEADLVLVVDSDVPWipkKIRPDA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 285 DAKIIQIDINPgsigAHSK-------VDMALVGDIKSTLKALLPLLEEKTDRHFL------DKALEHYRDARKGLDD--L 349
Cdd:PRK08327 302 DARVIQIDVDP----LKSRiplwgfpCDLCIQADTSTALDQLEERLKSLASAERRrarrrrAAVRELRIRQEAAKRAeiE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 350 AKPSDKAIHPQYLAQQISHFADE-DAIFTcdvGTPTVWaaRYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVV 428
Cdd:PRK08327 378 RLKDRGPITPAYLSYCLGEVADEyDAIVT---EYPFVP--RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVI 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 429 AMCGDGGFsmLMGD---FLSLAQ-MKLPVKIVIFNNSVLGFVA---MEMKAGGY--------LTDGTElhDTNFARIAEA 493
Cdd:PRK08327 453 ATVGDGSF--IFGVpeaAHWVAErYGLPVLVVVFNNGGWLAVKeavLEVYPEGYaarkgtfpGTDFDP--RPDFAKIAEA 528
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 364517351 494 CGIKGIRVEKASEVDEALQTAF---RTDGP-VLVDVVVAK 529
Cdd:PRK08327 529 FGGYGERVEDPEELKGALRRALaavRKGRRsAVLDVIVDR 568
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-530 |
4.69e-41 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 156.68 E-value: 4.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLT-GELAVCAGSCGPGNL 79
Cdd:PRK11269 2 AKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV- 158
Cdd:PRK11269 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLId 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 159 LPGDVALKAAPESASSHwyhAPLPTVTPA--EEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHAL 234
Cdd:PRK11269 162 LPFDVQVAEIEFDPDTY---EPLPVYKPAatRAQIEKALEMLNAAERPLIVAGGGVinADASDLLVEFAELTGVPVIPTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 235 RGKEHVEYDNPYDVGMTGL-IGFASGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK11269 239 MGWGAIPDDHPLMAGMVGLqTSHRYGNATLLASDFVLGIGNRWANRhtgsvEVYTKGRKFVHVDIEPTQIGRVFGPDLGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 309 VGDIKSTLKALLPLLEEKTDRHFLDKALEHYRDARKGLDDLAKPSD---KAIHPQYLAQQISHFADEDAIFTCDVGTPTV 385
Cdd:PRK11269 319 VSDAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTLLRKTHfdnVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 386 WAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGF 465
Cdd:PRK11269 399 AAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 466 V-----AMEM--------------KAGGYLTDgtelhdtnFARIAEACGIKGIRVEKASEVDEALQTA------FRTdgP 520
Cdd:PRK11269 479 IrqaqrAFDMdycvqlafeninspELNGYGVD--------HVKVAEGLGCKAIRVFKPEDIAPALEQAkalmaeFRV--P 548
|
570
....*....|
gi 364517351 521 VLVDVVVAKE 530
Cdd:PRK11269 549 VVVEVILERV 558
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
5-535 |
3.03e-40 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 154.20 E-value: 3.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 5 VAAYIAKTLEQAGVKRIWGVtgdSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTG--ELAVCAGSCGPGNLHLI 82
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGF---PVNELFDAAAAAG-IRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 83 NGLFDCHRNHVPVLAIAAHIPSSEigsgyfQETHPQ----ELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVV 158
Cdd:PRK06154 98 GGVAQAYGDSVPVLFLPTGYPRGS------TDVAPNfeslRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 159 -LPGDVALKAAPESASSHwyhAPLPTVTPAEE--ELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHA 233
Cdd:PRK06154 172 eLPVDVLAEELDELPLDH---RPSRRSRPGADpvEVVEAAALLLAAERPVIYAGQGVlyAQATPELKELAELLEIPVMTT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 234 LRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQFPYRAF---YPTDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK06154 249 LNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYglpMPEGKTIIHSTLDDADLNKDYPIDHGLVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 311 DIKSTLKALLPLLEEKTDRHFLDKA-----LEHYRDA--RKGLDDLAKpSDKAIHPQYLAQQISH-FADEDAIFTCDVGT 382
Cdd:PRK06154 329 DAALVLKQMIEELRRRVGPDRGRAQqvaaeIEAVRAAwlAKWMPKLTS-DSTPINPYRVVWELQHaVDIKTVIITHDAGS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 383 P-----TVWAAR----YLKMnGKRRLLGSfnhgsmanAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPV 453
Cdd:PRK06154 408 PrdqlsPFYVASrpgsYLGW-GKTTQLGY--------GLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 454 KIVIFNNSVLGFVAMEMKAggyltdGTELHDTNF-----ARIAEACGIKGIRVEKASEVDEALQTAFRT--DG-PVLVDV 525
Cdd:PRK06154 479 LTILLNNFSMGGYDKVMPV------STTKYRATDisgdyAAIARALGGYGERVEDPEMLVPALLRALRKvkEGtPALLEV 552
|
570
....*....|.
gi 364517351 526 VVAKE-ELAIP 535
Cdd:PRK06154 553 ITSEEtALSRP 563
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
191-319 |
6.99e-38 |
|
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: 136.15 E-value: 6.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 191 LRKLVQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPIVHALRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADT 268
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVrrSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 364517351 269 LILLGTQF-------PYRAFYPtDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKAL 319
Cdd:pfam00205 81 VLAVGARFddirttgKLPEFAP-DAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
64-529 |
7.93e-37 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 143.96 E-value: 7.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 64 TGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAA--HIPSSEIGSGYFQETHPQE-LFRECSHYCELVSTPEQIPQV 140
Cdd:PRK07524 62 SGKPGVCFIITGPGMTNIATAMGQAYADSIPMLVISSvnRRASLGKGRGKLHELPDQRaMVAGVAAFSHTLMSAEDLPEV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 141 LAVAMrkAVINRG----------VSVVVLPGDVALKAAPESASSHwyhaplptvTPAEEELRKLVQLIRYSSNIALMCGS 210
Cdd:PRK07524 142 LARAF--AVFDSArprpvhieipLDVLAAPADHLLPAPPTRPARP---------GPAPAALAQAAERLAAARRPLILAGG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 211 GCAGAHQELVEFAAKIKAPIVHALRGKEHVEYDNPYDVGMTGLIgfASGFHTMMNADTLILLGTQF-------PYRAFYP 283
Cdd:PRK07524 211 GALAAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSL--PAVRALIAEADVVLAVGTELgetdydvYFDGGFP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 284 TDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKALLPLLEEKTDRHflDKALEHYRDARKGLDdlakpsdKAIHPQYLA 363
Cdd:PRK07524 289 LPGELIRIDIDPDQLARNYPPALALVGDARAALEALLARLPGQAAAA--DWGAARVAALRQALR-------AEWDPLTAA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 364 QQ--ISHFADE--DAIFTCDvGTPTVWAAR-YLKMNGKRRLL-GSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFS 437
Cdd:PRK07524 360 QValLDTILAAlpDAIFVGD-STQPVYAGNlYFDADAPRRWFnASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQ 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 438 MLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRT 517
Cdd:PRK07524 439 FTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFAR 518
|
490
....*....|..
gi 364517351 518 DGPVLVDVVVAK 529
Cdd:PRK07524 519 PGPTLIEVDQAC 530
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
5-170 |
1.70e-36 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 133.51 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 5 VAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLING 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 85 LFDCHRNHVPVLAIAAHIPSSEIGSGYFQ-ETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVSVVVLPGD 162
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRpGPVYLEIPLD 160
|
....*...
gi 364517351 163 VALKAAPE 170
Cdd:pfam02776 161 VLLEEVDE 168
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
9-526 |
3.42e-36 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 142.17 E-value: 3.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK05858 11 AARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVI-NRGVSVVVLPGDVALKA 167
Cdd:PRK05858 90 QFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTpHRGPVFVDFPMDHAFSM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 168 APESASShwyhAPLPTV----TPAEEELRKLVQLIRYSSNIALMCGSGCAGAHQE--LVEFAAKIKAPIVHALRGKEHVE 241
Cdd:PRK05858 170 ADDDGRP----GALTELpagpTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEaaLLRLAEELGIPVLMNGMGRGVVP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 242 YDNPYDVgmTGLIGFASGfhtmmNADTLILLGTQFPYR---AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKA 318
Cdd:PRK05858 246 ADHPLAF--SRARGKALG-----EADVVLVVGVPMDFRlgfGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILSA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 319 LLPLLEEKTDRHFLDKALEHYRDARKGLDDLAKPSDKA-IHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKR 397
Cdd:PRK05858 319 LAGAGGDRTDHQGWIEELRTAETAARARDAAELADDRDpIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 398 RLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDG--GFSMLmgDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKA-GG 474
Cdd:PRK05858 399 CWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGafGFSLM--DVDTLVRHNLPVVSVIGNNGIWGLEKHPMEAlYG 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 364517351 475 YLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVV 526
Cdd:PRK05858 477 YDVAADLRPGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVL 528
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
359-527 |
4.36e-32 |
|
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: 121.63 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 359 PQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSM 438
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 439 LMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTD 518
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
....*....
gi 364517351 519 GPVLVDVVV 527
Cdd:cd02010 161 GVHVIDCPV 169
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
359-528 |
6.68e-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: 121.10 E-value: 6.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 359 PQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSM 438
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 439 LMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEM--KAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFR 516
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQqlSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 364517351 517 TDGPVLVDVVVA 528
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-539 |
1.31e-30 |
|
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: 125.66 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHeevaafaagaeaqltgELavCAGSC------ 74
Cdd:COG3961 3 MTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCN----------------EL--NAGYAadgyar 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 75 -----------GPGNLHLINGLFDCHRNHVPVLAIAAhIPSSEI-----------GSGYFqeTHPQELFRECSHYCELVs 132
Cdd:COG3961 65 vnglgalvttyGVGELSAINGIAGAYAERVPVVHIVG-APGTRAqrrgpllhhtlGDGDF--DHFLRMFEEVTVAQAVL- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 133 TPE----QIPQVLAVAMRKaviNRGVsVVVLPGDVAlkAAPESASSHWYHAPLPTVTPA--EEELRKLVQLIRYSSNIAL 206
Cdd:COG3961 141 TPEnaaaEIDRVLAAALRE---KRPV-YIELPRDVA--DAPIEPPEAPLPLPPPASDPAalAAAVAAAAERLAKAKRPVI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 207 MCGSGCA--GAHQELVEFAAKIKAPIVHALRGKEHVEYDNPYDVGM-TGLIGFASGFHTMMNADTLILLGTQFpyrafyp 283
Cdd:COG3961 215 LAGVEVHrfGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGVVF------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 284 TD-------AKIIQ---IDINPG--SIGAH--SKVDMAlvgdikSTLKALLPLLEEKTdrhfldkalEHYRDARKGLDDL 349
Cdd:COG3961 288 TDtntggftAQLDPertIDIQPDsvRVGGHiyPGVSLA------DFLEALAELLKKRS---------APLPAPAPPPPPP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 350 AKPSDKAIHPQYLAQQISHFADEDAIFTCDVGTPtVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVA 429
Cdd:COG3961 353 PAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTS-LFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVIL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 430 MCGDGGFsMLMGdfLSLAQM---KLPVKIVIFNNsvlgfvamemkaGGYLT-------DGT--ELHDTNFARIAEACG-- 495
Cdd:COG3961 432 LVGDGAF-QLTA--QELSTMlryGLKPIIFVLNN------------DGYTIeraihgpDGPynDIANWDYAKLPEAFGgg 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 364517351 496 -IKGIRVEKASEVDEALQTAFR-TDGPVLVDVVVAKEElaIPPQIK 539
Cdd:COG3961 497 nALGFRVTTEGELEEALAAAEAnTDRLTLIEVVLDKMD--APPLLK 540
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
357-533 |
3.93e-30 |
|
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: 116.84 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 357 IHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGF 436
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 437 SMLMGDFLSLAQMKLPVKIVIFNNSVLGfvaMEMKaggYLTD-------GTELHDTNFARIAEACGIKGIRVEKASEVDE 509
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWG---AEKK---NQVDfynnrfvGTELESESFAKIAEACGAKGITVDKPEDVGP 157
|
170 180
....*....|....*....|....*..
gi 364517351 510 ALQTAF--RTDG-PVLVDVVVAKEELA 533
Cdd:cd02013 158 ALQKAIamMAEGkTTVIEIVCDQELGD 184
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
69-527 |
3.28e-29 |
|
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: 122.16 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 69 VCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQET-HPQEL-------FRECSHYCELVSTPEQIPQV 140
Cdd:COG3962 87 ACTSSIGPGATNMVTAAALATANRLPVLLLPGDTFATRQPDPVLQQLeHFHDPtisvndaFRPVSRYWDRITRPEQLMSA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 141 LAVAMRkaVI----NRGVSVVVLPGDVALKA--APES--ASSHWY-HAPLPTvtpaEEELRKLVQLIRYSSNIALMCGSG 211
Cdd:COG3962 167 LPRAMR--VLtdpaETGAVTLALPQDVQAEAydYPESffAKRVHRiRRPPPD----PAELARAVELIRAAKRPLIIAGGG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 212 C--AGAHQELVEFAAKIKAPIVHALRGKEHVEYDNPYDVGMTGLIGFASGFHTMMNADTLILLGTQF------PYRAFYP 283
Cdd:COG3962 241 VrySEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLGGIGVTGTLAANALAAEADLVIGVGTRLqdfttgSKTLFAN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 284 TDAKIIQIDINPGSIGAHSKVdmALVGDIKSTLKALLPLLEE-KTDRHFLDKALEHYRDARKGLDDLAKPSDKAIHPQyl 362
Cdd:COG3962 321 PDVRFVNINVARFDAYKHDAL--PVVADAREGLEALTEALAGwRYPAAWTDEAAELKAEWDAEVDRLYAPTNGGLPTQ-- 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 363 AQQI---SHFADEDAIFTCDVGTP-----TVWAARYlkmngkrrlLGSFN--HG--SMANAMPQAIGAKATAPERQVVAM 430
Cdd:COG3962 397 AQVIgavNEAAGPDDIVVCAAGSLpgdlhKLWRTRD---------PGTYHveYGysCMGYEIAGGLGVKLAEPDREVYVM 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 431 CGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSvlGF-----VAMEMKAGGYltdGTELHDTN--------------FARIA 491
Cdd:COG3962 468 VGDGSYLMLNSELVTSVQEGKKIIVVLLDNH--GFgcinrLQMSTGSQSF---GTELRDRDtetgrldggllpvdFAANA 542
|
490 500 510
....*....|....*....|....*....|....*.
gi 364517351 492 EACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVV 527
Cdd:COG3962 543 ASLGAKAYRVTTIAELRAALERAKAADRTTVIVIKT 578
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
78-528 |
1.22e-28 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 119.67 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 78 NLHLING-------LFDCHRNHVPVLAIAAHIPSSEIGSGYF-QETHPQELFRECSHY-CElVSTPEQIPQVLA----VA 144
Cdd:PRK07092 78 NLHSAAGvgnamgnLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWsIE-PARAEDVPAAIArayhIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 145 MRKAvinRGVSVVVLPGDVALKAAPESASSHWYHAplptVTPAEEELRKLVQLIRYSSNIALMCGSGC--AGAHQELVEF 222
Cdd:PRK07092 157 MQPP---RGPVFVSIPYDDWDQPAEPLPARTVSSA----VRPDPAALARLGDALDAARRPALVVGPAVdrAGAWDDAVRL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 223 AAKIKAPI-VHALRGKEHVEYDNPYdvgmtgligFASGFHTMMNA--------DTLILLGT------QFPYRAFYPTDAK 287
Cdd:PRK07092 230 AERHRAPVwVAPMSGRCSFPEDHPL---------FAGFLPASREKisalldghDLVLVIGApvftyhVEGPGPHLPEGAE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 288 IIQIDINPGsIGAHSKVDMALVGDIKSTLKALLPLLEEkTDRhfldKALEhyrdARKGLDDLAKPSDkAIHPQYLAQQIS 367
Cdd:PRK07092 301 LVQLTDDPG-EAAWAPMGDAIVGDIRLALRDLLALLPP-SAR----PAPP----ARPMPPPAPAPGE-PLSVAFVLQTLA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 368 HFADEDAIFTCDV--GTPTVWaaRYLKMNGKrrllGSF---NHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGD 442
Cdd:PRK07092 370 ALRPADAIVVEEApsTRPAMQ--EHLPMRRQ----GSFytmASGGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 443 FLSLAQMKLPVKIVIFNNSvlGFVAME-----MKAGGylTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFRT 517
Cdd:PRK07092 444 LWSAAQLKLPVTFVILNNG--RYGALRwfapvFGVRD--VPGLDLPGLDFVALARGYGCEAVRVSDAAELADALARALAA 519
|
490
....*....|.
gi 364517351 518 DGPVLVDVVVA 528
Cdd:PRK07092 520 DGPVLVEVEVA 530
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
357-527 |
1.85e-25 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 103.06 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 357 IHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSfNHGSMANAMPQAIGAKATAPERQVVAMCGDGGF 436
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTL-RGGGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 437 SMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGTE------LHD--TNFARIAEACGIKGIRVEKASEVD 508
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENapdgldLLDpgIDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*....
gi 364517351 509 EALQTAFRTDGPVLVDVVV 527
Cdd:cd02002 160 EALREALAEGGPALIEVVV 178
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-160 |
9.86e-25 |
|
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: 100.30 E-value: 9.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 8 YIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFD 87
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPLLDALARSG-IRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 364517351 88 CHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINR-GVSVVVLP 160
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRpGPVALDLP 154
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
6-528 |
5.47e-19 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 90.43 E-value: 5.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK09259 13 FHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEG-IRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 86 FDCHRNHVPVLAIAAhipSSE-----IGSGYFQET--------HPQELFRecshycelVSTPEQIPQVLAVAMRKAVINR 152
Cdd:PRK09259 92 ANATTNCFPMIMISG---SSEreivdLQQGDYEELdqlnaakpFCKAAFR--------VNRAEDIGIGVARAIRTAVSGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 153 -GVSVVVLPGDV--ALKAAPESASSHWYHA-PLPTVTPAEEELRKLVQLIRYSSN--IALMCGSGCAGAHQELVEFAAKI 226
Cdd:PRK09259 161 pGGVYLDLPAKVlaQTMDADEALTSLVKVVdPAPAQLPAPEAVDRALDLLKKAKRplIILGKGAAYAQADEQIREFVEKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 227 KAPIVHALRGKEHVEYDNPYDVGmtgligfASGFHTMMNADTLILLGTQFPYRAFY---PT---DAKIIQIDINPGSIGA 300
Cdd:PRK09259 241 GIPFLPMSMAKGLLPDTHPQSAA-------AARSLALANADVVLLVGARLNWLLSHgkgKTwgaDKKFIQIDIEPQEIDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 301 HSKVDMALVGDIKSTLKALLPLLEE---KTDRHFLDKALEhyrDARKGLDDLAKPSDKAIHPQYLAQQISHFAD-----E 372
Cdd:PRK09259 314 NRPIAAPVVGDIGSVMQALLAGLKQntfKAPAEWLDALAE---RKEKNAAKMAEKLSTDTQPMNFYNALGAIRDvlkenP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 373 DAIFTCDvGTPTVWAAR-YLKMNGKRRLLGSFNHGSMANAMPQAIGAkATAPERQVVAMCGDGGFSMLMGDFLSLAQMKL 451
Cdd:PRK09259 391 DIYLVNE-GANTLDLARnIIDMYKPRHRLDCGTWGVMGIGMGYAIAA-AVETGKPVVAIEGDSAFGFSGMEVETICRYNL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 452 PVKIVIFNNSvlgfvamemkaGGYLTDGTEL------------HDTNFARIAEACGIKGIRVEKASEVDEALQTAFRTDG 519
Cdd:PRK09259 469 PVTVVIFNNG-----------GIYRGDDVNLsgagdpsptvlvHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIASGK 537
|
....*....
gi 364517351 520 PVLVDVVVA 528
Cdd:PRK09259 538 PTLINVVID 546
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
361-539 |
2.03e-18 |
|
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: 83.35 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 361 YLAQQISHFADEDAIFTCDVGTPTvWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLM 440
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSW-FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 441 GDFLSLAQMKLPVKIVIFNNSvlgfvamemkagGYLTDgTELHDT----------NFARIAEACG----IKGIRVEKASE 506
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINND------------GYTIE-RAIHGPeasyndianwNYTKLPEVFGggggGLSFRVKTEGE 151
|
170 180 190
....*....|....*....|....*....|....
gi 364517351 507 VDEALQTA-FRTDGPVLVDVVVAKEElaIPPQIK 539
Cdd:cd02005 152 LDEALKDAlFNRDKLSLIEVILPKDD--APEALK 183
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
62-527 |
6.64e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 83.77 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 62 QLTGELAVCAGSCGPGnlhLINGLFDCH---RNHVPVLAI-----AAHIP-----SSEIGSgyfqethpqeLFRECSHYC 128
Cdd:PRK12474 64 RIAGKPAVTLLHLGPG---LANGLANLHnarRAASPIVNIvgdhaVEHLQydaplTSDIDG----------FARPVSRWV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 129 ELVSTPEQIPQVLAVAMRKA-VINRGVSVVVLPGDVALKAAPESAsshwyhAPLPTVTPA---EEELRKLVQLIRYSSNI 204
Cdd:PRK12474 131 HRSASAGAVDSDVARAVQAAqSAPGGIATLIMPADVAWNEAAYAA------QPLRGIGPApvaAETVERIAALLRNGKKS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 205 ALMC-GSGCAGAHQEL---------VEFAAKIKAPIVHALRGKEHVEydnpyDVGMTGLIGFAsgfhTMMNADTLILLGT 274
Cdd:PRK12474 205 ALLLrGSALRGAPLEAagriqaktgVRLYCDTFAPRIERGAGRVPIE-----RIPYFHEQITA----FLKDVEQLVLVGA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 275 QFPYRAF-YPTdakiiqidiNPGSIGAHSKVDMALVGDIKSTLKALLPLLEEktdrhfLDKALEHYRDARKGLDDLAKps 353
Cdd:PRK12474 276 KPPVSFFaYPG---------KPSWGAPPGCEIVYLAQPDEDLAQALQDLADA------VDAPAEPAARTPLALPALPK-- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 354 dKAIHPQYLAQQISHFADEDAIFTCDVGTPTVW------AAR---YLKMNGkrrllgsfnhGSMANAMPQAIGAKATAPE 424
Cdd:PRK12474 339 -GALNSLGVAQLIAHRTPDQAIYADEALTSGLFfdmsydRARphtHLPLTG----------GSIGQGLPLAAGAAVAAPD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 425 RQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGT------ELH--DTNFARIAEACGI 496
Cdd:PRK12474 408 RKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGELQRVGAQGAGRnalsmlDLHnpELNWMKIAEGLGV 487
|
490 500 510
....*....|....*....|....*....|.
gi 364517351 497 KGIRVEKASEVDEALQTAFRTDGPVLVDVVV 527
Cdd:PRK12474 488 EASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
359-527 |
1.27e-15 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 79.50 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 359 PQYLAQQISHFADEDAIF-----TCDVG--TPTVWAARYLKMNgkrrLLGsfnhGSMANAMPQAIGAKATAPERQVVAMC 431
Cdd:PRK07586 339 PEAIAQVIAALLPENAIVvdesiTSGRGffPATAGAAPHDWLT----LTG----GAIGQGLPLATGAAVACPDRKVLALQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 432 GDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDG------TELHD--TNFARIAEACGIKGIRVEK 503
Cdd:PRK07586 411 GDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGELARVGAGNPGpraldmLDLDDpdLDWVALAEGMGVPARRVTT 490
|
170 180
....*....|....*....|....
gi 364517351 504 ASEVDEALQTAFRTDGPVLVDVVV 527
Cdd:PRK07586 491 AEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
357-529 |
1.27e-14 |
|
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: 72.70 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 357 IHPQYLAQQISHFADEDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAIGAKATAPERQVVAMCGDGGF 436
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 437 SMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKA-------------------GGYLTDgtelhdtnFARIAEACGIK 497
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAfdmdyqvnlafeninsselGGYGVD--------HVKVAEGLGCK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 364517351 498 GIRVEKASEVDEALQTAFRTDG----PVLVDVVVAK 529
Cdd:cd02006 160 AIRVTKPEELAAAFEQAKKLMAehrvPVVVEAILER 195
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
408-525 |
8.38e-14 |
|
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: 70.41 E-value: 8.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 408 MANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNS---VLGFVAMEMKAGGYltdGTELHD 484
Cdd:cd02003 50 MGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHgfgCINNLQESTGSGSF---GTEFRD 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 364517351 485 --------------TNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDV 525
Cdd:cd02003 127 rdqesgqldgallpVDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVI 181
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
360-536 |
1.51e-13 |
|
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: 72.39 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 360 QYLAQQISHFADEDAIftcdVGTpTVWAARYLKMNGKRRLLGSFNH----GSMANAMPQAIGAKATAPERQVVAMCGDGG 435
Cdd:TIGR03297 176 EAIAAILDHLPDNTVI----VST-TGKTSRELYELRDRIGQGHARDfltvGSMGHASQIALGLALARPDQRVVCLDGDGA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 436 FSMLMGDFLSLAQMKLPVKI-VIFNNSVLGFVamemkaGGYLTDGTelhDTNFARIAEACGI-KGIRVEKASEVDEALQT 513
Cdd:TIGR03297 251 ALMHMGGLATIGTQGPANLIhVLFNNGAHDSV------GGQPTVSQ---HLDFAQIAKACGYaKVYEVSTLEELETALTA 321
|
170 180
....*....|....*....|...
gi 364517351 514 AFRTDGPVLVDVVVAKEELAIPP 536
Cdd:TIGR03297 322 ASSANGPRLIEVKVRPGSRADLG 344
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
406-533 |
9.52e-13 |
|
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: 66.95 E-value: 9.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 406 GSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLP-VKIVIFNNSVLGFVamemkaGGYLTDGTelhD 484
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPAnLIHIVLNNGAHDSV------GGQPTVSF---D 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 364517351 485 TNFARIAEACGIKGIRVEKAS-EVDEALQTAFRTDGPVLVDVVVAKEELA 533
Cdd:cd03371 119 VSLPAIAKACGYRAVYEVPSLeELVAALAKALAADGPAFIEVKVRPGSRS 168
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
7-161 |
9.56e-12 |
|
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: 63.13 E-value: 9.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 7 AYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGeLAVCAGSCGPGNLHLINGLF 86
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 364517351 87 DCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAVAMRKAVINRGVSVVVLPG 161
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
366-527 |
1.31e-08 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 54.60 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 366 ISHFAD--EDAIFTCDVGTPT--VWAARylkmngkRRLLGSFNHGSMANAMPQAIGAkATAPERQVVAMCGDGGFSMLMG 441
Cdd:cd03372 5 IKTLIAdlKDELVVSNIGFPSkeLYAAG-------DRPLNFYMLGSMGLASSIGLGL-ALAQPRKVIVIDGDGSLLMNLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 442 DFLSLAQMKLP-VKIVIFNNSVLGFVAMEMKAGGYLTDgtelhdtnFARIAEACGIKgiRVEKASEVDEALQT-AFRTDG 519
Cdd:cd03372 77 ALATIAAEKPKnLIIVVLDNGAYGSTGNQPTHAGKKTD--------LEAVAKACGLD--NVATVASEEAFEKAvEQALDG 146
|
....*...
gi 364517351 520 PVLVDVVV 527
Cdd:cd03372 147 PSFIHVKI 154
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
406-523 |
4.77e-06 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 46.71 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 406 GSMANAMPQAIGAkATAPERQVVAMCGDGGFSMLMGDFLSLAQMK-LPVKIVIFNNSVLGfvamemKAGGYLTDGTelhD 484
Cdd:cd02001 42 GSMGLAGSIGLGL-ALGLSRKVIVVDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNRAYG------STGGQPTPSS---N 111
|
90 100 110
....*....|....*....|....*....|....*....
gi 364517351 485 TNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLV 523
Cdd:cd02001 112 VNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLL 150
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
406-525 |
1.93e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 45.98 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 406 GSMANAMPQAIGAKATAPERQVVAMCGDGGFSMLMGDFLSLAQMKLP-VKIVIFNNSVLGFvamemkAGGYLTDGTELHD 484
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKnLTIIVMDNGVYQI------TGGQPTLTSQTVD 130
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 364517351 485 tnFARIAEACGIKGIRVEKASEVDEAL-QTAFRTDGPVLVDV 525
Cdd:PRK06163 131 --VVAIARGAGLENSHWAADEAHFEALvDQALSGPGPSFIAV 170
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
415-527 |
6.72e-05 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 43.74 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 415 AIGAkATAPERQVVAMCGDggFSML--MGDFLSLAQMKLPVKIVIFNNSvlG---FvamEMKAGGYLTDGTE-----LHD 484
Cdd:cd02009 60 ALGI-ALATDKPTVLLTGD--LSFLhdLNGLLLGKQEPLNLTIVVINNN--GggiF---SLLPQASFEDEFErlfgtPQG 131
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 364517351 485 TNFARIAEACGIKGIRVEKASEVDEALQTAFRTDGPVLVDVVV 527
Cdd:cd02009 132 LDFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKT 174
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
407-531 |
3.38e-04 |
|
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: 41.88 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 407 SMANAMPQAIGAKATAPERQVVAMCGDGGFsMLMGdFLSLAQM---KLPVKIVIFNNSVlgfVAMemkAGG--------Y 475
Cdd:cd02008 52 CMGASIGVAIGMAKASEDKKVVAVIGDSTF-FHSG-ILGLINAvynKANITVVILDNRT---TAM---TGGqphpgtgkT 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 364517351 476 LTDGTELHDtnFARIAEACGIKGIRV---EKASEVDEALQTAFRTDGPvlvDVVVAKEE 531
Cdd:cd02008 124 LTEPTTVID--IEALVRAIGVKRVVVvdpYDLKAIREELKEALAVPGV---SVIIAKRP 177
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
385-526 |
5.56e-04 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 41.36 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 385 VWAARYLKMNGkrrllgsFN--HGsmaNAMPQAIGAKATAPERQVVAMCGDG-GFSMLMGDFLSLAQMKLPVKIVIFNNS 461
Cdd:cd03375 38 SRLPYYFNTYG-------FHtlHG---RALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 462 VLGfvameMKAG--------GYLT----DGTELHDTNFARIAEACGikGIRVEKASEVD-----EALQTAFRTDGPVLVD 524
Cdd:cd03375 108 IYG-----LTKGqaspttpeGFKTkttpYGNIEEPFNPLALALAAG--ATFVARGFSGDikqlkEIIKKAIQHKGFSFVE 180
|
..
gi 364517351 525 VV 526
Cdd:cd03375 181 VL 182
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
412-527 |
5.98e-04 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 42.10 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364517351 412 MPQAIGAkATAPERQ-----VVAMCGDGGFSMlmGDF---LSLAQ-MKLPVKIVIFNNsvlGFvAMemkaggyltdGTEL 482
Cdd:cd02000 110 VPLAAGA-ALALKYRgedrvAVCFFGDGATNE--GDFheaLNFAAlWKLPVIFVCENN---GY-AI----------STPT 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 364517351 483 HD----TNFARIAEACGIKGIRVE--KASEVDEALQTAF----RTDGPVLVDVVV 527
Cdd:cd02000 173 SRqtagTSIADRAAAYGIPGIRVDgnDVLAVYEAAKEAVerarAGGGPTLIEAVT 227
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
402-464 |
1.88e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 40.63 E-value: 1.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 364517351 402 SFN--HGSManaMPQAIGAKATAPERQVVAMCGDG-GFSMLMGDFLSLAQMKLPVKIVIFNNSVLG 464
Cdd:PRK05778 67 GLHtlHGRA---IAFATGAKLANPDLEVIVVGGDGdLASIGGGHFIHAGRRNIDITVIVENNGIYG 129
|
|
| |
