|
Name |
Accession |
Description |
Interval |
E-value |
| Gcl |
COG3960 |
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism]; |
2-594 |
0e+00 |
|
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443160 [Multi-domain] Cd Length: 588 Bit Score: 1293.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 2 ARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAVAGNIGVCIGTSGPAGT 81
Cdd:COG3960 1 ARMRAVDAAVAVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHVLARHVEGASHMAEGYTRAKAGNIGVCIGTSGPAGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLID 161
Cdd:COG3960 81 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVLEPAQVPRVFQQAFHLMRSGRPGPVLID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 162 LPIDVQLAEIEFDIETYEPLPAYKPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGW 241
Cdd:COG3960 161 LPIDVQMAEIEFDIDTYEPLPVYKPAATRAQIEKALDMLNAAERPLIVAGGGIINADASDLLVEFAELTGVPVIPTLMGW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 242 GSIPDDHPLMAGMCGLQTSHRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSD 321
Cdd:COG3960 241 GSIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRWANRHTGSLDVYTKGRKFVHVDIEPTQIGRVFAPDLGIVSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 322 AGAALKLFVEVAREWKAAGRLKDRSGWVAECQGRKNSVeyLRKTQFDDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQIA 401
Cdd:COG3960 321 AKAALELFVEVARERKAAGKLPDRSAWAAECQERKRTM--LRKTHFDNVPIKPQRVYEEMNKAFGRDTRYVSTIGLSQIA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 402 GAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLI 481
Cdd:COG3960 399 AAQFLHVYKPRHWINCGQAGPLGWTIPAALGVVAADPDRPVVALSGDYDFQFMIEELAVGAQFKLPYIHVVVNNSYLGLI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 482 RQAQRAFSIDYCVQLAFDNINMDEgeaSRGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAWMAEHRTPVVIECILE 561
Cdd:COG3960 479 RQAQRGFDMDYCVQLAFENINAPE---LGGYGVDHVKVAEGLGCKAIRVTDPEEIAPAFEEAKALMAEHRVPVVVEVILE 555
|
570 580 590
....*....|....*....|....*....|...
gi 317118330 562 RVTNISMGTEIDNVIEFEELAHSKADVPSALAL 594
Cdd:COG3960 556 RVTNISMGTEIDNVNEFEELAESPADAPTAIAL 588
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-596 |
0e+00 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 1280.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAVAGNIGVCIGTSGPAG 80
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIGVCIGTSGPAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLI 160
Cdd:PRK11269 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 161 DLPIDVQLAEIEFDIETYEPLPAYKPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMG 240
Cdd:PRK11269 161 DLPFDVQVAEIEFDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 241 WGSIPDDHPLMAGMCGLQTSHRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVS 320
Cdd:PRK11269 241 WGAIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 321 DAGAALKLFVEVAREWKAAGRLKDRSGWVAECQGRKNSVeyLRKTQFDDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQI 400
Cdd:PRK11269 321 DAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTL--LRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 401 AGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGL 480
Cdd:PRK11269 399 AAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 481 IRQAQRAFSIDYCVQLAFDNINMDEGEasrGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAWMAEHRTPVVIECIL 560
Cdd:PRK11269 479 IRQAQRAFDMDYCVQLAFENINSPELN---GYGVDHVKVAEGLGCKAIRVFKPEDIAPALEQAKALMAEFRVPVVVEVIL 555
|
570 580 590
....*....|....*....|....*....|....*.
gi 317118330 561 ERVTNISMGTEIDNVIEFEELAHSKADVPSALALLD 596
Cdd:PRK11269 556 ERVTNISMGTEIDAVNEFEELADNAADAPTAIMLLD 591
|
|
| glyox_carbo_lig |
TIGR01504 |
glyoxylate carboligase; Glyoxylate carboligase, also called tartronate-semialdehyde synthase, ... |
2-592 |
0e+00 |
|
glyoxylate carboligase; Glyoxylate carboligase, also called tartronate-semialdehyde synthase, releases CO2 while synthesizing a single molecule of tartronate semialdehyde from two molecules of glyoxylate. It is a thiamine pyrophosphate-dependent enzyme, closely related in sequence to the large subunit of acetolactate synthase. In the D-glycerate pathway, part of allantoin degradation in the Enterobacteriaceae, tartronate semialdehyde is converted to D-glycerate and then 3-phosphoglycerate, a product of glycolysis and entry point in the general metabolism.
Pssm-ID: 213633 [Multi-domain] Cd Length: 588 Bit Score: 1081.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 2 ARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAVAGNIGVCIGTSGPAGT 81
Cdd:TIGR01504 1 ARMRAVDAAVYVLEKEGITTAFGVPGAAINPFYSALKAHGGIRHILARHVEGASHMAEGYTRATAGNIGVCIGTSGPAGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLID 161
Cdd:TIGR01504 81 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 162 LPIDVQLAEIEFDIETYEPLPAYKPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGW 241
Cdd:TIGR01504 161 LPFDVQVAEIEFDPDTYEPLPVYKPAATRAQIEKAVEMLNAAERPLIVAGGGVINADAADLLQEFAELTGVPVIPTLMGW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 242 GSIPDDHPLMAGMCGLQTSHRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSD 321
Cdd:TIGR01504 241 GCIPDDHELMAGMVGLQTSHRYGNATLLESDFVFGIGNRWANRHTGSVDVYTEGRKFVHVDIEPTQIGRVFAPDLGIVSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 322 AGAALKLFVEVAREWKAAGRLKDRSGWVAECQGRKNSVeyLRKTQFDDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQIA 401
Cdd:TIGR01504 321 AKAALKLLVEVAQELKKAGRLPDRSEWAADCQQRKRTL--LRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 402 GAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLI 481
Cdd:TIGR01504 399 GAQMLHVYKPRHWINCGQAGPLGWTIPAALGVCAADPKRNVVALSGDYDFQFMIEELAVGAQHNIPYIHVLVNNAYLGLI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 482 RQAQRAFSIDYCVQLAFDNINMDEgeaSRGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAWMAEHRTPVVIECILE 561
Cdd:TIGR01504 479 RQAQRAFDMDYCVQLAFENINSSE---VNGYGVDHVKVAEGLGCKAIRVFKPEEIAPAFEQAKALMAEHRVPVVVEVILE 555
|
570 580 590
....*....|....*....|....*....|.
gi 317118330 562 RVTNISMGTEIDNVIEFEELAHSKADVPSAL 592
Cdd:TIGR01504 556 RVTNISMGSEIDNVVEFEDLADNAADAPTAT 586
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
2-570 |
5.65e-176 |
|
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: 509.70 E-value: 5.65e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 2 ARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGT 81
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARA-TGKPGVCLVTSGPGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLID 161
Cdd:COG0028 80 NLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 162 LPIDVQLAEIEFDiETYEPLPAYKP--AATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLM 239
Cdd:COG0028 160 IPKDVQAAEAEEE-PAPPELRGYRPrpAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 240 GWGSIPDDHPLMAGMCGLQtSHRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIV 319
Cdd:COG0028 239 GKGAFPEDHPLYLGMLGMH-GTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 320 SDAGAALKLFVEVAREwkaagRLKDRSGWVAECQGRKNsvEYLRKTQFDDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQ 399
Cdd:COG0028 318 GDAKAVLAALLEALEP-----RADDRAAWLARIAAWRA--EYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 400 IAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLG 479
Cdd:COG0028 391 MWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 480 LIRQAQRAFSIDYCVQLAFDNInmdegeasrgygvDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAwmaeHRTPVVIECI 559
Cdd:COG0028 471 MVRQWQELFYGGRYSGTDLPNP-------------DFAKLAEAFGAKGERVETPEELEAALEEALA----SDGPALIDVR 533
|
570
....*....|.
gi 317118330 560 LERVTNISMGT 570
Cdd:COG0028 534 VDPEENPPGAT 544
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
4-557 |
1.03e-150 |
|
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: 445.32 E-value: 1.03e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 4 MKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDM 83
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARA-SGKVGVVLVTSGPGATNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLP 163
Cdd:TIGR00118 80 VTGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 164 IDVQLAEIEFDIETYEPLPAYKPAATRN--QAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGW 241
Cdd:TIGR00118 160 KDVTTAEIEYPYPEKVNLPGYRPTVKGHplQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 242 GSIPDDHPLMAGMCGLQTShRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSD 321
Cdd:TIGR00118 240 GSFPEDHPLSLGMLGMHGT-KTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 322 AGAALKLFVEVAREWKAagrlKDRSGWVAECQGRKNsvEYLRKTQFDDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQIA 401
Cdd:TIGR00118 319 ARNVLEELLKKLFELKE----RKESAWLEQINKWKK--EYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 402 GAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLI 481
Cdd:TIGR00118 393 AAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317118330 482 RQAQRAFsidYcvqlafdninmdEGEASRGY---GVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeawmAEHRTPVVIE 557
Cdd:TIGR00118 473 RQWQELF---Y------------EERYSHTHmgsLPDFVKLAEAYGIKGIRIEKPEELDEKLKEA----LSSNEPVLLD 532
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
365-569 |
1.74e-135 |
|
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: 393.18 E-value: 1.74e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 365 TQFDDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVA 444
Cdd:cd02006 1 THFDDVPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 445 LSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQRAFSIDYCVQLAFDNINMDEgeaSRGYGVDHVKVVEGLG 524
Cdd:cd02006 81 LSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAFDMDYQVNLAFENINSSE---LGGYGVDHVKVAEGLG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 317118330 525 CKAIRVHHPEDFAPAMRQAEAWMAEHRTPVVIECILERVTNISMG 569
Cdd:cd02006 158 CKAIRVTKPEELAAAFEQAKKLMAEHRVPVVVEAILERVTNISMG 202
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-580 |
1.18e-132 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 399.15 E-value: 1.18e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMkAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAG 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDEL-YDSDLRHILVRHEQAAAHAADGYARA-TGKVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLI 160
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 161 DLPIDVQLAEIEFDIETYEPLPAYKP--AATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTL 238
Cdd:PRK06048 163 DLPKDVTTAEIDFDYPDKVELRGYKPtyKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 239 MGWGSIPDDHPLMAGMCGLQTShRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGI 318
Cdd:PRK06048 243 MGIGAIPTEHPLSLGMLGMHGT-KYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 319 VSDAGAALKLFVEVAREwkaagrlKDRSGWVAECQGRKNsvEY-LRKTQFDDVpMKPQRVYQCMNrNLDKDTCYVSTIGL 397
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQY-------CDRKEWLDKINQWKK--EYpLKYKEREDV-IKPQYVIEQIY-ELCPDAIIVTEVGQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 398 SQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSY 477
Cdd:PRK06048 391 HQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGY 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 478 LGLIRQAQRAFsidYCVQLAFDNInmdegeasrGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeawmAEHRTPVVIE 557
Cdd:PRK06048 471 LGMVRQWQELF---YDKRYSHTCI---------KGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEA----VASDRPVVID 534
|
570 580
....*....|....*....|....*..
gi 317118330 558 CILERVTNIS----MGTEIDNVIEFEE 580
Cdd:PRK06048 535 FIVECEENVSpmvpAGAAINEILDLEE 561
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
4-576 |
1.96e-124 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 379.10 E-value: 1.96e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 4 MKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKaHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDM 83
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALY-DSDLIHILTRHEQAAAHAADGYARA-SGKVGVCVATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLP 163
Cdd:PRK06276 79 VTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 164 IDVQlaEIEFDIETYE-----PLPAYKPAATRN--QAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIP 236
Cdd:PRK06276 159 KDVQ--EGELDLEKYPipakiDLPGYKPTTFGHplQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 237 TLMGWGSIPDDHPL---MAGMCGLQTShrygNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFA 313
Cdd:PRK06276 237 TLMGKGAFPEDHPLalgMVGMHGTKAA----NYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 314 PDYGIVSDAGAALK-LFVEVAREwkaagRLKDRSGWVAECQGRKNSVeyLRKTQFDDVPMKPQRVYQCMNRNLD-----K 387
Cdd:PRK06276 313 VDVPIVGDAKNVLRdLLAELMKK-----EIKNKSEWLERVKKLKKES--IPRMDFDDKPIKPQRVIKELMEVLReidpsK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 388 DTCYVSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLP 467
Cdd:PRK06276 386 NTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 468 YVHVLVNNSYLGLIRQAQRAFsidycvqlafdnINMDEGEASRGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeawm 547
Cdd:PRK06276 466 VVICIFDNRTLGMVYQWQNLY------------YGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEA---- 529
|
570 580 590
....*....|....*....|....*....|..
gi 317118330 548 AEHRTPVVIECILERVTNISM---GTEIDNVI 576
Cdd:PRK06276 530 IKSGEPYLLDIIIDPAEALPMvppGGNLTNIL 561
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-557 |
4.78e-124 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 378.94 E-value: 4.78e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAG 80
Cdd:PRK07789 28 PERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQA-TGRVGVCMATSGPGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLI 160
Cdd:PRK07789 107 TNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 161 DLPIDVQLAEIEFDIETYEPLPAYKPAATRN--QAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTL 238
Cdd:PRK07789 187 DIPKDALQAQTTFSWPPRMDLPGYRPVTKPHgkQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 239 MGWGSIPDDHPLMAGMCGLqtshrYGN----ATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAP 314
Cdd:PRK07789 267 MARGAFPDSHPQHLGMPGM-----HGTvaavAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 315 DYGIVSDAGAALKLFVEVAREWKAAGRLKDRSGWVAECQGrknsveyLRKT------QFDDVPMKPQRVYQCMNRNLDKD 388
Cdd:PRK07789 342 DVPIVGDVKEVIAELIAALRAEHAAGGKPDLTAWWAYLDG-------WRETyplgydEPSDGSLAPQYVIERLGEIAGPD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 389 TCYVSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPY 468
Cdd:PRK07789 415 AIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPI 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 469 VHVLVNNSYLGLIRQAQRAFsidYcvQLAFDNINMDEGEasrGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeawMA 548
Cdd:PRK07789 495 KVALINNGNLGMVRQWQTLF---Y--EERYSNTDLHTHS---HRIPDFVKLAEAYGCVGLRCEREEDVDAVIEKA---RA 563
|
....*....
gi 317118330 549 EHRTPVVIE 557
Cdd:PRK07789 564 INDRPVVID 572
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
14-565 |
1.97e-122 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 374.77 E-value: 1.97e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 14 LEKEGVSVAFGVPGAAINPLYAAM---KAHGGIGHILARHVEGASHMAEGYTRAVaGNIGVCIGTSGPAGTDMITGLYSA 90
Cdd:PRK07418 29 LKRHGVKHIFGYPGGAILPIYDELykaEAEGWLKHILVRHEQGAAHAADGYARAT-GKVGVCFGTSGPGATNLVTGIATA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 91 SADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDVQLAe 170
Cdd:PRK07418 108 QMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIPKDVGQE- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 171 iEFDIETYEP----LPAYKPAATRN--QAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGSI 244
Cdd:PRK07418 187 -EFDYVPVEPgsvkPPGYRPTVKGNprQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTTLMGKGAF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 245 PDDHPLMAGMCGLQTShRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDAGA 324
Cdd:PRK07418 266 DEHHPLSVGMLGMHGT-AYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVPIVGDVRK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 325 ALKLFVEVAREWKAAGRLKDrsgWVAECQGRKNsvEYLRKTQFDDVPMKPQRVYQCMnRNLDKDTCYVSTIGLSQIAGAQ 404
Cdd:PRK07418 345 VLVKLLERSLEPTTPPRTQA---WLERINRWKQ--DYPLVVPPYEGEIYPQEVLLAV-RDLAPDAYYTTDVGQHQMWAAQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 405 FLHvYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQA 484
Cdd:PRK07418 419 FLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGMVRQW 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 485 QRAFSIDycvqlAFDNINMDEGEAsrgygvDHVKVVEGLGCKAIRVHHPEDFAPAMRQaeawMAEHRTPVVIECILERVT 564
Cdd:PRK07418 498 QESFYGE-----RYSASNMEPGMP------DFVKLAEAFGVKGMVISERDQLKDAIAE----ALAHDGPVLIDVHVRRDE 562
|
.
gi 317118330 565 N 565
Cdd:PRK07418 563 N 563
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
7-566 |
4.07e-117 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 359.41 E-value: 4.07e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 7 IEAavcvLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDMITG 86
Cdd:PRK08527 10 CEA----LKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARA-SGKVGVAIVTSGPGFTNAVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 87 LYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDV 166
Cdd:PRK08527 85 LATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPKDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 167 QLAEIEFDIETYEPLPAYKPAATRN--QAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGSI 244
Cdd:PRK08527 165 TATLGEFEYPKEISLKTYKPTYKGNsrQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMARGVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 245 PDDHPLMAGMCGLQTSHRyGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDAGA 324
Cdd:PRK08527 245 RSDDPLLLGMLGMHGSYA-ANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGDLKN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 325 ALKLFVEVAREWKAagrlKDRSGWVaECQGRKNSVEYLRKTQFDDVpMKPQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQ 404
Cdd:PRK08527 324 VLKEMLEELKEENP----TTYKEWR-EILKRYNELHPLSYEDSDEV-LKPQWVIERVGELLGDDAIISTDVGQHQMWVAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 405 FLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQA 484
Cdd:PRK08527 398 FYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQW 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 485 QRAFsidYCVQLAFDNINMDEgeasrgygvDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeawmAEHRTPVVIECILERVT 564
Cdd:PRK08527 478 QTFF---YEERYSETDLSTQP---------DFVKLAESFGGIGFRVTTKEEFDKALKEA----LESDKVALIDVKIDRFE 541
|
..
gi 317118330 565 NI 566
Cdd:PRK08527 542 NV 543
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
14-518 |
7.70e-117 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 358.75 E-value: 7.70e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 14 LEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:PRK07282 20 LRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKS-TGKLGVAVVTSGPGATNAITGIADAMSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 94 SIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDVQLAEIEF 173
Cdd:PRK07282 99 SVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKDVSALETDF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 174 DIETYEPLPAYKPAATRN--QAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGSIPDDHPLM 251
Cdd:PRK07282 179 IYDPEVNLPSYQPTLEPNdmQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 252 AGMCGLQTSHRyGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDAGAALKLFVE 331
Cdd:PRK07282 259 LGMGGMHGSYA-ANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKKALQMLLA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 332 varEWKAAGRLKDrsgWVAECQGRKNSVeylRKTQFDDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLHVYKP 411
Cdd:PRK07282 338 ---EPTVHNNTEK---WIEKVTKDKNRV---RSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 412 RHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQRAFSID 491
Cdd:PRK07282 409 RQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESFYEG 488
|
490 500
....*....|....*....|....*..
gi 317118330 492 YCVQLAFDNINmDEGEASRGYGVDHVK 518
Cdd:PRK07282 489 RTSESVFDTLP-DFQLMAQAYGIKHYK 514
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
4-565 |
1.22e-116 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 359.02 E-value: 1.22e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 4 MKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDM 83
Cdd:PRK09107 11 MTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARS-TGKPGVVLVTSGPGATNA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLP 163
Cdd:PRK09107 90 VTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 164 IDVQLAEiefdiETYEP------LPAYKPAATRNQA--EKAISMLNEAERPLIVSGGGVINA--DASALLVELAELLHVP 233
Cdd:PRK09107 170 KDVQFAT-----GTYTPpqkapvHVSYQPKVKGDAEaiTEAVELLANAKRPVIYSGGGVINSgpEASRLLRELVELTGFP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 234 VIPTLMGWGSIPDDHPLMAGMCGLQTSHRyGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFA 313
Cdd:PRK09107 245 ITSTLMGLGAYPASGKNWLGMLGMHGTYE-ANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 314 PDYGIVSDAGAALKlfvEVAREWKAAGRLKDRSG---W---VAECQGRkNSVEYlrkTQFDDVpMKPQ----RVYQCMNr 383
Cdd:PRK09107 324 VDVPIIGDVGHVLE---DMLRLWKARGKKPDKEAladWwgqIARWRAR-NSLAY---TPSDDV-IMPQyaiqRLYELTK- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 384 nlDKDTcYVST-IGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGA 462
Cdd:PRK09107 395 --GRDT-YITTeVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 463 QFKLPYVHVLVNNSYLGLIRQAQrafsidycvQLAFDNinmdegEASRGYG---VDHVKVVEGLGCKAIRVHHPEDFAPA 539
Cdd:PRK09107 472 QYNLPVKIFILNNQYMGMVRQWQ---------QLLHGN------RLSHSYTeamPDFVKLAEAYGAVGIRCEKPGDLDDA 536
|
570 580
....*....|....*....|....*.
gi 317118330 540 MRQaeawMAEHRTPVVIECILERVTN 565
Cdd:PRK09107 537 IQE----MIDVDKPVIFDCRVANLEN 558
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
4-566 |
1.98e-113 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 350.04 E-value: 1.98e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 4 MKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAhGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDM 83
Cdd:PRK06725 15 VTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARA-SGKVGVVFATSGPGATNL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLP 163
Cdd:PRK06725 93 VTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 164 IDVQLAEIEFDIETYEPLPAYKPAATRN--QAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGW 241
Cdd:PRK06725 173 KDVQNEKVTSFYNEVVEIPGYKPEPRPDsmKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 242 GSIPDDHPLMAGMCGLQTSHRyGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSD 321
Cdd:PRK06725 253 GAYPPGDPLFLGMLGMHGTYA-ANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVGD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 322 AGAALKLFVEVAREWKAAGRLKDRSGWVAECQgrknsVEYLRKtqfdDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQIA 401
Cdd:PRK06725 332 VKKALHMLLHMSIHTQTDEWLQKVKTWKEEYP-----LSYKQK----ESELKPQHVINLVSELTNGEAIVTTEVGQHQMW 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 402 GAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLI 481
Cdd:PRK06725 403 AAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 482 RQAQRAFsidycvqlaFDNiNMDEgeaSRGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAwmaeHRTPVVIECILE 561
Cdd:PRK06725 483 RQWQEMF---------YEN-RLSE---SKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFA----HEGPVVVDFCVE 545
|
....*
gi 317118330 562 RVTNI 566
Cdd:PRK06725 546 EGENV 550
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
14-565 |
2.51e-110 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 342.45 E-value: 2.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 14 LEKEGVSVAFGVPGAAINPLYAAMKA---HGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDMITGLYSA 90
Cdd:CHL00099 20 LVRHGVKHIFGYPGGAILPIYDELYAwekKGLIKHILVRHEQGAAHAADGYARS-TGKVGVCFATSGPGATNLVTGIATA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 91 SADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDVQLAe 170
Cdd:CHL00099 99 QMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVGLE- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 171 iEFDIETYEP------LPAYKPA--ATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWG 242
Cdd:CHL00099 178 -KFDYYPPEPgntiikILGCRPIykPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLMGKG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 243 SIPDDHPLMAGMCGLQTShRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDA 322
Cdd:CHL00099 257 IFDEDHPLCLGMLGMHGT-AYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVAIVGDV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 323 GAALKLFVEVAREWKAAGRLKDRSGWVAECQGRKNsvEYLRKTQFDDVPMKPQRVYQCMNRnLDKDTCYVSTIGLSQIAG 402
Cdd:CHL00099 336 KKVLQELLELLKNSPNLLESEQTQAWRERINRWRK--EYPLLIPKPSTSLSPQEVINEISQ-LAPDAYFTTDVGQHQMWA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 403 AQFLHVyKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIR 482
Cdd:CHL00099 413 AQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMVR 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 483 QAQRAFsidYCVQlaFDNINMDEGEAsrgygvDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeawmAEHRTPVVIECILER 562
Cdd:CHL00099 492 QWQQAF---YGER--YSHSNMEEGAP------DFVKLAEAYGIKGLRIKSRKDLKSSLKEA----LDYDGPVLIDCQVIE 556
|
...
gi 317118330 563 VTN 565
Cdd:CHL00099 557 DEN 559
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
1-558 |
8.14e-109 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 338.27 E-value: 8.14e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVC------------VLEKEGVSVAFGVPGAAINPLYAAMkAHGGIGHILARHVEGASHMAEGYTRaVAGN 68
Cdd:PRK07710 1 TNVMRTMSSKTEeklmtgaqmlieALEKEGVEVIFGYPGGAVLPLYDAL-YDCGIPHILTRHEQGAIHAAEGYAR-ISGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 69 IGVCIGTSGPAGTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFH 148
Cdd:PRK07710 79 PGVVIATSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 149 LMRSGRPGPVLIDLPIDVQLAEIEFDIETYEPLPAYKPAATRN--QAEKAISMLNEAERPLIVSGGGVINADASALLVEL 226
Cdd:PRK07710 159 IATTGRPGPVLIDIPKDMVVEEGEFCYDVQMDLPGYQPNYEPNllQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 227 AELLHVPVIPTLMGWGSIPDDHPLMAGMCGLQTSHRyGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPT 306
Cdd:PRK07710 239 AEQQEIPVVHTLLGLGGFPADHPLFLGMAGMHGTYT-ANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 307 QIGRVFAPDYGIVSDAGAALKLFVevarewKAAGRLKDRSGWVAECQGRKNsvEYLRKTQFDDVPMKPQRVYQCMNRNLD 386
Cdd:PRK07710 318 EIGKNVPTEIPIVADAKQALQVLL------QQEGKKENHHEWLSLLKNWKE--KYPLSYKRNSESIKPQKAIEMLYEITK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 387 KDTCYVSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKL 466
Cdd:PRK07710 390 GEAIVTTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 467 PYVHVLVNNSYLGLIRQAQRAFSIDYCVQLAFDNinmdegeasrgyGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeaw 546
Cdd:PRK07710 470 PVKVVILNNEALGMVRQWQEEFYNQRYSHSLLSC------------QPDFVKLAEAYGIKGVRIDDELEAKEQLQHA--- 534
|
570
....*....|..
gi 317118330 547 mAEHRTPVVIEC 558
Cdd:PRK07710 535 -IELQEPVVIDC 545
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-517 |
2.58e-108 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 336.68 E-value: 2.58e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAG 80
Cdd:PRK08155 10 RKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMART-TGKPAVCMACSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLI 160
Cdd:PRK08155 89 TNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 161 DLPIDVQLAEIEFDIETYEPLPAYKPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMG 240
Cdd:PRK08155 169 DIPKDVQTAVIELEALPAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 241 WGSIPDDHPLMAGMCGLQTShRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVS 320
Cdd:PRK08155 249 LGMLPKAHPLSLGMLGMHGA-RSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 321 DAGAALKLFVEVAREwkaagrlKDRSGW---VAECQGRKNsveyLRKTQFDDvPMKPQRVYQCMNRNLDKDTCYVSTIGL 397
Cdd:PRK08155 328 DVDDVLAQLLPLVEA-------QPRAEWhqlVADLQREFP----CPIPKADD-PLSHYGLINAVAACVDDNAIITTDVGQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 398 SQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSY 477
Cdd:PRK08155 396 HQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEA 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 317118330 478 LGLIRQAQ------RAFSIDYCVQLAFDNInmdegeaSRGYGVDHV 517
Cdd:PRK08155 476 LGLVHQQQslfygqRVFAATYPGKINFMQI-------AAGFGLETC 514
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-543 |
1.23e-103 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 324.94 E-value: 1.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAG 80
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARS-TGKVGCVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLI 160
Cdd:PRK06882 80 TNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 161 DLPIDVQLAEIEFDIE--TYEPLPAYKPAAT--RNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIP 236
Cdd:PRK06882 160 DIPKDMVNPANKFTYEypEEVSLRSYNPTVQghKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 237 TLMGWGSIPDDHPLMAGMCGLQTSHRYGNAtMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDY 316
Cdd:PRK06882 240 SLMGLGAYPSTDKQFLGMLGMHGTYEANNA-MHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 317 GIVSDAGAALKLFVEVAREWKAAGRLKDRSGWVAECQGRKnSVEYLRKTQFDDVpMKPQRVYQCMNRNLDKDTCYVSTIG 396
Cdd:PRK06882 319 PIVGSAKNVLEEFLSLLEEENLAKSQTDLTAWWQQINEWK-AKKCLEFDRTSDV-IKPQQVVEAIYRLTNGDAYVASDVG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 397 LSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNS 476
Cdd:PRK06882 397 QHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNR 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 477 YLGLIRQAQrafSIDYcvqlafdninmdEGEASRGYG---VDHVKVVEGLGCKAIRVHHPEDFAPAMRQA 543
Cdd:PRK06882 477 FLGMVKQWQ---DLIY------------SGRHSQVYMnslPDFAKLAEAYGHVGIQIDTPDELEEKLTQA 531
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-545 |
2.97e-100 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 315.99 E-value: 2.97e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAVaGNIGVCIGTSGPAG 80
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARAT-GKVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLI 160
Cdd:PRK08979 80 TNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 161 DLPIDVQLAEIEFDIETYEPLP--AYKPAAT--RNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIP 236
Cdd:PRK08979 160 DLPKDCLNPAILHPYEYPESIKmrSYNPTTSghKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 237 TLMGWGSIPDDHPLMAGMCGLQTSHRyGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDY 316
Cdd:PRK08979 240 TLMGLGAFPGTHKNSLGMLGMHGRYE-ANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 317 GIVSDAGAALKLFVEVAREWKAAGRLKDRSGWVAECQG--RKNSVEYLRKTQfddvPMKPQRVYQCMNRNLDKDTCYVST 394
Cdd:PRK08979 319 PIVGSADKVLDSMLALLDESGETNDEAAIASWWNEIEVwrSRNCLAYDKSSE----RIKPQQVIETLYKLTNGDAYVASD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 395 IGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVN 474
Cdd:PRK08979 395 VGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLN 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 317118330 475 NSYLGLIRQAQrafsiDYCVQLAFDNINMDEGEasrgygvDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEA 545
Cdd:PRK08979 475 NRFLGMVKQWQ-----DMIYQGRHSHSYMDSVP-------DFAKIAEAYGHVGIRISDPDELESGLEKALA 533
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-551 |
2.93e-98 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 310.63 E-value: 2.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAVaGNIGVCIGTSGPAG 80
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARAT-GEVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLI 160
Cdd:PRK07979 80 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 161 DLPIDVQLAEIEFDIETYE--PLPAYKPAAT--RNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIP 236
Cdd:PRK07979 160 DLPKDILNPANKLPYVWPEsvSMRSYNPTTQghKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 237 TLMGWGSIPDDHPLMAGMCGLQTSHRyGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDY 316
Cdd:PRK07979 240 SLMGLGAFPATHRQSLGMLGMHGTYE-ANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 317 GIVSDAGAALKLFVEVAREWKAAGRLKD-RSGWVAECQGR-KNSVEYLRKTQfddvPMKPQRVYQCMNRnLDKDTCYV-S 393
Cdd:PRK07979 319 PIVGDARQVLEQMLELLSQESAHQPLDEiRDWWQQIEQWRaRQCLKYDTHSE----KIKPQAVIETLWR-LTKGDAYVtS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 394 TIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLV 473
Cdd:PRK07979 394 DVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 474 NNSYLGLIRQAQrafsidycvqlafDNINmdEGEASRGYG---VDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAWMAEH 550
Cdd:PRK07979 474 NNRYLGMVKQWQ-------------DMIY--SGRHSQSYMqslPDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNN 538
|
.
gi 317118330 551 R 551
Cdd:PRK07979 539 R 539
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-545 |
4.25e-98 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 310.52 E-value: 4.25e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAVaGNIGVCIGTSGPAG 80
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARAT-GKTGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLI 160
Cdd:PRK06466 80 TNAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 161 DLPIDVQLAEIEFDIETYEP--LPAYKPAAT--RNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIP 236
Cdd:PRK06466 160 DIPKDMTNPAEKFEYEYPKKvkLRSYSPAVRghSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 237 TLMGWGSIPDDHPLMAGMCGLQTSHRyGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDY 316
Cdd:PRK06466 240 TLMGLGGFPGTDRQFLGMLGMHGTYE-ANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 317 GIVSDAGAALKLFVEVAREWKAAGRLKDRSGWVAECQGRKNSVEYLRKTQFDDVPMKPQRVYQCMNRNLDKDTCYVSTIG 396
Cdd:PRK06466 319 PIVGPVESVLTEMLAILKEIGEKPDKEALAAWWKQIDEWRGRHGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 397 LSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNS 476
Cdd:PRK06466 399 QHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNG 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317118330 477 YLGLIRQAQrafSIDYcvqlafdninmdEGEASRGYG---VDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEA 545
Cdd:PRK06466 479 ALGMVRQWQ---DMQY------------EGRHSHSYMeslPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFA 535
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
2-543 |
4.21e-97 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 308.27 E-value: 4.21e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 2 ARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAVaGNIGVCIGTSGPAGT 81
Cdd:PRK06965 19 ADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARAT-GKVGVALVTSGPGVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLID 161
Cdd:PRK06965 98 NAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 162 LPIDVQLAEIEFDIETYEPLPAYKPA--ATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLM 239
Cdd:PRK06965 178 IPKDVSKTPCEYEYPKSVEMRSYNPVtkGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 240 GWGSIPDDHPLMAGMCGLQTSHRYGNAtMLASDFVLGIGNRWANRHTGSVDVYTKG-RKFVHVDIEPTQIGRVFAPDYGI 318
Cdd:PRK06965 258 GLGAYPASDKKFLGMLGMHGTYEANMA-MQHCDVLIAIGARFDDRVIGNPAHFASRpRKIIHIDIDPSSISKRVKVDIPI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 319 VSDAGAALKLFVEVAREWKAAGRLKDRSGWVAECQG--RKNSVEYLRKTQFddvpMKPQRVYQCMNRNLDKDTCYVSTIG 396
Cdd:PRK06965 337 VGDVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGwrSRDCLKYDRESEI----IKPQYVVEKLWELTDGDAFVCSDVG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 397 LSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNS 476
Cdd:PRK06965 413 QHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNR 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 477 YLGLIRQAQRafsIDYcvqlafdninmdEGEASRGYG---VDHVKVVEGLGCKAIRVHHPEDFAPAMRQA 543
Cdd:PRK06965 493 YLGMVRQWQE---IEY------------SKRYSHSYMdalPDFVKLAEAYGHVGMRIEKTSDVEPALREA 547
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
4-488 |
1.95e-93 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 297.18 E-value: 1.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 4 MKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMkAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDM 83
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARA-TGKVGVCIATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLP 163
Cdd:PRK08978 79 ITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 164 IDVQLAEIEFdiETYEPLPAYKPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGS 243
Cdd:PRK08978 159 KDIQLAEGEL--EPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 244 IPDDHPLMAGMCGLQTShRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDAG 323
Cdd:PRK08978 237 VEADHPYYLGMLGMHGT-KAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 324 A---ALKLFVEVArEWKA-AGRLKDRSGWVAECQGRKNSVEYLRKTQFDdvpMKPQrvyqcmnrnldkDTCYVSTIGLSQ 399
Cdd:PRK08978 316 AllpALQQPLNID-AWRQhCAQLRAEHAWRYDHPGEAIYAPALLKQLSD---RKPA------------DTVVTTDVGQHQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 400 IAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLG 479
Cdd:PRK08978 380 MWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLG 459
|
....*....
gi 317118330 480 LIRQAQRAF 488
Cdd:PRK08978 460 MVRQWQQLF 468
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
14-543 |
1.37e-92 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 295.98 E-value: 1.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 14 LEKEGVSVAFGVPGAAINPLYAAM---KAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDMITGLYSA 90
Cdd:PRK06456 12 LKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARA-SGVPGVCTATSGPGTTNLVTGLITA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 91 SADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDVQLAE 170
Cdd:PRK06456 91 YWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIPRDIFYEK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 171 IEfDIETYE-PL-PAYKPAAT---RNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGSIP 245
Cdd:PRK06456 171 ME-EIKWPEkPLvKGYRDFPTridRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTFPGKTAIP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 246 DDHPLMAGMCGLqtshrYGNA----TMLASDFVLGIGNRWANRHTGSVD-VYTKGRKFVHVDIEPTQIGRVFAPDYGIVS 320
Cdd:PRK06456 250 HDHPLYFGPMGY-----YGRAeasmAALESDAMLVVGARFSDRTFTSYDeMVETRKKFIMVNIDPTDGEKAIKVDVGIYG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 321 DAGAALKLFVEVAREwkaAGRLKDRSGWVAECQGRKnsvEYLRKTQF--DDVPMKPQRVYQCMNRNLDKDTCYVSTIGLS 398
Cdd:PRK06456 325 NAKIILRELIKAITE---LGQKRDRSAWLKRVKEYK---EYYSQFYYteENGKLKPWKIMKTIRQALPRDAIVTTGVGQH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 399 QIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYL 478
Cdd:PRK06456 399 QMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 317118330 479 GLIRQAQ------RAFSIDYcvqlafdninmdegeasrGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQA 543
Cdd:PRK06456 479 GLVRQVQdlffgkRIVGVDY------------------GPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSA 531
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
11-559 |
7.92e-89 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 286.63 E-value: 7.92e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 11 VCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDMITGLYSA 90
Cdd:PLN02470 20 VEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKA-SGKVGVCIATSGPGATNLVTGLADA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 91 SADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDVQLae 170
Cdd:PLN02470 99 LLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDIQQ-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 171 iEFDIETYEP---LPAY----KPAATRNQAEKAISMLNEAERPLIVSGGGVINadASALLVELAELLHVPVIPTLMGWGS 243
Cdd:PLN02470 177 -QLAVPNWNQpmkLPGYlsrlPKPPEKSQLEQIVRLISESKRPVVYVGGGCLN--SSEELREFVELTGIPVASTLMGLGA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 244 IPDDHPLMAGMCGLQTShRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDAG 323
Cdd:PLN02470 254 FPASDELSLQMLGMHGT-VYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADVK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 324 AALKLFVEVAREWKAAGrlKDRSGWVAECQGRKnsVEY-LRKTQFDDVpMKPQRVYQCMNRNLDKDTCYVSTIGLSQIAG 402
Cdd:PLN02470 333 LALQGLNKLLEERKAKR--PDFSAWRAELDEQK--EKFpLSYPTFGDA-IPPQYAIQVLDELTDGNAIISTGVGQHQMWA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 403 AQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIR 482
Cdd:PLN02470 408 AQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVV 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317118330 483 QAQRAFsidYCVQLAFDNINMDEGEASrgYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQaeawMAEHRTPVVIECI 559
Cdd:PLN02470 488 QWEDRF---YKANRAHTYLGDPDAEAE--IFPDFLKFAEGCKIPAARVTRKSDLREAIQK----MLDTPGPYLLDVI 555
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-557 |
1.91e-86 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 278.82 E-value: 1.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGG-IGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPA 79
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARS-TGRPGVCSVVPGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 80 GTDMITGLYSASADSIPILCITGQAP-------RARLHkedfQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRS 152
Cdd:PRK08266 80 VLNAGAALLTAYGCNSPVLCLTGQIPsaligkgRGHLH----EMPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 153 GRPGPVLIDLPIDV--QLAEIEfDIETYEPLPAykPAATRNQAEKAISMLNEAERPLIVSGGGVinADASALLVELAELL 230
Cdd:PRK08266 156 GRPRPVALEMPWDVfgQRAPVA-AAPPLRPAPP--PAPDPDAIAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEML 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 231 HVPVIPTLMGWGSIPDDHPLMAGMCGlqtshryGNATMLASDFVLGIGNR-------WANRhtgsvdvyTKGRKFVHVDI 303
Cdd:PRK08266 231 QAPVVAFRSGRGIVSDRHPLGLNFAA-------AYELWPQTDVVIGIGSRlelptfrWPWR--------PDGLKVIRIDI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 304 EPTQIGRvFAPDYGIVSDAGAALKLFVEVARewKAAGRLKDRSGWVAECQGRKNSveylrktQFDDVpmKPQRVY-QCMN 382
Cdd:PRK08266 296 DPTEMRR-LKPDVAIVADAKAGTAALLDALS--KAGSKRPSRRAELRELKAAARQ-------RIQAV--QPQASYlRAIR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 383 RNLDKDTCYVSTigLSQIAGAQFLH--VYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAV 460
Cdd:PRK08266 364 EALPDDGIFVDE--LSQVGFASWFAfpVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELAT 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 461 GAQFKLPYVHVLVNNSYLGLIRQAQRAfsidycvqlAFDNINMdegeASRGYGVDHVKVVEGLGCKAIRVHHPEDFAPAM 540
Cdd:PRK08266 442 AVQHNIGVVTVVFNNNAYGNVRRDQKR---------RFGGRVV----ASDLVNPDFVKLAESFGVAAFRVDSPEELRAAL 508
|
570
....*....|....*..
gi 317118330 541 RQAEAwmaeHRTPVVIE 557
Cdd:PRK08266 509 EAALA----HGGPVLIE 521
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
4-558 |
3.10e-81 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 265.54 E-value: 3.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 4 MKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKaHGGIGHILARHVEGASHMAEGYTRaVAGNIGVCIGTSGPAGTDM 83
Cdd:PRK08322 1 MKAADLFVKCLENEGVEYIFGIPGEENLDLLEALR-DSSIKLILTRHEQGAAFMAATYGR-LTGKAGVCLSTLGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLP 163
Cdd:PRK08322 79 VTGVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 164 IDVqlAEIEFDIETYEPLPAYKPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGS 243
Cdd:PRK08322 159 EDI--AAEETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 244 IPDDHPLMAGMCGLQtSHRYGNATMLASDFVLGIGN--------RWaNRHTgsvdvytkGRKFVHVDIEPTQIGRVFAPD 315
Cdd:PRK08322 237 IPETHPLSLGTAGLS-QGDYVHCAIEHADLIINVGHdviekppfFM-NPNG--------DKKVIHINFLPAEVDPVYFPQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 316 YGIVSDAGAALklfvevareWKAAGRLKDRSGWVAEC--QGRKNSVEYLRKTQFDD-VPMKPQR----VYQCMNRN---- 384
Cdd:PRK08322 307 VEVVGDIANSL---------WQLKERLADQPHWDFPRflKIREAIEAHLEEGADDDrFPMKPQRivadLRKVMPDDdivi 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 385 LDkdtcyvstIGLSQIAGAQFLHVYKPRH-WINCGQAGpLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQ 463
Cdd:PRK08322 378 LD--------NGAYKIWFARNYRAYEPNTcLLDNALAT-MGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVR 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 464 FKLPYVHVLVNNSYLGLIR--QAQRAFSiDYCVQlaFDNinmdegeasrgygVDHVKVVEGLGCKAIRVHHPEDFAPAMR 541
Cdd:PRK08322 449 LGLPLVVLILNDNAYGMIRwkQENMGFE-DFGLD--FGN-------------PDFVKYAESYGAKGYRVESADDLLPTLE 512
|
570
....*....|....*....
gi 317118330 542 QAEAwmaehrTPVV--IEC 558
Cdd:PRK08322 513 EALA------QPGVhvIDC 525
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
4-561 |
5.44e-74 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 246.98 E-value: 5.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 4 MKAIEAAVCVLEKEGVSVAFG--VPGAainpLYAAMKAHGgIGHILARHVEGASHMAEGYTRaVAGNIGVCIGTSGPAGT 81
Cdd:PRK06112 14 GTVAHAIARALKRHGVEQIFGqsLPSA----LFLAAEAIG-IRQIAYRTENAGGAMADGYAR-VSGKVAVVTAQNGPAAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLID 161
Cdd:PRK06112 88 LLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 162 LPIDVqLAEiefdietyeplPAYKPAATRNQA----------------EKAISMLNEAERPLIVSGGGVINADASALLVE 225
Cdd:PRK06112 168 LPADL-LTA-----------AAAAPAAPRSNSlghfpldrtvpapqrlAEAASLLAQAQRPVVVAGGGVHISGASAALAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 226 LAELLHVPVIPTLMGWGSIPDDHPLMAGMCGL----QTSHRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHV 301
Cdd:PRK06112 236 LQSLAGLPVATTNMGKGAVDETHPLSLGVVGSlmgpRSPGRHLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 302 DIEPTQIGRvfapDYG---IVSDAGAALKLFVEVAREWKAAGRLKDRSGwVAEC--QGRKNSVEYLRK-TQFDDVPMKPQ 375
Cdd:PRK06112 316 DVDGEEVGR----NYEalrLVGDARLTLAALTDALRGRDLAARAGRRAA-LEPAiaAGREAHREDSAPvALSDASPIRPE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 376 RVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLHVYKP--RHWINCGQAGpLGWTVPAALGVRVADPERRIVALSGDYDFQF 453
Cdd:PRK06112 391 RIMAELQAVLTGDTIVVADASYSSIWVANFLTARRAgmRFLTPRGLAG-LGWGVPMAIGAKVARPGAPVICLVGDGGFAH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 454 MIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQRAFSIDYCVQLAFDninmdegeasrgyGVDHVKVVEGLGCKAIRVHHP 533
Cdd:PRK06112 470 VWAELETARRMGVPVTIVVLNNGILGFQKHAETVKFGTHTDACHFA-------------AVDHAAIARACGCDGVRVEDP 536
|
570 580
....*....|....*....|....*...
gi 317118330 534 EDFAPAMRQAEAwmaeHRTPVVIECILE 561
Cdd:PRK06112 537 AELAQALAAAMA----APGPTLIEVITD 560
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
14-561 |
2.98e-72 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 241.70 E-value: 2.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 14 LEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:PRK08199 18 LRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKL-TGRPGICFVTRGPGATNASIGVHTAFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 94 SIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDVQLAEIEF 173
Cdd:PRK08199 97 STPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPEDVLSETAEV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 174 -DIETYEPLPAYkPAATrnQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGSIPDDHPLMA 252
Cdd:PRK08199 177 pDAPPYRRVAAA-PGAA--DLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDLFDNRHPNYA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 253 GMCGLQTSHRYGnATMLASDFVLGIGNRWANRHTGS---VDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDAGAalklF 329
Cdd:PRK08199 254 GDLGLGINPALA-ARIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELGRVYRPDLAIVADPAA----F 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 330 VEVAREWKAAGRLKdRSGWVAECQGrknsvEYLRKTQFDDVPMKPQ--RVYQCMNRNLDKDTCYvsTIGlsqiAG--AQF 405
Cdd:PRK08199 329 AAALAALEPPASPA-WAEWTAAAHA-----DYLAWSAPLPGPGAVQlgEVMAWLRERLPADAII--TNG----AGnyATW 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 406 LHVYKP-RHWinCGQAGP----LGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGL 480
Cdd:PRK08199 397 LHRFFRfRRY--RTQLAPtsgsMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 481 IRQAQ-RAFSiDYCVQLAFDNinmdegeasrgygVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAwmaeHRTPVVIECI 559
Cdd:PRK08199 475 IRMHQeREYP-GRVSGTDLTN-------------PDFAALARAYGGHGETVERTEDFAPAFERALA----SGKPALIEIR 536
|
..
gi 317118330 560 LE 561
Cdd:PRK08199 537 ID 538
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-556 |
1.20e-70 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 237.98 E-value: 1.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAM-KAHGGIGHILARHVEGASHMAEGYTRaVAGNIGVCIGTSGPA 79
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrKEQDKIKFIQVRHEEVAALAAAAYAK-LTGKIGVCLSIGGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 80 GTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAfhlMRSG--RPGP 157
Cdd:PRK08611 80 AIHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQA---IRTAyeKKGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 158 VLIDLPIDVQLAEIEfdIETYEPLPAYKPAA---TRNQAEKAISMLNEAERPLIVSGGGVINADASalLVELAELLHVPV 234
Cdd:PRK08611 157 AVLTIPDDLPAQKIK--DTTNKTVDTFRPTVpspKPKDIKKAAKLINKAKKPVILAGLGAKHAKEE--LLAFAEKAKIPI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 235 IPTLMGWGSIPDDHPLMAGMCG-LQTSHRYgnATMLASDFVLGIGNRWAnrhtgSVDVYTKGRKFVHVDIEPTQIGRVFA 313
Cdd:PRK08611 233 IHTLPAKGIIPDDHPYSLGNLGkIGTKPAY--EAMQEADLLIMVGTNYP-----YVDYLPKKAKAIQIDTDPANIGKRYP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 314 PDYGIVSDAGAALKLFVEvarewkAAGRLKDRSgWVAECQGRKNSVEYL--RKTQFDDVPMKPQRVYQCMNRNLDKDTCY 391
Cdd:PRK08611 306 VNVGLVGDAKKALHQLTE------NIKHVEDRR-FLEACQENMAKWWKWmeEDENNASTPIKPERVMAAIQKIADDDAVL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 392 VSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHV 471
Cdd:PRK08611 379 SVDVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 472 LVNNSYLGLIRQAQRAF-SIDYCVQLAfdniNMdegeasrgygvDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeawMAEH 550
Cdd:PRK08611 459 VLNNQQLAFIKYEQQAAgELEYAIDLS----DM-----------DYAKFAEACGGKGYRVEKAEELDPAFEEA---LAQD 520
|
....*.
gi 317118330 551 RtPVVI 556
Cdd:PRK08611 521 K-PVII 525
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
8-557 |
2.22e-68 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 231.02 E-value: 2.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 8 EAAVCVLEKEGVSVAFGVPGAAINPLYAAMkAHGGIGHILARHVEGASHMAEGYTRaVAGNIGVCIGTSGPAGTDMITGL 87
Cdd:PRK07524 6 EALVRLLEAYGVETVFGIPGVHTVELYRGL-AGSGIRHVTPRHEQGAGFMADGYAR-VSGKPGVCFIITGPGMTNIATAM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 88 YSASADSIPILCITGQAPRARLHKED---FQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPI 164
Cdd:PRK07524 84 GQAYADSIPMLVISSVNRRASLGKGRgklHELPDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 165 DVQLAEIEFDIeTYEPLPAYKPAATRNQAEKAISMLNEAERPLIVSGGGVInaDASALLVELAELLHVPVIPTLMGWGSI 244
Cdd:PRK07524 164 DVLAAPADHLL-PAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGAL--AAAAALRALAERLDAPVALTINAKGLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 245 PDDHPLMAGMCglqTSHRYGNATMLASDFVLGIGNRWANRhtgSVDVYTKGR-----KFVHVDIEPTQIGRVFAPDYGIV 319
Cdd:PRK07524 241 PAGHPLLLGAS---QSLPAVRALIAEADVVLAVGTELGET---DYDVYFDGGfplpgELIRIDIDPDQLARNYPPALALV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 320 SDAGAALKLFVEVAREWKAAGRlkdrsgWVAEcqgrknSVEYLRKTQF--DDVPMKPQ-RVYQCMNRNLDkDTCYVSTIG 396
Cdd:PRK07524 315 GDARAALEALLARLPGQAAAAD------WGAA------RVAALRQALRaeWDPLTAAQvALLDTILAALP-DAIFVGDST 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 397 LSQIAGAQFLHVYKPRHWINCGQA-GPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNN 475
Cdd:PRK07524 382 QPVYAGNLYFDADAPRRWFNASTGyGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 476 SYLGLIRqaqrafsiDYCVQLAFDNINMDEgeasrgYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeawmAEHRTPVV 555
Cdd:PRK07524 462 DGYGEIR--------RYMVARDIEPVGVDP------YTPDFIALARAFGCAAERVADLEQLQAALRAA----FARPGPTL 523
|
..
gi 317118330 556 IE 557
Cdd:PRK07524 524 IE 525
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
4-567 |
5.47e-64 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 220.07 E-value: 5.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 4 MKAIEAAVCVLEKEGVSVAFGVPgaaINPLYAAmKAHGGIGHILARHVEGASHMAEGYTRAVAG-NIGVCIGTSGPAGTD 82
Cdd:PRK06154 20 MKVAEAVAEILKEEGVELLFGFP---VNELFDA-AAAAGIRPVIARTERVAVHMADGYARATSGeRVGVFAVQYGPGAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 83 MITGLYSASADSIPILCITGQAPRARLHKE-DFQAvdiAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLID 161
Cdd:PRK06154 96 AFGGVAQAYGDSVPVLFLPTGYPRGSTDVApNFES---LRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 162 LPIDV---QLAEIEFDietYEPLPAYKPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTL 238
Cdd:PRK06154 173 LPVDVlaeELDELPLD---HRPSRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 239 MGWGSIPDDHPLMAGMCGL----QTSHRYGNAtmlasDFVLGIGNRWANRHTGSvdVYTKGRKFVHVDIEPTQIGRVFAP 314
Cdd:PRK06154 250 NGKSAFPEDHPLALGSGGRarpaTVAHFLREA-----DVLFGIGCSLTRSYYGL--PMPEGKTIIHSTLDDADLNKDYPI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 315 DYGIVSDAGAALKLFVEVARE--WKAAGRLKDRSGWVAECQgRKNSVEYLRKTQFDDVPMKPQRVYQCMNRNLDKDTCYV 392
Cdd:PRK06154 323 DHGLVGDAALVLKQMIEELRRrvGPDRGRAQQVAAEIEAVR-AAWLAKWMPKLTSDSTPINPYRVVWELQHAVDIKTVII 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 393 S-TIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHV 471
Cdd:PRK06154 402 ThDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTI 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 472 LVNNSYLGLIRQAQRAFSIDYcvqlafdninmdegeASRGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeAWMAEHR 551
Cdd:PRK06154 482 LLNNFSMGGYDKVMPVSTTKY---------------RATDISGDYAAIARALGGYGERVEDPEMLVPALLRA-LRKVKEG 545
|
570
....*....|....*.
gi 317118330 552 TPVVIECILERVTNIS 567
Cdd:PRK06154 546 TPALLEVITSEETALS 561
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-563 |
8.95e-60 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 209.08 E-value: 8.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLEKEGVSVAFGVPGAAINP---LYAAmkahGGIGHILARHVEGASHMAEGYTRaVAGNIGVCIGTSG 77
Cdd:PRK07525 3 KMKMTPSEAFVETLQAHGITHAFGIIGSAFMDasdLFPP----AGIRFIDVAHEQNAGHMADGYTR-VTGRMGMVIGQNG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 78 PAGTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVP----RAFQQAFHLMrsg 153
Cdd:PRK07525 78 PGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAevlnRVFDKAKRES--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 154 rpGPVLIDLPIDVQLAEIefDIETYEPLPAYKPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVP 233
Cdd:PRK07525 155 --GPAQINIPRDYFYGVI--DVEIPQPVRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 234 VIPTLMGWGSIPDDHPLMAGMCGLQTShrygNATM--LA-SDFVLGIGNRWANRHT---GSVDVYTKGRKFVHVDIEPTQ 307
Cdd:PRK07525 231 VACGYLHNDAFPGSHPLWVGPLGYNGS----KAAMelIAkADVVLALGTRLNPFGTlpqYGIDYWPKDAKIIQVDINPDR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 308 IGRVFAPDYGIVSDAGaalklfvEVAREWKAagRLKDRSGWVAECQGRKNSVEYLRK---------TQFDDVP------- 371
Cdd:PRK07525 307 IGLTKKVSVGICGDAK-------AVARELLA--RLAERLAGDAGREERKALIAAEKSaweqelsswDHEDDDPgtdwnee 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 372 --------MKPQRVYQCMNRNLDKDTCYVSTIG-LSQIAGAqFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRI 442
Cdd:PRK07525 378 ararkpdyMHPRQALREIQKALPEDAIVSTDIGnNCSIANS-YLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 443 VALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGlirqAQRAFSIDYcvqlaFDNiNMDEGEASRgyGVDHVKVVEG 522
Cdd:PRK07525 457 VGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWG----AEKKNQVDF-----YNN-RFVGTELDN--NVSYAGIAEA 524
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 317118330 523 LGCKAIRVHHPEDFAPAMRQAEAwMAEHRTPVVIECILERV 563
Cdd:PRK07525 525 MGAEGVVVDTQEELGPALKRAID-AQNEGKTTVIEIMCNQE 564
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-164 |
5.43e-56 |
|
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: 185.81 E-value: 5.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 8 EAAVCVLEKEGVSVAFGVPGAAINPLYAAMkAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDMITGL 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDAL-ARSGIRYILVRHEQGAVGMADGYARA-TGKPGVVLVTSGPGLTNAVTGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317118330 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPI 164
Cdd:cd07035 79 ANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
14-557 |
2.38e-55 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 196.23 E-value: 2.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 14 LEKEGVSVAFGVPGAAINPLYAAMKaHGGIGHILARHVEGASHMAEGYTRaVAGNIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:PRK08617 15 LINQGVKYVFGIPGAKIDRVFDALE-DSGPELIVTRHEQNAAFMAAAIGR-LTGKPGVVLVTSGPGVSNLATGLVTATAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 94 SIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDVQLAEIef 173
Cdd:PRK08617 93 GDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQDVVDAPV-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 174 DIETYEPLPAYKP-AATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGSIPDDH-PLM 251
Cdd:PRK08617 171 TSKAIAPLSKPKLgPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAAGVISRELeDHF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 252 AGMCGL---QTshryGNATMLASDFVLGIG--------NRWANRHTgsvdvytkgRKFVHVDIEPTQIGRVFAPDYGIVS 320
Cdd:PRK08617 251 FGRVGLfrnQP----GDELLKKADLVITIGydpieyepRNWNSEGD---------ATIIHIDVLPAEIDNYYQPERELIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 321 DAGAALKLFVEVAREWkaagRLKDRSgwVAECQGRKNSVE--YLRKTQFDDVPMKPQRVYQCMNRNLDKDTCYVSTIGLS 398
Cdd:PRK08617 318 DIAATLDLLAEKLDGL----SLSPQS--LEILEELRAQLEelAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 399 QIAGAQFLHVYKPRHW-INCGQAgPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVL-VNNS 476
Cdd:PRK08617 392 YIWMARYFRSYEPRHLlFSNGMQ-TLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIwNDGH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 477 YlglirqaqrafsidycvqlafdniNMDEGEASRGYG---------VDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeawM 547
Cdd:PRK08617 471 Y------------------------NMVEFQEEMKYGrssgvdfgpVDFVKYAESFGAKGLRVTSPDELEPVLREA---L 523
|
570
....*....|
gi 317118330 548 AEhRTPVVIE 557
Cdd:PRK08617 524 AT-DGPVVID 532
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
8-561 |
1.25e-53 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 191.58 E-value: 1.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 8 EAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGgIGHILARHVEGAShMAEGYTRAVAGNIGVCIGTSGPAGTDMITGL 87
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSK-VKYVQVRHEEGAA-LAASVEAKITGKPSACMGTSGPGSIHLLNGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRpGPVLIDLPIDVQ 167
Cdd:PRK06457 84 YDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 168 LAEIEFDIETYEPLPAYKPAATRNQAEKAIsmlNEAERPLIVSGGGVInaDASALLVELAELLHVPVIPTLMGWGSIPDD 247
Cdd:PRK06457 163 RKSSEYKGSKNTEVGKVKYSIDFSRAKELI---KESEKPVLLIGGGTR--GLGKEINRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 248 HPLMAGMCGLQTSHRYGNAtMLASDFVLGIGNRWAnrhtgSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDAGAALK 327
Cdd:PRK06457 238 DPKVMGGIGLLGTKPSIEA-MDKADLLIMLGTSFP-----YVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 328 LFVEVAREwKAAGRLK-DRSGWVAECQGRKNSVeylrktqfdDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQFL 406
Cdd:PRK06457 312 IDIEEKSD-KFYEELKgKKEDWLDSISKQENSL---------DKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 407 HVYKPRHWINCGQAGPLGWTVPAALGVRVA-DPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQ 485
Cdd:PRK06457 382 RASGEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQ 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317118330 486 RAFSI-DYCVQLafdninmdegeasrgYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQaeawMAEHRTPVVIECILE 561
Cdd:PRK06457 462 EVMGYpEWGVDL---------------YNPDFTKIAESIGFKGFRLEEPKEAEEIIEE----FLNTKGPAVLDAIVD 519
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
13-172 |
5.35e-53 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 178.58 E-value: 5.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 13 VLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDMITGLYSASA 92
Cdd:pfam02776 8 VLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARA-TGKPGVVLVTSGPGATNALTGLANAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 93 DSIPILCITGQAPRARLHKEDFQA-VDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDVQLAEI 171
Cdd:pfam02776 87 DSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLDVLLEEV 166
|
.
gi 317118330 172 E 172
Cdd:pfam02776 167 D 167
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
10-543 |
1.54e-46 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 171.83 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 10 AVCVLEKEGVSVAFGVPGAAINPLYAAMKaHGGIGHILARHVEGASHMAEGYTRaVAGNIGVCIGTSGPAGTDMITGLYS 89
Cdd:PRK05858 11 AARRLKAHGVDTMFTLSGGHLFPLYDGAR-EEGIRLIDVRHEQTAAFAAEAWAK-LTRVPGVAVLTAGPGVTNGMSAMAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 90 ASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDV--Q 167
Cdd:PRK05858 89 AQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDHafS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 168 LAEIEFDIETYEPLPAyKPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGSIPDD 247
Cdd:PRK05858 169 MADDDGRPGALTELPA-GPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVVPAD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 248 HPLMAGmcglqtshRYGNATMLASDFVLGIGNRWANRHtgSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDAGAALK 327
Cdd:PRK05858 248 HPLAFS--------RARGKALGEADVVLVVGVPMDFRL--GFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 328 LFVEvarewkAAGRLKDRSGWVAECQGRKNSVEYLRKTQFDD--VPMKPQRVYQCMNRNLDKDTCYVSTIG-LSQIAGaQ 404
Cdd:PRK05858 318 ALAG------AGGDRTDHQGWIEELRTAETAARARDAAELADdrDPIHPMRVYGELAPLLDRDAIVIGDGGdFVSYAG-R 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 405 FLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQA 484
Cdd:PRK05858 391 YIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKHP 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 485 QRA-FSIDYCVQLAfdninmdegeasrgYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQA 543
Cdd:PRK05858 471 MEAlYGYDVAADLR--------------PGTRYDEVVRALGGHGELVTVPAELGPALERA 516
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
8-557 |
6.90e-46 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 170.17 E-value: 6.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 8 EAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAvAGNIGVCIGTSGPAGTDMITGL 87
Cdd:PRK07064 7 ELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARV-SGGLGVALTSTGTGAGNAAGAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 88 YSASADSIPILCITGQAPRARLHKED---FQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPI 164
Cdd:PRK07064 86 VEALTAGTPLLHITGQIETPYLDQDLgyiHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 165 DVQLAEIEFDIETyEPLPAYKPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAEllhVPVIPTLMGWGSI 244
Cdd:PRK07064 166 DIQAAEIELPDDL-APVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVDLG---FGVVTSTQGRGVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 245 PDDHPLMAGMCGLQTShryGNATMLASDFVLGIGNRWANRHTGSvdvYTKG--RKFVHVDIEPTQIGRVFAPDYGIVSDA 322
Cdd:PRK07064 242 PEDHPASLGAFNNSAA---VEALYKTCDLLLVVGSRLRGNETLK---YSLAlpRPLIRVDADAAADGRGYPNDLFVHGDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 323 GAALKLFVEvarewKAAGRLKDRSGWVAECQG-RKNSVEYLRKTqfddvpMKPQRVY-QCMNRNLDKDTCYVSTIGLSQI 400
Cdd:PRK07064 316 ARVLARLAD-----RLEGRLSVDPAFAADLRAaREAAVADLRKG------LGPYAKLvDALRAALPRDGNWVRDVTISNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 401 A-GAQFLHVYKPRHWINcGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLG 479
Cdd:PRK07064 385 TwGNRLLPIFEPRANVH-ALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 480 LIRQAQRAfsidYCvqlafdninmdegeASRGYGV-----DHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAwmaeHRTPV 554
Cdd:PRK07064 464 VIRNIQDA----QY--------------GGRRYYVelhtpDFALLAASLGLPHWRVTSADDFEAVLREALA----KEGPV 521
|
...
gi 317118330 555 VIE 557
Cdd:PRK07064 522 LVE 524
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
395-558 |
1.37e-42 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 150.04 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 395 IGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVN 474
Cdd:pfam02775 2 IGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 475 NSYLGLIRQAQRAFSIDYCVQLAFDNinmdegeasrGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAeawmAEHRTPV 554
Cdd:pfam02775 82 NGGYGMTRGQQTPFGGGRYSGPSGKI----------LPPVDFAKLAEAYGAKGARVESPEELEEALKEA----LEHDGPA 147
|
....
gi 317118330 555 VIEC 558
Cdd:pfam02775 148 LIDV 151
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-563 |
6.65e-41 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 156.31 E-value: 6.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAIEAAVCVLE---KEGVSVAFGVPGAAINPLYAAMKAHGGIGH-----ILARHVEGASHMAEGY------TRAVA 66
Cdd:PRK08327 1 SMALTMYTAAELFLEllkELGVDYIFINSGTDYPPIIEAKARARAAGRplpefVICPHEIVAISMAHGYalvtgkPQAVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 67 gnIGVCIGTSGPAGtdmitGLYSASADSIPILCITGQAP---RARL-HKEDF-----QAVDIAAIAKPVTKWATTVLEPA 137
Cdd:PRK08327 81 --VHVDVGTANALG-----GVHNAARSRIPVLVFAGRSPyteEGELgSRNTRihwtqEMRDQGGLVREYVKWDYEIRRGD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 138 QVPRAFQQAFHLMRSGRPGPVLIDLPIDVQLAEIEFDIETYEPLPA-YKPAATRNQAEKAISMLNEAERPLIVSGGGVIN 216
Cdd:PRK08327 154 QIGEVVARAIQIAMSEPKGPVYLTLPREVLAEEVPEVKADAGRQMApAPPAPDPEDIARAAEMLAAAERPVIITWRAGRT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 217 ADASALLVELAELLHVPVI---PTLMgwgSIPDDHPLMAGMcglqtshrYGNATMLASDFVLGIGNR--WANRHTGSVDv 291
Cdd:PRK08327 234 AEGFASLRRLAEELAIPVVeyaGEVV---NYPSDHPLHLGP--------DPRADLAEADLVLVVDSDvpWIPKKIRPDA- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 292 ytkGRKFVHVDIEP--TQIG-RVFAPDYGIVSDAGAALK-LFVEVAREWKAAGRLKD-RSGWVAECQGRknsVEYLRKTQ 366
Cdd:PRK08327 302 ---DARVIQIDVDPlkSRIPlWGFPCDLCIQADTSTALDqLEERLKSLASAERRRARrRRAAVRELRIR---QEAAKRAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 367 F----DDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQiagaQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRI 442
Cdd:PRK08327 376 IerlkDRGPITPAYLSYCLGEVADEYDAIVTEYPFVP----RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 443 VALSGDYDFQFMIEE--LAVGAQFKLPYVHVLVNNSYLGLIRQAQR-------AFSIDYCVQLAFD-NINMDE-GEASRG 511
Cdd:PRK08327 452 IATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLevypegyAARKGTFPGTDFDpRPDFAKiAEAFGG 531
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 317118330 512 YGVdhvkvveglgckaiRVHHPEDFAPAMRQAEAWMAEHRTPVVIECILERV 563
Cdd:PRK08327 532 YGE--------------RVEDPEELKGALRRALAAVRKGRRSAVLDVIVDRV 569
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
14-557 |
4.19e-40 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 154.38 E-value: 4.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 14 LEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGAShMAEGYTRAVAGNIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:PRK09124 13 LEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAA-FAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDCHRN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 94 SIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAfhlMRS--GRPGPVLIDLPIDVQLAEI 171
Cdd:PRK09124 92 HVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIA---MRKaiLNRGVAVVVLPGDVALKPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 172 EfDIETYEPLPAYKPAATRNQAE--KAISMLNEAERPLIVSGGGVinADASALLVELAELLHVPVIPTLMGWGSIPDDHP 249
Cdd:PRK09124 169 P-ERATPHWYHAPQPVVTPAEEElrKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALRGKEHVEYDNP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 250 LMAGMCGLqTSHRYGNATMLASDFVLGIGNRWANRhtgsvDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDAGAALKLF 329
Cdd:PRK09124 246 YDVGMTGL-IGFSSGYHAMMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKATLAAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 330 VEVAREwKAAGRLKDRSgwVAECQGRKNSVEYLRKTQFDDVPMKPQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLHVY 409
Cdd:PRK09124 320 LPLLEE-KTDRKFLDKA--LEHYRKARKGLDDLAVPSDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 410 KPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQRAFS 489
Cdd:PRK09124 397 GKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMKAGG 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317118330 490 IdycVQLAFDNINMDEGEASRGYGVdhvkvveglgcKAIRVHHPEDFAPAMRQAEAwmaeHRTPVVIE 557
Cdd:PRK09124 477 Y---LTDGTDLHNPDFAAIAEACGI-----------TGIRVEKASELDGALQRAFA----HDGPALVD 526
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
14-571 |
1.03e-37 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 147.44 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 14 LEKEGVSVAFGVPGAAINPLyAAMKAHGGIGHILARHVEGAshmaeGYTRAVAGNI----GVCIGTSGPAGTDMITGLYS 89
Cdd:PRK09259 20 LKLNGIDTIYGVVGIPITDL-ARLAQAEGIRYIGFRHEQSA-----GNAAAAAGFLtqkpGVCLTVSAPGFLNGLTALAN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 90 ASADSIPILCITGQAPRA--RLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLPIDVQ 167
Cdd:PRK09259 94 ATTNCFPMIMISGSSEREivDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 168 LAEIEFD------IETYEPLPAYKPAatRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGW 241
Cdd:PRK09259 174 AQTMDADealtslVKVVDPAPAQLPA--PEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSMAK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 242 GSIPDDHPLMAGMCglqtshrygNATMLA-SDFVLGIGNR--WANRHtGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGI 318
Cdd:PRK09259 252 GLLPDTHPQSAAAA---------RSLALAnADVVLLVGARlnWLLSH-GKGKTWGADKKFIQIDIEPQEIDSNRPIAAPV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 319 VSDAGAALKLFVEVArewkAAGRLKDRSGWVAECQGRK--NSVEYLRKTQFDDVPMKPQRVYQCMNRNLDK--DTCYVSt 394
Cdd:PRK09259 322 VGDIGSVMQALLAGL----KQNTFKAPAEWLDALAERKekNAAKMAEKLSTDTQPMNFYNALGAIRDVLKEnpDIYLVN- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 395 iglsqiAGAQFLHV-------YKPRHWINCGQAGPLGWTVPAALGVRVADpERRIVALSGDYDFQFMIEELAVGAQFKLP 467
Cdd:PRK09259 397 ------EGANTLDLarniidmYKPRHRLDCGTWGVMGIGMGYAIAAAVET-GKPVVAIEGDSAFGFSGMEVETICRYNLP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 468 YVHVLVNNS--YLGlirqaqrafsidycvqlafDNINM----DEGEASRGYGVDHVKVVEGLGCKAIRVHHPEDFAPAMR 541
Cdd:PRK09259 470 VTVVIFNNGgiYRG-------------------DDVNLsgagDPSPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALT 530
|
570 580 590
....*....|....*....|....*....|
gi 317118330 542 QAeawMAEHRtPVVIECILERvtniSMGTE 571
Cdd:PRK09259 531 EA---IASGK-PTLINVVIDP----AAGTE 552
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-559 |
3.00e-37 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 145.90 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 1 MARMKAiEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHvEGASHMAEGYTRAVAGNIGVCIGTSGPAG 80
Cdd:PRK06546 1 MAKTVA-EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRH-EEAAAFAAAAEAQLTGKLAVCAGSCGPGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAF-HLMrsGRPGPVL 159
Cdd:PRK06546 79 LHLINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIqHAV--AGGGVSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 160 IDLPIDVQLAEIEfdiETYEPLPAYKPAAT----RNQAEKAISMLNEAERPLIVSGGGVinADASALLVELAELLHVPVI 235
Cdd:PRK06546 157 VTLPGDIADEPAP---EGFAPSVISPRRPTvvpdPAEVRALADAINEAKKVTLFAGAGV--RGAHAEVLALAEKIKAPVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 236 PTLMGWGSIPDDHPLMAGMCGLQTshrYGNAT--MLASDFVLGIGNRWAnrhtgsVDVYTKGRKFVHVDIEPTQIGRVFA 313
Cdd:PRK06546 232 HSLRGKEWIQYDNPFDVGMSGLLG---YGAAHeaMHEADLLILLGTDFP------YDQFLPDVRTAQVDIDPEHLGRRTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 314 PDYGIVSDAGAAL-KLFVEVARewKAAGRLKDRSgwVAECQGRKNSV--EYLRKTQfDDVPMKPQRVYQCMNRNLDKDTC 390
Cdd:PRK06546 303 VDLAVHGDVAETIrALLPLVKE--KTDRRFLDRM--LKKHARKLEKVvgAYTRKVE-KHTPIHPEYVASILDELAADDAV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 391 YVSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVH 470
Cdd:PRK06546 378 FTVDTGMCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 471 VLVNNSYLGLIR-----QAQRAFSIDYcvqlafdninmdegeasrgYGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEA 545
Cdd:PRK06546 458 VVFNNSTLGMVKlemlvDGLPDFGTDH-------------------PPVDYAAIAAALGIHAVRVEDPKDVRGALREAFA 518
|
570
....*....|....
gi 317118330 546 wmaeHRTPVVIECI 559
Cdd:PRK06546 519 ----HPGPALVDVV 528
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
376-559 |
3.49e-37 |
|
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: 135.85 E-value: 3.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 376 RVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMI 455
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 456 EELAVGAQFKLPYVHVLVNNSYLGLIRQAQRAFSIdycvqlafdninmDEGEASRGYGVDHVKVVEGLGCKAIRVHHPED 535
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYG-------------GRVSGTDLSNPDFAALAEAYGAKGVRVEDPED 147
|
170 180
....*....|....*....|....
gi 317118330 536 FAPAMRQAEAwmaeHRTPVVIECI 559
Cdd:cd00568 148 LEAALAEALA----AGGPALIEVK 167
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
14-562 |
4.03e-36 |
|
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: 142.22 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 14 LEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRaVAGnIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYAR-VNG-LGALVTTYGVGELSAINGIAGAYAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 94 SIPILCITG------QAPRARLH----KEDFQAVdiAAIAKPVTKwATTVLEP----AQVPRAFQQAFHLMRsgrpgPVL 159
Cdd:COG3961 93 RVPVVHIVGapgtraQRRGPLLHhtlgDGDFDHF--LRMFEEVTV-AQAVLTPenaaAEIDRVLAAALREKR-----PVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 160 IDLPIDVQLAEIEfdiETYEPLPAYKPAATRNQAEKAI----SMLNEAERPLIVSGGGVINADASALLVELAELLHVPVI 235
Cdd:COG3961 165 IELPRDVADAPIE---PPEAPLPLPPPASDPAALAAAVaaaaERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 236 PTLMGWGSIPDDHPLMAGMCGLQTSHRYGNATMLASDFVLGIGNRWanrhtgsVDVYT-------KGRKFVHVDIEPTQI 308
Cdd:COG3961 242 TTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVF-------TDTNTggftaqlDPERTIDIQPDSVRV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 309 G-RVFAPDYgiVSDAGAALklfvevarewkaAGRLKDRSG-WVAECQGRKNSVEylrktqFDDVPMKPQRVYQCMNRNLD 386
Cdd:COG3961 315 GgHIYPGVS--LADFLEAL------------AELLKKRSApLPAPAPPPPPPPA------APDAPLTQDRLWQRLQAFLD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 387 KDTCYVSTIGLSqIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKL 466
Cdd:COG3961 375 PGDIVVADTGTS-LFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 467 PYVHVLVNNS-YLglirqAQRAF-SIDYcvqlAFDNINMdegeasrgygVDHVKVVEGLGCK---AIRVHHPEDFAPAMR 541
Cdd:COG3961 454 KPIIFVLNNDgYT-----IERAIhGPDG----PYNDIAN----------WDYAKLPEAFGGGnalGFRVTTEGELEEALA 514
|
570 580
....*....|....*....|.
gi 317118330 542 QAEawmAEHRTPVVIECILER 562
Cdd:COG3961 515 AAE---ANTDRLTLIEVVLDK 532
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
194-327 |
1.39e-34 |
|
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: 127.68 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 194 EKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGSIPDDHPLMAGMCGLqTSHRYGNATMLASDF 273
Cdd:pfam00205 2 EKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGM-HGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 317118330 274 VLGIGNRWA-NRHTGSVDVYTKGRKFVHVDIEPTQIGRVFAPDYGIVSDAGAALK 327
Cdd:pfam00205 81 VLAVGARFDdIRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLE 135
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
18-557 |
3.62e-34 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 137.35 E-value: 3.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 18 GVSVAFGVPGAAINPLYAAM-KAHGGIGHILARHVEGASHMAEGYTRaVAGNIGVCIGTSGPAGTDMITGLYSASADSIP 96
Cdd:PRK08273 17 GVRRVFGYPGDGINGLLGALgRADDKPEFVQARHEEMAAFMAVAHAK-FTGEVGVCLATSGPGAIHLLNGLYDAKLDHVP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 97 ILCITGQAPRARLHKEDFQAVDIAAIAKPV-TKWATTVLEPAQVPRAFQQAFHLMRSGRpGPVLIDLPIDVQLAEiefdi 175
Cdd:PRK08273 96 VVAIVGQQARAALGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTALAER-TVTAVILPNDVQELE----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 176 etYEPLP-AYK----------PAATRNQAE--KAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPviPTLMGWG 242
Cdd:PRK08273 170 --YEPPPhAHGtvhsgvgytrPRVVPYDEDlrRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGVA--KALLGKA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 243 SIPDDHPLMAGMCGLQTShRYGNATMLASDFVLGIgnrwanrhtGSVDVYT-------KGRKfVHVDIEPTQIGRVFAPD 315
Cdd:PRK08273 246 ALPDDLPWVTGSIGLLGT-KPSYELMRECDTLLMV---------GSSFPYSeflpkegQARG-VQIDIDGRMLGLRYPME 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 316 YGIVSDAGAALKLFVEVAREwkaagrlKDRSGWVAE-CQGRKNSVEYLRKTQFDDV-PMKPQRVYQCMNRNLDKDTCYVS 393
Cdd:PRK08273 315 VNLVGDAAETLRALLPLLER-------KKDRSWRERiEKWVARWWETLEARAMVPAdPVNPQRVFWELSPRLPDNAILTA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 394 TIGLSQIAGAQFLhvyKPRHWINCGQAGPL---GWTVPAALGVRVADPERRIVALSGDYDFQfM--IEELAVGA----QF 464
Cdd:PRK08273 388 DSGSCANWYARDL---RMRRGMMASLSGTLatmGPAVPYAIAAKFAHPDRPVIALVGDGAMQ-MngMAELITVAkywrQW 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 465 KLPYVHVLV-NNSYLGLIRQAQRAFsidycvqlafdninmdEG----EASRGY-GVDHVKVVEGLGCKAIRVHHPEDFAP 538
Cdd:PRK08273 464 SDPRLIVLVlNNRDLNQVTWEQRVM----------------EGdpkfEASQDLpDVPYARFAELLGLKGIRVDDPEQLGA 527
|
570
....*....|....*....
gi 317118330 539 AMRQAeawMAEHRtPVVIE 557
Cdd:PRK08273 528 AWDEA---LAADR-PVVLE 542
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
8-170 |
4.76e-34 |
|
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: 126.90 E-value: 4.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 8 EAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRaVAGNIGVCIGTSGPAGTDMITGL 87
Cdd:cd07039 4 DVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAK-LTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAfhlMRS--GRPGPVLIDLPID 165
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRA---IRTaiAKRGVAVLILPGD 159
|
....*
gi 317118330 166 VQLAE 170
Cdd:cd07039 160 VQDAP 164
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
8-557 |
1.20e-33 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 134.70 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 8 EAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAhgGIGHILARHVEGASHMAEGYTRAvAGNIGVcIGTSGPAGTDMITG- 86
Cdd:PRK07092 16 DATIDLLRRFGITTVFGNPGSTELPFLRDFPD--DFRYVLGLQEAVVVGMADGYAQA-TGNAAF-VNLHSAAGVGNAMGn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 87 LYSASADSIPILCITGQAPRARLHKEDF-QAVDIAAIAKPVTKWATtvlEPAQ---VPRAFQQAFHLMRSGRPGPVLIDL 162
Cdd:PRK07092 92 LFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSI---EPARaedVPAAIARAYHIAMQPPRGPVFVSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 163 PIDvqlaeiEFDIETyEPLPAYKPAATRNQAEKAI----SMLNEAERPLIVSGGGVINADASALLVELAELLHVPV-IPT 237
Cdd:PRK07092 169 PYD------DWDQPA-EPLPARTVSSAVRPDPAALarlgDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPVwVAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 238 LMGWGSIPDDHPLMAGMcgLQTSHRYGNATMLASDFVLGIGNRWANRHT-GSVDVYTKGRKFVHVDIEPTQIGRVFAPDy 316
Cdd:PRK07092 242 MSGRCSFPEDHPLFAGF--LPASREKISALLDGHDLVLVIGAPVFTYHVeGPGPHLPEGAELVQLTDDPGEAAWAPMGD- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 317 GIVSDAGAALKLFVEVAREWK-AAGRLKDRSGWVAEcqgrknsveylrktqfDDVPMKPQRVYQCMNRNLDKDTCYV--- 392
Cdd:PRK07092 319 AIVGDIRLALRDLLALLPPSArPAPPARPMPPPAPA----------------PGEPLSVAFVLQTLAALRPADAIVVeea 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 393 -STIGLSQiagaQFLHVYKPRHWINcGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHV 471
Cdd:PRK07092 383 pSTRPAMQ----EHLPMRRQGSFYT-MASGGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 472 LVNNSYLGLIRQAQRAFSIDYCVQLAFDninmdegeasrgyGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAwmaeHR 551
Cdd:PRK07092 458 ILNNGRYGALRWFAPVFGVRDVPGLDLP-------------GLDFVALARGYGCEAVRVSDAAELADALARALA----AD 520
|
....*.
gi 317118330 552 TPVVIE 557
Cdd:PRK07092 521 GPVLVE 526
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
373-568 |
1.04e-32 |
|
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: 124.15 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 373 KPQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQ 452
Cdd:cd02015 2 KPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 453 FMIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQRAFsidycvqlaFDNINMdegEASRGYGVDHVKVVEGLGCKAIRVHH 532
Cdd:cd02015 82 MNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELF---------YEGRYS---HTTLDSNPDFVKLAEAYGIKGLRVEK 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 317118330 533 PEDFAPAMRQAeawmAEHRTPVVIECILERVTNISM 568
Cdd:cd02015 150 PEELEAALKEA----LASDGPVLLDVLVDPEENVLP 181
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
48-556 |
7.93e-32 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 443162 [Multi-domain] Cd Length: 622 Bit Score: 130.25 E-value: 7.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 48 ARHVEGASHMAEGYTRAVagN---IGVCIGTSGPAGTDMITGLYSASADSIPILCITG-----QAPRARLHK-EDFQAVD 118
Cdd:COG3962 63 GRNEQGMAHAAIAYAKQK--NrrrIMACTSSIGPGATNMVTAAALATANRLPVLLLPGdtfatRQPDPVLQQlEHFHDPT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 119 IAA--IAKPVTKWATTVLEPAQVPRAFQQAFHLMRSgrP---GPVLIDLPIDVQlAEiEFDietYeplPAY--------- 184
Cdd:COG3962 141 ISVndAFRPVSRYWDRITRPEQLMSALPRAMRVLTD--PaetGAVTLALPQDVQ-AE-AYD---Y---PESffakrvhri 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 185 -KPAATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVIPTLMGWGSIPDDHPLMAGMCGLqTSHRY 263
Cdd:COG3962 211 rRPPPDPAELARAVELIRAAKRPLIIAGGGVRYSEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLGGIGV-TGTLA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 264 GNAtmLAS--DFVLGIGNRWANRHTGSVDVYT-KGRKFVHVDIEPTQIGRVFApdYGIVSDAGAALKLFVEVAREWKAag 340
Cdd:COG3962 290 ANA--LAAeaDLVIGVGTRLQDFTTGSKTLFAnPDVRFVNINVARFDAYKHDA--LPVVADAREGLEALTEALAGWRY-- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 341 rlkdRSGWVAECQGRKNS----VEYLRKTQFDDVPMKPQrVYQCMNRNLDKDTCYVSTIGlSQIAGaqfLHvykpRHWiN 416
Cdd:COG3962 364 ----PAAWTDEAAELKAEwdaeVDRLYAPTNGGLPTQAQ-VIGAVNEAAGPDDIVVCAAG-SLPGD---LH----KLW-R 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 417 CGQAGP---------LGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQRA 487
Cdd:COG3962 430 TRDPGTyhveygyscMGYEIAGGLGVKLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKIIVVLLDNHGFGCINRLQMS 509
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317118330 488 F-SIDYCVQLAFDNI--NMDEGEASRgygVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAwmaeHRTPVVI 556
Cdd:COG3962 510 TgSQSFGTELRDRDTetGRLDGGLLP---VDFAANAASLGAKAYRVTTIAELRAALERAKA----ADRTTVI 574
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
371-562 |
2.47e-28 |
|
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: 111.47 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 371 PMKPQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYD 450
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 451 FQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQRAFS-IDYCVQLafdninmdegeasrgYGVDHVKVVEGLGCKAIR 529
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGqPEFGVDL---------------PNPDFAKIAEAMGIKGIR 145
|
170 180 190
....*....|....*....|....*....|...
gi 317118330 530 VHHPEDFAPAMRQAEAwmaeHRTPVVIECILER 562
Cdd:cd02014 146 VEDPDELEAALDEALA----ADGPVVIDVVTDP 174
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
13-163 |
1.63e-23 |
|
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: 97.03 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 13 VLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYtrAVAGNIGVCIGTSGPAGTDMITGLYSASA 92
Cdd:cd06586 6 VLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGY--ARAGGPPVVIVTSGTGLLNAINGLADAAA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 317118330 93 DSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGrPGPVLIDLP 163
Cdd:cd06586 84 EHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLP 153
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
374-561 |
3.19e-23 |
|
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: 96.83 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 374 PQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYDFQF 453
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 454 MIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQRafsidycvqlafDNINMDEGEASRGYGVDHVKVVEGLGCKAIRVHHP 533
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQ------------LSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTP 148
|
170 180
....*....|....*....|....*...
gi 317118330 534 EDFAPAMRQAEAwmaeHRTPVVIECILE 561
Cdd:cd02004 149 EELKPALKRALA----SGKPALINVIID 172
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
371-562 |
1.66e-20 |
|
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: 89.88 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 371 PMKPQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLHVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYD 450
Cdd:cd02013 3 PMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 451 FQFMIEELAVGAQFKLPYVHVLVNNSYLGlirqAQRAFSIDycvqlaFDNINMDEGEASrgyGVDHVKVVEGLGCKAIRV 530
Cdd:cd02013 83 WGMSMMEIMTAVRHKLPVTAVVFRNRQWG----AEKKNQVD------FYNNRFVGTELE---SESFAKIAEACGAKGITV 149
|
170 180 190
....*....|....*....|....*....|..
gi 317118330 531 HHPEDFAPAMRQAEAWMAEHRTpVVIECILER 562
Cdd:cd02013 150 DKPEDVGPALQKAIAMMAEGKT-TVIEIVCDQ 180
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
404-560 |
1.23e-19 |
|
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: 86.50 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 404 QFLHVYKPRHWINCGqAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLP-YVHVLVNNSYLGLiR 482
Cdd:cd02002 33 DQLPLTRPGSYFTLR-GGGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALWTAARYGLPvTVVILNNRGYGAL-R 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317118330 483 QAQRAFSIDYCVQLAFDNINMDEGeasrgyGVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAwmaeHRTPVVIECIL 560
Cdd:cd02002 111 SFLKRVGPEGPGENAPDGLDLLDP------GIDFAAIAKAFGVEAERVETPEELDEALREALA----EGGPALIEVVV 178
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
374-558 |
2.14e-19 |
|
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: 85.80 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 374 PQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLHVYKPRH-WINCGQAgPLGWTVPAALGVRVADPERRIVALSGDYDFQ 452
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTcLISNGLA-TMGVALPGAIGAKLVYPDRKVVAVSGDGGFM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 453 FMIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQ-----RAFSIDycvqlaFDNInmdegeasrgygvDHVKVVEGLGCKA 527
Cdd:cd02010 80 MNSQELETAVRLKIPLVVLIWNDNGYGLIKWKQekeygRDSGVD------FGNP-------------DFVKYAESFGAKG 140
|
170 180 190
....*....|....*....|....*....|.
gi 317118330 528 IRVHHPEDFAPAMRQAeawMAEHrTPVVIEC 558
Cdd:cd02010 141 YRIESADDLLPVLERA---LAAD-GVHVIDC 167
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
371-562 |
1.72e-14 |
|
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: 71.80 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 371 PMKPQRVYQCMNRNLDKDTCYVSTIGLSQIAGAQFLhVYKPRHWINCGQAGPLGWTVPAALGVRVADPERRIVALSGDYD 450
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLK-LPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 451 FQFMIEELAVGAQFKL-PYVHVLVNNSYlglirqaqrafSIDYCVQ---LAFDNINMdegeasrgygVDHVKVVEGLGC- 525
Cdd:cd02005 80 FQMTVQELSTMIRYGLnPIIFLINNDGY-----------TIERAIHgpeASYNDIAN----------WNYTKLPEVFGGg 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 317118330 526 ---KAIRVHHPEDFAPAMRQAEawmAEHRTPVVIECILER 562
Cdd:cd02005 139 gggLSFRVKTEGELDEALKDAL---FNRDKLSLIEVILPK 175
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
423-557 |
1.08e-12 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 67.33 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 423 LGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQAQRAFSID-------YCVQ 495
Cdd:cd02003 50 MGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGsfgtefrDRDQ 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317118330 496 lafdNINMDEGEASRgygVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAwmaeHRTPVVIE 557
Cdd:cd02003 130 ----ESGQLDGALLP---VDFAANARSLGARVEKVKTIEELKAALAKAKA----SDRTTVIV 180
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
4-560 |
3.01e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 56.42 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 4 MKAIEAAVCVLEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRaVAGNIGVCIGTSGPAGTDM 83
Cdd:PRK12474 5 MNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGR-IAGKPAVTLLHLGPGLANG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHLMRSGRPGPVLIDLP 163
Cdd:PRK12474 84 LANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 164 IDVQLAEIEFdieTYEPLPAYKP------------AATRNQAEKAISMLNEAERPLIVSGGGVINADASALLVELAELLH 231
Cdd:PRK12474 164 ADVAWNEAAY---AAQPLRGIGPapvaaetveriaALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVRLYCDTFAPR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 232 vpvipTLMGWGSIPddhplmagMCGLQTSHRYGNATMLASDFVLGIGnrwanrhtgsvdvytkGRKFVHVDIEPTQIGRV 311
Cdd:PRK12474 241 -----IERGAGRVP--------IERIPYFHEQITAFLKDVEQLVLVG----------------AKPPVSFFAYPGKPSWG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 312 FAPDYGIVSDAGAALKLfvEVAREWKAAGRlkdrsgwvaecqgrknsveylrktqfdDVPMKPQRVYQCMNRNLDKDTcy 391
Cdd:PRK12474 292 APPGCEIVYLAQPDEDL--AQALQDLADAV---------------------------DAPAEPAARTPLALPALPKGA-- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 392 vstigLSQIAGAQFLHVYKPRHWINCGQA------------------------GPLGWTVPAALGVRVADPERRIVALSG 447
Cdd:PRK12474 341 -----LNSLGVAQLIAHRTPDQAIYADEAltsglffdmsydrarphthlpltgGSIGQGLPLAAGAAVAAPDRKVVCPQG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 448 DYDFQFMIEELAVGAQFKLPYVHVL-VNNSYLGLIRQAQRAfsidyCVQLAFDN----INMDEGEasrgygVDHVKVVEG 522
Cdd:PRK12474 416 DGGAAYTMQALWTMARENLDVTVVIfANRSYAILNGELQRV-----GAQGAGRNalsmLDLHNPE------LNWMKIAEG 484
|
570 580 590
....*....|....*....|....*....|....*...
gi 317118330 523 LGCKAIRVHHPEDFApamRQAEAWMAEhRTPVVIECIL 560
Cdd:PRK12474 485 LGVEASRATTAEEFS---AQYAAAMAQ-RGPRLIEAMI 518
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
18-475 |
2.04e-07 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 53.94 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 18 GVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRAVAgnIGVCIGTSGPAGTDMITGLYSASADSIPI 97
Cdd:PLN02573 30 GVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARG--VGACVVTFTVGGLSVLNAIAGAYSENLPV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 98 LCITGqAPRAR-------LHKE----DF-QAVdiaAIAKPVTKWATTV--LEPA--QVPRAFQQAFHlmrsgRPGPVLID 161
Cdd:PLN02573 108 ICIVG-GPNSNdygtnriLHHTiglpDFsQEL---RCFQTVTCYQAVInnLEDAheLIDTAISTALK-----ESKPVYIS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 162 lpIDVQLAEIEFDIETYEPLPAYKPAATRNQA------EKAISMLNEAERPLIVSGGGVINADASALLVELAELLHVPVI 235
Cdd:PLN02573 179 --VSCNLAAIPHPTFSREPVPFFLTPRLSNKMsleaavEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADASGYPVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 236 PTLMGWGSIPDDHPLMAGMCGLQTSHRYGNATMLASDFVLGIGNRWANRHTGSVDVYTKGRKFVHVDIEPTQIGRvfAPD 315
Cdd:PLN02573 257 VMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGN--GPA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 316 YGIVsdagaALKLFVEVArewkaAGRLKdrsgwvaecqgrKNS---VEYLRKTQFDDVPMK-----PQRV---YQCMNRN 384
Cdd:PLN02573 335 FGCV-----LMKDFLEAL-----AKRVK------------KNTtayENYKRIFVPEGEPLKsepgePLRVnvlFKHIQKM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 385 LDKDTCYVSTIGLSqiagaqFLHVYKPRHWINCG-----QAGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELA 459
Cdd:PLN02573 393 LSGDTAVIAETGDS------WFNCQKLKLPEGCGyefqmQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVS 466
|
490
....*....|....*.
gi 317118330 460 VGAQFKLPYVHVLVNN 475
Cdd:PLN02573 467 TMIRCGQKSIIFLINN 482
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
14-164 |
1.53e-06 |
|
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: 48.26 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 14 LEKEGVSVAFGVPGAAINPLYAAMKAHGGIGHILARHVEGASHMAEGYTRaVAGnIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYAR-VKG-LGALVTTYGVGELSALNGIAGAYAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 94 SIPILCITG------QAPRARLH----KEDFQAvdIAAIAKPVTKwATTVLE-----PAQVPRAFQQAFHLMRsgrpgPV 158
Cdd:cd07038 85 HVPVVHIVGapstkaQASGLLLHhtlgDGDFDV--FLKMFEEITC-AAARLTdpenaAEEIDRVLRTALRESR-----PV 156
|
....*.
gi 317118330 159 LIDLPI 164
Cdd:cd07038 157 YIEIPR 162
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
26-164 |
1.97e-06 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) 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. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 47.88 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 26 PGAAINPLYAAMKAHGGIghILARHVE--GASHMAEGYTRAvAGNIGVCIGTSGPAGTDMITGLYSASADSIPILCITGQ 103
Cdd:cd07037 19 PGSRSAPLALAAAEHPEF--RLHVRVDerSAAFFALGLAKA-SGRPVAVVCTSGTAVANLLPAVVEAYYSGVPLLVLTAD 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 317118330 104 APRARLHKEDFQAVDIAAIAKPVTKWATTVLEP------AQVPRAFQQAFHLMRSGRPGPVLIDLPI 164
Cdd:cd07037 96 RPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPeddddlWYLLRLANRAVLEALSAPPGPVHLNLPF 162
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
411-557 |
8.25e-06 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 48.69 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317118330 411 PRH-WI-NCGqaGPLGWTVPAALGVRVADPERRIVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNsylglirqaqRAF 488
Cdd:PRK07586 375 APHdWLtLTG--GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFAN----------RAY 442
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317118330 489 SIdycVQLAFDNINMDE-GEASRGY------GVDHVKVVEGLGCKAIRVHHPEDFAPAMRQAEAwmaeHRTPVVIE 557
Cdd:PRK07586 443 AI---LRGELARVGAGNpGPRALDMldlddpDLDWVALAEGMGVPARRVTTAEEFADALAAALA----EPGPHLIE 511
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
110-165 |
9.17e-04 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 42.28 E-value: 9.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 317118330 110 HKEDFQAVDIAAIAKPVTKWATTVLEPAQVPRAFQQAFHlmrsgRPGPVLIDLPID 165
Cdd:PRK06546 480 FGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFA-----HPGPALVDVVTD 530
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
421-448 |
3.54e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 39.04 E-value: 3.54e-03
10 20
....*....|....*....|....*...
gi 317118330 421 GPLGWTVPAALGVRVADPERRIVALSGD 448
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGD 84
|
|
| |
