|
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: 1176.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK09124 1 MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 81 LINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLP 160
Cdd:PRK09124 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVVLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 161 GDVALKAAPENASTHWYAAPLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGCAGAHAELVQFAAKLKAPVVHALRGKEHV 240
Cdd:PRK09124 161 GDVALKPAPERATPHWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRGKEHV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLAALL 320
Cdd:PRK09124 241 EYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKATLAALL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 321 PHLEEKTDRAFLDKALEHYREARKGLDDLAKPSD--KAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRR 398
Cdd:PRK09124 321 PLLEEKTDRKFLDKALEHYRKARKGLDDLAVPSDggKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 399 LIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYLTD 478
Cdd:PRK09124 401 LLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMKAGGYLTD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 479 GTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGR 558
Cdd:PRK09124 481 GTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMPPQIKLEQAKGFSLYMLRAIISGR 560
|
570
....*....|....
gi 490998273 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: 753.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK06546 1 MAKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 81 LINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLP 160
Cdd:PRK06546 81 LINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGGGVSVVTLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 161 GDVALKAAPENASTHWYAAPLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGCAGAHAELVQFAAKLKAPVVHALRGKEHV 240
Cdd:PRK06546 161 GDIADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGKEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPtDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLAALL 320
Cdd:PRK06546 241 QYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFPYDQFLP-DVRTAQVDIDPEHLGRRTRVDLAVHGDVAETIRALL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 321 PHLEEKTDRAFLDKAL-EHYREARKGLDDLAKPSDK--AIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRR 397
Cdd:PRK06546 320 PLVKEKTDRRFLDRMLkKHARKLEKVVGAYTRKVEKhtPIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 398 RLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYLT 477
Cdd:PRK06546 400 RVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMLVDGLPD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 478 DGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISG 557
Cdd:PRK06546 480 FGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTDPNALSIPPTITGEQVKGFALAASKTVLNG 559
|
570
....*....|....*
gi 490998273 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: 550.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 81 LINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVL 159
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRpGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 160 PGDVALKAAPENASTHWYAAPLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHALRGK 237
Cdd:COG0028 161 PKDVQAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGArrAGAAEELRALAERLGAPVVTTLMGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 238 EHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPtDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:COG0028 241 GAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRvtgnwdEFAP-DAKIIHIDIDPAEIGKNYPVDLPIVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 312 IKSTLAALLPHLEEKTDRAflDKALEHYREARKGLDDLAKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYL 391
Cdd:COG0028 320 AKAVLAALLEALEPRADDR--AAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 392 KMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMK 471
Cdd:COG0028 398 RFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998273 472 A-GGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIPPQIK 539
Cdd:COG0028 478 LfYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENPPGATLD 546
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-555 |
1.27e-160 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 470.64 E-value: 1.27e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM-GTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08611 2 AKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 80 HLINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVL 159
Cdd:PRK08611 82 HLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVLTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 160 PGDvaLKAAPENASTHWYAA--PLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGCAGAHAELVQFAAKLKAPVVHALRGK 237
Cdd:PRK08611 162 PDD--LPAQKIKDTTNKTVDtfRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 238 EHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLA 317
Cdd:PRK08611 240 GIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYVDYLPKKAKAIQIDTDPANIGKRYPVNVGLVGDAKKALH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 318 ALLPHLEEKTDRAFLDKALEHYREARKGLD-DLAKPSDkAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGR 396
Cdd:PRK08611 320 QLTENIKHVEDRRFLEACQENMAKWWKWMEeDENNAST-PIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNLGTN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 397 RRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYL 476
Cdd:PRK08611 399 QKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGEL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998273 477 TDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAII 555
Cdd:PRK08611 479 EYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAPLPGKIVNDEALGYSKWAIKSLF 557
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-558 |
1.11e-130 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 393.04 E-value: 1.11e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLnRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAI-RKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 84 GLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPGDV 163
Cdd:PRK06457 82 GLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINLPVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 164 aLKAAPENASTHWYAAPLPTVTPpeeEIKKLAQVLRYSSNIALLCGSGCAGAHAELVQFAAKLKAPVVHALRGKEHVEYD 243
Cdd:PRK06457 162 -LRKSSEYKGSKNTEVGKVKYSI---DFSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 244 NPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLAallPHL 323
Cdd:PRK06457 238 DPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLN---IDI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 324 EEKTDRAFLdkalEHYREARKGLDDLAK---PSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLI 400
Cdd:PRK06457 315 EEKSDKFYE----ELKGKKEDWLDSISKqenSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 401 GSFNHGSMANAMPQAIGAK-ATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYLTDG 479
Cdd:PRK06457 391 FSAWLGSMGIGVPGSVGASfAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMGYPEWG 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998273 480 TELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGR 558
Cdd:PRK06457 471 VDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMPPKLTFKQAGEYVLSIFREKLEGI 549
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-570 |
5.62e-126 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 382.34 E-value: 5.62e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM-GTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08273 1 MSQTVADFILERLREWGVRRVFGYPGDGINGLLGALGRAdDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 80 HLINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSH-YCELVSTPEQIPQVLAIAMRKAVINRGVSVVV 158
Cdd:PRK08273 81 HLLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAGaFVQMVTVPEQLRHLVDRAVRTALAERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 159 LPGDVALKAAPENASTH--------WyaaPLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGCAGAHAELVQFAAKLKAPV 230
Cdd:PRK08273 161 LPNDVQELEYEPPPHAHgtvhsgvgY---TRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 231 VHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPT--DAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK08273 238 AKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFPYSEFLPKegQARGVQIDIDGRMLGLRYPMEVNL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 309 VGDIKSTLAALLPHLEEKTDRAFLDKALEHYREARKGLDDLAKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAA 388
Cdd:PRK08273 318 VGDAAETLRALLPLLERKKDRSWRERIEKWVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADSGSCANWYA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 389 RYLKMngRRRLIGSFNHG--SMANAMPQAIGAKATAPDRQVVAMCGDGGFSML-MGDFLSLA----QMKLPVKII-IFNN 460
Cdd:PRK08273 398 RDLRM--RRGMMASLSGTlaTMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAkywrQWSDPRLIVlVLNN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 461 SVLGFVAMEMKA-GG--YLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIPPQ 537
Cdd:PRK08273 476 RDLNQVTWEQRVmEGdpKFEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDPNVPPLPPH 555
|
570 580 590
....*....|....*....|....*....|....*.
gi 490998273 538 IKLEQAKGFslymLRAIISGRGDE---VIELAKTNW 570
Cdd:PRK08273 556 ITLEQAKAF----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 |
8.66e-107 |
|
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: 332.19 E-value: 8.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSL-NRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLING 84
Cdd:TIGR02720 2 SAAVLKVLEAWGVDHIYGIPGGSFNSTMDALsAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 85 LFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPGDVA 164
Cdd:TIGR02720 82 LYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHNGVAVVTIPVDFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 165 LKAAPENastHWYAAPLPTVT-----PPEEEIKKLAQVLRYSSNIALLCGSGCAGAHAELVQFAAKLKAPVVHALRGKEH 239
Cdd:TIGR02720 162 WQEIPDN---DYYASSVSYQTpllpaPDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 240 VEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPT--DAK-IIQIDINPGSIGAHSKVDMALVGDIKSTL 316
Cdd:TIGR02720 239 IEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKAfkNTKyFIQIDIDPAKLGKRHHTDIAVLADAKKAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 317 AALLPHLEEKTDRAFLDKALEHYREARKGLDDLAKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGR 396
Cdd:TIGR02720 319 AAILAQVEPRESTPWWQANVANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 397 RRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYL 476
Cdd:TIGR02720 399 NKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQP 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 490998273 477 TDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTA--FSTDGPVLVDVVV 527
Cdd:TIGR02720 479 LIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAkaIKQGKPVLIDAKI 531
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
3-538 |
4.68e-101 |
|
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: 316.67 E-value: 4.68e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 3 QTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLI 82
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 83 NGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPG 161
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVdLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 162 DVALKAA----PENASTHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHALR 235
Cdd:TIGR00118 161 DVTTAEIeypyPEKVNLPGYR---PTVKGHPLQIKKAAELINLAKKPVILVGGGViiAGASEELKELAERIQIPVTTTLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:TIGR00118 238 GLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRvtgnlAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 311 DIKSTLAALLPHL---EEKTDRAFLDKaLEHYReARKGLDDLAKPsdKAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWA 387
Cdd:TIGR00118 318 DARNVLEELLKKLfelKERKESAWLEQ-INKWK-KEYPLKMDYTE--EGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 388 ARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVA 467
Cdd:TIGR00118 394 AQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVR 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998273 468 --MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIPPQI 538
Cdd:TIGR00118 474 qwQELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVA 546
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
357-533 |
4.04e-96 |
|
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: 290.59 E-value: 4.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 357 IHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 437 SMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFS 516
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALA 161
|
170
....*....|....*..
gi 490998273 517 TDGPVLVDVVVAKEELA 533
Cdd:cd02014 162 ADGPVVIDVVTDPNEPP 178
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
2-535 |
5.98e-83 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 269.72 E-value: 5.98e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 2 KQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:PRK06048 7 KMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD-LRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 82 INGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LP 160
Cdd:PRK06048 86 VTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIdLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 161 GDVALKAA----PENASTHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHAL 234
Cdd:PRK06048 166 KDVTTAEIdfdyPDKVELRGYK---PTYKGNPQQIKRAAELIMKAERPIIYAGGGVisSNASEELVELAETIPAPVTTTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPtDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK06048 243 MGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRvtgklaSFAP-NAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 309 VGDIKSTLAALLPHLEEKTDRAFLDKALEHYREArkgldDLA-KPSDKAIHPQYLAQQIGQfAADDAIFTCDVGTPTVWA 387
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDRKEWLDKINQWKKEY-----PLKyKEREDVIKPQYVIEQIYE-LCPDAIIVTEVGQHQMWA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 388 ARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVA 467
Cdd:PRK06048 396 AQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVR 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 468 --MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK06048 476 qwQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSP 545
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
9-540 |
3.26e-81 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 265.85 E-value: 3.26e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMpTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK06276 7 IIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHIL-TRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGIATA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 89 HRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVA--- 164
Cdd:PRK06276 86 YADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIdLPKDVQege 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 165 ----LKAAPENASTHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHALRGKE 238
Cdd:PRK06276 166 ldleKYPIPAKIDLPGYK---PTTFGHPLQIKKAAELIAEAERPVILAGGGViiSGASEELIELSELVKIPVCTTLMGKG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 239 HVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALVGDI 312
Cdd:PRK06276 243 AFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTtgdissFAP-NAKIIHIDIDPAEIGKNVRVDVPIVGDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 313 KSTLAALLPHLEEKTDRAFlDKALEHYREARKGLDDLAKPSDKAIHPQYLAQQIGQFAAD-----DAIFTCDVGTPTVWA 387
Cdd:PRK06276 322 KNVLRDLLAELMKKEIKNK-SEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQMWM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 388 ARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVA 467
Cdd:PRK06276 401 AHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVY 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998273 468 mEMKAGGYLTDGTELH---DTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEEL--AIPPQIKL 540
Cdd:PRK06276 481 -QWQNLYYGKRQSEVHlgeTPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAlpMVPPGGNL 557
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
4-166 |
5.77e-77 |
|
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: 240.53 E-value: 5.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 84 GLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPGDV 163
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKRGVAVLILPGDV 160
|
...
gi 490998273 164 ALK 166
Cdd:cd07039 161 QDA 163
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-535 |
3.07e-73 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 244.24 E-value: 3.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 81 LINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-L 159
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIdI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 160 PGDVALKAA----PENASTHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHA 233
Cdd:PRK08527 161 PKDVTATLGefeyPKEISLKTYK---PTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAilSNASEEIRELVKKTGIPAVET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 234 LRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTD-----AKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK08527 238 LMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSefakhAKIIHVDIDPSSISKIVNADYPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 309 VGDIKSTLAALLPHLEEKTDRAFLD--KALEHYREarkgLDDLA-KPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPTV 385
Cdd:PRK08527 318 VGDLKNVLKEMLEELKEENPTTYKEwrEILKRYNE----LHPLSyEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 386 WAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGF 465
Cdd:PRK08527 394 WVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGM 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998273 466 V----AMEMKAGGYLTDGTELHDtnFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK08527 474 VrqwqTFFYEERYSETDLSTQPD--FVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLP 545
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
1-531 |
4.75e-71 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 239.57 E-value: 4.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMP---TRHEEVAAFAAGAEAQLTGELAVCAGSCGPG 77
Cdd:PRK07418 17 QRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAEGWLKhilVRHEQGAAHAADGYARATGKVGVCFGTSGPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 78 NLHLINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVV 157
Cdd:PRK07418 97 ATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 158 V-LPGDVALK------AAPENASTHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKA 228
Cdd:PRK07418 177 IdIPKDVGQEefdyvpVEPGSVKPPGYR---PTVKGNPRQINAALKLIEEAERPLLYVGGGAisAGAHAELKELAERFQI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 229 PVVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPTdAKIIQIDINPGSIGAHS 302
Cdd:PRK07418 254 PVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVtgkldeFASR-AKVIHIDIDPAEVGKNR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 303 KVDMALVGDIKSTLAALLPHLEEKTD----RAFLDKaLEHYREaRKGLddLAKPSDKAIHPQYLAQQIGQFAAdDAIFTC 378
Cdd:PRK07418 333 RPDVPIVGDVRKVLVKLLERSLEPTTpprtQAWLER-INRWKQ-DYPL--VVPPYEGEIYPQEVLLAVRDLAP-DAYYTT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 379 DVGTPTVWAARYLKmNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIF 458
Cdd:PRK07418 408 DVGQHQMWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVII 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 459 NNSVLGFV-------------AMEMKAGgyltdgtelhDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDV 525
Cdd:PRK07418 487 NNGWQGMVrqwqesfygerysASNMEPG----------MPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDV 556
|
....*.
gi 490998273 526 VVAKEE 531
Cdd:PRK07418 557 HVRRDE 562
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
6-539 |
4.32e-67 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 227.78 E-value: 4.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 86 FDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDV- 163
Cdd:PRK08979 87 ATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIdLPKDCl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 164 --ALK---AAPENASTHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHALRG 236
Cdd:PRK08979 167 npAILhpyEYPESIKMRSYN---PTTSGHKGQIKRGLQALLAAKKPVLYVGGGAiiSGADKQILQLAEKLNLPVVSTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAF-----YPTDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:PRK08979 244 LGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTnnlekYCPNATILHIDIDPSSISKTVRVDIPIVGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 312 IKSTLAALLPHLEEKTDR------AFLDKALEHYREaRKGLDdLAKPSDKaIHPQYLAQQIGQFAADDAIFTCDVGTPTV 385
Cdd:PRK08979 324 ADKVLDSMLALLDESGETndeaaiASWWNEIEVWRS-RNCLA-YDKSSER-IKPQQVIETLYKLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 386 WAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGF 465
Cdd:PRK08979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGM 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998273 466 VA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFS-TDGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK08979 481 VKqwQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAmKDRLVFVDINVDETEHVYPMQIR 557
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
4-535 |
5.75e-67 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 228.71 E-value: 5.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK07789 32 TGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 84 GLFDCHRNHVPVVAIAAHIPSSEIGSGYFQE------THPqelfreCSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVV 157
Cdd:PRK07789 112 PIADANMDSVPVVAITGQVGRGLIGTDAFQEadivgiTMP------ITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 158 VlpgDVALKAAPENASTHW--------YAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLK 227
Cdd:PRK07789 186 V---DIPKDALQAQTTFSWpprmdlpgYR---PVTKPHGKQIREAAKLIAAARRPVLYVGGGVirAEASAELRELAELTG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 228 APVVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPtDAKIIQIDINPGSIGAH 301
Cdd:PRK07789 260 IPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRvtgkldSFAP-DAKVIHADIDPAEIGKN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 302 SKVDMALVGDIKSTLAALLPHLEektdRAFLDKALEHYREARKGLDDL--------AKPSDKAIHPQYLAQQIGQFAADD 373
Cdd:PRK07789 339 RHADVPIVGDVKEVIAELIAALR----AEHAAGGKPDLTAWWAYLDGWretyplgyDEPSDGSLAPQYVIERLGEIAGPD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 374 AIFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPV 453
Cdd:PRK07789 415 AIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPI 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 454 KIIIFNNSVLGFVAMEMK---AGGYltDGTELHD-----TNFARIAEACGITGIRVEKASEVDSALQTAFST-DGPVLVD 524
Cdd:PRK07789 495 KVALINNGNLGMVRQWQTlfyEERY--SNTDLHThshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAInDRPVVID 572
|
570
....*....|.
gi 490998273 525 VVVAKEELAIP 535
Cdd:PRK07789 573 FVVGKDAMVWP 583
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-535 |
1.34e-66 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 226.51 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08155 11 KRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 81 LINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-L 159
Cdd:PRK08155 91 LVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIdI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 160 PGDV-----ALKAAPENASthwyAAPLPTVTPpeEEIKKLAQVLRYSSNIALLCGSG--CAGAHAELVQFAAKLKAPVVH 232
Cdd:PRK08155 171 PKDVqtaviELEALPAPAE----KDAAPAFDE--ESIRDAAAMINAAKRPVLYLGGGviNSGAPARARELAEKAQLPTTM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 233 ALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDM 306
Cdd:PRK08155 245 TLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAigkteqFCP-NAKIIHVDIDRAELGKIKQPHV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 307 ALVGDIKSTLAALLPHLEEKTDRAFLDKALEHYRE---ARKGLDDlakpsdkAIHPQYLAQQIGQFAADDAIFTCDVGTP 383
Cdd:PRK08155 324 AIQADVDDVLAQLLPLVEAQPRAEWHQLVADLQREfpcPIPKADD-------PLSHYGLINAVAACVDDNAIITTDVGQH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 384 TVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVL 463
Cdd:PRK08155 397 QMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEAL 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998273 464 GFV--AMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK08155 477 GLVhqQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYP 550
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
9-535 |
1.77e-66 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 226.24 E-value: 1.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK07282 16 VLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITGIADA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 89 HRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDV-ALK 166
Cdd:PRK07282 96 MSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIdLPKDVsALE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 167 AAPENASTHWYAAPLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHALRGKEHVEYDN 244
Cdd:PRK07282 176 TDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGInyAEAATELNAFAERYQIPVVTTLLGQGTIATSH 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 245 PYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLAAL 319
Cdd:PRK07282 256 PLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRltgnpKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKKALQML 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 320 LPHLEEKTD-RAFLDKALEHYREARKglddlAKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRR 398
Cdd:PRK07282 336 LAEPTVHNNtEKWIEKVTKDKNRVRS-----YDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 399 LIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKA--GGYL 476
Cdd:PRK07282 411 LVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESfyEGRT 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 490998273 477 TDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTaFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK07282 491 SESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLEV-ITEDVPMLIEVDISRKEHVLP 548
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
13-535 |
8.43e-66 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 224.62 E-value: 8.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 13 LEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDCHRNH 92
Cdd:PLN02470 23 LEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGLADALLDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 93 VPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVALKAAPEN 171
Cdd:PLN02470 103 VPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVdIPKDIQQQLAVPN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 172 AST----HWYAAPLPTvtPPEEEikKLAQVLRY---SSNIALLCGSGCAGAHAELVQFAAKLKAPVVHALRGKEHVEYDN 244
Cdd:PLN02470 183 WNQpmklPGYLSRLPK--PPEKS--QLEQIVRLiseSKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGLGAFPASD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 245 PYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFyPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLAA 318
Cdd:PLN02470 259 ELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRvtgkleAF-ASRASIVHIDIDPAEIGKNKQPHVSVCADVKLALQG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 319 LLPHLEEKTD--------RAFLDKALEHYREARKGLDDlakpsdkAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARY 390
Cdd:PLN02470 338 LNKLLEERKAkrpdfsawRAELDEQKEKFPLSYPTFGD-------AIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQW 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 391 LKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAM-- 468
Cdd:PLN02470 411 YKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQwe 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998273 469 -----EMKAGGYLTDGTELHDT--NFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PLN02470 491 drfykANRAHTYLGDPDAEAEIfpDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLP 564
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
1-531 |
9.21e-66 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 224.58 E-value: 9.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSL---NRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPG 77
Cdd:CHL00099 8 REKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 78 NLHLINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVV 157
Cdd:CHL00099 88 ATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 158 V-LPGDVALKA----APENASTHWYAAPLPTVTPPE-EEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAP 229
Cdd:CHL00099 168 IdIPKDVGLEKfdyyPPEPGNTIIKILGCRPIYKPTiKRIEQAAKLILQSSQPLLYVGGGAiiSDAHQEITELAELYKIP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 230 VVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAF-----YPTDAKIIQIDINPGSIGAHSKV 304
Cdd:CHL00099 248 VTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTgkldeFACNAQVIHIDIDPAEIGKNRIP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 305 DMALVGDIKSTLAALLPHLEEKTDRAFLDKA---LEHYREARKGLDDLAKPSDKAIHPQYLAQQIGQFAADdAIFTCDVG 381
Cdd:CHL00099 328 QVAIVGDVKKVLQELLELLKNSPNLLESEQTqawRERINRWRKEYPLLIPKPSTSLSPQEVINEISQLAPD-AYFTTDVG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 382 TPTVWAARYLKMnGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNS 461
Cdd:CHL00099 407 QHQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNK 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998273 462 VLGFVAM-------EMKAGGYLTDGTelhdTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEE 531
Cdd:CHL00099 486 WQGMVRQwqqafygERYSHSNMEEGA----PDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDE 558
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-535 |
2.29e-65 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 223.48 E-value: 2.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK07710 19 AQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCG-IPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 86 FDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVA 164
Cdd:PRK07710 98 ADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIdIPKDMV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 165 LkAAPENASTHWYAAP--LPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHALRGKEHV 240
Cdd:PRK07710 178 V-EEGEFCYDVQMDLPgyQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVlhAKASKELTSYAEQQEIPVVHTLLGLGGF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKST 315
Cdd:PRK07710 257 PADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRvtgnlAYFAKEATVAHIDIDPAEIGKNVPTEIPIVADAKQA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 316 LAALLPHLEEKTDRaflDKALEHYREARKGLDDLAKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNG 395
Cdd:PRK07710 337 LQVLLQQEGKKENH---HEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 396 RRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVA--MEMKAG 473
Cdd:PRK07710 414 PDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRqwQEEFYN 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998273 474 GYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK07710 494 QRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMP 555
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
6-525 |
2.06e-64 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 221.22 E-value: 2.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 86 FDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQipqvLAIAMRKAV-INR----GVSVVVLP 160
Cdd:PRK06965 104 ATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRD----LAETVKKAFyIARtgrpGPVVVDIP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 161 GDVALKAA----PENASTHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHAL 234
Cdd:PRK06965 180 KDVSKTPCeyeyPKSVEMRSYN---PVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVilANASRELRQLADLLGYPVTNTL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPTDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK06965 257 MGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVignpahFASRPRKIIHIDIDPSSISKRVKVDIPI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 309 VGDIKSTLAALLPHLEE---KTDRAFLDKALEHYREARKgLDDLA-KPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPT 384
Cdd:PRK06965 337 VGDVKEVLKELIEQLQTaehGPDADALAQWWKQIEGWRS-RDCLKyDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 385 VWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLG 464
Cdd:PRK06965 416 MWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLG 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998273 465 FVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFS-TDGPVLVDV 525
Cdd:PRK06965 496 MVRqwQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRlKDRTVFLDF 559
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
4-535 |
3.81e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 220.22 E-value: 3.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06725 16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 84 GLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGD 162
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRpGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 163 VALKAA----PENASTHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHALRG 236
Cdd:PRK06725 175 VQNEKVtsfyNEVVEIPGYK---PEPRPDSMKLREVAKAISKAKRPLLYIGGGVihSGGSEELIEFARENRIPVVSTLMG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK06725 252 LGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVtgklelFSP-HSKKVHIDIDPSEFHKNVAVEYPVVG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 311 DIKSTLAALLPHLEEKTDRAFLDKALEHYREARKGLDdlAKPSDkaIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARY 390
Cdd:PRK06725 331 DVKKALHMLLHMSIHTQTDEWLQKVKTWKEEYPLSYK--QKESE--LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 391 LKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVA--M 468
Cdd:PRK06725 407 YKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRqwQ 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998273 469 EMKAGGYLTDgTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK06725 487 EMFYENRLSE-SKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFP 552
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
6-539 |
3.04e-62 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 214.99 E-value: 3.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06466 7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 86 FDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVA 164
Cdd:PRK06466 87 ATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVdIPKDMT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 165 LKAA------PENASTHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHALRG 236
Cdd:PRK06466 167 NPAEkfeyeyPKKVKLRSYS---PAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVvlGNASALLTELAHLLNLPVTNTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK06466 244 LGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVtngpakFCP-NAKIIHIDIDPASISKTIKADIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 311 DIKSTLA---ALLPHLEEKTDRAFLD---KALEHYReARKGLDDLAKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPT 384
Cdd:PRK06466 323 PVESVLTemlAILKEIGEKPDKEALAawwKQIDEWR-GRHGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 385 VWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLG 464
Cdd:PRK06466 402 MFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALG 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998273 465 FVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFS-TDGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK06466 482 MVRqwQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVDRSEHVYPMQIA 559
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
2-535 |
1.05e-61 |
|
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: 213.57 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 2 KQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAG-IRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 82 INGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPG 161
Cdd:TIGR03457 80 VTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREMGPAQLNIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 162 DvalkaapenastHWYAA-------PLPTVTPP--EEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPV 230
Cdd:TIGR03457 160 D------------YFYGEidveiprPVRLDRGAggATSLAQAARLLAEAKFPVIISGGGVvmGDAVEECKALAERLGAPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 231 VHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQF-PYRA-------FYPTDAKIIQIDINPGSIGAHS 302
Cdd:TIGR03457 228 VNSYLHNDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLgPFGTlpqygidYWPKNAKIIQVDANAKMIGLVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 303 KVDMALVGDIKSTLAALLPHLEEKTDRAFLDKALEHYREAR----KGLDDLAKPSDKA---------------IHPQYLA 363
Cdd:TIGR03457 308 KVTVGICGDAKAAAAEILQRLAGKAGDANRAERKAKIQAERsaweQELSEMTHERDPFsldmiveqrqeegnwLHPRQVL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 364 QQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDF 443
Cdd:TIGR03457 388 RELEKAMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 444 LSLAQMKLPVKIIIFNNSVLGfvaMEMKAGGYLTD----GTELH-DTNFARIAEACGITGIRVEKASEVDSALQTAFS-- 516
Cdd:TIGR03457 468 MTAVRHDIPVTAVVFRNRQWG---AEKKNQVDFYNnrfvGTELEsELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAaq 544
|
570
....*....|....*....
gi 490998273 517 TDGPVLVDVVVAKEELAIP 535
Cdd:TIGR03457 545 AEGKTTVIEIVCTRELGDP 563
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
2-539 |
1.56e-61 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 213.24 E-value: 1.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 2 KQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:PRK06882 3 KLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 82 INGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LP 160
Cdd:PRK06882 83 ITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIdIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 161 GDValkAAPENASTHWYAAPL------PTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVH 232
Cdd:PRK06882 163 KDM---VNPANKFTYEYPEEVslrsynPTVQGHKGQIKKALKALLVAKKPVLFVGGGVitAECSEQLTQFAQKLNLPVTS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 233 ALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMA 307
Cdd:PRK06882 240 SLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRttnnlAKYCPNAKVIHIDIDPTSISKNVPAYIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 308 LVGDIKSTLAALLPHLEEKT---DRAFLDKALEHYRE--ARKGLDdlAKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGT 382
Cdd:PRK06882 320 IVGSAKNVLEEFLSLLEEENlakSQTDLTAWWQQINEwkAKKCLE--FDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 383 PTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSV 462
Cdd:PRK06882 398 HQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 463 LGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFST-DGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK06882 478 LGMVKqwQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIkDKLVFVDVNVDETEHVYPMQIR 557
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
64-531 |
1.94e-61 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 212.05 E-value: 1.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 64 TGELAVCAGSCGPGNLHLINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAI 143
Cdd:PRK08978 61 TGKVGVCIATSGPGATNLITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 144 AMRKAVINRGVSVVV-LPGDVALKAAPenaSTHWYAAPLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELV 220
Cdd:PRK08978 141 AFEIASSGRPGPVLVdIPKDIQLAEGE---LEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVgmAGAVPALR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 221 QFAAKLKAPVVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDIN 294
Cdd:PRK08978 218 EFLAATGMPAVATLKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVtgklntFAP-HAKVIHLDID 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 295 PGSIGAHSKVDMALVGDIKstlaALLPHLEEKTDrafLDKALEHYREARKGLDDLAKPSDKAIHPQYLAQQIGQFAADDA 374
Cdd:PRK08978 297 PAEINKLRQAHVALQGDLN----ALLPALQQPLN---IDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADT 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 375 IFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVK 454
Cdd:PRK08978 370 VVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVK 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 455 IIIFNNSVLGFVAMEMK---AGGYltDGTELHDT-NFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKE 530
Cdd:PRK08978 450 IVLLDNQRLGMVRQWQQlffDERY--SETDLSDNpDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDEL 527
|
.
gi 490998273 531 E 531
Cdd:PRK08978 528 E 528
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
6-539 |
2.68e-60 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 209.71 E-value: 2.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK07979 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 86 FDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGDV- 163
Cdd:PRK07979 87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKDIl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 164 --ALK---AAPENASTHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHALRG 236
Cdd:PRK07979 167 npANKlpyVWPESVSMRSYN---PTTQGHKGQIKRALQTLVAAKKPVVYVGGGAinAACHQQLKELVEKLNLPVVSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:PRK07979 244 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRttnnlAKYCPNATVLHIDIDPTSISKTVTADIPIVGD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 312 IKSTLAALLPHLEEKTDRAFLD------KALEHYReARKGLDdLAKPSDKaIHPQYLAQQIGQFAADDAIFTCDVGTPTV 385
Cdd:PRK07979 324 ARQVLEQMLELLSQESAHQPLDeirdwwQQIEQWR-ARQCLK-YDTHSEK-IKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 386 WAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGF 465
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998273 466 VA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAF---STDGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK07979 481 VKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALeqvRNNRLVFVDVTVDGSEHVYPMQIR 559
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
6-542 |
4.72e-60 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 208.92 E-value: 4.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLN---RMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLI 82
Cdd:PRK06456 5 ARILVDSLKREGVKVIFGIPGLSNMQIYDAFVedlANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 83 NGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPG 161
Cdd:PRK06456 85 TGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRpGPVVIDIPR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 162 DVALKAA-----PENASTHWYaAPLPTVTPPeEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHAL 234
Cdd:PRK06456 165 DIFYEKMeeikwPEKPLVKGY-RDFPTRIDR-LALKKAAEILINAERPIILVGTGVvwSNATPEVLELAELLHIPIVSTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYP------TDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK06456 243 PGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSydemveTRKKFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 309 VGDIKSTLAALL---PHLEEKTDRAFLDKALEHYREARKGLddLAKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPTV 385
Cdd:PRK06456 323 YGNAKIILRELIkaiTELGQKRDRSAWLKRVKEYKEYYSQF--YYTEENGKLKPWKIMKTIRQALPRDAIVTTGVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 386 WAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGF 465
Cdd:PRK06456 401 WAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 466 V--AMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELA---IPPQIKL 540
Cdd:PRK06456 481 VrqVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELAlptLPPGGRL 560
|
..
gi 490998273 541 EQ 542
Cdd:PRK06456 561 KQ 562
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
4-536 |
3.50e-59 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 206.92 E-value: 3.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWmptRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFGQSLPSALFLAAEAIGIRQIAY---RTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 84 GLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGD 162
Cdd:PRK06112 92 PLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRpGPVVLLLPAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 163 V-----ALKAAPENAST-HWyaaPLPTVTPPEEEIKKLAQVLRYSSNIALLCGSG--CAGAHAELVQFAAKLKAPVVHAL 234
Cdd:PRK06112 172 LltaaaAAPAAPRSNSLgHF---PLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGvhISGASAALAALQSLAGLPVATTN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 235 RGKEHVEYDNPYDVGMTG-LIG-FSSGFHTM---MNADTLVLLGTQFPYRA-----FYPTDAKIIQIDINPGSIGAHSKV 304
Cdd:PRK06112 249 MGKGAVDETHPLSLGVVGsLMGpRSPGRHLRdlvREADVVLLVGTRTNQNGtdswsLYPEQAQYIHIDVDGEEVGRNYEA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 305 dMALVGDIKSTLAALLPHLE------EKTDRAFLDKALEHYREA-RKGLDDLAKPSDKAIHPQYLAQQIGQFAADDAIFT 377
Cdd:PRK06112 329 -LRLVGDARLTLAALTDALRgrdlaaRAGRRAALEPAIAAGREAhREDSAPVALSDASPIRPERIMAELQAVLTGDTIVV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 378 CDVGTPTVWAARYLKM-NGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKII 456
Cdd:PRK06112 408 ADASYSSIWVANFLTArRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIV 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 457 IFNNSVLGFV--AMEMKAGGYlTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVakEELAI 534
Cdd:PRK06112 488 VLNNGILGFQkhAETVKFGTH-TDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVIT--DPSAF 564
|
..
gi 490998273 535 PP 536
Cdd:PRK06112 565 PP 566
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-535 |
5.02e-59 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 206.39 E-value: 5.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK07525 4 MKMTPSEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAG-IRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 81 LINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLP 160
Cdd:PRK07525 83 FVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESGPAQINIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 161 GDvalkaapenastHWYA---APLPTV------TPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAP 229
Cdd:PRK07525 163 RD------------YFYGvidVEIPQPvrlergAGGEQSLAEAAELLSEAKFPVILSGAGVvlSDAIEECKALAERLDAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 230 VVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQF-PYRA-------FYPTDAKIIQIDINPGSIGAH 301
Cdd:PRK07525 231 VACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLnPFGTlpqygidYWPKDAKIIQVDINPDRIGLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 302 SKVDMALVGDIKSTLAALLPHLEEKT----DRAfLDKALEHYREAR--KGLDDLAKPSD---------------KAIHPQ 360
Cdd:PRK07525 311 KKVSVGICGDAKAVARELLARLAERLagdaGRE-ERKALIAAEKSAweQELSSWDHEDDdpgtdwneeararkpDYMHPR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 361 YLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLM 440
Cdd:PRK07525 390 QALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 441 GDFLSLAQMKLPVKIIIFNNSVLG-------------FVamemkaggyltdGTEL-HDTNFARIAEACGITGIRVEKASE 506
Cdd:PRK07525 470 NEVMTAVRHNWPVTAVVFRNYQWGaekknqvdfynnrFV------------GTELdNNVSYAGIAEAMGAEGVVVDTQEE 537
|
570 580 590
....*....|....*....|....*....|.
gi 490998273 507 VDSALQTAFS--TDGPVLVDVVVAKEELAIP 535
Cdd:PRK07525 538 LGPALKRAIDaqNEGKTTVIEIMCNQELGEP 568
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-535 |
1.49e-58 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 204.09 E-value: 1.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGT-IAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08266 2 TTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 80 HLINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQ--ETHPQ-ELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSV 156
Cdd:PRK08266 82 NAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMPDQlATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 157 VV-LPGDVALKAAPENASTHwyAAPLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGCAGAHAELVQFAAKLKAPVVHALR 235
Cdd:PRK08266 162 ALeMPWDVFGQRAPVAAAPP--LRPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 236 GKEHVeyDNPYDVGMTgligFSSGFHTMMNADTLVLLGT----QFPYRAFYPTDAKIIQIDINPGSIGAHsKVDMALVGD 311
Cdd:PRK08266 240 GRGIV--SDRHPLGLN----FAAAYELWPQTDVVIGIGSrlelPTFRWPWRPDGLKVIRIDIDPTEMRRL-KPDVAIVAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 312 IKSTLAALLPHLEEKTDRAfldkalEHYREARKGLDDLAKPSDKAIHPQ--YLaQQIGQFAADDAIFT---CDVGtptvW 386
Cdd:PRK08266 313 AKAGTAALLDALSKAGSKR------PSRRAELRELKAAARQRIQAVQPQasYL-RAIREALPDDGIFVdelSQVG----F 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 387 AARY-LKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGF 465
Cdd:PRK08266 382 ASWFaFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGN 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998273 466 VAMEMK---AGGYLtdGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK08266 462 VRRDQKrrfGGRVV--ASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEASP 532
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-527 |
3.39e-58 |
|
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: 203.06 E-value: 3.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:TIGR02418 2 ADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKG-IELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 86 FDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGDVA 164
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKpGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 165 lkAAPENASThWYAAPLPTV-TPPEEEIKKLAQVLRYSSNIALLCG--SGCAGAHAELVQFAAKLKAPVVHALRGKEHVE 241
Cdd:TIGR02418 161 --DSPVSVKA-IPASYAPKLgAAPDDAIDEVAEAIQNAKLPVLLLGlrASSPETTEAVRRLLKKTQLPVVETFQGAGAVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 242 YDN-PYDVGMTGLIGFSSGFHTMMNADTLVLLG-TQFPYRAFY---PTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTL 316
Cdd:TIGR02418 238 RELeDHFFGRVGLFRNQPGDRLLKQADLVITIGyDPIEYEPRNwnsENDATIVHIDVEPAQIDNNYQPDLELVGDIASTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 317 AALLPHLEE----KTDRAFLdKALEHYREARKGLDdlAKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLK 392
Cdd:TIGR02418 318 DLLAERIPGyelpPDALAIL-EDLKQQREALDRVP--ATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 393 MNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAM--EM 470
Cdd:TIGR02418 395 SYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFqeEM 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 490998273 471 KAGgyLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVV 527
Cdd:TIGR02418 475 KYQ--RSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPV 529
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-527 |
7.20e-56 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 197.00 E-value: 7.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTG---DSL-NGLSDSlnrmgTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGP 76
Cdd:PRK08617 3 KKKYGADLVVDSLINQGVKYVFGIPGakiDRVfDALEDS-----GPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 77 GNLHLINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVS 155
Cdd:PRK08617 78 GVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRpGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 156 VVVLPGDVALKAAPENAsthwyAAPLPTVT---PPEEEIKKLAQVLRYSSNIALLCG--SGCAGAHAELVQFAAKLKAPV 230
Cdd:PRK08617 158 FVSLPQDVVDAPVTSKA-----IAPLSKPKlgpASPEDINYLAELIKNAKLPVLLLGmrASSPEVTAAIRRLLERTNLPV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 231 VHALRGKEHV--EYDNPYdVGMTGLIGFSSGFHTMMNADTLVLLGtqfpYRAF-Y-------PTDAKIIQIDINPGSIGA 300
Cdd:PRK08617 233 VETFQAAGVIsrELEDHF-FGRVGLFRNQPGDELLKKADLVITIG----YDPIeYeprnwnsEGDATIIHIDVLPAEIDN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 301 HSKVDMALVGDIKSTLAALLPHLEE-KTDRAFLDkALEHYREARKGLDDLAKPSDK-AIHPQYLAQQIGQFAADDAIFTC 378
Cdd:PRK08617 308 YYQPERELIGDIAATLDLLAEKLDGlSLSPQSLE-ILEELRAQLEELAERPARLEEgAVHPLRIIRALQDIVTDDTTVTV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 379 DVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFsMLMGDFLSLA-QMKLPVKIII 457
Cdd:PRK08617 387 DVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGF-LFSAMELETAvRLKLNIVHII 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998273 458 FNNSVLGFVAM--EMKAGGylTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVV 527
Cdd:PRK08617 466 WNDGHYNMVEFqeEMKYGR--SSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPV 535
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
4-535 |
9.00e-56 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 198.01 E-value: 9.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK09107 12 TGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 84 GLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGD 162
Cdd:PRK09107 92 PLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVdIPKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 163 VALKA----APENA-STHWYAaplPTVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHA-----ELVQFAAklkAPV 230
Cdd:PRK09107 172 VQFATgtytPPQKApVHVSYQ---PKVKGDAEAITEAVELLANAKRPVIYSGGGVinSGPEAsrllrELVELTG---FPI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 231 VHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPTdAKIIQIDINPGSIGAHSKV 304
Cdd:PRK09107 246 TSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRitgrldAFSPN-SKKIHIDIDPSSINKNVRV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 305 DMALVGDIKSTLAALLPHLE---EKTDRAFLDK---ALEHYReARKGLDdlAKPSDKAIHPQYLAQQIGQFAAD-DAIFT 377
Cdd:PRK09107 325 DVPIIGDVGHVLEDMLRLWKargKKPDKEALADwwgQIARWR-ARNSLA--YTPSDDVIMPQYAIQRLYELTKGrDTYIT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 378 CDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIII 457
Cdd:PRK09107 402 TEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFI 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 458 FNNSVLGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK09107 482 LNNQYMGMVRqwQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFP 561
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
357-535 |
1.34e-54 |
|
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: 183.08 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 357 IHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 437 SMLMGDFLSLAQMKLPVKIIIFNNSVLGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTA 514
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRqwQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|.
gi 490998273 515 FSTDGPVLVDVVVAKEELAIP 535
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLP 181
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
11-527 |
6.40e-54 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 191.58 E-value: 6.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 11 KTLEQAGVKRIWGVTG----DSLNGLSDSlnrmgTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLF 86
Cdd:PRK08322 9 KCLENEGVEYIFGIPGeenlDLLEALRDS-----SIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 87 DCHRNHVPVVAIAAHIP--SSEIGSgyFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRgvsvvvlPGDVA 164
Cdd:PRK08322 84 YAQLGGMPMVAITGQKPikRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEER-------PGAVH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 165 LkAAPEN-ASTHWYAAPLP-----TVTPPEEEIKKLAQVLRYSSNIALLCGSGCAGAHA--ELVQFAAKLKAPVVHALRG 236
Cdd:PRK08322 155 L-ELPEDiAAEETDGKPLPrsysrRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTAskALTEFVDKTGIPFFTTQMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 237 KEHVEYDNPYDVGMTGL-----IGFssGFHtmmNADTLVLLGTQF----PYRAFYPTDAKIIQIDINPGSIGAHSKVDMA 307
Cdd:PRK08322 234 KGVIPETHPLSLGTAGLsqgdyVHC--AIE---HADLIINVGHDViekpPFFMNPNGDKKVIHINFLPAEVDPVYFPQVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 308 LVGDIKSTLAALLPHLEEKTDRAFldKALEHYREA-RKGLDDLAKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPTVW 386
Cdd:PRK08322 309 VVGDIANSLWQLKERLADQPHWDF--PRFLKIREAiEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 387 AARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFV 466
Cdd:PRK08322 387 FARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998273 467 AMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVV 527
Cdd:PRK08322 467 RWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPV 527
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
379-525 |
7.01e-52 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 174.31 E-value: 7.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 379 DVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIF 458
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998273 459 NNSVLGFVAMEMKAGG----YLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDV 525
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGggrySGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
362-527 |
1.09e-45 |
|
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: 158.57 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 362 LAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMG 441
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 442 DFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYLTD-GTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGP 520
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVsGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGGP 161
|
....*..
gi 490998273 521 VLVDVVV 527
Cdd:cd00568 162 ALIEVKT 168
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
1-539 |
2.74e-45 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 167.86 E-value: 2.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTgdSLNGLS--DSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGN 78
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVI--SIHNMPilDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 79 LHLINGLFDCHRNHVPVVAIAAHIPSSEIGS--GYFQETHPQ-ELFRECSHYCELVSTPEQIPQVLAIAMRKAV-INRGV 154
Cdd:PRK07064 79 GNAAGALVEALTAGTPLLHITGQIETPYLDQdlGYIHEAPDQlTMLRAVSKAAFRVRSAETALATIREAVRVALtAPTGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 155 SVVVLPGDV--ALKAAPENASthwyAAPLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGCAGAHAElVQFAAKLKAPVVH 232
Cdd:PRK07064 159 VSVEIPIDIqaAEIELPDDLA----PVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAE-VKRLVDLGFGVVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 233 ALRGKEHVEYDNPYDVGMTGLIGFSSGFHTmmNADTLVLLGTQF------PYRAFYPTDakIIQIDINPGSIGAHSKVDM 306
Cdd:PRK07064 234 STQGRGVVPEDHPASLGAFNNSAAVEALYK--TCDLLLVVGSRLrgnetlKYSLALPRP--LIRVDADAAADGRGYPNDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 307 ALVGDIKSTLAALLPHLEE--KTDRAFlDKALEHYREA-----RKGLDDLAKpsdkaihpqyLAQQIGQFAADDAIFTCD 379
Cdd:PRK07064 310 FVHGDAARVLARLADRLEGrlSVDPAF-AADLRAAREAavadlRKGLGPYAK----------LVDALRAALPRDGNWVRD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 380 VGTP-TVWAARYLKMNGRRRLIGSFNhGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIF 458
Cdd:PRK07064 379 VTISnSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLM 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 459 NNSVLGFV-AMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVA-----KEEL 532
Cdd:PRK07064 458 NDGGYGVIrNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVDMLsigpfAAAF 537
|
....*..
gi 490998273 533 AIPPQIK 539
Cdd:PRK07064 538 AGPPVKK 544
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-542 |
1.59e-42 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 160.43 E-value: 1.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08199 6 RARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 81 LINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVL 159
Cdd:PRK08199 86 ASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRpGPVVLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 160 PGDVALKAAPenasthwyAAPLPTVTPPE-----EEIKKLAQVL-RYSSNIALLCGSG-CAGAHAELVQFAAKLKAPVVH 232
Cdd:PRK08199 166 PEDVLSETAE--------VPDAPPYRRVAaapgaADLARLAELLaRAERPLVILGGSGwTEAAVADLRAFAERWGLPVAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 233 ALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFP------YRAF---YPtDAKIIQIDINPGSIGAHSK 303
Cdd:PRK08199 238 AFRRQDLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGevttqgYTLLdipVP-RQTLVHVHPDAEELGRVYR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 304 VDMALVGDIKSTLAALL----PHLEEKTDRAflDKALEHYREARKglddlAKPSDKAIHPQYLAQQIGQFAADDAIFTCD 379
Cdd:PRK08199 317 PDLAIVADPAAFAAALAalepPASPAWAEWT--AAAHADYLAWSA-----PLPGPGAVQLGEVMAWLRERLPADAIITNG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 380 VGTPTVWAARYLKMNGRRRLIGSFNhGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFN 459
Cdd:PRK08199 390 AGNYATWLHRFFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVN 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 460 NSVLGFVAM--EMKAGGYlTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAKEelAIPPQ 537
Cdd:PRK08199 469 NGMYGTIRMhqEREYPGR-VSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPE--AITPT 545
|
....*
gi 490998273 538 IKLEQ 542
Cdd:PRK08199 546 ATLSQ 550
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
62-529 |
5.78e-42 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 159.01 E-value: 5.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 62 QLTGELAVCAGSCGPGNLHLINGLFDCHRNHVPVVAIAAHIPSSEIGS--------GYFQETHPQ-ELFRECSHYCELVS 132
Cdd:PRK08327 71 LVTGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrntriHWTQEMRDQgGLVREYVKWDYEIR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 133 TPEQIPQVLAIAMRKAVIN-RGVSVVVLPGDVALKAAPENASTHWYAAPLPTVTPPEEEIKKLAQVLRYSSNIALLC--G 209
Cdd:PRK08327 151 RGDQIGEVVARAIQIAMSEpKGPVYLTLPREVLAEEVPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITwrA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 210 SGCAGAHAELVQFAAKLKAPVVHAlRGkEHVEY--DNPYDVGmtgligfSSGFHTMMNADTLVLLGTQFPY---RAFYPT 284
Cdd:PRK08327 231 GRTAEGFASLRRLAEELAIPVVEY-AG-EVVNYpsDHPLHLG-------PDPRADLAEADLVLVVDSDVPWipkKIRPDA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 285 DAKIIQIDINPgsigAHSK-------VDMALVGDIKSTLAALLPHL--EEKTDRAFLDKALEHYREARKGLDDL------ 349
Cdd:PRK08327 302 DARVIQIDVDP----LKSRiplwgfpCDLCIQADTSTALDQLEERLksLASAERRRARRRRAAVRELRIRQEAAkraeie 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 350 AKPSDKAIHPQYLAQQIGQFAAD-DAIFTcdvGTPTVWaaRYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVV 428
Cdd:PRK08327 378 RLKDRGPITPAYLSYCLGEVADEyDAIVT---EYPFVP--RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVI 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 429 AMCGDGGFsmLMGD---FLSLAQ-MKLPVKIIIFNNSVLGFVA---MEMKAGGY--------LTDGTElhDTNFARIAEA 493
Cdd:PRK08327 453 ATVGDGSF--IFGVpeaAHWVAErYGLPVLVVVFNNGGWLAVKeavLEVYPEGYaarkgtfpGTDFDP--RPDFAKIAEA 528
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 490998273 494 CGITGIRVEKASEVDSALQTAF----STDGPVLVDVVVAK 529
Cdd:PRK08327 529 FGGYGERVEDPEELKGALRRALaavrKGRRSAVLDVIVDR 568
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-530 |
3.96e-38 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 148.20 E-value: 3.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLT-GELAVCAGSCGPGNL 79
Cdd:PRK11269 2 AKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 80 HLINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV- 158
Cdd:PRK11269 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLId 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 159 LPGDVALKAAPENASTHwyaAPLP--TVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHAL 234
Cdd:PRK11269 162 LPFDVQVAEIEFDPDTY---EPLPvyKPAATRAQIEKALEMLNAAERPLIVAGGGVinADASDLLVEFAELTGVPVIPTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 235 RGKEHVEYDNPYDVGMTGL-IGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK11269 239 MGWGAIPDDHPLMAGMVGLqTSHRYGNATLLASDFVLGIGNRWANRhtgsvEVYTKGRKFVHVDIEPTQIGRVFGPDLGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 309 VGDIKSTLAALLPHLEEKTDRAFLDKALEHYREARKGLDDLAKPSD---KAIHPQYLAQQIGQFAADDAIFTCDVGTPTV 385
Cdd:PRK11269 319 VSDAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTLLRKTHfdnVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 386 WAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGF 465
Cdd:PRK11269 399 AAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 466 V-----AMEM--------------KAGGYLTDgtelhdtnFARIAEACGITGIRVEKASEVDSALQTA------FSTdgP 520
Cdd:PRK11269 479 IrqaqrAFDMdycvqlafeninspELNGYGVD--------HVKVAEGLGCKAIRVFKPEDIAPALEQAkalmaeFRV--P 548
|
570
....*....|
gi 490998273 521 VLVDVVVAKE 530
Cdd:PRK11269 549 VVVEVILERV 558
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
5-535 |
4.48e-38 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 148.04 E-value: 4.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 5 VAAYIAKTLEQAGVKRIWGVtgdSLNGLSDSLNRMGtIAWMPTRHEEVAAFAAGAEAQLTG--ELAVCAGSCGPGNLHLI 82
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGF---PVNELFDAAAAAG-IRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 83 NGLFDCHRNHVPVVAIAAHIPSSEigsgyfQETHPQ----ELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV 158
Cdd:PRK06154 98 GGVAQAYGDSVPVLFLPTGYPRGS------TDVAPNfeslRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 159 -LPGDVALKAAPENASTHwyAAPLPTVTPPEE-EIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHAL 234
Cdd:PRK06154 172 eLPVDVLAEELDELPLDH--RPSRRSRPGADPvEVVEAAALLLAAERPVIYAGQGVlyAQATPELKELAELLEIPVMTTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAF---YPTDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:PRK06154 250 NGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYglpMPEGKTIIHSTLDDADLNKDYPIDHGLVGD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 312 IKSTLAALLP-----HLEEKTDRAFLDKALEHYREA--RKGLDDLAKpSDKAIHPQYLAQQIGQ-FAADDAIFTCDVGTP 383
Cdd:PRK06154 330 AALVLKQMIEelrrrVGPDRGRAQQVAAEIEAVRAAwlAKWMPKLTS-DSTPINPYRVVWELQHaVDIKTVIITHDAGSP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 384 TVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVL 463
Cdd:PRK06154 409 RDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNFSM 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 464 GFVAMEMKAggyltdGTELHDTNF-----ARIAEACGITGIRVEKASEVDSALQTAF--STDG-PVLVDVVVAKE-ELAI 534
Cdd:PRK06154 489 GGYDKVMPV------STTKYRATDisgdyAAIARALGGYGERVEDPEMLVPALLRALrkVKEGtPALLEVITSEEtALSR 562
|
.
gi 490998273 535 P 535
Cdd:PRK06154 563 P 563
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
9-526 |
8.88e-38 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 146.79 E-value: 8.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK05858 11 AARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 89 HRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVI-NRGVSVVVLPGDVALKA 167
Cdd:PRK05858 90 QFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTpHRGPVFVDFPMDHAFSM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 168 APENASthwyaaPLPTVTPPEE------EIKKLAQVLRYSSNIALLCGSGCAGAHAE--LVQFAAKLKAPVVHALRGKEH 239
Cdd:PRK05858 170 ADDDGR------PGALTELPAGptpdpdALARAAGLLAEAQRPVIMAGTDVWWGHAEaaLLRLAEELGIPVLMNGMGRGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 240 VEYDNPydvgmtglIGFSSGFHTMM-NADTLVLLGTQFPYR---AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKST 315
Cdd:PRK05858 244 VPADHP--------LAFSRARGKALgEADVVLVVGVPMDFRlgfGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 316 LAALLPHLEEKTDRAFLDKALEHYREARKGLDDLAKPSDKA-IHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMN 394
Cdd:PRK05858 316 LSALAGAGGDRTDHQGWIEELRTAETAARARDAAELADDRDpIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 395 GRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDG--GFSMLmgDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKA 472
Cdd:PRK05858 396 RPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGafGFSLM--DVDTLVRHNLPVVSVIGNNGIWGLEKHPMEA 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 490998273 473 -GGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVV 526
Cdd:PRK05858 474 lYGYDVAADLRPGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVL 528
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
108-529 |
9.65e-38 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 146.66 E-value: 9.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 108 GSGYFQETHPQE-LFRECSHYCELVSTPEQIPQVLAIAMrkAVINRG----------VSVVVLPGDVALKAAPENAsthw 176
Cdd:PRK07524 108 GRGKLHELPDQRaMVAGVAAFSHTLMSAEDLPEVLARAF--AVFDSArprpvhieipLDVLAAPADHLLPAPPTRP---- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 177 yAAPlptvTPPEEEIKKLAQVLRYSSNIALLCGSGCAGAHAELVQFAAKLKAPVVHALRGKEHVEYDNPYDVGMTGLIgf 256
Cdd:PRK07524 182 -ARP----GPAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSL-- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 257 SSGFHTMMNADTLVLLGTQF-------PYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLAALLPHLEEKTDR 329
Cdd:PRK07524 255 PAVRALIAEADVVLAVGTELgetdydvYFDGGFPLPGELIRIDIDPDQLARNYPPALALVGDARAALEALLARLPGQAAA 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 330 AflDKALEHYREARKgldDLAKPSDKAIHPQYLAQQIGQFAADDAIFTCDvGTPTVWAAR-YLKMNGRRR-LIGSFNHGS 407
Cdd:PRK07524 335 A--DWGAARVAALRQ---ALRAEWDPLTAAQVALLDTILAALPDAIFVGD-STQPVYAGNlYFDADAPRRwFNASTGYGT 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 408 MANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYLTDGTELHDTNF 487
Cdd:PRK07524 409 LGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDF 488
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 490998273 488 ARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVVAK 529
Cdd:PRK07524 489 IALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQAC 530
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
191-319 |
1.66e-37 |
|
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: 135.38 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 191 IKKLAQVLRYSSNIALLCGSGC--AGAHAELVQFAAKLKAPVVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADT 268
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVrrSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 490998273 269 LVLLGTQF-------PYRAFYPtDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLAAL 319
Cdd:pfam00205 81 VLAVGARFddirttgKLPEFAP-DAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
5-170 |
7.42e-36 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 131.97 E-value: 7.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 5 VAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLING 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 85 LFDCHRNHVPVVAIAAHIPSSEIGSGYFQ-ETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGD 162
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRpGPVYLEIPLD 160
|
....*...
gi 490998273 163 VALKAAPE 170
Cdd:pfam02776 161 VLLEEVDE 168
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
359-527 |
1.50e-31 |
|
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: 120.47 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 359 PQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSM 438
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 439 LMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFSTD 518
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
....*....
gi 490998273 519 GPVLVDVVV 527
Cdd:cd02010 161 GVHVIDCPV 169
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
78-528 |
6.92e-31 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 126.61 E-value: 6.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 78 NLHLING-------LFDCHRNHVPVVAIAAHIPSSEIGSGYF-QETHPQELFRECSHY-CElVSTPEQIPQVLA----IA 144
Cdd:PRK07092 78 NLHSAAGvgnamgnLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWsIE-PARAEDVPAAIArayhIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 145 MRKAvinRGVSVVVLPGDVALKAAPENASTHWYAAplptVTPPEEEIKKLAQVLRYSSNIALLCGSGC--AGAHAELVQF 222
Cdd:PRK07092 157 MQPP---RGPVFVSIPYDDWDQPAEPLPARTVSSA----VRPDPAALARLGDALDAARRPALVVGPAVdrAGAWDDAVRL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 223 AAKLKAPVVHAlrgkehveydnPydvgMTGLIGFSS------GFHTMMNA---------DTLVLLGT------QFPYRAF 281
Cdd:PRK07092 230 AERHRAPVWVA-----------P----MSGRCSFPEdhplfaGFLPASREkisalldghDLVLVIGApvftyhVEGPGPH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 282 YPTDAKIIQIDINPGsIGAHSKVDMALVGDIKSTLAALLPHLEEkTDRAFLdkalehyrEARKGLDDLAKPSDkAIHPQY 361
Cdd:PRK07092 295 LPEGAELVQLTDDPG-EAAWAPMGDAIVGDIRLALRDLLALLPP-SARPAP--------PARPMPPPAPAPGE-PLSVAF 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 362 LAQQIGQFAADDAIFTCDV--GTPTVWaaRYLKMNGRrrliGSF---NHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:PRK07092 364 VLQTLAALRPADAIVVEEApsTRPAMQ--EHLPMRRQ----GSFytmASGGLGYGLPAAVGVALAQPGRRVIGLIGDGSA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 437 SMLMGDFLSLAQMKLPVKIIIFNNSvlGFVAME-----MKAGGylTDGTELHDTNFARIAEACGITGIRVEKASEVDSAL 511
Cdd:PRK07092 438 MYSIQALWSAAQLKLPVTFVILNNG--RYGALRwfapvFGVRD--VPGLDLPGLDFVALARGYGCEAVRVSDAAELADAL 513
|
490
....*....|....*..
gi 490998273 512 QTAFSTDGPVLVDVVVA 528
Cdd:PRK07092 514 ARALAADGPVLVEVEVA 530
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
359-528 |
8.11e-30 |
|
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: 115.32 E-value: 8.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 359 PQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSM 438
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 439 LMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEM--KAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEVDSALQTAFS 516
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQqlSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 490998273 517 TDGPVLVDVVVA 528
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-539 |
8.46e-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: 123.34 E-value: 8.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHeevaafaagaeaqltgELavCAGSC------ 74
Cdd:COG3961 3 MTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCN----------------EL--NAGYAadgyar 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 75 -----------GPGNLHLINGLFDCHRNHVPVVAIAAhIPSSEI-----------GSGYFqeTHPQELFRECSHYCELVs 132
Cdd:COG3961 65 vnglgalvttyGVGELSAINGIAGAYAERVPVVHIVG-APGTRAqrrgpllhhtlGDGDF--DHFLRMFEEVTVAQAVL- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 133 TPE----QIPQVLAIAMRKaviNRGVsVVVLPGDVAlkAAPENASTHWYAAPLPTVTPP--EEEIKKLAQVLRYSSNIAL 206
Cdd:COG3961 141 TPEnaaaEIDRVLAAALRE---KRPV-YIELPRDVA--DAPIEPPEAPLPLPPPASDPAalAAAVAAAAERLAKAKRPVI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 207 LCGSGCA--GAHAELVQFAAKLKAPVVHALRGKEHVEYDNPYDVGM-TGLIGFSSGFHTMMNADTLVLLGTQFpyrafyp 283
Cdd:COG3961 215 LAGVEVHrfGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGVVF------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 284 TD-------AKIIQ---IDINPG--SIGAH--SKVDMAlvgDIKSTLAALLPHLEEktdrafldkaleHYREARKGLDDL 349
Cdd:COG3961 288 TDtntggftAQLDPertIDIQPDsvRVGGHiyPGVSLA---DFLEALAELLKKRSA------------PLPAPAPPPPPP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 350 AKPSDKAIHPQYLAQQIGQFAADDAIFTCDVGTPtVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVA 429
Cdd:COG3961 353 PAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTS-LFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVIL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 430 MCGDGGFsMLMGdfLSLAQM---KLPVKIIIFNNsvlgfvamemkaGGYLT-------DGT--ELHDTNFARIAEACG-- 495
Cdd:COG3961 432 LVGDGAF-QLTA--QELSTMlryGLKPIIFVLNN------------DGYTIeraihgpDGPynDIANWDYAKLPEAFGgg 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 490998273 496 -ITGIRVEKASEVDSALQTAFS-TDGPVLVDVVVAKEElaIPPQIK 539
Cdd:COG3961 497 nALGFRVTTEGELEEALAAAEAnTDRLTLIEVVLDKMD--APPLLK 540
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
69-527 |
2.15e-28 |
|
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: 119.85 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 69 VCAGSCGPGNLHLINGLFDCHRNHVPVVAIAAHIPSSEIGSGYFQET-HPQEL-------FRECSHYCELVSTPEQIPQV 140
Cdd:COG3962 87 ACTSSIGPGATNMVTAAALATANRLPVLLLPGDTFATRQPDPVLQQLeHFHDPtisvndaFRPVSRYWDRITRPEQLMSA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 141 LAIAMRkaVI----NRGVSVVVLPGDVALKA--APEN--ASTHWY-AAPLPTvtppEEEIKKLAQVLRYSSNIALLCGSG 211
Cdd:COG3962 167 LPRAMR--VLtdpaETGAVTLALPQDVQAEAydYPESffAKRVHRiRRPPPD----PAELARAVELIRAAKRPLIIAGGG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 212 C--AGAHAELVQFAAKLKAPVVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQF------PYRAFYP 283
Cdd:COG3962 241 VrySEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLGGIGVTGTLAANALAAEADLVIGVGTRLqdfttgSKTLFAN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 284 TDAKIIQIDINPGSIGAHSKVdmALVGDIKSTLAALLPHLEE-KTDRAFLDKALEHYREARKGLDDLAKPSDKAIHPQyl 362
Cdd:COG3962 321 PDVRFVNINVARFDAYKHDAL--PVVADAREGLEALTEALAGwRYPAAWTDEAAELKAEWDAEVDRLYAPTNGGLPTQ-- 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 363 AQQIG---QFAADDAIFTCDVGTP-----TVWAARYlkmngrrrlIGSFN--HG--SMANAMPQAIGAKATAPDRQVVAM 430
Cdd:COG3962 397 AQVIGavnEAAGPDDIVVCAAGSLpgdlhKLWRTRD---------PGTYHveYGysCMGYEIAGGLGVKLAEPDREVYVM 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 431 CGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSvlGF-----VAMEMKAGGYltdGTELHDTN--------------FARIA 491
Cdd:COG3962 468 VGDGSYLMLNSELVTSVQEGKKIIVVLLDNH--GFgcinrLQMSTGSQSF---GTELRDRDtetgrldggllpvdFAANA 542
|
490 500 510
....*....|....*....|....*....|....*.
gi 490998273 492 EACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVV 527
Cdd:COG3962 543 ASLGAKAYRVTTIAELRAALERAKAADRTTVIVIKT 578
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
357-533 |
1.47e-27 |
|
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: 109.91 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 357 IHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 437 SMLMGDFLSLAQMKLPVKIIIFNNSVLGfvaMEMKaggYLTD-------GTELHDTNFARIAEACGITGIRVEKASEVDS 509
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWG---AEKK---NQVDfynnrfvGTELESESFAKIAEACGAKGITVDKPEDVGP 157
|
170 180
....*....|....*....|....*..
gi 490998273 510 ALQTAFSTDG---PVLVDVVVAKEELA 533
Cdd:cd02013 158 ALQKAIAMMAegkTTVIEIVCDQELGD 184
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
357-527 |
1.81e-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: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 357 IHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLIGSfNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTL-RGGGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 437 SMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYLTDGTE------LHD--TNFARIAEACGITGIRVEKASEVD 508
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENapdgldLLDpgIDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*....
gi 490998273 509 SALQTAFSTDGPVLVDVVV 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 |
2.07e-24 |
|
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: 99.53 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 8 YIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFD 87
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPLLDALARSG-IRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490998273 88 CHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLP 160
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRpGPVALDLP 154
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
6-528 |
1.50e-18 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 89.27 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIAWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK09259 13 FHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEG-IRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 86 FDCHRNHVPVVAIAAhipSSE-----IGSGYFQET--------HPQELFRecshycelVSTPEQIPQVLAIAMRKAVINR 152
Cdd:PRK09259 92 ANATTNCFPMIMISG---SSEreivdLQQGDYEELdqlnaakpFCKAAFR--------VNRAEDIGIGVARAIRTAVSGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 153 -GVSVVVLPGDV--ALKAAPENASTHWYAA-PLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGCAGAHA--ELVQFAAKL 226
Cdd:PRK09259 161 pGGVYLDLPAKVlaQTMDADEALTSLVKVVdPAPAQLPAPEAVDRALDLLKKAKRPLIILGKGAAYAQAdeQIREFVEKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 227 KAPVVHALRGKEHVEYDNPYDVGmtgligfSSGFHTMMNADTLVLLGTQFPYRAFY---PT---DAKIIQIDINPGSIGA 300
Cdd:PRK09259 241 GIPFLPMSMAKGLLPDTHPQSAA-------AARSLALANADVVLLVGARLNWLLSHgkgKTwgaDKKFIQIDIEPQEIDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 301 HSKVDMALVGDIKSTLAALLPHLEEKTDRAFLD--KALEHYREarKGLDDLAKPSDKAIHPQYLAQQIGQFAA-----DD 373
Cdd:PRK09259 314 NRPIAAPVVGDIGSVMQALLAGLKQNTFKAPAEwlDALAERKE--KNAAKMAEKLSTDTQPMNFYNALGAIRDvlkenPD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 374 AIFTCDvGTPTVWAAR-----YLKmngRRRL-IGSFnhGSMANAMPQAIGAkATAPDRQVVAMCGDGGFSMLMGDFLSLA 447
Cdd:PRK09259 392 IYLVNE-GANTLDLARniidmYKP---RHRLdCGTW--GVMGIGMGYAIAA-AVETGKPVVAIEGDSAFGFSGMEVETIC 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 448 QMKLPVKIIIFNNSvlgfvamemkaGGYLTDGTEL------------HDTNFARIAEACGITGIRVEKASEVDSALQTAF 515
Cdd:PRK09259 465 RYNLPVTVVIFNNG-----------GIYRGDDVNLsgagdpsptvlvHHARYDKMMEAFGGVGYNVTTPDELRHALTEAI 533
|
570
....*....|...
gi 490998273 516 STDGPVLVDVVVA 528
Cdd:PRK09259 534 ASGKPTLINVVID 546
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
361-539 |
1.89e-17 |
|
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: 80.27 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 361 YLAQQIGQFAADDAIFTCDVGTPTvWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLM 440
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSW-FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 441 GDFLSLAQMKLPVKIIIFNNSvlgfvamemkagGYLTDgTELHDT----------NFARIAEACG----ITGIRVEKASE 506
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINND------------GYTIE-RAIHGPeasyndianwNYTKLPEVFGggggGLSFRVKTEGE 151
|
170 180 190
....*....|....*....|....*....|....
gi 490998273 507 VDSALQTA-FSTDGPVLVDVVVAKEElaIPPQIK 539
Cdd:cd02005 152 LDEALKDAlFNRDKLSLIEVILPKDD--APEALK 183
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
62-527 |
3.76e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 84.54 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 62 QLTGELAVCAGSCGPGnlhLINGLFDCH---RNHVPVVAI-----AAHIP-----SSEIGSgyfqethpqeLFRECSHYC 128
Cdd:PRK12474 64 RIAGKPAVTLLHLGPG---LANGLANLHnarRAASPIVNIvgdhaVEHLQydaplTSDIDG----------FARPVSRWV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 129 ELVSTPEQIPQVLAIAMRKA-VINRGVSVVVLPGDVALKAapenastHWYAAPLPTVTPPE----EEIKKLAQVLRYSSN 203
Cdd:PRK12474 131 HRSASAGAVDSDVARAVQAAqSAPGGIATLIMPADVAWNE-------AAYAAQPLRGIGPApvaaETVERIAALLRNGKK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 204 IALLC-GSGCAGAHAEL---------VQFAAKLKAPVVHALRGKEHVEydnpyDVGMTGLIGfssgfhTMM--NADTLVL 271
Cdd:PRK12474 204 SALLLrGSALRGAPLEAagriqaktgVRLYCDTFAPRIERGAGRVPIE-----RIPYFHEQI------TAFlkDVEQLVL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 272 LGTQFPYRAF-YPTdakiiqidiNPGSIGAHSKVDMALVGdikstlaallPHLEEKTDRAFLDKALEHYRE--ARKGLDd 348
Cdd:PRK12474 273 VGAKPPVSFFaYPG---------KPSWGAPPGCEIVYLAQ----------PDEDLAQALQDLADAVDAPAEpaARTPLA- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 349 LAKPSDKAIHPQYLAQQIGQFAADDAIFtCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVV 428
Cdd:PRK12474 333 LPALPKGALNSLGVAQLIAHRTPDQAIY-ADEALTSGLFFDMSYDRARPHTHLPLTGGSIGQGLPLAAGAAVAAPDRKVV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 429 AMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYLTDGT------ELH--DTNFARIAEACGITGIR 500
Cdd:PRK12474 412 CPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGELQRVGAQGAGRnalsmlDLHnpELNWMKIAEGLGVEASR 491
|
490 500
....*....|....*....|....*..
gi 490998273 501 VEKASEVDSALQTAFSTDGPVLVDVVV 527
Cdd:PRK12474 492 ATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
74-527 |
4.57e-17 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 84.13 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 74 CGPGnlhLINGLFDCH---RNHVPVVAI-----AAHIP-----SSEIGSgyfqethpqeLFRECSHYCELVSTPEQIPQV 140
Cdd:PRK07586 72 LGPG---LANGLANLHnarRARTPIVNIvgdhaTYHRKydaplTSDIEA----------LARPVSGWVRRSESAADVAAD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 141 LAIAMRKA-VINRGVSVVVLPGDVALKAAPENASThwyAAPLPTVTPPEEEIKKLAQVLRYSSNIALLCGSGCAGAHAel 219
Cdd:PRK07586 139 AAAAVAAArGAPGQVATLILPADVAWSEGGPPAPP---PPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERG-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 220 VQFAAKLKA-----------PVVHAlRGKEHVEYDN-PY--DVGMTGLIGFssgfhtmmnaDTLVLLGTQFPYRAF---- 281
Cdd:PRK07586 214 LAAAARIAAatgarllaetfPARME-RGAGRPAVERlPYfaEQALAQLAGV----------RHLVLVGAKAPVAFFaypg 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 282 -----YPTDAKIIQIDiNPGSIGAHSkvdmalvgdikstLAALLPHLEEKTDRAFLDKALEhyrearkglddlAKPSDKA 356
Cdd:PRK07586 283 kpsrlVPEGCEVHTLA-GPGEDAAAA-------------LEALADALGAKPAAPPLAAPAR------------PPLPTGA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 357 IHPQYLAQQIGQFAADDAIF-----TCDVG--TPTVWAAR--YLKMNGrrrligsfnhGSMANAMPQAIGAKATAPDRQV 427
Cdd:PRK07586 337 LTPEAIAQVIAALLPENAIVvdesiTSGRGffPATAGAAPhdWLTLTG----------GAIGQGLPLATGAAVACPDRKV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 428 VAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKAGGYLTDG------TELHD--TNFARIAEACGITGI 499
Cdd:PRK07586 407 LALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGELARVGAGNPGpraldmLDLDDpdLDWVALAEGMGVPAR 486
|
490 500
....*....|....*....|....*...
gi 490998273 500 RVEKASEVDSALQTAFSTDGPVLVDVVV 527
Cdd:PRK07586 487 RVTTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
357-529 |
1.02e-13 |
|
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: 70.00 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 357 IHPQYLAQQIGQFAADDAIFTCDVGTPTVWAARYLKMNGRRRLIGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 437 SMLMGDFLSLAQMKLPVKIIIFNNSVLGFVAMEMKA-------------------GGYLTDgtelhdtnFARIAEACGIT 497
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAfdmdyqvnlafeninsselGGYGVD--------HVKVAEGLGCK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 490998273 498 GIRVEKASEVDSALQTAFSTDG----PVLVDVVVAK 529
Cdd:cd02006 160 AIRVTKPEELAAAFEQAKKLMAehrvPVVVEAILER 195
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
406-536 |
2.46e-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: 71.62 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 406 GSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKI-IIFNNSVLGFVamemkaGGYLTDGTelhD 484
Cdd:TIGR03297 221 GSMGHASQIALGLALARPDQRVVCLDGDGAALMHMGGLATIGTQGPANLIhVLFNNGAHDSV------GGQPTVSQ---H 291
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 490998273 485 TNFARIAEACGITGIR-VEKASEVDSALQTAFSTDGPVLVDVVVAKEELAIPP 536
Cdd:TIGR03297 292 LDFAQIAKACGYAKVYeVSTLEELETALTAASSANGPRLIEVKVRPGSRADLG 344
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
406-533 |
3.12e-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: 68.49 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 406 GSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLP-VKIIIFNNSVLGFVamemkaGGYLTDGTelhD 484
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPAnLIHIVLNNGAHDSV------GGQPTVSF---D 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 490998273 485 TNFARIAEACGITGIRVEKAS-EVDSALQTAFSTDGPVLVDVVVAKEELA 533
Cdd:cd03371 119 VSLPAIAKACGYRAVYEVPSLeELVAALAKALAADGPAFIEVKVRPGSRS 168
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
408-525 |
1.54e-12 |
|
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: 66.95 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 408 MANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIIIFNNS---VLGFVAMEMKAGGYltdGTELHD 484
Cdd:cd02003 50 MGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHgfgCINNLQESTGSGSF---GTEFRD 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 490998273 485 --------------TNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDV 525
Cdd:cd02003 127 rdqesgqldgallpVDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVI 181
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
7-161 |
3.34e-11 |
|
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: 61.59 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 7 AYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIAWMPTRHEEVAAFAAGAEAQLTGeLAVCAGSCGPGNLHLINGLF 86
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998273 87 DCHRNHVPVVAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPG 161
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
371-527 |
1.53e-07 |
|
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: 51.52 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 371 ADDAIFTCDVGTPT--VWAARYLKMNgrrrligSFNHGSMANAMPQAIGAkATAPDRQVVAMCGDGGFSMLMGDFLSLAQ 448
Cdd:cd03372 12 LKDELVVSNIGFPSkeLYAAGDRPLN-------FYMLGSMGLASSIGLGL-ALAQPRKVIVIDGDGSLLMNLGALATIAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 449 MKLP-VKIIIFNNSVLGFVAMEMKAGGYLTDgtelhdtnFARIAEACGITgiRVEKASEVDSALQT-AFSTDGPVLVDVV 526
Cdd:cd03372 84 EKPKnLIIVVLDNGAYGSTGNQPTHAGKKTD--------LEAVAKACGLD--NVATVASEEAFEKAvEQALDGPSFIHVK 153
|
.
gi 490998273 527 V 527
Cdd:cd03372 154 I 154
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
406-523 |
9.61e-07 |
|
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: 48.64 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 406 GSMANAMPQAIGAKATAPdRQVVAMCGDGGFSMLMGDFLSLAQMK-LPVKIIIFNNSVLGfvamemKAGGYLTDGTelhD 484
Cdd:cd02001 42 GSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNRAYG------STGGQPTPSS---N 111
|
90 100 110
....*....|....*....|....*....|....*....
gi 490998273 485 TNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLV 523
Cdd:cd02001 112 VNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLL 150
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
406-525 |
8.50e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 44.05 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 406 GSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLP-VKIIIFNNSVLGFvamemkAGGYLTDGTELHD 484
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKnLTIIVMDNGVYQI------TGGQPTLTSQTVD 130
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490998273 485 tnFARIAEACGITGIRVEKASE-VDSALQTAFSTDGPVLVDV 525
Cdd:PRK06163 131 --VVAIARGAGLENSHWAADEAhFEALVDQALSGPGPSFIAV 170
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
399-464 |
2.34e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 43.33 E-value: 2.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998273 399 LIGSFN--HGSManaMPQAIGAKATAPDRQVVAMCGDG-GFSMLMGDFLSLAQMKLPVKIIIFNNSVLG 464
Cdd:PRK05778 64 LSHGLHtlHGRA---IAFATGAKLANPDLEVIVVGGDGdLASIGGGHFIHAGRRNIDITVIVENNGIYG 129
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
385-526 |
2.72e-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: 42.13 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 385 VWAARYLKMNGrrrligsFN--HGsmaNAMPQAIGAKATAPDRQVVAMCGDG-GFSMLMGDFLSLAQMKLPVKIIIFNNS 461
Cdd:cd03375 38 SRLPYYFNTYG-------FHtlHG---RALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 462 VLGfvameMKAG--------GYLT----DGTELHDTNFARIAEACGITGI------RVEKASEVdsaLQTAFSTDGPVLV 523
Cdd:cd03375 108 IYG-----LTKGqaspttpeGFKTkttpYGNIEEPFNPLALALAAGATFVargfsgDIKQLKEI---IKKAIQHKGFSFV 179
|
...
gi 490998273 524 DVV 526
Cdd:cd03375 180 EVL 182
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
415-527 |
3.14e-04 |
|
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: 41.81 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 415 AIGAkATAPDRQVVAMCGDggFSML--MGDFLSLAQMKLPVKIIIFNNSvlG---FvamEMKAGGYLTDGTE-----LHD 484
Cdd:cd02009 60 ALGI-ALATDKPTVLLTGD--LSFLhdLNGLLLGKQEPLNLTIVVINNN--GggiF---SLLPQASFEDEFErlfgtPQG 131
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490998273 485 TNFARIAEACGITGIRVEKASEVDSALQTAFSTDGPVLVDVVV 527
Cdd:cd02009 132 LDFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKT 174
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
412-527 |
1.93e-03 |
|
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: 40.56 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998273 412 MPQAIGA----KATAPDRQVVAMCGDGGFSMlmGDF---LSLAQ-MKLPVKIIIFNNsvlGFvAMemkaggyltdGTELH 483
Cdd:cd02000 110 VPLAAGAalalKYRGEDRVAVCFFGDGATNE--GDFheaLNFAAlWKLPVIFVCENN---GY-AI----------STPTS 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 490998273 484 D----TNFARIAEACGITGIRVE--KASEVDSALQTAF----STDGPVLVDVVV 527
Cdd:cd02000 174 RqtagTSIADRAAAYGIPGIRVDgnDVLAVYEAAKEAVerarAGGGPTLIEAVT 227
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
405-464 |
4.69e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 39.05 E-value: 4.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490998273 405 HGsmaNAMPQAIGAKATAPDRQVVAMCGDG-GFSMLMGDFLSLAQMKLPVKIIIFNNSVLG 464
Cdd:PRK11867 71 HG---RALAIATGLKLANPDLTVIVVTGDGdALAIGGNHFIHALRRNIDITYILFNNQIYG 128
|
|
| |
