|
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: 1183.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK09124 1 MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLP 160
Cdd:PRK09124 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVVLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 161 GDVALKPAPESASSHWYHAPQPTVTPADEELHKLAQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPVVHALRGKEHV 240
Cdd:PRK09124 161 GDVALKPAPERATPHWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRGKEHV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKALL 320
Cdd:PRK09124 241 EYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKATLAALL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 321 PLLEEKTDRRFLDKALEDYREARKGLDDLAKPSE--KALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRR 398
Cdd:PRK09124 321 PLLEEKTDRKFLDKALEHYRKARKGLDDLAVPSDggKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 399 LLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKAGGYLTD 478
Cdd:PRK09124 401 LLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMKAGGYLTD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 479 GTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGR 558
Cdd:PRK09124 481 GTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMPPQIKLEQAKGFSLYMLRAIISGR 560
|
570
....*....|....
gi 505807110 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: 770.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK06546 1 MAKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLP 160
Cdd:PRK06546 81 LINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGGGVSVVTLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 161 GDVALKPAPESASSHWYHAPQPTVTPADEELHKLAQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPVVHALRGKEHV 240
Cdd:PRK06546 161 GDIADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGKEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAFYPtDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKALL 320
Cdd:PRK06546 241 QYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFPYDQFLP-DVRTAQVDIDPEHLGRRTRVDLAVHGDVAETIRALL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 321 PLLEEKTDRRFLDKALEDYREARKG-LDDLAKPSEK--ALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKR 397
Cdd:PRK06546 320 PLVKEKTDRRFLDRMLKKHARKLEKvVGAYTRKVEKhtPIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 398 RLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKAGGYLT 477
Cdd:PRK06546 400 RVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMLVDGLPD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 478 DGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISG 557
Cdd:PRK06546 480 FGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTDPNALSIPPTITGEQVKGFALAASKTVLNG 559
|
570
....*....|....*
gi 505807110 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: 563.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVL 159
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRpGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 160 PGDVALKPAPESASSHWYHAPQPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALRGK 237
Cdd:COG0028 161 PKDVQAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGArrAGAAEELRALAERLGAPVVTTLMGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 238 EHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYR------AFYPtDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:COG0028 241 GAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRvtgnwdEFAP-DAKIIHIDIDPAEIGKNYPVDLPIVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 312 IKSTLKALLPLLEEKTDRRflDKALEDYREARKGLDDLAKPSEKALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYL 391
Cdd:COG0028 320 AKAVLAALLEALEPRADDR--AAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 392 QMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMK 471
Cdd:COG0028 398 RFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807110 472 A-GGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIPPQIK 539
Cdd:COG0028 478 LfYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENPPGATLD 546
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-555 |
1.24e-164 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 480.65 E-value: 1.24e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM-GTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08611 2 AKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVL 159
Cdd:PRK08611 82 HLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVLTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 160 PGDV---ALKPAPESASSHWyhaPQPTVTPADEELHKLAQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPVVHALRG 236
Cdd:PRK08611 162 PDDLpaqKIKDTTNKTVDTF---RPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTL 316
Cdd:PRK08611 239 KGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYVDYLPKKAKAIQIDTDPANIGKRYPVNVGLVGDAKKAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 317 KALLPLLEEKTDRRFLDKALEDYREARKGLDDLAKPSEKALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGK 396
Cdd:PRK08611 319 HQLTENIKHVEDRRFLEACQENMAKWWKWMEEDENNASTPIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNLGTN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 397 RRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKAGGYL 476
Cdd:PRK08611 399 QKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGEL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807110 477 TDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAII 555
Cdd:PRK08611 479 EYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAPLPGKIVNDEALGYSKWAIKSLF 557
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-558 |
1.36e-136 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 408.06 E-value: 1.36e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 4 TVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLnRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAI-RKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPGDV 163
Cdd:PRK06457 82 GLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINLPVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 164 aLKPAPESASSHWYHAPQPTVTPadeELHKLAQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPVVHALRGKEHVEYD 243
Cdd:PRK06457 162 -LRKSSEYKGSKNTEVGKVKYSI---DFSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 244 NPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKallPLL 323
Cdd:PRK06457 238 DPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLN---IDI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 324 EEKTDRrFLDKALEDYREARKGLDDLAKPSEKALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSF 403
Cdd:PRK06457 315 EEKSDK-FYEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 404 NHGSMANAMPQAIGAK-ATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKAGGYLTDGTEL 482
Cdd:PRK06457 394 WLGSMGIGVPGSVGASfAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMGYPEWGVDL 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807110 483 HDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGR 558
Cdd:PRK06457 474 YNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMPPKLTFKQAGEYVLSIFREKLEGI 549
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-570 |
2.02e-126 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 383.49 E-value: 2.02e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM-GTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08273 1 MSQTVADFILERLREWGVRRVFGYPGDGINGLLGALGRAdDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSH-YCELVSTPEQIPQVLAIAMRKAVINRGVSVVV 158
Cdd:PRK08273 81 HLLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAGaFVQMVTVPEQLRHLVDRAVRTALAERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 159 LPGDVALKPAPESASSHWY-----HAPQPTVTPADEELHKLAQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPVVHA 233
Cdd:PRK08273 161 LPNDVQELEYEPPPHAHGTvhsgvGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 234 LRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAFYPT--DAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:PRK08273 241 LLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFPYSEFLPKegQARGVQIDIDGRMLGLRYPMEVNLVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 312 IKSTLKALLPLLEEKTDRRFLDKALEDYREARKGLDDLAKPSEKALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYL 391
Cdd:PRK08273 321 AAETLRALLPLLERKKDRSWRERIEKWVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADSGSCANWYARDL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 392 QMngKRRLLGSFNHG--SMANAMPQAIGAKATAPNRQVIAMCGDGGFSML-MGDFLSLA----QMKLPVKIV-IFNNSIL 463
Cdd:PRK08273 401 RM--RRGMMASLSGTlaTMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAkywrQWSDPRLIVlVLNNRDL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 464 GFVAMEMKA-GG--YLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIPPQIKL 540
Cdd:PRK08273 479 NQVTWEQRVmEGdpKFEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDPNVPPLPPHITL 558
|
570 580 590
....*....|....*....|....*....|...
gi 505807110 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 ... |
11-527 |
2.59e-108 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 336.04 E-value: 2.59e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 11 KTLEQAGVKRIWGVTGDSLNGLSDSL-NRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDCH 89
Cdd:TIGR02720 7 KVLEAWGVDHIYGIPGGSFNSTMDALsAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYDAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 90 RNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPGDVALKPAP 169
Cdd:TIGR02720 87 EDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHNGVAVVTIPVDFGWQEIP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 170 E----SASSHWYHAPQPtvTPADEELHKLAQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPVVHALRGKEHVEYDNP 245
Cdd:TIGR02720 167 DndyyASSVSYQTPLLP--APDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGIIEDRYP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 246 YDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAFYPT--DAK-IIQIDINPGSIGAHSKVDMALVGDIKSTLKALLPL 322
Cdd:TIGR02720 245 AYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKAfkNTKyFIQIDIDPAKLGKRHHTDIAVLADAKKALAAILAQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 323 LEEKTDRRFLDKALEDYREARKGLDDLAKPSEKALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGS 402
Cdd:TIGR02720 325 VEPRESTPWWQANVANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNKWITS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 403 FNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKAGGYLTDGTEL 482
Cdd:TIGR02720 405 NLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQPLIGVDF 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 505807110 483 HDTNFARIAEACGIKGIRVEKASEVDEALQTA--FSTDGPVLVDVVV 527
Cdd:TIGR02720 485 NDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAkaIKQGKPVLIDAKI 531
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
3-538 |
3.70e-103 |
|
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: 322.06 E-value: 3.70e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 3 QTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLI 82
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 83 NGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPG 161
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVdLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 162 DVALK----PAPESASSHWYhapQPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALR 235
Cdd:TIGR00118 161 DVTTAeieyPYPEKVNLPGY---RPTVKGHPLQIKKAAELINLAKKPVILVGGGViiAGASEELKELAERIQIPVTTTLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:TIGR00118 238 GLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRvtgnlAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 311 DIKSTLKALLPLLEEKTDRRflDKALEDYREARKGLDDLAKP-SEKALHPQYLAQQISRFADDDAIFTCDVGTPTVWAAR 389
Cdd:TIGR00118 318 DARNVLEELLKKLFELKERK--ESAWLEQINKWKKEYPLKMDyTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 390 YLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVA-- 467
Cdd:TIGR00118 396 FYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRqw 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807110 468 MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIPPQI 538
Cdd:TIGR00118 476 QELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVA 546
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
357-533 |
5.76e-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: 295.21 E-value: 5.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 357 LHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGF 436
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 437 SMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFS 516
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALA 161
|
170
....*....|....*..
gi 505807110 517 TDGPVLVDVVVAKEELA 533
Cdd:cd02014 162 ADGPVVIDVVTDPNEPP 178
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
6-540 |
1.77e-83 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 271.63 E-value: 1.77e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 6 ASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRmGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVA 164
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIdLPKDVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 165 -------LKPAPESASSHWYhapQPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALR 235
Cdd:PRK06276 163 egeldleKYPIPAKIDLPGY---KPTTFGHPLQIKKAAELIAEAERPVILAGGGViiSGASEELIELSELVKIPVCTTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALV 309
Cdd:PRK06276 240 GKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTtgdissFAP-NAKIIHIDIDPAEIGKNVRVDVPIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 310 GDIKSTLKALLPLLEEKTDRRFlDKALEDYREARKGLDDLAKPSEKALHPQYLAQQISRFADD-----DAIFTCDVGTPT 384
Cdd:PRK06276 319 GDAKNVLRDLLAELMKKEIKNK-SEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 385 VWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILG 464
Cdd:PRK06276 398 MWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 465 FVAmEMKAGGYLTDGTELH---DTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEEL--AIPPQIK 539
Cdd:PRK06276 478 MVY-QWQNLYYGKRQSEVHlgeTPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAlpMVPPGGN 556
|
.
gi 505807110 540 L 540
Cdd:PRK06276 557 L 557
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
4-167 |
7.40e-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: 248.23 E-value: 7.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 4 TVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPGDV 163
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKRGVAVLILPGDV 160
|
....
gi 505807110 164 ALKP 167
Cdd:cd07039 161 QDAP 164
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
2-535 |
1.82e-79 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 260.48 E-value: 1.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 2 KQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:PRK06048 7 KMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD-LRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LP 160
Cdd:PRK06048 86 VTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIdLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 161 GDVALKPA----PESASSHWYhapQPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHAL 234
Cdd:PRK06048 166 KDVTTAEIdfdyPDKVELRGY---KPTYKGNPQQIKRAAELIMKAERPIIYAGGGVisSNASEELVELAETIPAPVTTTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYR------AFYPtDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK06048 243 MGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRvtgklaSFAP-NAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 309 VGDIKSTLKALLPLLEEKTDRRFLDKALE---DYREARKGLDDLAKPsekalhpQYLAQQISRFADDdAIFTCDVGTPTV 385
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDRKEWLDKINQwkkEYPLKYKEREDVIKP-------QYVIEQIYELCPD-AIIVTEVGQHQM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 386 WAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGF 465
Cdd:PRK06048 394 WAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGM 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807110 466 VA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK06048 474 VRqwQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSP 545
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
1-531 |
1.48e-73 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 246.12 E-value: 1.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM---GTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPG 77
Cdd:PRK07418 17 QRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAeaeGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 78 NLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVV 157
Cdd:PRK07418 97 ATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 158 V-LPGDVALK-----P-APESASSHWYHapqPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKA 228
Cdd:PRK07418 177 IdIPKDVGQEefdyvPvEPGSVKPPGYR---PTVKGNPRQINAALKLIEEAERPLLYVGGGAisAGAHAELKELAERFQI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 229 PVVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRA------FYPTdAKIIQIDINPGSIGAHS 302
Cdd:PRK07418 254 PVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVtgkldeFASR-AKVIHIDIDPAEVGKNR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 303 KVDMALVGDIKSTLKALLPLLEEKTDRRFLDKALEDYREARKGLDDLAKPSEKALHPQYLAQQISRFAdDDAIFTCDVGT 382
Cdd:PRK07418 333 RPDVPIVGDVRKVLVKLLERSLEPTTPPRTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLA-PDAYYTTDVGQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 383 PTVWAARYLQmNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSI 462
Cdd:PRK07418 412 HQMWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGW 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 463 LGFV-------------AMEMKAGgyltdgtelhDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAK 529
Cdd:PRK07418 491 QGMVrqwqesfygerysASNMEPG----------MPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRR 560
|
..
gi 505807110 530 EE 531
Cdd:PRK07418 561 DE 562
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-535 |
3.45e-73 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 243.85 E-value: 3.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-L 159
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIdI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 160 PGDVALKPA----PESASSHWYhapQPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHA 233
Cdd:PRK08527 161 PKDVTATLGefeyPKEISLKTY---KPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAilSNASEEIRELVKKTGIPAVET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 234 LRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAFYPTD-----AKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK08527 238 LMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSefakhAKIIHVDIDPSSISKIVNADYPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 309 VGDIKSTLKALLPLLEEKTDRRFLD--KALEDYREarkgLDDLA-KPSEKALHPQYLAQQISRFADDDAIFTCDVGTPTV 385
Cdd:PRK08527 318 VGDLKNVLKEMLEELKEENPTTYKEwrEILKRYNE----LHPLSyEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 386 WAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGF 465
Cdd:PRK08527 394 WVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGM 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807110 466 V----AMEMKAGGYLTDGTELHDtnFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK08527 474 VrqwqTFFYEERYSETDLSTQPD--FVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLP 545
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
9-535 |
8.87e-71 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 237.80 E-value: 8.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK07282 16 VLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITGIADA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVALKP 167
Cdd:PRK07282 96 MSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIdLPKDVSALE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 168 APESASSHwYHAP--QPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALRGKEHVEYD 243
Cdd:PRK07282 176 TDFIYDPE-VNLPsyQPTLEPNDMQIKKILKQLSKAKKPVILAGGGInyAEAATELNAFAERYQIPVVTTLLGQGTIATS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 244 NPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKA 318
Cdd:PRK07282 255 HPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRltgnpKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKKALQM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 319 LLPLLEEKTD-RRFLDKALEDYREARKglddlAKPSEKALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKR 397
Cdd:PRK07282 335 LLAEPTVHNNtEKWIEKVTKDKNRVRS-----YDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNER 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 398 RLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKA--GGY 475
Cdd:PRK07282 410 QLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESfyEGR 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 476 LTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTaFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK07282 490 TSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLEV-ITEDVPMLIEVDISRKEHVLP 548
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
1-531 |
3.78e-70 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 236.52 E-value: 3.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSL---NRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPG 77
Cdd:CHL00099 8 REKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 78 NLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVV 157
Cdd:CHL00099 88 ATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 158 V-LPGDVALKP----APESASSHwYHAP--QPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKA 228
Cdd:CHL00099 168 IdIPKDVGLEKfdyyPPEPGNTI-IKILgcRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAiiSDAHQEITELAELYKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 229 PVVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAF-----YPTDAKIIQIDINPGSIGAHSK 303
Cdd:CHL00099 247 PVTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTgkldeFACNAQVIHIDIDPAEIGKNRI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 304 VDMALVGDIKSTLKALLPLLEeKTDRRFLDKALEDYREA----RKGLDDLAKPSEKALHPQYLAQQISRFADDdAIFTCD 379
Cdd:CHL00099 327 PQVAIVGDVKKVLQELLELLK-NSPNLLESEQTQAWRERinrwRKEYPLLIPKPSTSLSPQEVINEISQLAPD-AYFTTD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 380 VGTPTVWAARYLQMnGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFN 459
Cdd:CHL00099 405 VGQHQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIIN 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807110 460 NSILGFVAM-------EMKAGGYLTDGTelhdTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEE 531
Cdd:CHL00099 484 NKWQGMVRQwqqafygERYSHSNMEEGA----PDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDE 558
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-535 |
1.44e-69 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 234.22 E-value: 1.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08155 11 KRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-L 159
Cdd:PRK08155 91 LVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIdI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 160 PGDV-----ALKPAPESAsshwyhAPQPTVTPADEELHKLAQLIRYSSNIALMCGSG--CAGAHQELVEFAAKIKAPVVH 232
Cdd:PRK08155 171 PKDVqtaviELEALPAPA------EKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGviNSGAPARARELAEKAQLPTTM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 233 ALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDM 306
Cdd:PRK08155 245 TLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAigkteqFCP-NAKIIHVDIDRAELGKIKQPHV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 307 ALVGDIKSTLKALLPLLEEKTDRRFLDKALEDYRE---ARKGLDDlakpsekALHPQYLAQQISRFADDDAIFTCDVGTP 383
Cdd:PRK08155 324 AIQADVDDVLAQLLPLVEAQPRAEWHQLVADLQREfpcPIPKADD-------PLSHYGLINAVAACVDDNAIITTDVGQH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 384 TVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSIL 463
Cdd:PRK08155 397 QMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEAL 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807110 464 GFV--AMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK08155 477 GLVhqQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYP 550
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
4-535 |
2.27e-68 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 231.40 E-value: 2.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 4 TVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06725 16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGD 162
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRpGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 163 VALkpapESASSHWYH-----APQPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALR 235
Cdd:PRK06725 175 VQN----EKVTSFYNEvveipGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVihSGGSEELIEFARENRIPVVSTLM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALV 309
Cdd:PRK06725 251 GLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVtgklelFSP-HSKKVHIDIDPSEFHKNVAVEYPVV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 310 GDIKSTLKALLPLLEEKTDRRFLDKaLEDYREARKgLDDLAKPSEkaLHPQYLAQQISRFADDDAIFTCDVGTPTVWAAR 389
Cdd:PRK06725 330 GDVKKALHMLLHMSIHTQTDEWLQK-VKTWKEEYP-LSYKQKESE--LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAH 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 390 YLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVA-- 467
Cdd:PRK06725 406 FYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRqw 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807110 468 MEMKAGGYLTDgTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK06725 486 QEMFYENRLSE-SKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFP 552
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
4-535 |
4.30e-68 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 231.41 E-value: 4.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 4 TVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK07789 32 TGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQE------THPqelfreCSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVV 157
Cdd:PRK07789 112 PIADANMDSVPVVAITGQVGRGLIGTDAFQEadivgiTMP------ITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 158 VlpgDVALKPAPESASSHW--------YHapqPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIK 227
Cdd:PRK07789 186 V---DIPKDALQAQTTFSWpprmdlpgYR---PVTKPHGKQIREAAKLIAAARRPVLYVGGGVirAEASAELRELAELTG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 228 APVVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYR------AFYPtDAKIIQIDINPGSIGAH 301
Cdd:PRK07789 260 IPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRvtgkldSFAP-DAKVIHADIDPAEIGKN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 302 SKVDMALVGDIKSTLKALLPLLEektdRRFLDKALEDYREARKGLDDL--------AKPSEKALHPQYLAQQISRFADDD 373
Cdd:PRK07789 339 RHADVPIVGDVKEVIAELIAALR----AEHAAGGKPDLTAWWAYLDGWretyplgyDEPSDGSLAPQYVIERLGEIAGPD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 374 AIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPV 453
Cdd:PRK07789 415 AIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPI 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 454 KIVIFNNSILGFVAMEMK---AGGYltDGTELHD-----TNFARIAEACGIKGIRVEKASEVDEALQTAFST-DGPVLVD 524
Cdd:PRK07789 495 KVALINNGNLGMVRQWQTlfyEERY--SNTDLHThshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAInDRPVVID 572
|
570
....*....|.
gi 505807110 525 VVVAKEELAIP 535
Cdd:PRK07789 573 FVVGKDAMVWP 583
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-535 |
6.27e-68 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 230.03 E-value: 6.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 6 ASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMpTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK07710 19 AQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHIL-TRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVA 164
Cdd:PRK07710 98 ADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIdIPKDMV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 165 LKPApESASSHWYHAP--QPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALRGKEHV 240
Cdd:PRK07710 178 VEEG-EFCYDVQMDLPgyQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVlhAKASKELTSYAEQQEIPVVHTLLGLGGF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKST 315
Cdd:PRK07710 257 PADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRvtgnlAYFAKEATVAHIDIDPAEIGKNVPTEIPIVADAKQA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 316 LKALLPLLEEKTDRrflDKALEDYREARKGLDDLAKPSEKALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNG 395
Cdd:PRK07710 337 LQVLLQQEGKKENH---HEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 396 KRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVA--MEMKAG 473
Cdd:PRK07710 414 PDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRqwQEEFYN 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807110 474 GYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK07710 494 QRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMP 555
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
13-535 |
1.37e-65 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 224.23 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 13 LEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDCHRNH 92
Cdd:PLN02470 23 LEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGLADALLDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 93 VPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVALKPA--- 168
Cdd:PLN02470 103 VPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVdIPKDIQQQLAvpn 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 169 ---PESASSHWYHAPQPtvtPADEELHKLAQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPVVHALRGKEHVEYDNP 245
Cdd:PLN02470 183 wnqPMKLPGYLSRLPKP---PEKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGLGAFPASDE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 246 YDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYR------AFyPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKAL 319
Cdd:PLN02470 260 LSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRvtgkleAF-ASRASIVHIDIDPAEIGKNKQPHVSVCADVKLALQGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 320 LPLLEEKTDRRFldkaleDYREARKGLDD------LAKPS-EKALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQ 392
Cdd:PLN02470 339 NKLLEERKAKRP------DFSAWRAELDEqkekfpLSYPTfGDAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 393 MNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAM---- 468
Cdd:PLN02470 413 YKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQwedr 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505807110 469 ---EMKAGGYLTDGTELHDT--NFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PLN02470 493 fykANRAHTYLGDPDAEAEIfpDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLP 564
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
6-539 |
5.34e-65 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 222.39 E-value: 5.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 6 ASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVa 164
Cdd:PRK08979 87 ATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIdLPKDC- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 165 LKPA-------PESASSHWYHapqPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALR 235
Cdd:PRK08979 166 LNPAilhpyeyPESIKMRSYN---PTTSGHKGQIKRGLQALLAAKKPVLYVGGGAiiSGADKQILQLAEKLNLPVVSTLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAF-----YPTDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK08979 243 GLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTnnlekYCPNATILHIDIDPSSISKTVRVDIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 311 DIKSTLKALLPLLEEKTDRRflDKA--------LEDYREaRKGLDdLAKPSEKaLHPQYLAQQISRFADDDAIFTCDVGT 382
Cdd:PRK08979 323 SADKVLDSMLALLDESGETN--DEAaiaswwneIEVWRS-RNCLA-YDKSSER-IKPQQVIETLYKLTNGDAYVASDVGQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 383 PTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSI 462
Cdd:PRK08979 398 HQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 463 LGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFS-TDGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK08979 478 LGMVKqwQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAmKDRLVFVDINVDETEHVYPMQIR 557
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
6-531 |
2.02e-63 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 217.44 E-value: 2.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 6 ASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK08978 4 AQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVA 164
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVdIPKDIQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 165 LKPAPesaSSHWYHAPQPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALRGKEHVEY 242
Cdd:PRK08978 163 LAEGE---LEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVgmAGAVPALREFLAATGMPAVATLKGLGAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 243 DNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALVGDikstL 316
Cdd:PRK08978 240 DHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVtgklntFAP-HAKVIHLDIDPAEINKLRQAHVALQGD----L 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 317 KALLPLLEEKTDrrfldkaLEDYREARKGLDDLAK-----PSEkALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYL 391
Cdd:PRK08978 315 NALLPALQQPLN-------IDAWRQHCAQLRAEHAwrydhPGE-AIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 392 QMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMK 471
Cdd:PRK08978 387 RFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQ 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807110 472 ---AGGYltDGTELHDT-NFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEE 531
Cdd:PRK08978 467 lffDERY--SETDLSDNpDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDELE 528
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
2-535 |
2.70e-63 |
|
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: 217.81 E-value: 2.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 2 KQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAG-IRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPG 161
Cdd:TIGR03457 80 VTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREMGPAQLNIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 162 DvalkpapesassHWYHA-----PQPTV---TPADE-ELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPV 230
Cdd:TIGR03457 160 D------------YFYGEidveiPRPVRldrGAGGAtSLAQAARLLAEAKFPVIISGGGVvmGDAVEECKALAERLGAPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 231 VHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQF-PYRA-------FYPTDAKIIQIDINPGSIGAHS 302
Cdd:TIGR03457 228 VNSYLHNDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLgPFGTlpqygidYWPKNAKIIQVDANAKMIGLVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 303 KVDMALVGDIKSTLKALLPLLEEKT--------------DRRFLDKALEDYREARK--GLDDLAKPSEKA---LHPQYLA 363
Cdd:TIGR03457 308 KVTVGICGDAKAAAAEILQRLAGKAgdanraerkakiqaERSAWEQELSEMTHERDpfSLDMIVEQRQEEgnwLHPRQVL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 364 QQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDF 443
Cdd:TIGR03457 388 RELEKAMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 444 LSLAQMKLPVKIVIFNNSILGfvaMEMKAGGYLTD----GTELH-DTNFARIAEACGIKGIRVEKASEVDEALQTAFS-- 516
Cdd:TIGR03457 468 MTAVRHDIPVTAVVFRNRQWG---AEKKNQVDFYNnrfvGTELEsELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAaq 544
|
570
....*....|....*....
gi 505807110 517 TDGPVLVDVVVAKEELAIP 535
Cdd:TIGR03457 545 AEGKTTVIEIVCTRELGDP 563
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-527 |
6.26e-63 |
|
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: 216.15 E-value: 6.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 6 ASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:TIGR02418 2 ADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKG-IELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGDVA 164
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKpGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 165 LKPAPESASShwyHAPQPTVTPA-DEELHKLAQLIRYSSNIALMCGSGcaGAHQELVE----FAAKIKAPVVHALRGKEH 239
Cdd:TIGR02418 161 DSPVSVKAIP---ASYAPKLGAApDDAIDEVAEAIQNAKLPVLLLGLR--ASSPETTEavrrLLKKTQLPVVETFQGAGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 240 VEYDN-PYDVGMTGLIGFSSGFHTMMNADTLILLG-TQFPYRAFY---PTDAKIIQIDINPGSIGAHSKVDMALVGDIKS 314
Cdd:TIGR02418 236 VSRELeDHFFGRVGLFRNQPGDRLLKQADLVITIGyDPIEYEPRNwnsENDATIVHIDVEPAQIDNNYQPDLELVGDIAS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 315 TLKALLPLLEEKTDRRFLDKALEDYREARKGLDDL-AKPSEKALHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQM 393
Cdd:TIGR02418 316 TLDLLAERIPGYELPPDALAILEDLKQQREALDRVpATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFRS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 394 NGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAM--EMK 471
Cdd:TIGR02418 396 YRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFqeEMK 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 505807110 472 AGgyLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVV 527
Cdd:TIGR02418 476 YQ--RSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPV 529
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
6-525 |
4.23e-62 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 215.05 E-value: 4.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 6 ASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQipqvLAIAMRKAV-INR----GVSVVVLP 160
Cdd:PRK06965 104 ATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRD----LAETVKKAFyIARtgrpGPVVVDIP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 161 GDVALKPAPesasshwYHAPQ--------PTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPV 230
Cdd:PRK06965 180 KDVSKTPCE-------YEYPKsvemrsynPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVilANASRELRQLADLLGYPV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 231 VHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRA------FYPTDAKIIQIDINPGSIGAHSKV 304
Cdd:PRK06965 253 TNTLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVignpahFASRPRKIIHIDIDPSSISKRVKV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 305 DMALVGDIKSTLKALLPLLEE---KTDRRFLDKALEDYREARKgLDDLA-KPSEKALHPQYLAQQISRFADDDAIFTCDV 380
Cdd:PRK06965 333 DIPIVGDVKEVLKELIEQLQTaehGPDADALAQWWKQIEGWRS-RDCLKyDRESEIIKPQYVVEKLWELTDGDAFVCSDV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 381 GTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNN 460
Cdd:PRK06965 412 GQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNN 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807110 461 SILGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFS-TDGPVLVDV 525
Cdd:PRK06965 492 RYLGMVRqwQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRlKDRTVFLDF 559
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-527 |
3.47e-61 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 211.64 E-value: 3.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTG---DSL-NGLSDSlnrmgTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGP 76
Cdd:PRK08617 3 KKKYGADLVVDSLINQGVKYVFGIPGakiDRVfDALEDS-----GPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 77 GNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVS 155
Cdd:PRK08617 78 GVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRpGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 156 VVVLPGDVALKPAPESASSHwyhAPQPTVTPA-DEELHKLAQLIRYSSNIALMCG-----SGCAGAHQELVEfaaKIKAP 229
Cdd:PRK08617 158 FVSLPQDVVDAPVTSKAIAP---LSKPKLGPAsPEDINYLAELIKNAKLPVLLLGmrassPEVTAAIRRLLE---RTNLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 230 VVHALRGKEHV--EYDNPYdVGMTGLIGFSSGFHTMMNADTLILLGtqfpYRAF-Y-------PTDAKIIQIDINPGSIG 299
Cdd:PRK08617 232 VVETFQAAGVIsrELEDHF-FGRVGLFRNQPGDELLKKADLVITIG----YDPIeYeprnwnsEGDATIIHIDVLPAEID 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 300 AHSKVDMALVGDIKSTLKALLPLLEE-KTDRRFLDkALEDYREARKGLDDLAKP-SEKALHPQYLAQQISRFADDDAIFT 377
Cdd:PRK08617 307 NYYQPERELIGDIAATLDLLAEKLDGlSLSPQSLE-ILEELRAQLEELAERPARlEEGAVHPLRIIRALQDIVTDDTTVT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 378 CDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFsMLMGDFLSLA-QMKLPVKIV 456
Cdd:PRK08617 386 VDVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGF-LFSAMELETAvRLKLNIVHI 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807110 457 IFNNSILGFVAM--EMKAGGylTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVV 527
Cdd:PRK08617 465 IWNDGHYNMVEFqeEMKYGR--SSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPV 535
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-535 |
5.66e-61 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 210.64 E-value: 5.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGT-IEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08266 2 TTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQ--ETHPQ-ELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSV 156
Cdd:PRK08266 82 NAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMPDQlATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 157 VV-LPGDVALKPAPESASSHWYHAPQPTVTPadEELHKLAQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPVVHALR 235
Cdd:PRK08266 162 ALeMPWDVFGQRAPVAAAPPLRPAPPPAPDP--DAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 236 GKEHVeyDNPYDVGMTgligFSSGFHTMMNADTLILLGT----QFPYRAFYPTDAKIIQIDINPGSIGAHsKVDMALVGD 311
Cdd:PRK08266 240 GRGIV--SDRHPLGLN----FAAAYELWPQTDVVIGIGSrlelPTFRWPWRPDGLKVIRIDIDPTEMRRL-KPDVAIVAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 312 IKSTLKALLPLLEEKTDRRfldkalEDYREARKGLDDLAKPSEKALHPQ--YLaQQISRFADDDAIFT---CDVGtptvW 386
Cdd:PRK08266 313 AKAGTAALLDALSKAGSKR------PSRRAELRELKAAARQRIQAVQPQasYL-RAIREALPDDGIFVdelSQVG----F 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 387 AARY-LQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGF 465
Cdd:PRK08266 382 ASWFaFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGN 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505807110 466 VAMEMK---AGGYLtdGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK08266 462 VRRDQKrrfGGRVV--ASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEASP 532
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
2-539 |
6.14e-60 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 208.61 E-value: 6.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 2 KQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:PRK06882 3 KLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LP 160
Cdd:PRK06882 83 ITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIdIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 161 GDVaLKPA-------PESASSHWYHapqPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVV 231
Cdd:PRK06882 163 KDM-VNPAnkftyeyPEEVSLRSYN---PTVQGHKGQIKKALKALLVAKKPVLFVGGGVitAECSEQLTQFAQKLNLPVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 232 HALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDM 306
Cdd:PRK06882 239 SSLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRttnnlAKYCPNAKVIHIDIDPTSISKNVPAYI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 307 ALVGDIKSTLKALLPLLEEKTdrrfLDKALEDYREARKGLDDL-AKP------SEKALHPQYLAQQISRFADDDAIFTCD 379
Cdd:PRK06882 319 PIVGSAKNVLEEFLSLLEEEN----LAKSQTDLTAWWQQINEWkAKKclefdrTSDVIKPQQVVEAIYRLTNGDAYVASD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 380 VGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFN 459
Cdd:PRK06882 395 VGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 460 NSILGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFST-DGPVLVDVVVAKEELAIPP 536
Cdd:PRK06882 475 NRFLGMVKqwQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIkDKLVFVDVNVDETEHVYPM 554
|
...
gi 505807110 537 QIK 539
Cdd:PRK06882 555 QIR 557
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-535 |
1.75e-59 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 207.93 E-value: 1.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK07525 4 MKMTPSEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAG-IRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLP 160
Cdd:PRK07525 83 FVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESGPAQINIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 161 GDvalkpapesassHWYHA-----PQPTVTPA----DEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAP 229
Cdd:PRK07525 163 RD------------YFYGVidveiPQPVRLERgaggEQSLAEAAELLSEAKFPVILSGAGVvlSDAIEECKALAERLDAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 230 VVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQF-PYRA-------FYPTDAKIIQIDINPGSIGAH 301
Cdd:PRK07525 231 VACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLnPFGTlpqygidYWPKDAKIIQVDINPDRIGLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 302 SKVDMALVGDIKSTLKALLPLLEEKTdrrfldkALEDYREARKGL-------------------DDL-------AKPSEK 355
Cdd:PRK07525 311 KKVSVGICGDAKAVARELLARLAERL-------AGDAGREERKALiaaeksaweqelsswdhedDDPgtdwneeARARKP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 356 A-LHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDG 434
Cdd:PRK07525 384 DyMHPRQALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 435 GFSMLMGDFLSLAQMKLPVKIVIFNNSILG-------------FVamemkaggyltdGTEL-HDTNFARIAEACGIKGIR 500
Cdd:PRK07525 464 AWGISMNEVMTAVRHNWPVTAVVFRNYQWGaekknqvdfynnrFV------------GTELdNNVSYAGIAEAMGAEGVV 531
|
570 580 590
....*....|....*....|....*....|....*..
gi 505807110 501 VEKASEVDEALQTAFS--TDGPVLVDVVVAKEELAIP 535
Cdd:PRK07525 532 VDTQEELGPALKRAIDaqNEGKTTVIEIMCNQELGEP 568
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
4-536 |
3.68e-59 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 206.92 E-value: 3.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 4 TVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWmptRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFGQSLPSALFLAAEAIGIRQIAY---RTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGD 162
Cdd:PRK06112 92 PLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRpGPVVLLLPAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 163 VALKPAPESA---SSHWYHAPQPTVTPADEELHKLAQLIRYSSNIALMCGSG--CAGAHQELVEFAAKIKAPVVHALRGK 237
Cdd:PRK06112 172 LLTAAAAAPAaprSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGvhISGASAALAALQSLAGLPVATTNMGK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 238 EHVEYDNPYDVGMTG-LIG-FSSGFHTM---MNADTLILLGTQFPYRA-----FYPTDAKIIQIDINPGSIGAHSKVdMA 307
Cdd:PRK06112 252 GAVDETHPLSLGVVGsLMGpRSPGRHLRdlvREADVVLLVGTRTNQNGtdswsLYPEQAQYIHIDVDGEEVGRNYEA-LR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 308 LVGDIKSTLKALLPLLE------EKTDRRFLDKALEDYREA-RKGLDDLAKPSEKALHPQYLAQQISRFADDDAIFTCDV 380
Cdd:PRK06112 331 LVGDARLTLAALTDALRgrdlaaRAGRRAALEPAIAAGREAhREDSAPVALSDASPIRPERIMAELQAVLTGDTIVVADA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 381 GTPTVWAARYLQMNGKR-RLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFN 459
Cdd:PRK06112 411 SYSSIWVANFLTARRAGmRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLN 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807110 460 NSILGFV--AMEMKAGGYlTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVakEELAIPP 536
Cdd:PRK06112 491 NGILGFQkhAETVKFGTH-TDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVIT--DPSAFPP 566
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
6-539 |
1.32e-58 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 205.08 E-value: 1.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 6 ASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK07979 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVa 164
Cdd:PRK07979 87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVdLPKDI- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 165 LKPA-------PESASSHWYHapqPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALR 235
Cdd:PRK07979 166 LNPAnklpyvwPESVSMRSYN---PTTQGHKGQIKRALQTLVAAKKPVVYVGGGAinAACHQQLKELVEKLNLPVVSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK07979 243 GLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRttnnlAKYCPNATVLHIDIDPTSISKTVTADIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 311 DIKSTLKALLPLLEEKTDRRFLD------KALEDYReARKGLDdLAKPSEKaLHPQYLAQQISRFADDDAIFTCDVGTPT 384
Cdd:PRK07979 323 DARQVLEQMLELLSQESAHQPLDeirdwwQQIEQWR-ARQCLK-YDTHSEK-IKPQAVIETLWRLTKGDAYVTSDVGQHQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 385 VWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILG 464
Cdd:PRK07979 400 MFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 465 FVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAF---STDGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK07979 480 MVKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALeqvRNNRLVFVDVTVDGSEHVYPMQIR 559
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
6-539 |
3.70e-58 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 203.82 E-value: 3.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 6 ASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06466 7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVA 164
Cdd:PRK06466 87 ATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVdIPKDMT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 165 lKPA-------PESASSHWYhapQPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALR 235
Cdd:PRK06466 167 -NPAekfeyeyPKKVKLRSY---SPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVvlGNASALLTELAHLLNLPVTNTLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALV 309
Cdd:PRK06466 243 GLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVtngpakFCP-NAKIIHIDIDPASISKTIKADIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 310 GDIKSTLKALLPLLEE---KTDRRFLD---KALEDYReARKGLDDLAKPSEKALHPQYLAQQISRFADDDAIFTCDVGTP 383
Cdd:PRK06466 322 GPVESVLTEMLAILKEigeKPDKEALAawwKQIDEWR-GRHGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVGQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 384 TVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSIL 463
Cdd:PRK06466 401 QMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGAL 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807110 464 GFVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFS-TDGPVLVDVVVAKEELAIPPQIK 539
Cdd:PRK06466 481 GMVRqwQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVDRSEHVYPMQIA 559
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
6-542 |
2.80e-57 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 201.60 E-value: 2.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 6 ASYIAKTLEQAGVKRIWGVTGDSLNGLSDSL---NRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLI 82
Cdd:PRK06456 5 ARILVDSLKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 83 NGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPG 161
Cdd:PRK06456 85 TGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRpGPVVIDIPR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 162 DVALKPA-----PESASSHWYHaPQPTVTPAdEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHAL 234
Cdd:PRK06456 165 DIFYEKMeeikwPEKPLVKGYR-DFPTRIDR-LALKKAAEILINAERPIILVGTGVvwSNATPEVLELAELLHIPIVSTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAFYP------TDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK06456 243 PGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSydemveTRKKFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 309 VGDIKSTLKALLPLLEE---KTDRRFLDKALEDYREARKGLDDLAKPseKALHPQYLAQQISRFADDDAIFTCDVGTPTV 385
Cdd:PRK06456 323 YGNAKIILRELIKAITElgqKRDRSAWLKRVKEYKEYYSQFYYTEEN--GKLKPWKIMKTIRQALPRDAIVTTGVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 386 WAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGF 465
Cdd:PRK06456 401 WAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 466 V--AMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELA---IPPQIKL 540
Cdd:PRK06456 481 VrqVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELAlptLPPGGRL 560
|
..
gi 505807110 541 EQ 542
Cdd:PRK06456 561 KQ 562
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
4-535 |
1.62e-56 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 199.93 E-value: 1.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 4 TVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK09107 12 TGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGD 162
Cdd:PRK09107 92 PLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVdIPKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 163 VAL-----KPAPESASSHWYhapQPTVTPADEELHKLAQLIRYSSNIALMCGSGC----AGAHQELVEFAAKIKAPVVHA 233
Cdd:PRK09107 172 VQFatgtyTPPQKAPVHVSY---QPKVKGDAEAITEAVELLANAKRPVIYSGGGVinsgPEASRLLRELVELTGFPITST 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 234 LRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYR------AFYPTdAKIIQIDINPGSIGAHSKVDMA 307
Cdd:PRK09107 249 LMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRitgrldAFSPN-SKKIHIDIDPSSINKNVRVDVP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 308 LVGDIKSTLKALLPLLE---EKTDRRFLDK---ALEDYReARKGLDdlAKPSEKALHPQYLAQQISRFADD-DAIFTCDV 380
Cdd:PRK09107 328 IIGDVGHVLEDMLRLWKargKKPDKEALADwwgQIARWR-ARNSLA--YTPSDDVIMPQYAIQRLYELTKGrDTYITTEV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 381 GTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNN 460
Cdd:PRK09107 405 GQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807110 461 SILGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIP 535
Cdd:PRK09107 485 QYMGMVRqwQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFP 561
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
357-535 |
1.59e-54 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 182.70 E-value: 1.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 357 LHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGF 436
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 437 SMLMGDFLSLAQMKLPVKIVIFNNSILGFVA--MEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTA 514
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRqwQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|.
gi 505807110 515 FSTDGPVLVDVVVAKEELAIP 535
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLP 181
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
379-525 |
5.65e-53 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 177.39 E-value: 5.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 379 DVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIF 458
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807110 459 NNSILGFVAMEMKAGG----YLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDV 525
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGggrySGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
11-527 |
1.82e-52 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 187.73 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 11 KTLEQAGVKRIWGVTG----DSLNGLSDSlnrmgTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLF 86
Cdd:PRK08322 9 KCLENEGVEYIFGIPGeenlDLLEALRDS-----SIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 87 DCHRNHVPVLAIAAHIP--SSEIGSgyFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGDV 163
Cdd:PRK08322 84 YAQLGGMPMVAITGQKPikRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERpGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 164 A-----LKPAPESasshwyhaPQPTVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALRG 236
Cdd:PRK08322 162 AaeetdGKPLPRS--------YSRRPYASPKAIERAAEAIQAAKNPLILIGAGAnrKTASKALTEFVDKTGIPFFTTQMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 237 KEHVEYDNPYDVGMTGL-----IGFssGFHtmmNADTLILLGTQF----PYRAFYPTDAKIIQIDINPGSIGAHSKVDMA 307
Cdd:PRK08322 234 KGVIPETHPLSLGTAGLsqgdyVHC--AIE---HADLIINVGHDViekpPFFMNPNGDKKVIHINFLPAEVDPVYFPQVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 308 LVGDIKSTLKALLPLLEEKTDRRFldKALEDYREA-----RKGLDDLAKPsekaLHPQYLAQQISRFADDDAIFTCDVGT 382
Cdd:PRK08322 309 VVGDIANSLWQLKERLADQPHWDF--PRFLKIREAieahlEEGADDDRFP----MKPQRIVADLRKVMPDDDIVILDNGA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 383 PTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSI 462
Cdd:PRK08322 383 YKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNA 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807110 463 LGFVAMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVV 527
Cdd:PRK08322 463 YGMIRWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPV 527
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
362-527 |
4.58e-47 |
|
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: 162.42 E-value: 4.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 362 LAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMG 441
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 442 DFLSLAQMKLPVKIVIFNNSILGFVAMEMKAGGYLTD-GTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGP 520
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVsGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGGP 161
|
....*..
gi 505807110 521 VLVDVVV 527
Cdd:cd00568 162 ALIEVKT 168
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
1-539 |
2.94e-43 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 162.08 E-value: 2.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTgdSLNGLS--DSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGN 78
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVI--SIHNMPilDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 79 LHLINGLFDCHRNHVPVLAIAAHIPSSEIGS--GYFQETHPQ-ELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVS 155
Cdd:PRK07064 79 GNAAGALVEALTAGTPLLHITGQIETPYLDQdlGYIHEAPDQlTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 156 VVV-LPGDVALKPAPESASSHWYHAPQPTvtPADEELHKLAQLIRYSSNIALMCGSGCAGAHQELVEFAAkIKAPVVHAL 234
Cdd:PRK07064 159 VSVeIPIDIQAAEIELPDDLAPVHVAVPE--PDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVD-LGFGVVTST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTmmNADTLILLGTQF------PYRAFYPTDakIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK07064 236 QGRGVVPEDHPASLGAFNNSAAVEALYK--TCDLLLVVGSRLrgnetlKYSLALPRP--LIRVDADAAADGRGYPNDLFV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 309 VGDIKSTLKALLPLLEE--KTDRRFlDKALEDYREA-----RKGLDDLAKpsekalhpqyLAQQISRFADDDAIFTCDVG 381
Cdd:PRK07064 312 HGDAARVLARLADRLEGrlSVDPAF-AADLRAAREAavadlRKGLGPYAK----------LVDALRAALPRDGNWVRDVT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 382 TP-TVWAARYLQMNGKRRLLGSFNhGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNN 460
Cdd:PRK07064 381 ISnSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMND 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 461 SILGFV-AMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVA-----KEELAI 534
Cdd:PRK07064 460 GGYGVIrNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVDMLsigpfAAAFAG 539
|
....*
gi 505807110 535 PPQIK 539
Cdd:PRK07064 540 PPVKK 544
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-542 |
1.50e-42 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 160.43 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08199 6 RARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVL 159
Cdd:PRK08199 86 ASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRpGPVVLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 160 PGD-------VALKPAPESASSHwyhapqptvtPADEELHKLAQLI-RYSSNIALMCGSG-CAGAHQELVEFAAKIKAPV 230
Cdd:PRK08199 166 PEDvlsetaeVPDAPPYRRVAAA----------PGAADLARLAELLaRAERPLVILGGSGwTEAAVADLRAFAERWGLPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 231 VHALRGKEHVEYDNPYDVGMTGLiGFSSGF-HTMMNADTLILLGTQFP------YRAF---YPtDAKIIQIDINPGSIGA 300
Cdd:PRK08199 236 ACAFRRQDLFDNRHPNYAGDLGL-GINPALaARIREADLVLAVGTRLGevttqgYTLLdipVP-RQTLVHVHPDAEELGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 301 HSKVDMALVGDIKSTLKALLPLLEEKTDRRF--LDKALEDYREARKglddlAKPSEKALHPQYLAQQISRFADDDAIFTC 378
Cdd:PRK08199 314 VYRPDLAIVADPAAFAAALAALEPPASPAWAewTAAAHADYLAWSA-----PLPGPGAVQLGEVMAWLRERLPADAIITN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 379 DVGTPTVWAARYLQMNGKRRLLGSFNhGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIF 458
Cdd:PRK08199 389 GAGNYATWLHRFFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 459 NNSILGFVAM--EMKAGGYlTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEelAIPP 536
Cdd:PRK08199 468 NNGMYGTIRMhqEREYPGR-VSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPE--AITP 544
|
....*.
gi 505807110 537 QIKLEQ 542
Cdd:PRK08199 545 TATLSQ 550
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
62-529 |
5.68e-41 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 156.31 E-value: 5.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 62 QLTGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGS--------GYFQETHPQ-ELFRECSHYCELVS 132
Cdd:PRK08327 71 LVTGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrntriHWTQEMRDQgGLVREYVKWDYEIR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 133 TPEQIPQVLAIAMRKAVIN-RGVSVVVLPGDVALKPAPESASshwYHAPQPTVTPA---DEELHKLAQLIRYSSNIALMC 208
Cdd:PRK08327 151 RGDQIGEVVARAIQIAMSEpKGPVYLTLPREVLAEEVPEVKA---DAGRQMAPAPPapdPEDIARAAEMLAAAERPVIIT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 209 --GSGCAGAHQELVEFAAKIKAPVVHAlRGkEHVEYdnPYDVGMtgLIGFSSGFhTMMNADTLILLGTQFPY---RAFYP 283
Cdd:PRK08327 228 wrAGRTAEGFASLRRLAEELAIPVVEY-AG-EVVNY--PSDHPL--HLGPDPRA-DLAEADLVLVVDSDVPWipkKIRPD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 284 TDAKIIQIDINPgsigAHSK-------VDMALVGDIKSTLKALLPLL--EEKTDRRFLDKALEDYREARKgLDDLAK--- 351
Cdd:PRK08327 301 ADARVIQIDVDP----LKSRiplwgfpCDLCIQADTSTALDQLEERLksLASAERRRARRRRAAVRELRI-RQEAAKrae 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 352 ----PSEKALHPQYLAQQISRFADD-DAIFTcdvGTPTVWaaRYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQ 426
Cdd:PRK08327 376 ierlKDRGPITPAYLSYCLGEVADEyDAIVT---EYPFVP--RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 427 VIAMCGDGGFsmLMGD---FLSLAQ-MKLPVKIVIFNNSILGFVA---MEMKAGGY--------LTDGTElhDTNFARIA 491
Cdd:PRK08327 451 VIATVGDGSF--IFGVpeaAHWVAErYGLPVLVVVFNNGGWLAVKeavLEVYPEGYaarkgtfpGTDFDP--RPDFAKIA 526
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 505807110 492 EACGIKGIRVEKASEVDEALQTAF----STDGPVLVDVVVAK 529
Cdd:PRK08327 527 EAFGGYGERVEDPEELKGALRRALaavrKGRRSAVLDVIVDR 568
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
5-535 |
1.56e-39 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 152.27 E-value: 1.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 5 VASYIAKTLEQAGVKRIWGVtgdSLNGLSDSLNRMGtIEWMPTRHEEVAAFAAGAEAQLTG--ELAVCAGSCGPGNLHLI 82
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGF---PVNELFDAAAAAG-IRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 83 NGLFDCHRNHVPVLAIAAHIPSSEigsgyfQETHPQ----ELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV 158
Cdd:PRK06154 98 GGVAQAYGDSVPVLFLPTGYPRGS------TDVAPNfeslRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 159 -LPGDVALKPAPESASSHwyhAPQPTVTPA--DEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHA 233
Cdd:PRK06154 172 eLPVDVLAEELDELPLDH---RPSRRSRPGadPVEVVEAAALLLAAERPVIYAGQGVlyAQATPELKELAELLEIPVMTT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 234 LRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRAF---YPTDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK06154 249 LNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYglpMPEGKTIIHSTLDDADLNKDYPIDHGLVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 311 DIKSTLKALLPLLEEKTDRRFLDKA-----LEDYREA--RKGLDDLAKpSEKALHPQYLAQQISR-FADDDAIFTCDVGT 382
Cdd:PRK06154 329 DAALVLKQMIEELRRRVGPDRGRAQqvaaeIEAVRAAwlAKWMPKLTS-DSTPINPYRVVWELQHaVDIKTVIITHDAGS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 383 P-----TVWAAR----YLQMnGKRRLLGSfnhgsmanAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPV 453
Cdd:PRK06154 408 PrdqlsPFYVASrpgsYLGW-GKTTQLGY--------GLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 454 KIVIFNNSILGFVAMEMKAggyltdGTELHDTNF-----ARIAEACGIKGIRVEKASEVDEALQTAF--STDG-PVLVDV 525
Cdd:PRK06154 479 LTILLNNFSMGGYDKVMPV------STTKYRATDisgdyAAIARALGGYGERVEDPEMLVPALLRALrkVKEGtPALLEV 552
|
570
....*....|.
gi 505807110 526 VVAKE-ELAIP 535
Cdd:PRK06154 553 ITSEEtALSRP 563
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
9-526 |
3.35e-39 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 150.64 E-value: 3.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK05858 11 AARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVI-NRGVSVVVLPGDVALKP 167
Cdd:PRK05858 90 QFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTpHRGPVFVDFPMDHAFSM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 168 APESASSHWYHAPQPTVTPADEELHKLAQLIRYSSNIALMCGSGCAGAHQE--LVEFAAKIKAPVVHALRGKEHVEYDNP 245
Cdd:PRK05858 170 ADDDGRPGALTELPAGPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEaaLLRLAEELGIPVLMNGMGRGVVPADHP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 246 ydvgmtglIGFSSGFHTMM-NADTLILLGTQFPYR---AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKALLP 321
Cdd:PRK05858 250 --------LAFSRARGKALgEADVVLVVGVPMDFRlgfGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILSALAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 322 LLEEKTDRRFLDKALEDYREARKGLDDLAKPSEKA-LHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLL 400
Cdd:PRK05858 322 AGGDRTDHQGWIEELRTAETAARARDAAELADDRDpIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 401 GSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDG--GFSMLmgDFLSLAQMKLPVKIVIFNNSILGFVAMEMKA-GGYLT 477
Cdd:PRK05858 402 DPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGafGFSLM--DVDTLVRHNLPVVSVIGNNGIWGLEKHPMEAlYGYDV 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 505807110 478 DGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVV 526
Cdd:PRK05858 480 AADLRPGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVL 528
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-530 |
7.66e-39 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 150.52 E-value: 7.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLT-GELAVCAGSCGPGNL 79
Cdd:PRK11269 2 AKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV- 158
Cdd:PRK11269 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLId 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 159 LPGDVALKPA---PESASSHWYHAPQPTVTPADEELHKLAQlirySSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHA 233
Cdd:PRK11269 162 LPFDVQVAEIefdPDTYEPLPVYKPAATRAQIEKALEMLNA----AERPLIVAGGGVinADASDLLVEFAELTGVPVIPT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 234 LRGKEHVEYDNPYDVGMTGL-IGFSSGFHTMMNADTLILLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMA 307
Cdd:PRK11269 238 LMGWGAIPDDHPLMAGMVGLqTSHRYGNATLLASDFVLGIGNRWANRhtgsvEVYTKGRKFVHVDIEPTQIGRVFGPDLG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 308 LVGDIKSTLKALLPLLEE-KTDRRFLDKA--LEDYREARKGLDDLAKPSEKALHPQYLAQQISRFADDDAIFTCDVGTPT 384
Cdd:PRK11269 318 IVSDAKAALELLVEVAREwKAAGRLPDRSawVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 385 VWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILG 464
Cdd:PRK11269 398 IAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 465 FV-----AMEM--------------KAGGYLTDgtelhdtnFARIAEACGIKGIRVEKASEVDEALQTA------FSTdg 519
Cdd:PRK11269 478 LIrqaqrAFDMdycvqlafeninspELNGYGVD--------HVKVAEGLGCKAIRVFKPEDIAPALEQAkalmaeFRV-- 547
|
570
....*....|.
gi 505807110 520 PVLVDVVVAKE 530
Cdd:PRK11269 548 PVVVEVILERV 558
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
191-319 |
1.96e-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: 137.70 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 191 LHKLAQLIRYSSNIALMCGSGC--AGAHQELVEFAAKIKAPVVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADT 268
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVrrSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 505807110 269 LILLGTQF-------PYRAFYPtDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLKAL 319
Cdd:pfam00205 81 VLAVGARFddirttgKLPEFAP-DAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
4-529 |
9.46e-38 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 146.66 E-value: 9.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 4 TVASYIAKTLEQAGVKRIWGVTG----DSLNGLSDSLNRMGTiewmpTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK07524 3 TCGEALVRLLEAYGVETVFGIPGvhtvELYRGLAGSGIRHVT-----PRHEQGAGFMADGYARVSGKPGVCFIITGPGMT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 80 HLINGLFDCHRNHVPVLAIAA--HIPSSEIGSGYFQETHPQE-LFRECSHYCELVSTPEQIPQVLAIAMrkAVIN--RGV 154
Cdd:PRK07524 78 NIATAMGQAYADSIPMLVISSvnRRASLGKGRGKLHELPDQRaMVAGVAAFSHTLMSAEDLPEVLARAF--AVFDsaRPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 155 SV-VVLPGDVALKPAPESASSHWYHAPQPTvtPADEELHKLAQLIRYSSNIALMCGSGCAGAHQELVEFAAKIKAPVVHA 233
Cdd:PRK07524 156 PVhIEIPLDVLAAPADHLLPAPPTRPARPG--PAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVALT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 234 LRGKEHVEYDNPYDVGMTGLIgfSSGFHTMMNADTLILLGTQF-------PYRAFYPTDAKIIQIDINPGSIGAHSKVDM 306
Cdd:PRK07524 234 INAKGLLPAGHPLLLGASQSL--PAVRALIAEADVVLAVGTELgetdydvYFDGGFPLPGELIRIDIDPDQLARNYPPAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 307 ALVGDIKSTLKALLPLLEEKTDRRflDKALEDYREARKGLddlakpsEKALHPQYLAQQ--ISRFAD--DDAIFTCDvGT 382
Cdd:PRK07524 312 ALVGDARAALEALLARLPGQAAAA--DWGAARVAALRQAL-------RAEWDPLTAAQValLDTILAalPDAIFVGD-ST 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 383 PTVWAAR-YLQMNGKRRLL-GSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNN 460
Cdd:PRK07524 382 QPVYAGNlYFDADAPRRWFnASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNN 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505807110 461 SILGFVAMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVVAK 529
Cdd:PRK07524 462 DGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQAC 530
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
5-170 |
1.06e-37 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 136.98 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 5 VASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLING 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 85 LFDCHRNHVPVLAIAAHIPSSEIGSGYFQ-ETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGD 162
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRpGPVYLEIPLD 160
|
....*...
gi 505807110 163 VALKPAPE 170
Cdd:pfam02776 161 VLLEEVDE 168
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-539 |
5.75e-33 |
|
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: 132.59 E-value: 5.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 1 MKQTVASYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHeevaafaagaeaqltgELavCAGSC------ 74
Cdd:COG3961 3 MTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCN----------------EL--NAGYAadgyar 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 75 -----------GPGNLHLINGLFDCHRNHVPVLAIAAhIPSSEI-----------GSGYFqeTHPQELFRECSHYCELVs 132
Cdd:COG3961 65 vnglgalvttyGVGELSAINGIAGAYAERVPVVHIVG-APGTRAqrrgpllhhtlGDGDF--DHFLRMFEEVTVAQAVL- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 133 TPE----QIPQVLAIAMRKaviNRGVsVVVLPGDVALKPAPESASSHWYHAPQPTVTPADEELHKLAQLIRYSSNIALMC 208
Cdd:COG3961 141 TPEnaaaEIDRVLAAALRE---KRPV-YIELPRDVADAPIEPPEAPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 209 GSGCA--GAHQELVEFAAKIKAPVVHALRGKEHVEYDNPYDVGM-TGLIGFSSGFHTMMNADTLILLGTQFpyrafypTD 285
Cdd:COG3961 217 GVEVHrfGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGVVF-------TD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 286 -------AKIIQ---IDINPG--SIGAH--SKVDMAlvgdikSTLKALLPLLEEKTDRRfldkaledyREARKGLDDLAK 351
Cdd:COG3961 290 tntggftAQLDPertIDIQPDsvRVGGHiyPGVSLA------DFLEALAELLKKRSAPL---------PAPAPPPPPPPA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 352 PSEKALHPQYLAQQISRFADDDAIFTCDVGTPtVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMC 431
Cdd:COG3961 355 APDAPLTQDRLWQRLQAFLDPGDIVVADTGTS-LFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 432 GDGGFsMLMGdfLSLAQM---KLPVKIVIFNNsilgfvamemkaGGYLT-------DGT--ELHDTNFARIAEACG---I 496
Cdd:COG3961 434 GDGAF-QLTA--QELSTMlryGLKPIIFVLNN------------DGYTIeraihgpDGPynDIANWDYAKLPEAFGggnA 498
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 505807110 497 KGIRVEKASEVDEALQTAFS-TDGPVLVDVVVAKEElaIPPQIK 539
Cdd:COG3961 499 LGFRVTTEGELEEALAAAEAnTDRLTLIEVVLDKMD--APPLLK 540
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
359-527 |
1.81e-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: 122.78 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 359 PQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSM 438
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 439 LMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFSTD 518
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
....*....
gi 505807110 519 GPVLVDVVV 527
Cdd:cd02010 161 GVHVIDCPV 169
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
359-528 |
4.44e-32 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 121.49 E-value: 4.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 359 PQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSM 438
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 439 LMGDFLSLAQMKLPVKIVIFNNSILGFVAMEM--KAGGYLTDGTELHDTNFARIAEACGIKGIRVEKASEVDEALQTAFS 516
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQqlSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 505807110 517 TDGPVLVDVVVA 528
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
78-528 |
3.43e-30 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 124.30 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 78 NLHLING-------LFDCHRNHVPVLAIAAHIPSSEIGSGYF-QETHPQELFRECSHY-CElVSTPEQIPQVLA----IA 144
Cdd:PRK07092 78 NLHSAAGvgnamgnLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWsIE-PARAEDVPAAIArayhIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 145 MRKAvinRGVSVVVLPGDVALKPAPESASSHWYHApqptVTPADEELHKLAQLIRYSSNIALMCGSGC--AGAHQELVEF 222
Cdd:PRK07092 157 MQPP---RGPVFVSIPYDDWDQPAEPLPARTVSSA----VRPDPAALARLGDALDAARRPALVVGPAVdrAGAWDDAVRL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 223 AAKIKAPVVHAlrgkehveydnPydvgMTGLIGFSS------GFHTMMNA---------DTLILLGT------QFPYRAF 281
Cdd:PRK07092 230 AERHRAPVWVA-----------P----MSGRCSFPEdhplfaGFLPASREkisalldghDLVLVIGApvftyhVEGPGPH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 282 YPTDAKIIQIDINPGsIGAHSKVDMALVGDIKSTLKALLPLLEEkTDRRFLdkaledyrEARKGLDDLAKPSEkALHPQY 361
Cdd:PRK07092 295 LPEGAELVQLTDDPG-EAAWAPMGDAIVGDIRLALRDLLALLPP-SARPAP--------PARPMPPPAPAPGE-PLSVAF 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 362 LAQQISRFADDDAIFTCDV--GTPTVWaaRYLQMNGKrrllGSF---NHGSMANAMPQAIGAKATAPNRQVIAMCGDGGF 436
Cdd:PRK07092 364 VLQTLAALRPADAIVVEEApsTRPAMQ--EHLPMRRQ----GSFytmASGGLGYGLPAAVGVALAQPGRRVIGLIGDGSA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 437 SMLMGDFLSLAQMKLPVKIVIFNNSilGFVAME-----MKAGGylTDGTELHDTNFARIAEACGIKGIRVEKASEVDEAL 511
Cdd:PRK07092 438 MYSIQALWSAAQLKLPVTFVILNNG--RYGALRwfapvFGVRD--VPGLDLPGLDFVALARGYGCEAVRVSDAAELADAL 513
|
490
....*....|....*..
gi 505807110 512 QTAFSTDGPVLVDVVVA 528
Cdd:PRK07092 514 ARALAADGPVLVEVEVA 530
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
357-533 |
2.48e-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: 111.83 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 357 LHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGF 436
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 437 SMLMGDFLSLAQMKLPVKIVIFNNSILGfvaMEMKaggYLTD-------GTELHDTNFARIAEACGIKGIRVEKASEVDE 509
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWG---AEKK---NQVDfynnrfvGTELESESFAKIAEACGAKGITVDKPEDVGP 157
|
170 180
....*....|....*....|....*..
gi 505807110 510 ALQTAFSTDG---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 |
8.37e-26 |
|
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: 103.38 E-value: 8.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 8 YIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIEWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFD 87
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPLLDALARSG-IRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807110 88 CHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLP 160
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRpGPVALDLP 154
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
357-527 |
2.93e-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: 102.67 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 357 LHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSfNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGF 436
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTL-RGGGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 437 SMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKAGGYLTDGTE------LHD--TNFARIAEACGIKGIRVEKASEVD 508
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENapdgldLLDpgIDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*....
gi 505807110 509 EALQTAFSTDGPVLVDVVV 527
Cdd:cd02002 160 EALREALAEGGPALIEVVV 178
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
6-528 |
5.10e-19 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 90.43 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 6 ASYIAKTLEQAGVKRIWGVTGDSLNGLSdslnRMGTIEWMPT---RHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLI 82
Cdd:PRK09259 13 FHLVIDALKLNGIDTIYGVVGIPITDLA----RLAQAEGIRYigfRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 83 NGLFDCHRNHVPVLAIAAhipSSE-----IGSGYFQET--------HPQELFRecshycelVSTPEQIPQVLAIAMRKAV 149
Cdd:PRK09259 89 TALANATTNCFPMIMISG---SSEreivdLQQGDYEELdqlnaakpFCKAAFR--------VNRAEDIGIGVARAIRTAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 150 INR-GVSVVVLPGDV--ALKPAPESASSHWYHA-PQPTVTPADEELHKLAQLIRYSSN--IALMCGSGCAGAHQELVEFA 223
Cdd:PRK09259 158 SGRpGGVYLDLPAKVlaQTMDADEALTSLVKVVdPAPAQLPAPEAVDRALDLLKKAKRplIILGKGAAYAQADEQIREFV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 224 AKIKAPVVHALRGKEHVEYDNPYDVGmtgligfSSGFHTMMNADTLILLGTQFPYRAFY---PT---DAKIIQIDINPGS 297
Cdd:PRK09259 238 EKTGIPFLPMSMAKGLLPDTHPQSAA-------AARSLALANADVVLLVGARLNWLLSHgkgKTwgaDKKFIQIDIEPQE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 298 IGAHSKVDMALVGDIKSTLKALLPLLEE---KTDRRFLDkALEDYREarKGLDDLAKPSEKALHPQYLAQQISRFAD--- 371
Cdd:PRK09259 311 IDSNRPIAAPVVGDIGSVMQALLAGLKQntfKAPAEWLD-ALAERKE--KNAAKMAEKLSTDTQPMNFYNALGAIRDvlk 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 372 --DDAIFTCDvGTPTVWAAR-YLQMNGKRRLLGSFNHGSMANAMPQAIGAkATAPNRQVIAMCGDGGFSMLMGDFLSLAQ 448
Cdd:PRK09259 388 enPDIYLVNE-GANTLDLARnIIDMYKPRHRLDCGTWGVMGIGMGYAIAA-AVETGKPVVAIEGDSAFGFSGMEVETICR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 449 MKLPVKIVIFNNSilgfvamemkaGGYLTDGTEL------------HDTNFARIAEACGIKGIRVEKASEVDEALQTAFS 516
Cdd:PRK09259 466 YNLPVTVVIFNNG-----------GIYRGDDVNLsgagdpsptvlvHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIA 534
|
570
....*....|..
gi 505807110 517 TDGPVLVDVVVA 528
Cdd:PRK09259 535 SGKPTLINVVID 546
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
62-527 |
2.77e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 88.01 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 62 QLTGELAVCAGSCGPGnlhLINGLFDCH---RNHVPVLAI-----AAHIP-----SSEIGSgyfqethpqeLFRECSHYC 128
Cdd:PRK12474 64 RIAGKPAVTLLHLGPG---LANGLANLHnarRAASPIVNIvgdhaVEHLQydaplTSDIDG----------FARPVSRWV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 129 ELVSTPEQIPQVLAIAMRKA-VINRGVSVVVLPGDVALKPAPESASSHWYHAPQPTvtpADEELHKLAQLIRYSSNIALM 207
Cdd:PRK12474 131 HRSASAGAVDSDVARAVQAAqSAPGGIATLIMPADVAWNEAAYAAQPLRGIGPAPV---AAETVERIAALLRNGKKSALL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 208 C-GSGCAGAHQEL---------VEFAAKIKAPVVHALRGKEHVEydnpyDVGMTGLIGfssgfhTMM--NADTLILLGTQ 275
Cdd:PRK12474 208 LrGSALRGAPLEAagriqaktgVRLYCDTFAPRIERGAGRVPIE-----RIPYFHEQI------TAFlkDVEQLVLVGAK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 276 FPYRAF-YPTdakiiqidiNPGSIGAHSKVDMALVGDIKSTLKALLPLLEEktdrrfLDKALEDYREARKGLDDLAKpse 354
Cdd:PRK12474 277 PPVSFFaYPG---------KPSWGAPPGCEIVYLAQPDEDLAQALQDLADA------VDAPAEPAARTPLALPALPK--- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 355 KALHPQYLAQQISRFADDDAIFTCDVGTPTVW------AAR---YLQMNGkrrllgsfnhGSMANAMPQAIGAKATAPNR 425
Cdd:PRK12474 339 GALNSLGVAQLIAHRTPDQAIYADEALTSGLFfdmsydRARphtHLPLTG----------GSIGQGLPLAAGAAVAAPDR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 426 QVIAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKAGGYLTDGT------ELH--DTNFARIAEACGIK 497
Cdd:PRK12474 409 KVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGELQRVGAQGAGRnalsmlDLHnpELNWMKIAEGLGVE 488
|
490 500 510
....*....|....*....|....*....|
gi 505807110 498 GIRVEKASEVDEALQTAFSTDGPVLVDVVV 527
Cdd:PRK12474 489 ASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
74-527 |
3.48e-18 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 87.59 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 74 CGPGnlhLINGLFDCH---RNHVPVLAI-----AAHIP-----SSEIGSgyfqethpqeLFRECSHYCELVSTPEQIPQV 140
Cdd:PRK07586 72 LGPG---LANGLANLHnarRARTPIVNIvgdhaTYHRKydaplTSDIEA----------LARPVSGWVRRSESAADVAAD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 141 LAIAMRKA-VINRGVSVVVLPGDVALKPAPESASshwyHAPQPTVTPADEE-LHKLAQLIRYSSNIALMCGSGCAGAHQe 218
Cdd:PRK07586 139 AAAAVAAArGAPGQVATLILPADVAWSEGGPPAP----PPPAPAPAAVDPAaVEAAAAALRSGEPTVLLLGGRALRERG- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 219 lVEFAAKIKA-----------PVVHAlRGKEHVEYDN-PY--DVGMTGLIGFssgfhtmmnaDTLILLGTQFPYRAF-YP 283
Cdd:PRK07586 214 -LAAAARIAAatgarllaetfPARME-RGAGRPAVERlPYfaEQALAQLAGV----------RHLVLVGAKAPVAFFaYP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 284 tdakiiqidinpgsigahskvdmalvgDIKSTLK----ALLPLLEEKTDRRFLDKALEDYREARKGLDDLAKPSEK---- 355
Cdd:PRK07586 282 ---------------------------GKPSRLVpegcEVHTLAGPGEDAAAALEALADALGAKPAAPPLAAPARPplpt 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 356 -ALHPQYLAQQISRFADDDAIF-----TCDVG--TPTVWAAR--YLQMNGkrrllgsfnhGSMANAMPQAIGAKATAPNR 425
Cdd:PRK07586 335 gALTPEAIAQVIAALLPENAIVvdesiTSGRGffPATAGAAPhdWLTLTG----------GAIGQGLPLATGAAVACPDR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 426 QVIAMCGDGGFsMLMGDFL-SLAQMKLPVKIVIFNNSILGFVAMEMKAGGYLTDG------TELHD--TNFARIAEACGI 496
Cdd:PRK07586 405 KVLALQGDGSA-MYTIQALwTQARENLDVTTVIFANRAYAILRGELARVGAGNPGpraldmLDLDDpdLDWVALAEGMGV 483
|
490 500 510
....*....|....*....|....*....|.
gi 505807110 497 KGIRVEKASEVDEALQTAFSTDGPVLVDVVV 527
Cdd:PRK07586 484 PARRVTTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
361-539 |
4.86e-18 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 82.20 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 361 YLAQQISRFADDDAIFTCDVGTPTvWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLM 440
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSW-FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 441 GDFLSLAQMKLPVKIVIFNNSilgfvamemkagGYLTDgTELHDT----------NFARIAEACG----IKGIRVEKASE 506
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINND------------GYTIE-RAIHGPeasyndianwNYTKLPEVFGggggGLSFRVKTEGE 151
|
170 180 190
....*....|....*....|....*....|....
gi 505807110 507 VDEALQTA-FSTDGPVLVDVVVAKEElaIPPQIK 539
Cdd:cd02005 152 LDEALKDAlFNRDKLSLIEVILPKDD--APEALK 183
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
357-529 |
1.32e-13 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 70.00 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 357 LHPQYLAQQISRFADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPNRQVIAMCGDGGF 436
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 437 SMLMGDFLSLAQMKLPVKIVIFNNSILGFVAMEMKA-------------------GGYLTDgtelhdtnFARIAEACGIK 497
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAfdmdyqvnlafeninsselGGYGVD--------HVKVAEGLGCK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 505807110 498 GIRVEKASEVDEALQTAFSTDG----PVLVDVVVAK 529
Cdd:cd02006 160 AIRVTKPEELAAAFEQAKKLMAehrvPVVVEAILER 195
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
350-536 |
4.38e-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: 70.85 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 350 AKPSEKALHP------QYLAQQISRFADDDAIftcdVGTpTVWAARYLQMNGKRRLLGSFNH----GSMANAMPQAIGAK 419
Cdd:TIGR03297 160 LKGGPANPYAtlmtreEAIAAILDHLPDNTVI----VST-TGKTSRELYELRDRIGQGHARDfltvGSMGHASQIALGLA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 420 ATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLPVKI-VIFNNSILGFVamemkaGGYLTDGTelhDTNFARIAEACGI-K 497
Cdd:TIGR03297 235 LARPDQRVVCLDGDGAALMHMGGLATIGTQGPANLIhVLFNNGAHDSV------GGQPTVSQ---HLDFAQIAKACGYaK 305
|
170 180 190
....*....|....*....|....*....|....*....
gi 505807110 498 GIRVEKASEVDEALQTAFSTDGPVLVDVVVAKEELAIPP 536
Cdd:TIGR03297 306 VYEVSTLEELETALTAASSANGPRLIEVKVRPGSRADLG 344
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
366-525 |
8.45e-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: 67.33 E-value: 8.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 366 ISRFADDDAIFTCDVGTPtvwaARYLQMNGKRRLLGSFN----HGSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMG 441
Cdd:cd02003 8 LNEAIGDDDVVINAAGSL----PGDLHKLWRARTPGGYHleygYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 442 DFLSLAQMKLPVKIVIFNNSilGF-----VAMEMKAGGYltdGTELHD--------------TNFARIAEACGIKGIRVE 502
Cdd:cd02003 84 EIVTAVQEGLKIIIVLFDNH--GFgcinnLQESTGSGSF---GTEFRDrdqesgqldgallpVDFAANARSLGARVEKVK 158
|
170 180
....*....|....*....|...
gi 505807110 503 KASEVDEALQTAFSTDGPVLVDV 525
Cdd:cd02003 159 TIEELKAALAKAKASDRTTVIVI 181
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
362-533 |
3.35e-12 |
|
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: 65.41 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 362 LAQQISRFADDDAIftcdVGTpTVWAARYLQMNGKRRLLGSFNH----GSMANAMPQAIGAKATAPNRQVIAMCGDGGFS 437
Cdd:cd03371 5 IEIVLSRAPATAAV----VST-TGMTSRELFELRDRPGGGHAQDfltvGSMGHASQIALGIALARPDRKVVCIDGDGAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 438 MLMGDFLSLAQMKLP-VKIVIFNNSilgfvAMEMkAGGYLTDGTelhDTNFARIAEACGIKGIRVEKAS-EVDEALQTAF 515
Cdd:cd03371 80 MHMGGLATIGGLAPAnLIHIVLNNG-----AHDS-VGGQPTVSF---DVSLPAIAKACGYRAVYEVPSLeELVAALAKAL 150
|
170
....*....|....*...
gi 505807110 516 STDGPVLVDVVVAKEELA 533
Cdd:cd03371 151 AADGPAFIEVKVRPGSRS 168
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
8-161 |
4.81e-11 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 61.21 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 8 YIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHEEVAAFAAGAEAQLTGeLAVCAGSCGPGNLHLINGLFD 87
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807110 88 CHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPG 161
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
366-527 |
1.58e-08 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 54.60 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 366 ISRFADD--DAIFTCDVGTPT--VWAARylqmngkRRLLGSFNHGSMANAMPQAIGAkATAPNRQVIAMCGDGGFSMLMG 441
Cdd:cd03372 5 IKTLIADlkDELVVSNIGFPSkeLYAAG-------DRPLNFYMLGSMGLASSIGLGL-ALAQPRKVIVIDGDGSLLMNLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 442 DFLSLAQMKLP-VKIVIFNNSILGFVAMEMKAGGYLTDgtelhdtnFARIAEACGIKgiRVEKASEVDEALQT-AFSTDG 519
Cdd:cd03372 77 ALATIAAEKPKnLIIVVLDNGAYGSTGNQPTHAGKKTD--------LEAVAKACGLD--NVATVASEEAFEKAvEQALDG 146
|
....*...
gi 505807110 520 PVLVDVVV 527
Cdd:cd03372 147 PSFIHVKI 154
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
406-523 |
4.10e-06 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 47.10 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 406 GSMANAMPQAIGAKATAPnRQVIAMCGDGGFSMLMGDFLSLAQMK-LPVKIVIFNNSILGfvamemKAGGYLTDGTelhD 484
Cdd:cd02001 42 GSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNRAYG------STGGQPTPSS---N 111
|
90 100 110
....*....|....*....|....*....|....*....
gi 505807110 485 TNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLV 523
Cdd:cd02001 112 VNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLL 150
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
406-525 |
1.13e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 46.36 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 406 GSMANAMPQAIGAKATAPNRQVIAMCGDGGFSMLMGDFLSLAQMKLP-VKIVIFNNSILGFvamemkAGGYLTDGTELHD 484
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKnLTIIVMDNGVYQI------TGGQPTLTSQTVD 130
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 505807110 485 tnFARIAEACGIKGIRVEKASEVDEAL-QTAFSTDGPVLVDV 525
Cdd:PRK06163 131 --VVAIARGAGLENSHWAADEAHFEALvDQALSGPGPSFIAV 170
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
415-527 |
7.66e-05 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 43.74 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 415 AIGAkATAPNRQVIAMCGDggFSML--MGDFLSLAQMKLPVKIVIFNNS---IlgFvamEMKAGGYLTDGTE-----LHD 484
Cdd:cd02009 60 ALGI-ALATDKPTVLLTGD--LSFLhdLNGLLLGKQEPLNLTIVVINNNgggI--F---SLLPQASFEDEFErlfgtPQG 131
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 505807110 485 TNFARIAEACGIKGIRVEKASEVDEALQTAFSTDGPVLVDVVV 527
Cdd:cd02009 132 LDFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKT 174
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
407-531 |
1.48e-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: 42.65 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 407 SMANAMPQAIGAKATAPNRQVIAMCGDGGFsMLMGdFLSLAQM---KLPVKIVIFNNSIlgfVAM----EMKAGGY-LTD 478
Cdd:cd02008 52 CMGASIGVAIGMAKASEDKKVVAVIGDSTF-FHSG-ILGLINAvynKANITVVILDNRT---TAMtggqPHPGTGKtLTE 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 505807110 479 GTELHDtnFARIAEACGIKGIRV---EKASEVDEALQTAFSTDGPvlvDVVVAKEE 531
Cdd:cd02008 127 PTTVID--IEALVRAIGVKRVVVvdpYDLKAIREELKEALAVPGV---SVIIAKRP 177
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
405-526 |
3.70e-04 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 41.74 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 405 HGsmaNAMPQAIGAKATAPNRQVIAMCGDG-GFSMLMGDFLSLAQMKLPVKIVIFNNSILGfvameMKAG--------GY 475
Cdd:cd03375 53 HG---RALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQIYG-----LTKGqaspttpeGF 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 476 LT----DGTELHDTNFARIAEACGikGIRVEKASEVD-----EALQTAFSTDGPVLVDVV 526
Cdd:cd03375 125 KTkttpYGNIEEPFNPLALALAAG--ATFVARGFSGDikqlkEIIKKAIQHKGFSFVEVL 182
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
412-527 |
4.16e-04 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 42.48 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 412 MPQAIGA----KATAPNRQVIAMCGDGGFSMlmGDF---LSLAQ-MKLPVKIVIFNNSIlgfvAMemkaggyltdGTELH 483
Cdd:cd02000 110 VPLAAGAalalKYRGEDRVAVCFFGDGATNE--GDFheaLNFAAlWKLPVIFVCENNGY----AI----------STPTS 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 505807110 484 D----TNFARIAEACGIKGIRVE--KASEVDEALQTAF----STDGPVLVDVVV 527
Cdd:cd02000 174 RqtagTSIADRAAAYGIPGIRVDgnDVLAVYEAAKEAVerarAGGGPTLIEAVT 227
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
405-464 |
2.35e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 40.21 E-value: 2.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807110 405 HGsmaNAMPQAIGAKATAPNRQVIAMCGDG-GFSMLMGDFLSLAQMKLPVKIVIFNNSILG 464
Cdd:PRK11867 71 HG---RALAIATGLKLANPDLTVIVVTGDGdALAIGGNHFIHALRRNIDITYILFNNQIYG 128
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
402-464 |
2.39e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 40.25 E-value: 2.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807110 402 SFN--HGSManaMPQAIGAKATAPNRQVIAMCGDG-GFSMLMGDFLSLAQMKLPVKIVIFNNSILG 464
Cdd:PRK05778 67 GLHtlHGRA---IAFATGAKLANPDLEVIVVGGDGdLASIGGGHFIHAGRRNIDITVIVENNGIYG 129
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
405-526 |
3.82e-03 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440637 [Multi-domain] Cd Length: 262 Bit Score: 39.36 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 405 HGSMANAMPQAIGAKATAPNRQVIAMCGDGG-FSMLMGDFLSLAQMKLPVKIVIFNNSI-------------LGFVAmem 470
Cdd:COG1013 63 HTLHGRAAAVATGIKLANPDLTVIVFGGDGDtYDIGGNHLIHAARRNEDITYIVYDNEIygntggqrspttpLGAKT--- 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807110 471 KAGGYltdGTELHDTNFARIAEACGIKgiRVEKASEVD-----EALQTAFSTDGPVLVDVV 526
Cdd:COG1013 140 TTTPY---GKPEPPKDPAEIAAAHGAT--YVARASVGDpkdlkKKIKKAIEHKGFSFIEVL 195
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
8-147 |
4.47e-03 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 38.24 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 8 YIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMPTRHeevaafaagaeaqltgEL---------------AVCAG 72
Cdd:cd07038 2 YLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCN----------------ELnagyaadgyarvkglGALVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807110 73 SCGPGNLHLINGLFDCHRNHVPVLAIAAhIPSSE-----------IGSGYFQetHPQELFRECSHYCELVST----PEQI 137
Cdd:cd07038 66 TYGVGELSALNGIAGAYAEHVPVVHIVG-APSTKaqasglllhhtLGDGDFD--VFLKMFEEITCAAARLTDpenaAEEI 142
|
170
....*....|
gi 505807110 138 PQVLAIAMRK 147
Cdd:cd07038 143 DRVLRTALRE 152
|
|
| |
