|
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: 1180.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLH 80
Cdd:PRK09124 1 MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLP 160
Cdd:PRK09124 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVVLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 161 GDVALKPAPEGATTHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHV 240
Cdd:PRK09124 161 GDVALKPAPERATPHWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRGKEHV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPASIGAHSKVDMALVGDIKSTLRALL 320
Cdd:PRK09124 241 EYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKATLAALL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 321 PLVEEKADRKFLDKALEDYRDARKGLDDLAKPSE--KAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRR 398
Cdd:PRK09124 321 PLLEEKTDRKFLDKALEHYRKARKGLDDLAVPSDggKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 399 LLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYLTD 478
Cdd:PRK09124 401 LLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMKAGGYLTD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 479 GTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGR 558
Cdd:PRK09124 481 GTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMPPQIKLEQAKGFSLYMLRAIISGR 560
|
570
....*....|....
gi 15830211 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: 765.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLH 80
Cdd:PRK06546 1 MAKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLP 160
Cdd:PRK06546 81 LINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGGGVSVVTLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 161 GDVALKPAPEGATTHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHV 240
Cdd:PRK06546 161 GDIADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGKEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPtDAKIIQIDINPASIGAHSKVDMALVGDIKSTLRALL 320
Cdd:PRK06546 241 QYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFPYDQFLP-DVRTAQVDIDPEHLGRRTRVDLAVHGDVAETIRALL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 321 PLVEEKADRKFLDKALEDYRDARKG-LDDLAKPSEK--AIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKR 397
Cdd:PRK06546 320 PLVKEKTDRRFLDRMLKKHARKLEKvVGAYTRKVEKhtPIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 398 RLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYLT 477
Cdd:PRK06546 400 RVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMLVDGLPD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 478 DGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISG 557
Cdd:PRK06546 480 FGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTDPNALSIPPTITGEQVKGFALAASKTVLNG 559
|
570
....*....|....*
gi 15830211 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: 555.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLH 80
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNR-GVSVVVL 159
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRpGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 160 PGDVALKPAPEGATTHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALRGK 237
Cdd:COG0028 161 PKDVQAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGArrAGAAEELRALAERLGAPVVTTLMGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 238 EHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPtDAKIIQIDINPASIGAHSKVDMALVGD 311
Cdd:COG0028 241 GAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRvtgnwdEFAP-DAKIIHIDIDPAEIGKNYPVDLPIVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 312 IKSTLRALLPLVEEKADRKflDKALEDYRDARKGLDDLAKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYL 391
Cdd:COG0028 320 AKAVLAALLEALEPRADDR--AAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 392 KMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMK 471
Cdd:COG0028 398 RFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830211 472 A-GGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIPPQIK 539
Cdd:COG0028 478 LfYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENPPGATLD 546
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-555 |
1.46e-163 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 477.96 E-value: 1.46e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRM-GTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNL 79
Cdd:PRK08611 2 AKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVL 159
Cdd:PRK08611 82 HLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVLTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 160 PGDValkPAPEGATTHWYHAP---QPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRG 236
Cdd:PRK08611 162 PDDL---PAQKIKDTTNKTVDtfrPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPASIGAHSKVDMALVGDIKSTL 316
Cdd:PRK08611 239 KGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYVDYLPKKAKAIQIDTDPANIGKRYPVNVGLVGDAKKAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 317 RALLPLVEEKADRKFLDKALEDYRDARKGLDDLAKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGK 396
Cdd:PRK08611 319 HQLTENIKHVEDRRFLEACQENMAKWWKWMEEDENNASTPIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNLGTN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 397 RRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYL 476
Cdd:PRK08611 399 QKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGEL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830211 477 TDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAII 555
Cdd:PRK08611 479 EYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAPLPGKIVNDEALGYSKWAIKSLF 557
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-558 |
2.75e-133 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 399.59 E-value: 2.75e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 4 TVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLnRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAI-RKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPGDV 163
Cdd:PRK06457 82 GLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINLPVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 164 aLKPAPEGATTHWYHAPQPVVTPEeeeLRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHVEYD 243
Cdd:PRK06457 162 -LRKSSEYKGSKNTEVGKVKYSID---FSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 244 NPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPASIGAHSKVDMALVGDIKSTLRallPLV 323
Cdd:PRK06457 238 DPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLN---IDI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 324 EEKADrKFLDKALEDYRDARKGLDDLAKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSF 403
Cdd:PRK06457 315 EEKSD-KFYEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 404 NHGSMANAMPQALGAQ-ATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYLTDGTEL 482
Cdd:PRK06457 394 WLGSMGIGVPGSVGASfAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMGYPEWGVDL 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830211 483 HDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGR 558
Cdd:PRK06457 474 YNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMPPKLTFKQAGEYVLSIFREKLEGI 549
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-570 |
9.22e-125 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 379.25 E-value: 9.22e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRM-GTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNL 79
Cdd:PRK08273 1 MSQTVADFILERLREWGVRRVFGYPGDGINGLLGALGRAdDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSH-YCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV 158
Cdd:PRK08273 81 HLLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAGaFVQMVTVPEQLRHLVDRAVRTALAERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 159 LPGDVALKPAPEGATTHWY-----HAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHA 233
Cdd:PRK08273 161 LPNDVQELEYEPPPHAHGTvhsgvGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 234 LRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPT--DAKIIQIDINPASIGAHSKVDMALVGD 311
Cdd:PRK08273 241 LLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFPYSEFLPKegQARGVQIDIDGRMLGLRYPMEVNLVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 312 IKSTLRALLPLVEEKADRKFLDKALEDYRDARKGLDDLAKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYL 391
Cdd:PRK08273 321 AAETLRALLPLLERKKDRSWRERIEKWVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADSGSCANWYARDL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 392 KMngKRRLLGSFNHG--SMANAMPQALGAQATEPERQVVAMCGDGGFSML-MGDFLSVV----QMKLPVKII-VFNNSVL 463
Cdd:PRK08273 401 RM--RRGMMASLSGTlaTMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAkywrQWSDPRLIVlVLNNRDL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 464 GFVAMEMKA-GG--YLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIPPQIKL 540
Cdd:PRK08273 479 NQVTWEQRVmEGdpKFEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDPNVPPLPPHITL 558
|
570 580 590
....*....|....*....|....*....|...
gi 15830211 541 EQAKGFslymLRAIISGRGDE---VIELAKTNW 570
Cdd:PRK08273 559 EQAKAF----ASALLKGDPDAggvIVQTAKQVL 587
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
6-527 |
5.36e-108 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 335.27 E-value: 5.36e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 6 AAYIAKTLESAGVKRIWGVTGDSLNGLSDSL-NRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLING 84
Cdd:TIGR02720 2 SAAVLKVLEAWGVDHIYGIPGGSFNSTMDALsAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 85 LFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPGDVA 164
Cdd:TIGR02720 82 LYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHNGVAVVTIPVDFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 165 LKPAPEgatTHWYHAPQP-----VVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEH 239
Cdd:TIGR02720 162 WQEIPD---NDYYASSVSyqtplLPAPDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 240 VEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPT--DAK-IIQIDINPASIGAHSKVDMALVGDIKSTL 316
Cdd:TIGR02720 239 IEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKAfkNTKyFIQIDIDPAKLGKRHHTDIAVLADAKKAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 317 RALLPLVEEKADRKFLDKALEDYRDARKGLDDLAKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGK 396
Cdd:TIGR02720 319 AAILAQVEPRESTPWWQANVANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 397 RRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYL 476
Cdd:TIGR02720 399 NKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQP 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15830211 477 TDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSI--DGPVLVDVVV 527
Cdd:TIGR02720 479 LIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAKAIkqGKPVLIDAKI 531
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
3-538 |
4.19e-102 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 319.36 E-value: 4.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 3 QTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLI 82
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 83 NGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPG 161
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVdLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 162 DVALK----PAPEGATTHWYhapQPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALR 235
Cdd:TIGR00118 161 DVTTAeieyPYPEKVNLPGY---RPTVKGHPLQIKKAAELINLAKKPVILVGGGViiAGASEELKELAERIQIPVTTTLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPASIGAHSKVDMALVG 310
Cdd:TIGR00118 238 GLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRvtgnlAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 311 DIKSTLRALLPLVEEKADRKflDKALEDYRDARKGLDDLAKP-SEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAAR 389
Cdd:TIGR00118 318 DARNVLEELLKKLFELKERK--ESAWLEQINKWKKEYPLKMDyTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 390 YLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVA-- 467
Cdd:TIGR00118 396 FYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRqw 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830211 468 MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIPPQI 538
Cdd:TIGR00118 476 QELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVA 546
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
357-533 |
1.34e-98 |
|
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: 296.75 E-value: 1.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 357 IHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGF 436
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 437 SMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFS 516
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALA 161
|
170
....*....|....*..
gi 15830211 517 IDGPVLVDVVVAKEELA 533
Cdd:cd02014 162 ADGPVVIDVVTDPNEPP 178
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
2-535 |
2.29e-80 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 262.79 E-value: 2.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 2 KQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHL 81
Cdd:PRK06048 7 KMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD-LRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LP 160
Cdd:PRK06048 86 VTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIdLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 161 GDVALKPA----PEGATTHWYhapQPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHAL 234
Cdd:PRK06048 166 KDVTTAEIdfdyPDKVELRGY---KPTYKGNPQQIKRAAELIMKAERPIIYAGGGVisSNASEELVELAETIPAPVTTTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPtDAKIIQIDINPASIGAHSKVDMAL 308
Cdd:PRK06048 243 MGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRvtgklaSFAP-NAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 309 VGDIKSTLRALLPLVEEKADRKFLDKALEdyrdARKGLDDLAKPSEKAIHPQYLAQQISHfAADDAIFTCDVGTPTVWAA 388
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDRKEWLDKINQ----WKKEYPLKYKEREDVIKPQYVIEQIYE-LCPDAIIVTEVGQHQMWAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 389 RYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVA- 467
Cdd:PRK06048 397 QYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRq 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830211 468 -MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIP 535
Cdd:PRK06048 477 wQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSP 545
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
4-167 |
7.72e-80 |
|
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: 247.85 E-value: 7.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 4 TVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLIN 83
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPGDV 163
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKRGVAVLILPGDV 160
|
....
gi 15830211 164 ALKP 167
Cdd:cd07039 161 QDAP 164
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
9-540 |
3.12e-79 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 260.46 E-value: 3.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 9 IAKTLESAGVKRIWGVTGDSLNGLSDSLNRmGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK06276 7 IIKALEAEGVKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGIATA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPGDVA--- 164
Cdd:PRK06276 86 YADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIdLPKDVQege 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 165 ----LKPAPEGATTHWYhapQPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALRGKE 238
Cdd:PRK06276 166 ldleKYPIPAKIDLPGY---KPTTFGHPLQIKKAAELIAEAERPVILAGGGViiSGASEELIELSELVKIPVCTTLMGKG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 239 HVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPASIGAHSKVDMALVGDI 312
Cdd:PRK06276 243 AFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTtgdissFAP-NAKIIHIDIDPAEIGKNVRVDVPIVGDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 313 KSTLRALLPLVEEKaDRKFLDKALEDYRDARKGLDDLAKPSEKAIHPQYLAQQISHFAAD-----DAIFTCDVGTPTVWA 387
Cdd:PRK06276 322 KNVLRDLLAELMKK-EIKNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQMWM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 388 ARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVA 467
Cdd:PRK06276 401 AHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVY 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830211 468 mEMKAGGYLTDGTELH---DTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEEL--AIPPQIKL 540
Cdd:PRK06276 481 -QWQNLYYGKRQSEVHlgeTPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAlpMVPPGGNL 557
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
4-535 |
2.49e-70 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 237.57 E-value: 2.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 4 TVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLIN 83
Cdd:PRK07789 32 TGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQE------THPqelfreCSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVV 157
Cdd:PRK07789 112 PIADANMDSVPVVAITGQVGRGLIGTDAFQEadivgiTMP------ITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 158 VlpgDVAlKPAPEGATT-HW--------YHapqPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKI 226
Cdd:PRK07789 186 V---DIP-KDALQAQTTfSWpprmdlpgYR---PVTKPHGKQIREAAKLIAAARRPVLYVGGGVirAEASAELRELAELT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 227 KAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPtDAKIIQIDINPASIGA 300
Cdd:PRK07789 259 GIPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRvtgkldSFAP-DAKVIHADIDPAEIGK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 301 HSKVDMALVGDIKSTLRALLPLVEekadRKFLDKALEDYRDARKGLDDL--------AKPSEKAIHPQYLAQQISHFAAD 372
Cdd:PRK07789 338 NRHADVPIVGDVKEVIAELIAALR----AEHAAGGKPDLTAWWAYLDGWretyplgyDEPSDGSLAPQYVIERLGEIAGP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 373 DAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLP 452
Cdd:PRK07789 414 DAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIP 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 453 VKIIVFNNSVLGFVAMEMK---AGGYltDGTELHD-----TNFARIAEACGITGIRVEKASEIDEALQRAFSI-DGPVLV 523
Cdd:PRK07789 494 IKVALINNGNLGMVRQWQTlfyEERY--SNTDLHThshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAInDRPVVI 571
|
570
....*....|..
gi 15830211 524 DVVVAKEELAIP 535
Cdd:PRK07789 572 DFVVGKDAMVWP 583
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-535 |
1.75e-68 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 231.53 E-value: 1.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLH 80
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-L 159
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIdI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 160 PGDVALKPA----PEGATTHWYhapQPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHA 233
Cdd:PRK08527 161 PKDVTATLGefeyPKEISLKTY---KPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAilSNASEEIRELVKKTGIPAVET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 234 LRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTD-----AKIIQIDINPASIGAHSKVDMAL 308
Cdd:PRK08527 238 LMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSefakhAKIIHVDIDPSSISKIVNADYPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 309 VGDIKSTLRALLPLVEEKADRKFLD--KALEDYRDarkgLDDLA-KPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTV 385
Cdd:PRK08527 318 VGDLKNVLKEMLEELKEENPTTYKEwrEILKRYNE----LHPLSyEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 386 WAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGF 465
Cdd:PRK08527 394 WVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGM 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830211 466 V----AMEMKAGGYLTDGTELHDtnFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIP 535
Cdd:PRK08527 474 VrqwqTFFYEERYSETDLSTQPD--FVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLP 545
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
4-535 |
6.28e-67 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 227.54 E-value: 6.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 4 TVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06725 16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNR-GVSVVVLPGD 162
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRpGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 163 VALkpapEGATTHWYH-----APQPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALR 235
Cdd:PRK06725 175 VQN----EKVTSFYNEvveipGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVihSGGSEELIEFARENRIPVVSTLM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPASIGAHSKVDMALV 309
Cdd:PRK06725 251 GLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVtgklelFSP-HSKKVHIDIDPSEFHKNVAVEYPVV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 310 GDIKSTLRALLPLVEEKADRKFLDKALEdyRDARKGLDDLAKPSEkaIHPQYLAQQISHFAADDAIFTCDVGTPTVWAAR 389
Cdd:PRK06725 330 GDVKKALHMLLHMSIHTQTDEWLQKVKT--WKEEYPLSYKQKESE--LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAH 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 390 YLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVA-- 467
Cdd:PRK06725 406 FYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRqw 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830211 468 MEMKAGGYLTDgTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIP 535
Cdd:PRK06725 486 QEMFYENRLSE-SKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFP 552
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-535 |
1.25e-66 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 226.51 E-value: 1.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLH 80
Cdd:PRK08155 11 KRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-L 159
Cdd:PRK08155 91 LVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIdI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 160 PGDVALK-------PAPEGatthwyhaPQPVVTPEEEELRKLAQLLRYSSNIALMCGSG--CAGAHKELVEFAGKIKAPI 230
Cdd:PRK08155 171 PKDVQTAvielealPAPAE--------KDAAPAFDEESIRDAAAMINAAKRPVLYLGGGviNSGAPARARELAEKAQLPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 231 VHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPASIGAHSKV 304
Cdd:PRK08155 243 TMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAigkteqFCP-NAKIIHVDIDRAELGKIKQP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 305 DMALVGDIKSTLRALLPLVEEKADRKFLDKALEDYRD---ARKGLDDlakpsekAIHPQYLAQQISHFAADDAIFTCDVG 381
Cdd:PRK08155 322 HVAIQADVDDVLAQLLPLVEAQPRAEWHQLVADLQREfpcPIPKADD-------PLSHYGLINAVAACVDDNAIITTDVG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 382 TPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNS 461
Cdd:PRK08155 395 QHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNE 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830211 462 VLGFV--AMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIP 535
Cdd:PRK08155 475 ALGLVhqQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYP 550
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
1-531 |
3.90e-66 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 225.73 E-value: 3.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSL---NRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPG 77
Cdd:CHL00099 8 REKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 78 NLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVV 157
Cdd:CHL00099 88 ATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 158 V-LPGDVALK-----PAPEGATTHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAP 229
Cdd:CHL00099 168 IdIPKDVGLEkfdyyPPEPGNTIIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAiiSDAHQEITELAELYKIP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 230 IVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAF-----YPTDAKIIQIDINPASIGAHSKV 304
Cdd:CHL00099 248 VTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTgkldeFACNAQVIHIDIDPAEIGKNRIP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 305 DMALVGDIKSTLRALLPLVeEKADRKFLDKALEDYRDA----RKGLDDLAKPSEKAIHPQYLAQQISHFAAdDAIFTCDV 380
Cdd:CHL00099 328 QVAIVGDVKKVLQELLELL-KNSPNLLESEQTQAWRERinrwRKEYPLLIPKPSTSLSPQEVINEISQLAP-DAYFTTDV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 381 GTPTVWAARYLKMnGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNN 460
Cdd:CHL00099 406 GQHQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINN 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830211 461 SVLGFVAM-------EMKAGGYLTDGTelhdTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEE 531
Cdd:CHL00099 485 KWQGMVRQwqqafygERYSHSNMEEGA----PDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDE 558
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-535 |
4.64e-66 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 225.02 E-value: 4.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 6 AAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMsTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK07710 19 AQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHIL-TRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPGDVA 164
Cdd:PRK07710 98 ADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIdIPKDMV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 165 LKPApEGATTHWYHAP--QPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALRGKEHV 240
Cdd:PRK07710 178 VEEG-EFCYDVQMDLPgyQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVlhAKASKELTSYAEQQEIPVVHTLLGLGGF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPASIGAHSKVDMALVGDIKST 315
Cdd:PRK07710 257 PADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRvtgnlAYFAKEATVAHIDIDPAEIGKNVPTEIPIVADAKQA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 316 LRALLPLVEEKADRKFLDKALedyrDARKGLDDLA-KPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMN 394
Cdd:PRK07710 337 LQVLLQQEGKKENHHEWLSLL----KNWKEKYPLSyKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 395 GKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDfLSVVQ-MKLPVKIIVFNNSVLGFVA--MEMK 471
Cdd:PRK07710 413 TPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQE-LSVIKeLSLPVKVVILNNEALGMVRqwQEEF 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830211 472 AGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIP 535
Cdd:PRK07710 492 YNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMP 555
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
13-535 |
1.72e-65 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 223.85 E-value: 1.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 13 LESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFDCHRNH 92
Cdd:PLN02470 23 LEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGLADALLDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 93 VPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPGDVALKPA--- 168
Cdd:PLN02470 103 VPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVdIPKDIQQQLAvpn 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 169 ---PEGATTHWYHAPQPvvtPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHVEYDNP 245
Cdd:PLN02470 183 wnqPMKLPGYLSRLPKP---PEKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGLGAFPASDE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 246 YDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFyPTDAKIIQIDINPASIGAHSKVDMALVGDIKSTLRAL 319
Cdd:PLN02470 260 LSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRvtgkleAF-ASRASIVHIDIDPAEIGKNKQPHVSVCADVKLALQGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 320 LPLVEEKAD--------RKFLDKALEDYRDARKGLDDlakpsekAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYL 391
Cdd:PLN02470 339 NKLLEERKAkrpdfsawRAELDEQKEKFPLSYPTFGD-------AIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWY 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 392 KMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAM--- 468
Cdd:PLN02470 412 KYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQwed 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830211 469 ----EMKAGGYLTDGTELHDT--NFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIP 535
Cdd:PLN02470 492 rfykANRAHTYLGDPDAEAEIfpDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLP 564
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
9-535 |
2.99e-65 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 222.77 E-value: 2.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 9 IAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK07282 16 VLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITGIADA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPGDVALKp 167
Cdd:PRK07282 96 MSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIdLPKDVSAL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 168 apegaTTHWYHAP-------QPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALRGKE 238
Cdd:PRK07282 175 -----ETDFIYDPevnlpsyQPTLEPNDMQIKKILKQLSKAKKPVILAGGGInyAEAATELNAFAERYQIPVVTTLLGQG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 239 HVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPASIGAHSKVDMALVGDIK 313
Cdd:PRK07282 250 TIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRltgnpKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 314 STLRALLPLVEEKAD-RKFLDKALEDYRDARKglddlAKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLK 392
Cdd:PRK07282 330 KALQMLLAEPTVHNNtEKWIEKVTKDKNRVRS-----YDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 393 MNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKA 472
Cdd:PRK07282 405 YQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQES 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830211 473 --GGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQrAFSIDGPVLVDVVVAKEELAIP 535
Cdd:PRK07282 485 fyEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLE-VITEDVPMLIEVDISRKEHVLP 548
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
6-539 |
1.33e-64 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 221.23 E-value: 1.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 6 AAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPGDVa 164
Cdd:PRK08979 87 ATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIdLPKDC- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 165 LKPApegaTTHWYHAPQ--------PVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHAL 234
Cdd:PRK08979 166 LNPA----ILHPYEYPEsikmrsynPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAiiSGADKQILQLAEKLNLPVVSTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAF-----YPTDAKIIQIDINPASIGAHSKVDMALV 309
Cdd:PRK08979 242 MGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTnnlekYCPNATILHIDIDPSSISKTVRVDIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 310 GDIKSTLRALLPLVEEKADRKflDKA--------LEDYRDaRKGLDdLAKPSEKaIHPQYLAQQISHFAADDAIFTCDVG 381
Cdd:PRK08979 322 GSADKVLDSMLALLDESGETN--DEAaiaswwneIEVWRS-RNCLA-YDKSSER-IKPQQVIETLYKLTNGDAYVASDVG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 382 TPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNS 461
Cdd:PRK08979 397 QHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 462 VLGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSI-DGPVLVDVVVAKEELAIPPQI 538
Cdd:PRK08979 477 FLGMVKqwQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAMkDRLVFVDINVDETEHVYPMQI 556
|
.
gi 15830211 539 K 539
Cdd:PRK08979 557 R 557
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
6-525 |
3.87e-64 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 220.44 E-value: 3.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 6 AAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPGDVA 164
Cdd:PRK06965 104 ATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVdIPKDVS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 165 LKPAPegatthwYHAPQ--------PVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHAL 234
Cdd:PRK06965 184 KTPCE-------YEYPKsvemrsynPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVilANASRELRQLADLLGYPVTNTL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPTDAKIIQIDINPASIGAHSKVDMAL 308
Cdd:PRK06965 257 MGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVignpahFASRPRKIIHIDIDPSSISKRVKVDIPI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 309 VGDIKSTLRALLPLVEE---KADRKFLDKALEDYRDARKgLDDLA-KPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPT 384
Cdd:PRK06965 337 VGDVKEVLKELIEQLQTaehGPDADALAQWWKQIEGWRS-RDCLKyDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 385 VWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLG 464
Cdd:PRK06965 416 MWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLG 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830211 465 FVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSI-DGPVLVDV 525
Cdd:PRK06965 496 MVRqwQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRLkDRTVFLDF 559
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
1-531 |
8.46e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 219.92 E-value: 8.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRM---GTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPG 77
Cdd:PRK07418 17 QRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAeaeGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 78 NLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVV 157
Cdd:PRK07418 97 ATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 158 V-LPGDVALK-----P-APEGATTHWYHAPQPvvtPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKA 228
Cdd:PRK07418 177 IdIPKDVGQEefdyvPvEPGSVKPPGYRPTVK---GNPRQINAALKLIEEAERPLLYVGGGAisAGAHAELKELAERFQI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 229 PIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPTdAKIIQIDINPASIGAHS 302
Cdd:PRK07418 254 PVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVtgkldeFASR-AKVIHIDIDPAEVGKNR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 303 KVDMALVGDIKSTLRALLPLVEEKADRKFLDKALEDYRDARKGLDDLAKPSEKAIHPQYLAQQISHFAAdDAIFTCDVGT 382
Cdd:PRK07418 333 RPDVPIVGDVRKVLVKLLERSLEPTTPPRTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAP-DAYYTTDVGQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 383 PTVWAARYLKmNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSV 462
Cdd:PRK07418 412 HQMWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGW 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 463 LGFV-------------AMEMKAGgyltdgtelhDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAK 529
Cdd:PRK07418 491 QGMVrqwqesfygerysASNMEPG----------MPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRR 560
|
..
gi 15830211 530 EE 531
Cdd:PRK07418 561 DE 562
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
6-539 |
2.53e-62 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 215.38 E-value: 2.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 6 AAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06466 7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPGDVA 164
Cdd:PRK06466 87 ATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVdIPKDMT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 165 lKPA-------PEGATTHWYhapQPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALR 235
Cdd:PRK06466 167 -NPAekfeyeyPKKVKLRSY---SPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVvlGNASALLTELAHLLNLPVTNTLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPASIGAHSKVDMALV 309
Cdd:PRK06466 243 GLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVtngpakFCP-NAKIIHIDIDPASISKTIKADIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 310 GDIKSTLRALLPLVEE---KADRKFLD---KALEDYRdARKGLDDLAKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTP 383
Cdd:PRK06466 322 GPVESVLTEMLAILKEigeKPDKEALAawwKQIDEWR-GRHGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVGQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 384 TVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVL 463
Cdd:PRK06466 401 QMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGAL 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830211 464 GFVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSI-DGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK06466 481 GMVRqwQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAMkDRLVFIDIYVDRSEHVYPMQIA 559
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
2-535 |
8.23e-62 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 213.96 E-value: 8.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 2 KQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHL 81
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAG-IRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPG 161
Cdd:TIGR03457 80 VTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREMGPAQLNIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 162 DvalkpapegattHWYHA-----PQPVV----TPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPI 230
Cdd:TIGR03457 160 D------------YFYGEidveiPRPVRldrgAGGATSLAQAARLLAEAKFPVIISGGGVvmGDAVEECKALAERLGAPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 231 VHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQF-PYRA-------FYPTDAKIIQIDINPASIGAHS 302
Cdd:TIGR03457 228 VNSYLHNDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLgPFGTlpqygidYWPKNAKIIQVDANAKMIGLVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 303 KVDMALVGDIKSTLRALLPLVE------EKADRKFL--------DKALEDYRDARK--GLDDLAKPSEKA---IHPQYLA 363
Cdd:TIGR03457 308 KVTVGICGDAKAAAAEILQRLAgkagdaNRAERKAKiqaersawEQELSEMTHERDpfSLDMIVEQRQEEgnwLHPRQVL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 364 QQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDF 443
Cdd:TIGR03457 388 RELEKAMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 444 LSVVQMKLPVKIIVFNNSVLGfvaMEMKAGGYLTD----GTELH-DTNFARIAEACGITGIRVEKASEIDEALQRAFS-- 516
Cdd:TIGR03457 468 MTAVRHDIPVTAVVFRNRQWG---AEKKNQVDFYNnrfvGTELEsELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAaq 544
|
570
....*....|....*....
gi 15830211 517 IDGPVLVDVVVAKEELAIP 535
Cdd:TIGR03457 545 AEGKTTVIEIVCTRELGDP 563
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
6-531 |
1.46e-61 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 212.43 E-value: 1.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 6 AAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK08978 4 AQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPGDVA 164
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVdIPKDIQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 165 LKPAPegaTTHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALRGKEHVEY 242
Cdd:PRK08978 163 LAEGE---LEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVgmAGAVPALREFLAATGMPAVATLKGLGAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 243 DNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPASIGAHSKVDMALVGDIKSTL 316
Cdd:PRK08978 240 DHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVtgklntFAP-HAKVIHLDIDPAEINKLRQAHVALQGDLNALL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 317 RAL-LPLveekadrkfldkALEDYRDARKGLDDLAK-----PSEkAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARY 390
Cdd:PRK08978 319 PALqQPL------------NIDAWRQHCAQLRAEHAwrydhPGE-AIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 391 LKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEM 470
Cdd:PRK08978 386 MRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQ 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830211 471 K---AGGYltDGTELHDT-NFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEE 531
Cdd:PRK08978 466 QlffDERY--SETDLSDNpDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDELE 528
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-535 |
1.56e-61 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 212.18 E-value: 1.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGT-IEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNL 79
Cdd:PRK08266 2 TTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQ--ETHPQ-ELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSV 156
Cdd:PRK08266 82 NAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMPDQlATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 157 VV-LPGDVALKPAPEGATTHWYHAPQPvvTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALR 235
Cdd:PRK08266 162 ALeMPWDVFGQRAPVAAAPPLRPAPPP--APDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 236 GKEHVeyDNPYDVGMTgligFSSGFHTMMNADTLVLLGT----QFPYRAFYPTDAKIIQIDINPASIGAHsKVDMALVGD 311
Cdd:PRK08266 240 GRGIV--SDRHPLGLN----FAAAYELWPQTDVVIGIGSrlelPTFRWPWRPDGLKVIRIDIDPTEMRRL-KPDVAIVAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 312 IKSTLRALLPLVEEKADRKfldkalEDYRDARKGLDDLAKPSEKAIHPQ--YLaQQISHFAADDAIFT---CDVGtptvW 386
Cdd:PRK08266 313 AKAGTAALLDALSKAGSKR------PSRRAELRELKAAARQRIQAVQPQasYL-RAIREALPDDGIFVdelSQVG----F 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 387 AARY-LKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGF 465
Cdd:PRK08266 382 ASWFaFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGN 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830211 466 VAMEMK---AGGYLtdGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIP 535
Cdd:PRK08266 462 VRRDQKrrfGGRVV--ASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEASP 532
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
4-535 |
5.47e-60 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 209.18 E-value: 5.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 4 TVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLIN 83
Cdd:PRK09107 12 TGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPGD 162
Cdd:PRK09107 92 PLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVdIPKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 163 VALKP----APEGATTHwyHAPQPVVTPEEEELRKLAQLLR-------YSSNIALMCGSGCAGAHKELVEFAGkikAPIV 231
Cdd:PRK09107 172 VQFATgtytPPQKAPVH--VSYQPKVKGDAEAITEAVELLAnakrpviYSGGGVINSGPEASRLLRELVELTG---FPIT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 232 HALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPTdAKIIQIDINPASIGAHSKVD 305
Cdd:PRK09107 247 STLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRitgrldAFSPN-SKKIHIDIDPSSINKNVRVD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 306 MALVGDIKSTLRALLPLVEeKADRKFLDKALEDYR---DARKGLDDLA-KPSEKAIHPQYLAQQISHFAAD-DAIFTCDV 380
Cdd:PRK09107 326 VPIIGDVGHVLEDMLRLWK-ARGKKPDKEALADWWgqiARWRARNSLAyTPSDDVIMPQYAIQRLYELTKGrDTYITTEV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 381 GTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNN 460
Cdd:PRK09107 405 GQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830211 461 SVLGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELAIP 535
Cdd:PRK09107 485 QYMGMVRqwQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFP 561
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
2-539 |
9.84e-60 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 208.23 E-value: 9.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 2 KQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHL 81
Cdd:PRK06882 3 KLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LP 160
Cdd:PRK06882 83 ITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIdIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 161 GDVaLKPA-------PEGATTHWYHapqPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIV 231
Cdd:PRK06882 163 KDM-VNPAnkftyeyPEEVSLRSYN---PTVQGHKGQIKKALKALLVAKKPVLFVGGGVitAECSEQLTQFAQKLNLPVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 232 HALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPASIGAHSKVDM 306
Cdd:PRK06882 239 SSLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRttnnlAKYCPNAKVIHIDIDPTSISKNVPAYI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 307 ALVGDIKSTLRALLPLVEE------KADRKFLDKALEDYRdARKGLDdlAKPSEKAIHPQYLAQQISHFAADDAIFTCDV 380
Cdd:PRK06882 319 PIVGSAKNVLEEFLSLLEEenlaksQTDLTAWWQQINEWK-AKKCLE--FDRTSDVIKPQQVVEAIYRLTNGDAYVASDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 381 GTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNN 460
Cdd:PRK06882 396 GQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 461 SVLGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSI-DGPVLVDVVVAKEELAIPPQ 537
Cdd:PRK06882 476 RFLGMVKqwQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIkDKLVFVDVNVDETEHVYPMQ 555
|
..
gi 15830211 538 IK 539
Cdd:PRK06882 556 IR 557
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-535 |
2.61e-59 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 207.16 E-value: 2.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLH 80
Cdd:PRK07525 4 MKMTPSEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAG-IRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLP 160
Cdd:PRK07525 83 FVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESGPAQINIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 161 GDvalkpapegattHWYHA-----PQPVVTPE----EEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAP 229
Cdd:PRK07525 163 RD------------YFYGVidveiPQPVRLERgaggEQSLAEAAELLSEAKFPVILSGAGVvlSDAIEECKALAERLDAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 230 IVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQF-PYRA-------FYPTDAKIIQIDINPASIGAH 301
Cdd:PRK07525 231 VACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLnPFGTlpqygidYWPKDAKIIQVDINPDRIGLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 302 SKVDMALVGDIKSTLRALLPLVEE-------KADRKFL--------DKALE--DYRDARKGLDDLAKPSEKA---IHPQY 361
Cdd:PRK07525 311 KKVSVGICGDAKAVARELLARLAErlagdagREERKALiaaeksawEQELSswDHEDDDPGTDWNEEARARKpdyMHPRQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 362 LAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMG 441
Cdd:PRK07525 391 ALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 442 DFLSVVQMKLPVKIIVFNNSVLG-------------FVamemkaggyltdGTEL-HDTNFARIAEACGITGIRVEKASEI 507
Cdd:PRK07525 471 EVMTAVRHNWPVTAVVFRNYQWGaekknqvdfynnrFV------------GTELdNNVSYAGIAEAMGAEGVVVDTQEEL 538
|
570 580 590
....*....|....*....|....*....|
gi 15830211 508 DEALQRAFSI--DGPVLVDVVVAKEELAIP 535
Cdd:PRK07525 539 GPALKRAIDAqnEGKTTVIEIMCNQELGEP 568
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-527 |
6.81e-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: 202.29 E-value: 6.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 6 AAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGL 85
Cdd:TIGR02418 2 ADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKG-IELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNR-GVSVVVLPGDVA 164
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKpGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 165 LKPAPEGATTHWYhAPQPVVTPeEEELRKLAQLLRYSSNIALMCGSGcaGAHKELVE----FAGKIKAPIVHALRGKEHV 240
Cdd:TIGR02418 161 DSPVSVKAIPASY-APKLGAAP-DDAIDEVAEAIQNAKLPVLLLGLR--ASSPETTEavrrLLKKTQLPVVETFQGAGAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 241 EYDN-PYDVGMTGLIGFSSGFHTMMNADTLVLLG-TQFPYRAFY---PTDAKIIQIDINPASIGAHSKVDMALVGDIKST 315
Cdd:TIGR02418 237 SRELeDHFFGRVGLFRNQPGDRLLKQADLVITIGyDPIEYEPRNwnsENDATIVHIDVEPAQIDNNYQPDLELVGDIAST 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 316 LRALLPLVEEKADRKFLDKALEDYRDARKGLDDL-AKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMN 394
Cdd:TIGR02418 317 LDLLAERIPGYELPPDALAILEDLKQQREALDRVpATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFRSY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 395 GKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAM--EMKA 472
Cdd:TIGR02418 397 RARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFqeEMKY 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15830211 473 GgyLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVV 527
Cdd:TIGR02418 477 Q--RSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPV 529
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
6-542 |
7.19e-58 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 203.15 E-value: 7.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 6 AAYIAKTLESAGVKRIWGVTGDSLNGLSDSLN---RMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLI 82
Cdd:PRK06456 5 ARILVDSLKREGVKVIFGIPGLSNMQIYDAFVedlANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 83 NGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNR-GVSVVVLPG 161
Cdd:PRK06456 85 TGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRpGPVVIDIPR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 162 DVALKPA-----PEGATTHWYHAPQPVVTPeeEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHAL 234
Cdd:PRK06456 165 DIFYEKMeeikwPEKPLVKGYRDFPTRIDR--LALKKAAEILINAERPIILVGTGVvwSNATPEVLELAELLHIPIVSTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYP------TDAKIIQIDINPASIGAHSKVDMAL 308
Cdd:PRK06456 243 PGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSydemveTRKKFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 309 VGDIKSTLRALLPLVEE---KADRKFLDKALEDYRDARKGLDDLAKPseKAIHPQYLAQQISHFAADDAIFTCDVGTPTV 385
Cdd:PRK06456 323 YGNAKIILRELIKAITElgqKRDRSAWLKRVKEYKEYYSQFYYTEEN--GKLKPWKIMKTIRQALPRDAIVTTGVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 386 WAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGF 465
Cdd:PRK06456 401 WAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 466 V--AMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEELA---IPPQIKL 540
Cdd:PRK06456 481 VrqVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELAlptLPPGGRL 560
|
..
gi 15830211 541 EQ 542
Cdd:PRK06456 561 KQ 562
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
6-539 |
9.01e-57 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 200.08 E-value: 9.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 6 AAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK07979 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV-LPGDVa 164
Cdd:PRK07979 87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVdLPKDI- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 165 LKPA-------PEGATTHWYHapqPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALR 235
Cdd:PRK07979 166 LNPAnklpyvwPESVSMRSYN---PTTQGHKGQIKRALQTLVAAKKPVVYVGGGAinAACHQQLKELVEKLNLPVVSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPASIGAHSKVDMALVG 310
Cdd:PRK07979 243 GLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRttnnlAKYCPNATVLHIDIDPTSISKTVTADIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 311 DIKSTLRALLPLVEEKADRKFLD------KALEDYRdARKGLDdLAKPSEKaIHPQYLAQQISHFAADDAIFTCDVGTPT 384
Cdd:PRK07979 323 DARQVLEQMLELLSQESAHQPLDeirdwwQQIEQWR-ARQCLK-YDTHSEK-IKPQAVIETLWRLTKGDAYVTSDVGQHQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 385 VWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLG 464
Cdd:PRK07979 400 MFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 465 FVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAF---SIDGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK07979 480 MVKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALeqvRNNRLVFVDVTVDGSEHVYPMQIR 559
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-527 |
2.19e-55 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 195.84 E-value: 2.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTG---DSL-NGLSDSlnrmgTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGP 76
Cdd:PRK08617 3 KKKYGADLVVDSLINQGVKYVFGIPGakiDRVfDALEDS-----GPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 77 GNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNR-GVS 155
Cdd:PRK08617 78 GVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRpGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 156 VVVLPGDVALKPApEGATTHWYHAPQPVVTPEEEeLRKLAQLLRYSSNIALMCG-----SGCAGAHKELVEfagKIKAPI 230
Cdd:PRK08617 158 FVSLPQDVVDAPV-TSKAIAPLSKPKLGPASPED-INYLAELIKNAKLPVLLLGmrassPEVTAAIRRLLE---RTNLPV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 231 VHALRGKEHV--EYDNPYdVGMTGLIGFSSGFHTMMNADTLVLLGtqfpYRAF-Y-------PTDAKIIQIDINPASIGA 300
Cdd:PRK08617 233 VETFQAAGVIsrELEDHF-FGRVGLFRNQPGDELLKKADLVITIG----YDPIeYeprnwnsEGDATIIHIDVLPAEIDN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 301 HSKVDMALVGDIKSTLRALLPLVEEkadRKFLDKALEDYRDARKGLDDLAKP----SEKAIHPQYLAQQISHFAADDAIF 376
Cdd:PRK08617 308 YYQPERELIGDIAATLDLLAEKLDG---LSLSPQSLEILEELRAQLEELAERparlEEGAVHPLRIIRALQDIVTDDTTV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 377 TCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKII 456
Cdd:PRK08617 385 TVDVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHI 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830211 457 VFNNSVLGFVAM--EMKAGGylTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVV 527
Cdd:PRK08617 465 IWNDGHYNMVEFqeEMKYGR--SSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPV 535
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
4-536 |
1.40e-54 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 194.21 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 4 TVAAYIAKTLESAGVKRIWGVTGDSLNGLSdsLNRMGtIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFGQSLPSALFLA--AEAIG-IRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNR-GVSVVVLPGD 162
Cdd:PRK06112 92 PLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRpGPVVLLLPAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 163 VALKPAPEGA---TTHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSG--CAGAHKELVEFAGKIKAPIVHALRGK 237
Cdd:PRK06112 172 LLTAAAAAPAaprSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGvhISGASAALAALQSLAGLPVATTNMGK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 238 EHVEYDNPYDVGMTG-LIG-FSSGFHTM---MNADTLVLLGTQFPYRA-----FYPTDAKIIQIDINPASIGAHSKVdMA 307
Cdd:PRK06112 252 GAVDETHPLSLGVVGsLMGpRSPGRHLRdlvREADVVLLVGTRTNQNGtdswsLYPEQAQYIHIDVDGEEVGRNYEA-LR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 308 LVGDIKSTLRALLP------LVEEKADRKFLDKALEDYRDA-RKGLDDLAKPSEKAIHPQYLAQQISHFAADDAIFTCDV 380
Cdd:PRK06112 331 LVGDARLTLAALTDalrgrdLAARAGRRAALEPAIAAGREAhREDSAPVALSDASPIRPERIMAELQAVLTGDTIVVADA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 381 GTPTVWAARYLKMNGKR-RLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFN 459
Cdd:PRK06112 411 SYSSIWVANFLTARRAGmRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLN 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830211 460 NSVLGFV--AMEMKAGGYlTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVakEELAIPP 536
Cdd:PRK06112 491 NGILGFQkhAETVKFGTH-TDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVIT--DPSAFPP 566
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
379-525 |
1.71e-52 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 176.24 E-value: 1.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 379 DVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVF 458
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830211 459 NNSVLGFVAMEMKAGG----YLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDV 525
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGggrySGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
11-527 |
5.28e-52 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 186.57 E-value: 5.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 11 KTLESAGVKRIWGVTG----DSLNGLSDSlnrmgTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLF 86
Cdd:PRK08322 9 KCLENEGVEYIFGIPGeenlDLLEALRDS-----SIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 87 DCHRNHVPVLAIAAHIP--SSEIGSgyFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNR-GVSVVVLPGDV 163
Cdd:PRK08322 84 YAQLGGMPMVAITGQKPikRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERpGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 164 ALKPAPEGATTHwyHAPQPVVtPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALRGKEHVE 241
Cdd:PRK08322 162 AAEETDGKPLPR--SYSRRPY-ASPKAIERAAEAIQAAKNPLILIGAGAnrKTASKALTEFVDKTGIPFFTTQMGKGVIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 242 YDNPYDVGMTGL-----IGFssGFHtmmNADTLVLLGTQF----PYRAFYPTDAKIIQIDINPASIGAHSKVDMALVGDI 312
Cdd:PRK08322 239 ETHPLSLGTAGLsqgdyVHC--AIE---HADLIINVGHDViekpPFFMNPNGDKKVIHINFLPAEVDPVYFPQVEVVGDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 313 KSTLRALLPLVEEKADRKFldKALEDYRDA-----RKGLDDLAKPsekaIHPQYLAQQISHFAADDAIFTCDVGTPTVWA 387
Cdd:PRK08322 314 ANSLWQLKERLADQPHWDF--PRFLKIREAieahlEEGADDDRFP----MKPQRIVADLRKVMPDDDIVILDNGAYKIWF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 388 ARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVA 467
Cdd:PRK08322 388 ARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIR 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 468 MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVV 527
Cdd:PRK08322 468 WKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPV 527
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
357-535 |
7.44e-52 |
|
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: 175.76 E-value: 7.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 357 IHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGF 436
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 437 SMLMGDFLSVVQMKLPVKIIVFNNSVLGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRA 514
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRqwQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|.
gi 15830211 515 FSIDGPVLVDVVVAKEELAIP 535
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLP 181
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
362-527 |
4.70e-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: 157.03 E-value: 4.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 362 LAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMG 441
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 442 DFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYLTD-GTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGP 520
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVsGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGGP 161
|
....*..
gi 15830211 521 VLVDVVV 527
Cdd:cd00568 162 ALIEVKT 168
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-542 |
4.22e-43 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 161.97 E-value: 4.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLH 80
Cdd:PRK08199 6 RARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNR-GVSVVVL 159
Cdd:PRK08199 86 ASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRpGPVVLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 160 PGDVaLKPAPEGATTHWYHAPQPvvTPEEEELRKLAQLL-RYSSNIALMCGSG-CAGAHKELVEFAGKIKAPIVHALRGK 237
Cdd:PRK08199 166 PEDV-LSETAEVPDAPPYRRVAA--APGAADLARLAELLaRAERPLVILGGSGwTEAAVADLRAFAERWGLPVACAFRRQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 238 EHVEYDNPYDVGMTGLiGFSSGF-HTMMNADTLVLLGTQFP------YRAF---YPtDAKIIQIDINPASIGAHSKVDMA 307
Cdd:PRK08199 243 DLFDNRHPNYAGDLGL-GINPALaARIREADLVLAVGTRLGevttqgYTLLdipVP-RQTLVHVHPDAEELGRVYRPDLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 308 LVGDIKSTLRALLPL--VEEKADRKFLDKALEDYRDARKglddlAKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTV 385
Cdd:PRK08199 321 IVADPAAFAAALAALepPASPAWAEWTAAAHADYLAWSA-----PLPGPGAVQLGEVMAWLRERLPADAIITNGAGNYAT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 386 WAARYLKMNGKRRLLGSFNhGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGF 465
Cdd:PRK08199 396 WLHRFFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGT 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830211 466 VAM--EMKAGGYlTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAKEelAIPPQIKLEQ 542
Cdd:PRK08199 475 IRMhqEREYPGR-VSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPE--AITPTATLSQ 550
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
5-535 |
1.76e-42 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 160.36 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 5 VAAYIAKTLESAGVKRIWGVtgdSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGE-LAVCAGSCGPGNLHLIN 83
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGF---PVNELFDAAAAAGIRPVIARTERVAVHMADGYARATSGErVGVFAVQYGPGAENAFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 84 GLFDCHRNHVPVLAIAAHIPSSEigsgyfQETHPQ----ELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV- 158
Cdd:PRK06154 99 GVAQAYGDSVPVLFLPTGYPRGS------TDVAPNfeslRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLe 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 159 LPGDVALKPAPEGATTHwYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALRG 236
Cdd:PRK06154 173 LPVDVLAEELDELPLDH-RPSRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVlyAQATPELKELAELLEIPVMTTLNG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAF---YPTDAKIIQIDINPASIGAHSKVDMALVGDIK 313
Cdd:PRK06154 252 KSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYglpMPEGKTIIHSTLDDADLNKDYPIDHGLVGDAA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 314 STLRALLPLVEEKADRKFLDKA-----LEDYRDA--RKGLDDLAKpSEKAIHPQYLAQQISH-FAADDAIFTCDVGTP-- 383
Cdd:PRK06154 332 LVLKQMIEELRRRVGPDRGRAQqvaaeIEAVRAAwlAKWMPKLTS-DSTPINPYRVVWELQHaVDIKTVIITHDAGSPrd 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 384 ---TVWAAR----YLKMnGKRRLLGSfnhgsmanAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKII 456
Cdd:PRK06154 411 qlsPFYVASrpgsYLGW-GKTTQLGY--------GLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTI 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 457 VFNNSVLGFVAMEMKAggyltdGTELHDTNF-----ARIAEACGITGIRVEKASEIDEALQRAFSI--DG-PVLVDVVVA 528
Cdd:PRK06154 482 LLNNFSMGGYDKVMPV------STTKYRATDisgdyAAIARALGGYGERVEDPEMLVPALLRALRKvkEGtPALLEVITS 555
|
....*...
gi 15830211 529 KE-ELAIP 535
Cdd:PRK06154 556 EEtALSRP 563
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
76-529 |
1.48e-41 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 157.85 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 76 PGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGS--------GYFQETHPQ-ELFRECSHYCELVSSPEQIPQVLAIAMR 146
Cdd:PRK08327 85 VGTANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrntriHWTQEMRDQgGLVREYVKWDYEIRRGDQIGEVVARAIQ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 147 KAV-LNRGVSVVVLPGDVALKPAPEGATTHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMC--GSGCAGAHKELVEFA 223
Cdd:PRK08327 165 IAMsEPKGPVYLTLPREVLAEEVPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITwrAGRTAEGFASLRRLA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 224 GKIKAPIVHAlRGkEHVEYdnPYDVGMtgLIGFSSGFhTMMNADTLVLLGTQFPY---RAFYPTDAKIIQIDINPAsiga 300
Cdd:PRK08327 245 EELAIPVVEY-AG-EVVNY--PSDHPL--HLGPDPRA-DLAEADLVLVVDSDVPWipkKIRPDADARVIQIDVDPL---- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 301 HSK-------VDMALVGDIKSTLRALLPLV--EEKADRKFLDKALEDYRDARKgLDDLAK-------PSEKAIHPQYLAQ 364
Cdd:PRK08327 314 KSRiplwgfpCDLCIQADTSTALDQLEERLksLASAERRRARRRRAAVRELRI-RQEAAKraeierlKDRGPITPAYLSY 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 365 QISHFAAD-DAIFTcdvGTPTVWaaRYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFsmLMGDF 443
Cdd:PRK08327 393 CLGEVADEyDAIVT---EYPFVP--RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSF--IFGVP 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 444 LSVVQM----KLPVKIIVFNNSVLGFVA---MEMKAGGY--------LTDGTElhDTNFARIAEACGITGIRVEKASEID 508
Cdd:PRK08327 466 EAAHWVaeryGLPVLVVVFNNGGWLAVKeavLEVYPEGYaarkgtfpGTDFDP--RPDFAKIAEAFGGYGERVEDPEELK 543
|
490 500
....*....|....*....|....*
gi 15830211 509 EALQRAFSI----DGPVLVDVVVAK 529
Cdd:PRK08327 544 GALRRALAAvrkgRRSAVLDVIVDR 568
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
1-539 |
1.83e-40 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 154.38 E-value: 1.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTgdSLNGLS--DSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGN 78
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVI--SIHNMPilDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 79 LHLINGLFDCHRNHVPVLAIAAHIPSSEIGS--GYFQETHPQ-ELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVS 155
Cdd:PRK07064 79 GNAAGALVEALTAGTPLLHITGQIETPYLDQdlGYIHEAPDQlTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 156 VVV-LPGDV--ALKPAPEGATThwyhAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAgKIKAPIVH 232
Cdd:PRK07064 159 VSVeIPIDIqaAEIELPDDLAP----VHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLV-DLGFGVVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 233 ALRGKEHVEYDNPYDVGMTGLIGFSSGFHTmmNADTLVLLGTQF------PYRAFYPTDakIIQIDINPASIGAHSKVDM 306
Cdd:PRK07064 234 STQGRGVVPEDHPASLGAFNNSAAVEALYK--TCDLLLVVGSRLrgnetlKYSLALPRP--LIRVDADAAADGRGYPNDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 307 ALVGDIKSTLRALLPLVEE--KADRKFlDKALEDYRDA-----RKGLDDLAKpsekaihpqyLAQQISHFAADDAIFTCD 379
Cdd:PRK07064 310 FVHGDAARVLARLADRLEGrlSVDPAF-AADLRAAREAavadlRKGLGPYAK----------LVDALRAALPRDGNWVRD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 380 VGTP-TVWAARYLKMNGKRRLLGSFNhGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVF 458
Cdd:PRK07064 379 VTISnSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLM 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 459 NNSVLGFV-AMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVA-----KEEL 532
Cdd:PRK07064 458 NDGGYGVIrNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVDMLsigpfAAAF 537
|
....*..
gi 15830211 533 AIPPQIK 539
Cdd:PRK07064 538 AGPPVKK 544
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-530 |
4.85e-40 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 153.98 E-value: 4.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLS-GELAVCAGSCGPGNL 79
Cdd:PRK11269 2 AKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVV- 158
Cdd:PRK11269 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLId 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 159 LPGDVALKPAPEGATTHwyhAPQPVVTPE--EEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHAL 234
Cdd:PRK11269 162 LPFDVQVAEIEFDPDTY---EPLPVYKPAatRAQIEKALEMLNAAERPLIVAGGGVinADASDLLVEFAELTGVPVIPTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 235 RGKEHVEYDNPYDVGMTGL-IGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPASIGAHSKVDMAL 308
Cdd:PRK11269 239 MGWGAIPDDHPLMAGMVGLqTSHRYGNATLLASDFVLGIGNRWANRhtgsvEVYTKGRKFVHVDIEPTQIGRVFGPDLGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 309 VGDIKSTLRALLPLVEE-KADRKFLDKA--LEDYRDARKGLDDLAKPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTV 385
Cdd:PRK11269 319 VSDAKAALELLVEVAREwKAAGRLPDRSawVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 386 WAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGF 465
Cdd:PRK11269 399 AAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 466 V-----AMEM--------------KAGGYLTDgtelhdtnFARIAEACGITGIRVEKASEIDEALQRA------FSIdgP 520
Cdd:PRK11269 479 IrqaqrAFDMdycvqlafeninspELNGYGVD--------HVKVAEGLGCKAIRVFKPEDIAPALEQAkalmaeFRV--P 548
|
570
....*....|
gi 15830211 521 VLVDVVVAKE 530
Cdd:PRK11269 549 VVVEVILERV 558
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
4-529 |
8.28e-39 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 149.35 E-value: 8.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 4 TVAAYIAKTLESAGVKRIWGVTG----DSLNGLSDSlnrmgTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNL 79
Cdd:PRK07524 3 TCGEALVRLLEAYGVETVFGIPGvhtvELYRGLAGS-----GIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 80 HLINGLFDCHRNHVPVLAIAA--HIPSSEIGSGYFQETHPQE-LFRECSHYCELVSSPEQIPQVLAIAMrkAVLN--RGV 154
Cdd:PRK07524 78 NIATAMGQAYADSIPMLVISSvnRRASLGKGRGKLHELPDQRaMVAGVAAFSHTLMSAEDLPEVLARAF--AVFDsaRPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 155 SV-VVLPGDVALKPAPEGATTHWYHAPQPvvTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHA 233
Cdd:PRK07524 156 PVhIEIPLDVLAAPADHLLPAPPTRPARP--GPAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVALT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 234 LRGKEHVEYDNPYDVGMTGLIgfSSGFHTMMNADTLVLLGTQF-------PYRAFYPTDAKIIQIDINPASIGAHSKVDM 306
Cdd:PRK07524 234 INAKGLLPAGHPLLLGASQSL--PAVRALIAEADVVLAVGTELgetdydvYFDGGFPLPGELIRIDIDPDQLARNYPPAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 307 ALVGDIKSTLRALLPLVEEKADRKflDKALEDYRDARKGLddlakpsEKAIHPQYLAQQisHF------AADDAIFTCDv 380
Cdd:PRK07524 312 ALVGDARAALEALLARLPGQAAAA--DWGAARVAALRQAL-------RAEWDPLTAAQV--ALldtilaALPDAIFVGD- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 381 GTPTVWAAR-YLKMNGKRRLL-GSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVF 458
Cdd:PRK07524 380 STQPVYAGNlYFDADAPRRWFnASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLW 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830211 459 NNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVVAK 529
Cdd:PRK07524 460 NNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQAC 530
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
191-319 |
1.79e-38 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 138.08 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 191 LRKLAQLLRYSSNIALMCGSGC--AGAHKELVEFAGKIKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADT 268
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVrrSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830211 269 LVLLGTQF-------PYRAFYPtDAKIIQIDINPASIGAHSKVDMALVGDIKSTLRAL 319
Cdd:pfam00205 81 VLAVGARFddirttgKLPEFAP-DAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
9-526 |
2.27e-37 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 145.63 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 9 IAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK05858 11 AARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVL-NRGVSVVVLPGDVALKP 167
Cdd:PRK05858 90 QFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTpHRGPVFVDFPMDHAFSM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 168 APEGATTHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKE--LVEFAGKIKAPIVHALRGKEHVEYDNP 245
Cdd:PRK05858 170 ADDDGRPGALTELPAGPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEaaLLRLAEELGIPVLMNGMGRGVVPADHP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 246 ydvgmtglIGFSSGFHTMM-NADTLVLLGTQFPYR---AFYPTDAKIIQIDINPASIGAHSKVDMALVGDIKSTLRALLP 321
Cdd:PRK05858 250 --------LAFSRARGKALgEADVVLVVGVPMDFRlgfGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILSALAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 322 LVEEKADRKFLDKALEDYRDARKGLDDLAKPSEKA-IHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLL 400
Cdd:PRK05858 322 AGGDRTDHQGWIEELRTAETAARARDAAELADDRDpIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 401 GSFNHGSMANAMPQALGAQATEPERQVVAMCGDG--GFSMLmgDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKA-GGYLT 477
Cdd:PRK05858 402 DPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGafGFSLM--DVDTLVRHNLPVVSVIGNNGIWGLEKHPMEAlYGYDV 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15830211 478 DGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVV 526
Cdd:PRK05858 480 AADLRPGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVL 528
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
5-170 |
2.92e-37 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 135.83 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 5 VAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLING 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 85 LFDCHRNHVPVLAIAAHIPSSEIGSGYFQ-ETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNR-GVSVVVLPGD 162
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRpGPVYLEIPLD 160
|
....*...
gi 15830211 163 VALKPAPE 170
Cdd:pfam02776 161 VLLEEVDE 168
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
359-527 |
6.97e-32 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 121.24 E-value: 6.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 359 PQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSM 438
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 439 LMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFSID 518
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
....*....
gi 15830211 519 GPVLVDVVV 527
Cdd:cd02010 161 GVHVIDCPV 169
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
78-528 |
1.06e-31 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 128.92 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 78 NLHLING-------LFDCHRNHVPVLAIAAHIPSSEIGSGYF-QETHPQELFRECSHY-CElVSSPEQIPQVLA----IA 144
Cdd:PRK07092 78 NLHSAAGvgnamgnLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWsIE-PARAEDVPAAIArayhIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 145 MRKAvlnRGVSVVVLPGDVALKPAPEGATTHWYHApqpvVTPEEEELRKLAQLLRYSSNIALMCGSGC--AGAHKELVEF 222
Cdd:PRK07092 157 MQPP---RGPVFVSIPYDDWDQPAEPLPARTVSSA----VRPDPAALARLGDALDAARRPALVVGPAVdrAGAWDDAVRL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 223 AGKIKAPIVHAlrgkehveydnPydvgMTGLIGFSS------GFHTMMNA---------DTLVLLGT------QFPYRAF 281
Cdd:PRK07092 230 AERHRAPVWVA-----------P----MSGRCSFPEdhplfaGFLPASREkisalldghDLVLVIGApvftyhVEGPGPH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 282 YPTDAKIIQIdINPASIGAHSKVDMALVGDIKSTLRALLPLVEEKAdrkfldkaledyRDARKGLDDLAKPSEK--AIHP 359
Cdd:PRK07092 295 LPEGAELVQL-TDDPGEAAWAPMGDAIVGDIRLALRDLLALLPPSA------------RPAPPARPMPPPAPAPgePLSV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 360 QYLAQQISHFAADDAIFTCDV--GTPTVWaaRYLKMNGKrrllGSF---NHGSMANAMPQALGAQATEPERQVVAMCGDG 434
Cdd:PRK07092 362 AFVLQTLAALRPADAIVVEEApsTRPAMQ--EHLPMRRQ----GSFytmASGGLGYGLPAAVGVALAQPGRRVIGLIGDG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 435 GFSMLMGDFLSVVQMKLPVKIIVFNNSvlGFVAME-----MKAGGylTDGTELHDTNFARIAEACGITGIRVEKASEIDE 509
Cdd:PRK07092 436 SAMYSIQALWSAAQLKLPVTFVILNNG--RYGALRwfapvFGVRD--VPGLDLPGLDFVALARGYGCEAVRVSDAAELAD 511
|
490
....*....|....*....
gi 15830211 510 ALQRAFSIDGPVLVDVVVA 528
Cdd:PRK07092 512 ALARALAADGPVLVEVEVA 530
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
359-528 |
1.54e-31 |
|
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: 119.94 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 359 PQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSM 438
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 439 LMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEM--KAGGYLTDGTELHDTNFARIAEACGITGIRVEKASEIDEALQRAFS 516
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQqlSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 15830211 517 IDGPVLVDVVVA 528
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-539 |
3.21e-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: 124.50 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 1 MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHeevaafaagaeaqlsgELavCAGSC------ 74
Cdd:COG3961 3 MTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCN----------------EL--NAGYAadgyar 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 75 -----------GPGNLHLINGLFDCHRNHVPVLAIAAhIPSSEI-----------GSGYFqeTHPQELFRECSHYCELVS 132
Cdd:COG3961 65 vnglgalvttyGVGELSAINGIAGAYAERVPVVHIVG-APGTRAqrrgpllhhtlGDGDF--DHFLRMFEEVTVAQAVLT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 133 S---PEQIPQVLAIAMRKavlNRGVsVVVLPGDVALKPAPEGATTHwyHAPQPVVTPE--EEELRKLAQLLRYSSNIALM 207
Cdd:COG3961 142 PenaAAEIDRVLAAALRE---KRPV-YIELPRDVADAPIEPPEAPL--PLPPPASDPAalAAAVAAAAERLAKAKRPVIL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 208 CGSGCA--GAHKELVEFAGKIKAPIVHALRGKEHVEYDNPYDVGM-TGLIGFSSGFHTMMNADTLVLLGTQFP--YRAFY 282
Cdd:COG3961 216 AGVEVHrfGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGVVFTdtNTGGF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 283 ---PTDAKIIQIDINPASIGAH--SKVDMAlvgdikSTLRALLPLVEEKADRkfldkaledYRDARKGLDDLAKPSEKAI 357
Cdd:COG3961 296 taqLDPERTIDIQPDSVRVGGHiyPGVSLA------DFLEALAELLKKRSAP---------LPAPAPPPPPPPAAPDAPL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 358 HPQYLAQQISHFAADDAIFTCDVGTPtVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFS 437
Cdd:COG3961 361 TQDRLWQRLQAFLDPGDIVVADTGTS-LFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 438 MLMGDFLSVVQMKLPVKIIVFNNsvlgfvamemkaGGYLT-------DGT--ELHDTNFARIAEACG---ITGIRVEKAS 505
Cdd:COG3961 440 LTAQELSTMLRYGLKPIIFVLNN------------DGYTIeraihgpDGPynDIANWDYAKLPEAFGggnALGFRVTTEG 507
|
570 580 590
....*....|....*....|....*....|....*
gi 15830211 506 EIDEALQRAFSI-DGPVLVDVVVAKEElaIPPQIK 539
Cdd:COG3961 508 ELEEALAAAEANtDRLTLIEVVLDKMD--APPLLK 540
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
357-533 |
1.96e-28 |
|
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: 112.22 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 357 IHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGF 436
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 437 SMLMGDFLSVVQMKLPVKIIVFNNSVLGfvaMEMKaggYLTD-------GTELHDTNFARIAEACGITGIRVEKASEIDE 509
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWG---AEKK---NQVDfynnrfvGTELESESFAKIAEACGAKGITVDKPEDVGP 157
|
170 180
....*....|....*....|....*..
gi 15830211 510 ALQRAFSIDG---PVLVDVVVAKEELA 533
Cdd:cd02013 158 ALQKAIAMMAegkTTVIEIVCDQELGD 184
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-160 |
2.04e-25 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 102.22 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 8 YIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFD 87
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPLLDALARSG-IRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830211 88 CHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNR-GVSVVVLP 160
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRpGPVALDLP 154
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
357-527 |
2.12e-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: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 357 IHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSfNHGSMANAMPQALGAQATEPERQVVAMCGDGGF 436
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTL-RGGGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 437 SMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYLTDGTE------LHD--TNFARIAEACGITGIRVEKASEID 508
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENapdgldLLDpgIDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*....
gi 15830211 509 EALQRAFSIDGPVLVDVVV 527
Cdd:cd02002 160 EALREALAEGGPALIEVVV 178
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
361-539 |
8.60e-19 |
|
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: 84.12 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 361 YLAQQISHFAADDAIFTCDVGTPTvWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLM 440
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSW-FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 441 GDFLSVVQMKLPVKIIVFNNSvlgfvamemkagGYLTDgTELHDT----------NFARIAEACG----ITGIRVEKASE 506
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINND------------GYTIE-RAIHGPeasyndianwNYTKLPEVFGggggGLSFRVKTEGE 151
|
170 180 190
....*....|....*....|....*....|....
gi 15830211 507 IDEALQRA-FSIDGPVLVDVVVAKEElaIPPQIK 539
Cdd:cd02005 152 LDEALKDAlFNRDKLSLIEVILPKDD--APEALK 183
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
6-528 |
4.39e-16 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 81.19 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 6 AAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK09259 13 FHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEG-IRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 86 FDCHRNHVPVLAIAAhipSSE-----IGSGYFQET--------HPQELFRecshycelVSSPEQIPQVLAIAMRKAVLNR 152
Cdd:PRK09259 92 ANATTNCFPMIMISG---SSEreivdLQQGDYEELdqlnaakpFCKAAFR--------VNRAEDIGIGVARAIRTAVSGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 153 -GVSVVVLPGDV--ALKPAPEGATTHWYHA-PQPVVTPEEEELRKLAQLLRYSSN--IALMCGSGCAGAHKELVEFAGKI 226
Cdd:PRK09259 161 pGGVYLDLPAKVlaQTMDADEALTSLVKVVdPAPAQLPAPEAVDRALDLLKKAKRplIILGKGAAYAQADEQIREFVEKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 227 KAPIVHALRGKEHVEYDNPYDVGmtgligfSSGFHTMMNADTLVLLGTQFPYRAFY---PT---DAKIIQIDINPASIGA 300
Cdd:PRK09259 241 GIPFLPMSMAKGLLPDTHPQSAA-------AARSLALANADVVLLVGARLNWLLSHgkgKTwgaDKKFIQIDIEPQEIDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 301 HSKVDMALVGDIKSTLRALLPLVEE---KADRKFLDKALEdyrDARKGLDDLAKPSEKAIHPqylaqqISHFAADDAIFT 377
Cdd:PRK09259 314 NRPIAAPVVGDIGSVMQALLAGLKQntfKAPAEWLDALAE---RKEKNAAKMAEKLSTDTQP------MNFYNALGAIRD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 378 C-----DV-----GTPTVWAAR-YLKMNGKRRLLGSFNHGSMANAMPQALGAqATEPERQVVAMCGDGGFSMLMGDFLSV 446
Cdd:PRK09259 385 VlkenpDIylvneGANTLDLARnIIDMYKPRHRLDCGTWGVMGIGMGYAIAA-AVETGKPVVAIEGDSAFGFSGMEVETI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 447 VQMKLPVKIIVFNNSvlgfvamemkaGGYLTDGTEL------------HDTNFARIAEACGITGIRVEKASEIDEALQRA 514
Cdd:PRK09259 464 CRYNLPVTVVIFNNG-----------GIYRGDDVNLsgagdpsptvlvHHARYDKMMEAFGGVGYNVTTPDELRHALTEA 532
|
570
....*....|....
gi 15830211 515 FSIDGPVLVDVVVA 528
Cdd:PRK09259 533 IASGKPTLINVVID 546
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
62-527 |
1.79e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 79.15 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 62 QLSGELAVCAGSCGPGnlhLINGLFDCH---RNHVPVLAI-----AAHIP-----SSEIGSgyfqethpqeLFRECSHYC 128
Cdd:PRK12474 64 RIAGKPAVTLLHLGPG---LANGLANLHnarRAASPIVNIvgdhaVEHLQydaplTSDIDG----------FARPVSRWV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 129 ELVSSPEQIPQVLAIAMRKA-VLNRGVSVVVLPGDVALKPAPEGATTHWYHAPQPVVtpeEEELRKLAQLLRYSSNIALM 207
Cdd:PRK12474 131 HRSASAGAVDSDVARAVQAAqSAPGGIATLIMPADVAWNEAAYAAQPLRGIGPAPVA---AETVERIAALLRNGKKSALL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 208 C-GSGCAGAhkeLVEFAGKIKA------------PIVHALRGKEHVEydnpyDVGMTGLIGfssgfhTMM--NADTLVLL 272
Cdd:PRK12474 208 LrGSALRGA---PLEAAGRIQAktgvrlycdtfaPRIERGAGRVPIE-----RIPYFHEQI------TAFlkDVEQLVLV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 273 GTQFPYRAF-YPTdakiiqidiNPASIGAHSKVDMALVGDIKSTLRALLPLVEEkadrkfLDKALEDYRDARKGLDDLAK 351
Cdd:PRK12474 274 GAKPPVSFFaYPG---------KPSWGAPPGCEIVYLAQPDEDLAQALQDLADA------VDAPAEPAARTPLALPALPK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 352 pseKAIHPQYLAQQISHFAADDAIFTCDVGTPTVW------AAR---YLKMNGkrrllgsfnhGSMANAMPQALGAQATE 422
Cdd:PRK12474 339 ---GALNSLGVAQLIAHRTPDQAIYADEALTSGLFfdmsydRARphtHLPLTG----------GSIGQGLPLAAGAAVAA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 423 PERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYLTDGT------ELH--DTNFARIAEAC 494
Cdd:PRK12474 406 PDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGELQRVGAQGAGRnalsmlDLHnpELNWMKIAEGL 485
|
490 500 510
....*....|....*....|....*....|...
gi 15830211 495 GITGIRVEKASEIDEALQRAFSIDGPVLVDVVV 527
Cdd:PRK12474 486 GVEASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
74-527 |
4.70e-15 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 77.96 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 74 CGPGnlhLINGLFDCH---RNHVPVLAI-----AAHIP-----SSEIGSgyfqethpqeLFRECSHYCELVSSPEQIPQV 140
Cdd:PRK07586 72 LGPG---LANGLANLHnarRARTPIVNIvgdhaTYHRKydaplTSDIEA----------LARPVSGWVRRSESAADVAAD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 141 LAIAMRKA-VLNRGVSVVVLPGDVALKPAPEGATTHwyhAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKel 219
Cdd:PRK07586 139 AAAAVAAArGAPGQVATLILPADVAWSEGGPPAPPP---PAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERG-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 220 VEFAGKIKA-----------PIVHAlRGKEHVEYDN-PY--DVGMTGLIGFssgfhtmmnaDTLVLLGTQFPYRAF-YPt 284
Cdd:PRK07586 214 LAAAARIAAatgarllaetfPARME-RGAGRPAVERlPYfaEQALAQLAGV----------RHLVLVGAKAPVAFFaYP- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 285 dakiiqidinpasigahskvdmalvgDIKSTLrallplVEEKADRKFLDKALEDYRDARKGLDD----------LAKPSE 354
Cdd:PRK07586 282 --------------------------GKPSRL------VPEGCEVHTLAGPGEDAAAALEALADalgakpaappLAAPAR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 355 K-----AIHPQYLAQQISHFAADDAIF-----TCDVG--TPTVWAARYLKMNgkrrLLGsfnhGSMANAMPQALGAQATE 422
Cdd:PRK07586 330 PplptgALTPEAIAQVIAALLPENAIVvdesiTSGRGffPATAGAAPHDWLT----LTG----GAIGQGLPLATGAAVAC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 423 PERQVVAMCGDGGFsMLMGDFL-SVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYLTDG------TELHD--TNFARIAEA 493
Cdd:PRK07586 402 PDRKVLALQGDGSA-MYTIQALwTQARENLDVTTVIFANRAYAILRGELARVGAGNPGpraldmLDLDDpdLDWVALAEG 480
|
490 500 510
....*....|....*....|....*....|....
gi 15830211 494 CGITGIRVEKASEIDEALQRAFSIDGPVLVDVVV 527
Cdd:PRK07586 481 MGVPARRVTTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
357-529 |
4.17e-14 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 71.16 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 357 IHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGF 436
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 437 SMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKA-------------------GGYLTDgtelhdtnFARIAEACGIT 497
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAfdmdyqvnlafeninsselGGYGVD--------HVKVAEGLGCK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 15830211 498 GIRVEKASEIDEALQRAFSIDG----PVLVDVVVAK 529
Cdd:cd02006 160 AIRVTKPEELAAAFEQAKKLMAehrvPVVVEAILER 195
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
362-533 |
9.90e-14 |
|
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: 69.65 E-value: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 362 LAQQISHFAADDAIftcdVGTpTVWAARYLKMNGKRRLLGSFNH----GSMANAMPQALGAQATEPERQVVAMCGDGGFS 437
Cdd:cd03371 5 IEIVLSRAPATAAV----VST-TGMTSRELFELRDRPGGGHAQDfltvGSMGHASQIALGIALARPDRKVVCIDGDGAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 438 MLMGDFLSVVQMKLP-VKIIVFNNSVLGFVamemkaGGYLTDGTelhDTNFARIAEACGITGIRVEkaSEIDE---ALQR 513
Cdd:cd03371 80 MHMGGLATIGGLAPAnLIHIVLNNGAHDSV------GGQPTVSF---DVSLPAIAKACGYRAVYEV--PSLEElvaALAK 148
|
170 180
....*....|....*....|
gi 15830211 514 AFSIDGPVLVDVVVAKEELA 533
Cdd:cd03371 149 ALAADGPAFIEVKVRPGSRS 168
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
408-525 |
2.30e-13 |
|
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: 69.26 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 408 MANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNS---VLGFVAMEMKAGGYltdGTELHD 484
Cdd:cd02003 50 MGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHgfgCINNLQESTGSGSF---GTEFRD 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15830211 485 --------------TNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDV 525
Cdd:cd02003 127 rdqesgqldgallpVDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVI 181
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
360-536 |
2.67e-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: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 360 QYLAQQISHFAADDAIftcdVGTpTVWAARYLKMNGKRRLLGSFNH----GSMANAMPQALGAQATEPERQVVAMCGDGG 435
Cdd:TIGR03297 176 EAIAAILDHLPDNTVI----VST-TGKTSRELYELRDRIGQGHARDfltvGSMGHASQIALGLALARPDQRVVCLDGDGA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 436 FSMLMGDFLSVVQMKLPVKI-IVFNNSVLGFVamemkaGGYLTDGTelhDTNFARIAEACGITGIR-VEKASEIDEALQR 513
Cdd:TIGR03297 251 ALMHMGGLATIGTQGPANLIhVLFNNGAHDSV------GGQPTVSQ---HLDFAQIAKACGYAKVYeVSTLEELETALTA 321
|
170 180
....*....|....*....|...
gi 15830211 514 AFSIDGPVLVDVVVAKEELAIPP 536
Cdd:TIGR03297 322 ASSANGPRLIEVKVRPGSRADLG 344
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
7-161 |
9.62e-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: 60.44 E-value: 9.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 7 AYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGeLAVCAGSCGPGNLHLINGLF 86
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830211 87 DCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPG 161
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
366-527 |
9.97e-08 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 52.29 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 366 ISHFAAD--DAIFTCDVGTPT--VWAARylkmngkRRLLGSFNHGSMANAMPQALG-AQATEpeRQVVAMCGDGGFSMLM 440
Cdd:cd03372 5 IKTLIADlkDELVVSNIGFPSkeLYAAG-------DRPLNFYMLGSMGLASSIGLGlALAQP--RKVIVIDGDGSLLMNL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 441 GDFLSVVQMKLP-VKIIVFNNSVLGFVAMEMKAGGYLTDgtelhdtnFARIAEACGITGIRVEKAseiDEALQRAF--SI 517
Cdd:cd03372 76 GALATIAAEKPKnLIIVVLDNGAYGSTGNQPTHAGKKTD--------LEAVAKACGLDNVATVAS---EEAFEKAVeqAL 144
|
170
....*....|
gi 15830211 518 DGPVLVDVVV 527
Cdd:cd03372 145 DGPSFIHVKI 154
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
406-525 |
5.36e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 50.60 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 406 GSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKLP-VKIIVFNNSVLGFvamemkAGGYLTDGTELHD 484
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKnLTIIVMDNGVYQI------TGGQPTLTSQTVD 130
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15830211 485 tnFARIAEACGITGIRVEKASEIDEAL-QRAFSIDGPVLVDV 525
Cdd:PRK06163 131 --VVAIARGAGLENSHWAADEAHFEALvDQALSGPGPSFIAV 170
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
406-523 |
1.51e-05 |
|
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: 45.17 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 406 GSMANAMPQALGAqATEPERQVVAMCGDGGFSMLMGDFLSVVQMK-LPVKIIVFNNSVLGfvamemKAGGYLTDGTelhD 484
Cdd:cd02001 42 GSMGLAGSIGLGL-ALGLSRKVIVVDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNRAYG------STGGQPTPSS---N 111
|
90 100 110
....*....|....*....|....*....|....*....
gi 15830211 485 TNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLV 523
Cdd:cd02001 112 VNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLL 150
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
415-527 |
1.94e-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: 42.20 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 415 ALGAQATEPERqVVAMCGDggFSML--MGDFLSVVQMKLPVKIIVFNNSvlG---FvamEMKAGGYLTDGTE-----LHD 484
Cdd:cd02009 60 ALGIALATDKP-TVLLTGD--LSFLhdLNGLLLGKQEPLNLTIVVINNN--GggiF---SLLPQASFEDEFErlfgtPQG 131
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15830211 485 TNFARIAEACGITGIRVEKASEIDEALQRAFSIDGPVLVDVVV 527
Cdd:cd02009 132 LDFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKT 174
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
407-531 |
9.37e-04 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 40.34 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 407 SMANAMPQALGAQATEPERQVVAMCGDGGF--SMLMGdFLSVVQMKLPVKIIVFNNSVlgfVAM----EMKAGGY-LTDG 479
Cdd:cd02008 52 CMGASIGVAIGMAKASEDKKVVAVIGDSTFfhSGILG-LINAVYNKANITVVILDNRT---TAMtggqPHPGTGKtLTEP 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15830211 480 TELHDtnFARIAEACGITGIRV---EKASEIDEALQRAFSIDGPvlvDVVVAKEE 531
Cdd:cd02008 128 TTVID--IEALVRAIGVKRVVVvdpYDLKAIREELKEALAVPGV---SVIIAKRP 177
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
385-526 |
1.34e-03 |
|
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: 40.20 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 385 VWAARYLKMNGkrrllgsFN--HGsmaNAMPQALGAQATEPERQVVAMCGDG-GFSMLMGDFLSVVQMKLPVKIIVFNNS 461
Cdd:cd03375 38 SRLPYYFNTYG-------FHtlHG---RALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830211 462 VLGfvameMKAG--------GYLT----DGTELHDTNFARIAEACGITGIRVEKASEID---EALQRAFSIDGPVLVDVV 526
Cdd:cd03375 108 IYG-----LTKGqaspttpeGFKTkttpYGNIEEPFNPLALALAAGATFVARGFSGDIKqlkEIIKKAIQHKGFSFVEVL 182
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
402-464 |
3.75e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 39.48 E-value: 3.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830211 402 SFN--HGSManaMPQALGAQATEPERQVVAMCGDG-GFSMLMGDFLSVVQMKLPVKIIVFNNSVLG 464
Cdd:PRK05778 67 GLHtlHGRA---IAFATGAKLANPDLEVIVVGGDGdLASIGGGHFIHAGRRNIDITVIVENNGIYG 129
|
|
| |
