|
Name |
Accession |
Description |
Interval |
E-value |
| Gcl |
COG3960 |
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism]; |
2-591 |
0e+00 |
|
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443160 [Multi-domain] Cd Length: 588 Bit Score: 1305.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 2 AKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARHGNIGVCIGTSGPAGT 81
Cdd:COG3960 1 ARMRAVDAAVAVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHVLARHVEGASHMAEGYTRAKAGNIGVCIGTSGPAGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 82 DMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLID 161
Cdd:COG3960 81 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVLEPAQVPRVFQQAFHLMRSGRPGPVLID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 162 LPVDVQLAEIEFDPETYEPLSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGW 241
Cdd:COG3960 161 LPIDVQMAEIEFDIDTYEPLPVYKPAATRAQIEKALDMLNAAERPLIVAGGGIINADASDLLVEFAELTGVPVIPTLMGW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 242 GVIPDDHPLMAGMCGLQTSHRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSD 321
Cdd:COG3960 241 GSIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRWANRHTGSLDVYTKGRKFVHVDIEPTQIGRVFAPDLGIVSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 322 AGAALKLFLDVATEWKTAGKLRDWSAWAEECRERKRSMLRKTHFDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGA 401
Cdd:COG3960 321 AKAALELFVEVARERKAAGKLPDRSAWAAECQERKRTMLRKTHFDNVPIKPQRVYEEMNKAFGRDTRYVSTIGLSQIAAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 402 QFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQ 481
Cdd:COG3960 401 QFLHVYKPRHWINCGQAGPLGWTIPAALGVVAADPDRPVVALSGDYDFQFMIEELAVGAQFKLPYIHVVVNNSYLGLIRQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 482 AQRGFNMDFEVSLAFENINAdgDAEKGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQALMEEHQVPVVIEFILERVT 561
Cdd:COG3960 481 AQRGFDMDYCVQLAFENINA--PELGGYGVDHVKVAEGLGCKAIRVTDPEEIAPAFEEAKALMAEHRVPVVVEVILERVT 558
|
570 580 590
....*....|....*....|....*....|
gi 429555433 562 NIAMGADINAVVEFEELAERGEDAPTAIAA 591
Cdd:COG3960 559 NISMGTEIDNVNEFEELAESPADAPTAIAL 588
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-592 |
0e+00 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 1299.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARHGNIGVCIGTSGPAG 80
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIGVCIGTSGPAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLI 160
Cdd:PRK11269 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIEFDPETYEPLSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMG 240
Cdd:PRK11269 161 DLPFDVQVAEIEFDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 241 WGVIPDDHPLMAGMCGLQTSHRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVS 320
Cdd:PRK11269 241 WGAIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 321 DAGAALKLFLDVATEWKTAGKLRDWSAWAEECRERKRSMLRKTHFDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIAG 400
Cdd:PRK11269 321 DAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQIAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 401 AQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIR 480
Cdd:PRK11269 401 AQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 481 QAQRGFNMDFEVSLAFENINADGDAekGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQALMEEHQVPVVIEFILERV 560
Cdd:PRK11269 481 QAQRAFDMDYCVQLAFENINSPELN--GYGVDHVKVAEGLGCKAIRVFKPEDIAPALEQAKALMAEFRVPVVVEVILERV 558
|
570 580 590
....*....|....*....|....*....|..
gi 429555433 561 TNIAMGADINAVVEFEELAERGEDAPTAIAAL 592
Cdd:PRK11269 559 TNISMGTEIDAVNEFEELADNAADAPTAIMLL 590
|
|
| glyox_carbo_lig |
TIGR01504 |
glyoxylate carboligase; Glyoxylate carboligase, also called tartronate-semialdehyde synthase, ... |
2-589 |
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: 1124.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 2 AKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARHGNIGVCIGTSGPAGT 81
Cdd:TIGR01504 1 ARMRAVDAAVYVLEKEGITTAFGVPGAAINPFYSALKAHGGIRHILARHVEGASHMAEGYTRATAGNIGVCIGTSGPAGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 82 DMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLID 161
Cdd:TIGR01504 81 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 162 LPVDVQLAEIEFDPETYEPLSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGW 241
Cdd:TIGR01504 161 LPFDVQVAEIEFDPDTYEPLPVYKPAATRAQIEKAVEMLNAAERPLIVAGGGVINADAADLLQEFAELTGVPVIPTLMGW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 242 GVIPDDHPLMAGMCGLQTSHRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSD 321
Cdd:TIGR01504 241 GCIPDDHELMAGMVGLQTSHRYGNATLLESDFVFGIGNRWANRHTGSVDVYTEGRKFVHVDIEPTQIGRVFAPDLGIVSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 322 AGAALKLFLDVATEWKTAGKLRDWSAWAEECRERKRSMLRKTHFDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGA 401
Cdd:TIGR01504 321 AKAALKLLVEVAQELKKAGRLPDRSEWAADCQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAGA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 402 QFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQ 481
Cdd:TIGR01504 401 QMLHVYKPRHWINCGQAGPLGWTIPAALGVCAADPKRNVVALSGDYDFQFMIEELAVGAQHNIPYIHVLVNNAYLGLIRQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 482 AQRGFNMDFEVSLAFENINAdgDAEKGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQALMEEHQVPVVIEFILERVT 561
Cdd:TIGR01504 481 AQRAFDMDYCVQLAFENINS--SEVNGYGVDHVKVAEGLGCKAIRVFKPEEIAPAFEQAKALMAEHRVPVVVEVILERVT 558
|
570 580
....*....|....*....|....*...
gi 429555433 562 NIAMGADINAVVEFEELAERGEDAPTAI 589
Cdd:TIGR01504 559 NISMGSEIDNVVEFEDLADNAADAPTAT 586
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
2-567 |
0e+00 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 549.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 2 AKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGT 81
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARAT-GKPGVCLVTSGPGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 82 DMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLID 161
Cdd:COG0028 80 NLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 162 LPVDVQLAEIEFDPETYEpLSAYKP--AATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLM 239
Cdd:COG0028 160 IPKDVQAAEAEEEPAPPE-LRGYRPrpAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 240 GWGVIPDDHPLMAGMCGLQtSHRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIV 319
Cdd:COG0028 239 GKGAFPEDHPLYLGMLGMH-GTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 320 SDAGAALKLFLDVATEwktagKLRDWSAWAEECRERKRSMLRKTHFDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIA 399
Cdd:COG0028 318 GDAKAVLAALLEALEP-----RADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 400 GAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLI 479
Cdd:COG0028 393 AARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 480 RQAQRGF--NMDFEVSLAfeninadgdaekgyGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlmeeHQVPVVIEFIL 557
Cdd:COG0028 473 RQWQELFygGRYSGTDLP--------------NPDFAKLAEAFGAKGERVETPEELEAALEEALA----SDGPALIDVRV 534
|
570
....*....|
gi 429555433 558 ERVTNIAMGA 567
Cdd:COG0028 535 DPEENPPGAT 544
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
4-563 |
2.54e-155 |
|
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: 457.26 E-value: 2.54e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 4 MRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDM 83
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARAS-GKVGVVLVTSGPGATNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 84 ITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLP 163
Cdd:TIGR00118 80 VTGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 164 VDVQLAEIEFDPETYEPLSAYKPAAT--RAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGW 241
Cdd:TIGR00118 160 KDVTTAEIEYPYPEKVNLPGYRPTVKghPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 242 GVIPDDHPLMAGMCGLQTShRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSD 321
Cdd:TIGR00118 240 GSFPEDHPLSLGMLGMHGT-KTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 322 AGAALKLFLDVATEWKTagklRDWSAWAEECRE-RKRSMLRKTHfDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIAG 400
Cdd:TIGR00118 319 ARNVLEELLKKLFELKE----RKESAWLEQINKwKKEYPLKMDY-TEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 401 AQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIR 480
Cdd:TIGR00118 394 AQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 481 QAQRGFnmdFEVSLAFENINAdgdaekgyGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQalmeEHQVPVVIEFILERV 560
Cdd:TIGR00118 474 QWQELF---YEERYSHTHMGS--------LPDFVKLAEAYGIKGIRIEKPEELDEKLKEAL----SSNEPVLLDVVVDKP 538
|
...
gi 429555433 561 TNI 563
Cdd:TIGR00118 539 ENV 541
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-577 |
8.60e-145 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 430.35 E-value: 8.60e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGsIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAG 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD-LRHILVRHEQAAAHAADGYARAT-GKVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLI 160
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIEFD-PETYEpLSAYKP--AATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPT 237
Cdd:PRK06048 163 DLPKDVTTAEIDFDyPDKVE-LRGYKPtyKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 238 LMGWGVIPDDHPLMAGMCGLQTShRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFG 317
Cdd:PRK06048 242 LMGIGAIPTEHPLSLGMLGMHGT-KYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 318 IVSDAGAALKlfldvatEWKTAGKLRDWSAWAEECRERKRSMLRKTHFDQTPLKPQRVYEEMNKILgRDTCYVSTIGLSQ 397
Cdd:PRK06048 321 IVGDAKQVLK-------SLIKYVQYCDRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELC-PDAIIVTEVGQHQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 398 IAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLG 477
Cdd:PRK06048 393 MWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 478 LIRQAQRGFnmdFEVSLAFENInadgdaekGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQalmeEHQVPVVIEFIL 557
Cdd:PRK06048 473 MVRQWQELF---YDKRYSHTCI--------KGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAV----ASDRPVVIDFIV 537
|
570 580
....*....|....*....|....
gi 429555433 558 ERVTNIA----MGADINAVVEFEE 577
Cdd:PRK06048 538 ECEENVSpmvpAGAAINEILDLEE 561
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
363-566 |
1.02e-142 |
|
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: 411.29 E-value: 1.02e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 363 THFDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVA 442
Cdd:cd02006 1 THFDDVPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 443 LSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQAQRGFNMDFEVSLAFENINADGdaEKGYGVDHVAVAEGLGC 522
Cdd:cd02006 81 LSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAFDMDYQVNLAFENINSSE--LGGYGVDHVKVAEGLGC 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 429555433 523 KAIRVRSPNEFADAFDRAQALMEEHQVPVVIEFILERVTNIAMG 566
Cdd:cd02006 159 KAIRVTKPEELAAAFEQAKKLMAEHRVPVVVEAILERVTNISMG 202
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-556 |
2.40e-133 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 402.82 E-value: 2.40e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAG 80
Cdd:PRK07789 28 PERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQAT-GRVGVCMATSGPGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLI 160
Cdd:PRK07789 107 TNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIEFD-PETYEpLSAYKPaATRA---QAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVP 236
Cdd:PRK07789 187 DIPKDALQAQTTFSwPPRMD-LPGYRP-VTKPhgkQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 237 TLMGWGVIPDDHPLMAGMCGLqtshrYGN----ATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVF 312
Cdd:PRK07789 265 TLMARGAFPDSHPQHLGMPGM-----HGTvaavAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 313 APDFGIVSDAGAALKLFLDVATEWKTAGKLRDWSAWAEECRErkrsmLRKTH---FDQTP---LKPQRVYEEMNKILGRD 386
Cdd:PRK07789 340 HADVPIVGDVKEVIAELIAALRAEHAAGGKPDLTAWWAYLDG-----WRETYplgYDEPSdgsLAPQYVIERLGEIAGPD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 387 TCYVSTIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPY 466
Cdd:PRK07789 415 AIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPI 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 467 LHVVVNNSYLGLIRQAQrgfnmdfevSLAFEN--INADGDAEKGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQALm 544
Cdd:PRK07789 495 KVALINNGNLGMVRQWQ---------TLFYEErySNTDLHTHSHRIPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAI- 564
|
570
....*....|..
gi 429555433 545 eeHQVPVVIEFI 556
Cdd:PRK07789 565 --NDRPVVIDFV 574
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
4-554 |
4.12e-129 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 391.04 E-value: 4.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 4 MRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRaRGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDM 83
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALY-DSDLIHILTRHEQAAAHAADGYARAS-GKVGVCVATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 84 ITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLP 163
Cdd:PRK06276 79 VTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 164 VDVQlaEIEFDPETYE-----PLSAYKPaATRA---QAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVV 235
Cdd:PRK06276 159 KDVQ--EGELDLEKYPipakiDLPGYKP-TTFGhplQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 236 PTLMGWGVIPDDHPL---MAGMCGLQTShrygNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVF 312
Cdd:PRK06276 236 TTLMGKGAFPEDHPLalgMVGMHGTKAA----NYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 313 APDFGIVSDAGAALKLFLDVATEwktaGKLRDWSAWAEECRERKRSMLRKTHFDQTPLKPQRVYEEMNKIL-----GRDT 387
Cdd:PRK06276 312 RVDVPIVGDAKNVLRDLLAELMK----KEIKNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLreidpSKNT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 388 CYVSTIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYL 467
Cdd:PRK06276 388 IITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 468 HVVVNNSYLGLIRQAQRGF--NMDFEVSLafeninadgdaekGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQALME 545
Cdd:PRK06276 468 ICIFDNRTLGMVYQWQNLYygKRQSEVHL-------------GETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGE 534
|
....*....
gi 429555433 546 EHQVPVVIE 554
Cdd:PRK06276 535 PYLLDIIID 543
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
8-562 |
1.33e-123 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 377.85 E-value: 1.33e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 8 DAAVYVLEKEGIDCAFGVPGAAINPFYSAL---RARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMI 84
Cdd:PRK07418 23 YALMDSLKRHGVKHIFGYPGGAILPIYDELykaEAEGWLKHILVRHEQGAAHAADGYARAT-GKVGVCFGTSGPGATNLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 85 TGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLPV 164
Cdd:PRK07418 102 TGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 165 DVQLAEIEFDPetYEP----LSAYKP--AATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTL 238
Cdd:PRK07418 182 DVGQEEFDYVP--VEPgsvkPPGYRPtvKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTTL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 239 MGWGVIPDDHPLMAGMCGLQTShRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGI 318
Cdd:PRK07418 260 MGKGAFDEHHPLSVGMLGMHGT-AYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVPI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 319 VSDAGAALKLFLDVATEWKTAGKLRdwsAWAEECRERKRSMLRKTHFDQTPLKPQRVYEEMNKiLGRDTCYVSTIGLSQI 398
Cdd:PRK07418 339 VGDVRKVLVKLLERSLEPTTPPRTQ---AWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRD-LAPDAYYTTDVGQHQM 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 399 AGAQFLHvYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGL 478
Cdd:PRK07418 415 WAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGM 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 479 IRQAQRGFnmdfevslaFENINADGDAEKGYGvDHVAVAEGLGCKAIRVRSPNEFADAFdrAQALmeEHQVPVVIEFILE 558
Cdd:PRK07418 494 VRQWQESF---------YGERYSASNMEPGMP-DFVKLAEAFGVKGMVISERDQLKDAI--AEAL--AHDGPVLIDVHVR 559
|
....
gi 429555433 559 RVTN 562
Cdd:PRK07418 560 RDEN 563
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
14-559 |
6.35e-122 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 371.85 E-value: 6.35e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 14 LEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:PRK07282 20 LRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKST-GKLGVAVVTSGPGATNAITGIADAMSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 94 SIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLPVDVQLAEIEF 173
Cdd:PRK07282 99 SVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKDVSALETDF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 174 --DPETYEPlsAYKPA--ATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGVIPDDHP 249
Cdd:PRK07282 179 iyDPEVNLP--SYQPTlePNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 250 LMAGMCGLQTSHRyGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSDAGAALKLF 329
Cdd:PRK07282 257 LFLGMGGMHGSYA-ANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKKALQML 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 330 LDvatEWKTAGKLRDWSAWAEECRERKRSMlrktHFDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKP 409
Cdd:PRK07282 336 LA---EPTVHNNTEKWIEKVTKDKNRVRSY----DKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 410 RNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQAQRGFNMD 489
Cdd:PRK07282 409 RQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESFYEG 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 490 FEVSLAFeninadgDAEKGYGVdhvaVAEGLGCKAIRVRSPNEFADAFdraQALMEEhqVPVVIEFILER 559
Cdd:PRK07282 489 RTSESVF-------DTLPDFQL----MAQAYGIKHYKFDNPETLAQDL---EVITED--VPMLIEVDISR 542
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
14-563 |
5.77e-120 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 366.73 E-value: 5.77e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 14 LEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:PRK08527 13 LKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARAS-GKVGVAIVTSGPGFTNAVTGLATAYMD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 94 SIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLPVDVQLAEIEF 173
Cdd:PRK08527 92 SIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPKDVTATLGEF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 174 D-PETYEpLSAYKPA--ATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGVIPDDHPL 250
Cdd:PRK08527 172 EyPKEIS-LKTYKPTykGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMARGVLRSDDPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 251 MAGMCGLQTSHRyGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSDAGAALKLFL 330
Cdd:PRK08527 251 LLGMLGMHGSYA-ANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGDLKNVLKEML 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 331 DVATEWKTAgklrDWSAWAEECRERKRSMLRKTHFDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKPR 410
Cdd:PRK08527 330 EELKEENPT----TYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 411 NWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQAQRGFnmdf 490
Cdd:PRK08527 406 QLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQWQTFF---- 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429555433 491 evslaFENINADGDAEkgYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQalmeEHQVPVVIEFILERVTNI 563
Cdd:PRK08527 482 -----YEERYSETDLS--TQPDFVKLAESFGGIGFRVTTKEEFDKALKEAL----ESDKVALIDVKIDRFENV 543
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
4-563 |
3.18e-117 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 359.67 E-value: 3.18e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 4 MRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGsIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDM 83
Cdd:PRK06725 15 VTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARAS-GKVGVVFATSGPGATNL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 84 ITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLP 163
Cdd:PRK06725 93 VTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 164 VDVQLAEIEFD-PETYEpLSAYKPAAT--RAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMG 240
Cdd:PRK06725 173 KDVQNEKVTSFyNEVVE-IPGYKPEPRpdSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 241 WGVIPDDHPLMAGMCGLQTSHRyGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVS 320
Cdd:PRK06725 252 LGAYPPGDPLFLGMLGMHGTYA-ANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 321 DAGAALKLFLDVATEWKTAGKLRDWSAWAEEcrerkrsmlRKTHFDQTP--LKPQRVYEEMNKILGRDTCYVSTIGLSQI 398
Cdd:PRK06725 331 DVKKALHMLLHMSIHTQTDEWLQKVKTWKEE---------YPLSYKQKEseLKPQHVINLVSELTNGEAIVTTEVGQHQM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 399 AGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGL 478
Cdd:PRK06725 402 WAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGM 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 479 IRQAQRGFnmdFEVSLAFENINADgdaekgygvDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlmeeHQVPVVIEFILE 558
Cdd:PRK06725 482 VRQWQEMF---YENRLSESKIGSP---------DFVKVAEAYGVKGLRATNSTEAKQVMLEAFA----HEGPVVVDFCVE 545
|
....*
gi 429555433 559 RVTNI 563
Cdd:PRK06725 546 EGENV 550
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
3-562 |
4.22e-117 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 360.18 E-value: 4.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 3 KMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTD 82
Cdd:PRK09107 10 QMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARST-GKPGVVLVTSGPGATN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 83 MITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDL 162
Cdd:PRK09107 89 AVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 163 PVDVQLAEIEFD-PETYEPLSAYKP--AATRAQAEKALAMLNEAERPLIVAGGGIINA--DASDLLTEFAEITGVPVVPT 237
Cdd:PRK09107 169 PKDVQFATGTYTpPQKAPVHVSYQPkvKGDAEAITEAVELLANAKRPVIYSGGGVINSgpEASRLLRELVELTGFPITST 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 238 LMGWGVIPDDHPLMAGMCGLQTSHRyGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFG 317
Cdd:PRK09107 249 LMGLGAYPASGKNWLGMLGMHGTYE-ANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 318 IVSDAGAALKlflDVATEWKTAGK------LRDWsaWAEECRERKRSMLRKTHFDQTpLKPQ----RVYeEMNKilGRDT 387
Cdd:PRK09107 328 IIGDVGHVLE---DMLRLWKARGKkpdkeaLADW--WGQIARWRARNSLAYTPSDDV-IMPQyaiqRLY-ELTK--GRDT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 388 cYVST-IGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPY 466
Cdd:PRK09107 399 -YITTeVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 467 LHVVVNNSYLGLIRQAQR---GFNMDFEVSLAFEninadgdaekgygvDHVAVAEGLGCKAIRVRSPNEFADAFDRaqal 543
Cdd:PRK09107 478 KIFILNNQYMGMVRQWQQllhGNRLSHSYTEAMP--------------DFVKLAEAYGAVGIRCEKPGDLDDAIQE---- 539
|
570
....*....|....*....
gi 429555433 544 MEEHQVPVVIEFILERVTN 562
Cdd:PRK09107 540 MIDVDKPVIFDCRVANLEN 558
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-521 |
1.78e-113 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 349.78 E-value: 1.78e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAG 80
Cdd:PRK08155 10 RKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTT-GKPAVCMACSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLI 160
Cdd:PRK08155 89 TNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIEFD--PETYEPLSAykPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTL 238
Cdd:PRK08155 169 DIPKDVQTAVIELEalPAPAEKDAA--PAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 239 MGWGVIPDDHPLMAGMCGLQTShRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGI 318
Cdd:PRK08155 247 MALGMLPKAHPLSLGMLGMHGA-RSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 319 VSDAGAALKLFLDVAtewktagKLRDWSAWaeecRERKRSMLRKTHFDQ----TPLKPQRVYEEMNKILGRDTCYVSTIG 394
Cdd:PRK08155 326 QADVDDVLAQLLPLV-------EAQPRAEW----HQLVADLQREFPCPIpkadDPLSHYGLINAVAACVDDNAIITTDVG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 395 LSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNS 474
Cdd:PRK08155 395 QHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNE 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 429555433 475 YLGLIRQAQRGFnmdFEvslafENINAdgdAEKGYGVDHVAVAEGLG 521
Cdd:PRK08155 475 ALGLVHQQQSLF---YG-----QRVFA---ATYPGKINFMQIAAGFG 510
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
2-555 |
2.39e-113 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 349.83 E-value: 2.39e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 2 AKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGsIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGT 81
Cdd:PRK07710 14 KLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCG-IPHILTRHEQGAIHAAEGYARIS-GKPGVVIATSGPGAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 82 DMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLID 161
Cdd:PRK07710 92 NVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 162 LPVDVQLAEIEFDPETYEPLSAYKPAA--TRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLM 239
Cdd:PRK07710 172 IPKDMVVEEGEFCYDVQMDLPGYQPNYepNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 240 GWGVIPDDHPLMAGMCGLQTSHRyGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIV 319
Cdd:PRK07710 252 GLGGFPADHPLFLGMAGMHGTYT-ANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 320 SDAGAALKLFLdvatewKTAGKLRDWSAWAEECRERKRSMLRKTHFDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIA 399
Cdd:PRK07710 331 ADAKQALQVLL------QQEGKKENHHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 400 GAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLI 479
Cdd:PRK07710 405 AAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMV 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429555433 480 RQAQRGFnmdFEVSLAFENINADGdaekgygvDHVAVAEGLGCKAIRVRSPNEFADAFDRAQALMEehqvPVVIEF 555
Cdd:PRK07710 485 RQWQEEF---YNQRYSHSLLSCQP--------DFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQE----PVVIDC 545
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
14-562 |
4.77e-112 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 346.69 E-value: 4.77e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 14 LEKEGIDCAFGVPGAAINPFYSALRA---RGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMITGLYSA 90
Cdd:CHL00099 20 LVRHGVKHIFGYPGGAILPIYDELYAwekKGLIKHILVRHEQGAAHAADGYARST-GKVGVCFATSGPGATNLVTGIATA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 91 SADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLPVDVQLAE 170
Cdd:CHL00099 99 QMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVGLEK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 171 IE-FDPE---TYEPLSAYKPA--ATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGVI 244
Cdd:CHL00099 179 FDyYPPEpgnTIIKILGCRPIykPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLMGKGIF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 245 PDDHPLMAGMCGLQTShRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSDAGA 324
Cdd:CHL00099 259 DEDHPLCLGMLGMHGT-AYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVAIVGDVKK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 325 ALKLFLDVATEWKTAGKLRDWSAWaeecreRKR-SMLRKTHFDQTP-----LKPQRVYEEMNKIlGRDTCYVSTIGLSQI 398
Cdd:CHL00099 338 VLQELLELLKNSPNLLESEQTQAW------RERiNRWRKEYPLLIPkpstsLSPQEVINEISQL-APDAYFTTDVGQHQM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 399 AGAQFLHVyKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGL 478
Cdd:CHL00099 411 WAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGM 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 479 IRQAQRGFnmdfevslaFENINADGDAEKGyGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQalmeEHQVPVVIEFILE 558
Cdd:CHL00099 490 VRQWQQAF---------YGERYSHSNMEEG-APDFVKLAEAYGIKGLRIKSRKDLKSSLKEAL----DYDGPVLIDCQVI 555
|
....
gi 429555433 559 RVTN 562
Cdd:CHL00099 556 EDEN 559
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-543 |
4.53e-108 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 336.12 E-value: 4.53e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAG 80
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARST-GKVGCVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLI 160
Cdd:PRK06882 80 TNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIEFdpeTYE-----PLSAYKPAAT--RAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVP 233
Cdd:PRK06882 160 DIPKDMVNPANKF---TYEypeevSLRSYNPTVQghKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 234 VVPTLMGWGVIPDDHPLMAGMCGLQTSHRYGNAtLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFA 313
Cdd:PRK06882 237 VTSSLMGLGAYPSTDKQFLGMLGMHGTYEANNA-MHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 314 PDFGIVSDAGAALKLFLDVATEWKTAGKLRDWSAWAEECRERK-RSMLRkthFDQTP--LKPQRVYEEMNKILGRDTCYV 390
Cdd:PRK06882 316 AYIPIVGSAKNVLEEFLSLLEEENLAKSQTDLTAWWQQINEWKaKKCLE---FDRTSdvIKPQQVVEAIYRLTNGDAYVA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 391 STIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVV 470
Cdd:PRK06882 393 SDVGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVS 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429555433 471 VNNSYLGLIRQAQrgfnmdfevslafeNINADGDAEKGYG---VDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAL 543
Cdd:PRK06882 473 LNNRFLGMVKQWQ--------------DLIYSGRHSQVYMnslPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSI 534
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-553 |
5.84e-108 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 336.02 E-value: 5.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAG 80
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARAT-GKVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLI 160
Cdd:PRK08979 80 TNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIEFDPETYEPLS--AYKPAAT--RAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVP 236
Cdd:PRK08979 160 DLPKDCLNPAILHPYEYPESIKmrSYNPTTSghKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 237 TLMGWGVIPDDHPLMAGMCGLQTSHRyGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDF 316
Cdd:PRK08979 240 TLMGLGAFPGTHKNSLGMLGMHGRYE-ANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 317 GIVSDAGAALKL---FLDVATEWKTAGKLRDWsaWAEECRERKRSMLRkthFDQTP--LKPQRVYEEMNKILGRDTCYVS 391
Cdd:PRK08979 319 PIVGSADKVLDSmlaLLDESGETNDEAAIASW--WNEIEVWRSRNCLA---YDKSSerIKPQQVIETLYKLTNGDAYVAS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 392 TIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVV 471
Cdd:PRK08979 394 DVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 472 NNSYLGLIRQAQrgfnmdfevslafeNINADGDAEKGYgVDHV----AVAEGLGCKAIRVRSPNEFADAFDRAQALME-- 545
Cdd:PRK08979 474 NNRFLGMVKQWQ--------------DMIYQGRHSHSY-MDSVpdfaKIAEAYGHVGIRISDPDELESGLEKALAMKDrl 538
|
570
....*....|....*...
gi 429555433 546 ----------EHQVPVVI 553
Cdd:PRK08979 539 vfvdinvdetEHVYPMQI 556
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-543 |
3.57e-105 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 328.63 E-value: 3.57e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAG 80
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARAT-GKTGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLI 160
Cdd:PRK06466 80 TNAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIEFD---PETYEpLSAYKPAAT--RAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVV 235
Cdd:PRK06466 160 DIPKDMTNPAEKFEyeyPKKVK-LRSYSPAVRghSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 236 PTLMGWGVIPDDHPLMAGMCGLQTSHRyGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPD 315
Cdd:PRK06466 239 NTLMGLGGFPGTDRQFLGMLGMHGTYE-ANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 316 FGIVSDAGAALKLFLDVATEWKT---AGKLRDWSAWAEECRERkRSMLRKTHFDQTPLKPQRVYEEMNKILGRDTCYVST 392
Cdd:PRK06466 318 IPIVGPVESVLTEMLAILKEIGEkpdKEALAAWWKQIDEWRGR-HGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 393 IGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVN 472
Cdd:PRK06466 397 VGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLN 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429555433 473 NSYLGLIRQAQrgfNMDFEVSLAFENINADGdaekgygvDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAL 543
Cdd:PRK06466 477 NGALGMVRQWQ---DMQYEGRHSHSYMESLP--------DFVKLAEAYGHVGIRITDLKDLKPKLEEAFAM 536
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
4-486 |
8.19e-105 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 326.84 E-value: 8.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 4 MRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRArGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDM 83
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARAT-GKVGVCIATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 84 ITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLP 163
Cdd:PRK08978 79 ITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 164 VDVQLAEIEFDPETYEPlsAYKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGV 243
Cdd:PRK08978 159 KDIQLAEGELEPHLTTV--ENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 244 IPDDHPLMAGMCGLQTShRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSDAG 323
Cdd:PRK08978 237 VEADHPYYLGMLGMHGT-KAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 324 A---ALKLFLDVAtewktagklrdwsAWAEECRERKRSM-LRKTHFDQtPLKPQRVYEEMNKILGRDTCYVSTIGLSQIA 399
Cdd:PRK08978 316 AllpALQQPLNID-------------AWRQHCAQLRAEHaWRYDHPGE-AIYAPALLKQLSDRKPADTVVTTDVGQHQMW 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 400 GAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLI 479
Cdd:PRK08978 382 VAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMV 461
|
....*..
gi 429555433 480 RQAQRGF 486
Cdd:PRK08978 462 RQWQQLF 468
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-545 |
1.50e-102 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 321.80 E-value: 1.50e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAG 80
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARAT-GEVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLI 160
Cdd:PRK07979 80 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIEFD---PETYEpLSAYKPAAT--RAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVV 235
Cdd:PRK07979 160 DLPKDILNPANKLPyvwPESVS-MRSYNPTTQghKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 236 PTLMGWGVIPDDHPLMAGMCGLQTSHRyGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPD 315
Cdd:PRK07979 239 SSLMGLGAFPATHRQSLGMLGMHGTYE-ANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 316 FGIVSDAGAALKLFLDV-ATEWKTA--GKLRDWSAWAEECRERKrsmLRKTHFDQTPLKPQRVYEEMNKILGRDTCYVST 392
Cdd:PRK07979 318 IPIVGDARQVLEQMLELlSQESAHQplDEIRDWWQQIEQWRARQ---CLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 393 IGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVN 472
Cdd:PRK07979 395 VGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLN 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429555433 473 NSYLGLIRQAQrgfNMDFEvslafeninadGDAEKGYG---VDHVAVAEGLGCKAIRVRSPNEFADAFdrAQALME 545
Cdd:PRK07979 475 NRYLGMVKQWQ---DMIYS-----------GRHSQSYMqslPDFVRLAEAYGHVGIQISHPDELESKL--SEALEQ 534
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
2-543 |
1.30e-98 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 312.12 E-value: 1.30e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 2 AKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGT 81
Cdd:PRK06965 19 ADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARAT-GKVGVALVTSGPGVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 82 DMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLID 161
Cdd:PRK06965 98 NAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 162 LPVDVQLAEIEFD-PETYEpLSAYKPA--ATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTL 238
Cdd:PRK06965 178 IPKDVSKTPCEYEyPKSVE-MRSYNPVtkGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 239 MGWGVIPDDHPLMAGMCGLQTSHRYGNAtLLASDFVFGIGNRWANRHTGNIPTYTEG-RKFIHVDIEPTQIGRVFAPDFG 317
Cdd:PRK06965 257 MGLGAYPASDKKFLGMLGMHGTYEANMA-MQHCDVLIAIGARFDDRVIGNPAHFASRpRKIIHIDIDPSSISKRVKVDIP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 318 IVSDAGAALKLFLDVATEWKTAGKLRDWSAWAEECRE-RKRSMLRKTHFDQTpLKPQRVYEEMNKILGRDTCYVSTIGLS 396
Cdd:PRK06965 336 IVGDVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGwRSRDCLKYDRESEI-IKPQYVVEKLWELTDGDAFVCSDVGQH 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 397 QIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYL 476
Cdd:PRK06965 415 QMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYL 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 477 GLIRQAQRgfnmdfevslafenINADGDAEKGYG---VDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAL 543
Cdd:PRK06965 495 GMVRQWQE--------------IEYSKRYSHSYMdalPDFVKLAEAYGHVGMRIEKTSDVEPALREALRL 550
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
8-556 |
1.32e-98 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 312.06 E-value: 1.32e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 8 DAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMITGL 87
Cdd:PLN02470 17 DILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKAS-GKVGVCIATSGPGATNLVTGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 88 YSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLPVDVQ 167
Cdd:PLN02470 96 ADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDIQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 168 --LAEIEFDPETYEP--LSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIINadASDLLTEFAEITGVPVVPTLMGWGV 243
Cdd:PLN02470 176 qqLAVPNWNQPMKLPgyLSRLPKPPEKSQLEQIVRLISESKRPVVYVGGGCLN--SSEELREFVELTGIPVASTLMGLGA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 244 IPDDHPLMAGMCGLQTShRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSDAG 323
Cdd:PLN02470 254 FPASDELSLQMLGMHGT-VYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADVK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 324 AALKLFLDVATEWKTagKLRDWSAWAEECRERKRSM-LRKTHFDQTpLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQ 402
Cdd:PLN02470 333 LALQGLNKLLEERKA--KRPDFSAWRAELDEQKEKFpLSYPTFGDA-IPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 403 FLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQA 482
Cdd:PLN02470 410 WYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQW 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429555433 483 QRGFnmdFEVSLAFENInADGDAEKGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRaqalMEEHQVPVVIEFI 556
Cdd:PLN02470 490 EDRF---YKANRAHTYL-GDPDAEAEIFPDFLKFAEGCKIPAARVTRKSDLREAIQK----MLDTPGPYLLDVI 555
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
14-559 |
6.44e-97 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 307.15 E-value: 6.44e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 14 LEKEGIDCAFGVPGAAINPFYSAL---RARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMITGLYSA 90
Cdd:PRK06456 12 LKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARAS-GVPGVCTATSGPGTTNLVTGLITA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 91 SADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLPVDVQLAE 170
Cdd:PRK06456 91 YWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIPRDIFYEK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 171 IEFDPETYEPL-SAYKPAAT---RAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGVIPD 246
Cdd:PRK06456 171 MEEIKWPEKPLvKGYRDFPTridRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTFPGKTAIPH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 247 DHPLMAGMCGLqtshrYGNA----TLLASDFVFGIGNRWANRhtgNIPTYTE----GRKFIHVDIEPTQIGRVFAPDFGI 318
Cdd:PRK06456 251 DHPLYFGPMGY-----YGRAeasmAALESDAMLVVGARFSDR---TFTSYDEmvetRKKFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 319 VSDAGAALKLFLDVATEwktAGKLRDWSAWAEECRERKRSMLRKTHFDQ-TPLKPQRVYEEMNKILGRDTCYVSTIGLSQ 397
Cdd:PRK06456 323 YGNAKIILRELIKAITE---LGQKRDRSAWLKRVKEYKEYYSQFYYTEEnGKLKPWKIMKTIRQALPRDAIVTTGVGQHQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 398 IAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLG 477
Cdd:PRK06456 400 MWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 478 LIRQAQRGFNMDFEVSLAFeninadgdaekGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAqalMEEHqVPVVIEFIL 557
Cdd:PRK06456 480 LVRQVQDLFFGKRIVGVDY-----------GPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSA---IKED-IPAVIRVPV 544
|
..
gi 429555433 558 ER 559
Cdd:PRK06456 545 DK 546
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-559 |
9.09e-93 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 295.38 E-value: 9.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSAL-RARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPA 79
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALyKAGDRIRVIHTRHEQAAGYMAFGYARST-GRPGVCSVVPGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 80 GTDMITGLYSASADSIPILCITGQAPRARLDK---EDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPG 156
Cdd:PRK08266 80 VLNAGAALLTAYGCNSPVLCLTGQIPSALIGKgrgHLHEMPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 157 PVLIDLPVDV--QLAEIEfDPETYEPlsAYKPAATRAQAEKALAMLNEAERPLIVAGGGIinADASDLLTEFAEITGVPV 234
Cdd:PRK08266 160 PVALEMPWDVfgQRAPVA-AAPPLRP--APPPAPDPDAIAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEMLQAPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 235 VPTLMGWGVIPDDHPLMAGMCGlqtshryGNATLLASDFVFGIGNRWAnrhtgnIPTY-----TEGRKFIHVDIEPTQIG 309
Cdd:PRK08266 235 VAFRSGRGIVSDRHPLGLNFAA-------AYELWPQTDVVIGIGSRLE------LPTFrwpwrPDGLKVIRIDIDPTEMR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 310 RvFAPDFGIVSDAGAALKLFLD--VATEWKTAGKLRDWSAWAEECRERKRSmlrkthfdqtpLKPQRVY-EEMNKILGRD 386
Cdd:PRK08266 302 R-LKPDVAIVADAKAGTAALLDalSKAGSKRPSRRAELRELKAAARQRIQA-----------VQPQASYlRAIREALPDD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 387 TCYVSTigLSQIAGAQFLH--VYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKL 464
Cdd:PRK08266 370 GIFVDE--LSQVGFASWFAfpVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 465 PYLHVVVNNSYLGLIRQAQRgfnMDFE-VSLAFENINAdgdaekgygvDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAl 543
Cdd:PRK08266 448 GVVTVVFNNNAYGNVRRDQK---RRFGgRVVASDLVNP----------DFVKLAESFGVAAFRVDSPEELRAALEAALA- 513
|
570
....*....|....*.
gi 429555433 544 meeHQVPVVIEFILER 559
Cdd:PRK08266 514 ---HGGPVLIEVPVPR 526
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
4-554 |
6.19e-87 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 280.18 E-value: 6.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 4 MRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRaRGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDM 83
Cdd:PRK08322 1 MKAADLFVKCLENEGVEYIFGIPGEENLDLLEALR-DSSIKLILTRHEQGAAFMAATYGRLT-GKAGVCLSTLGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 84 ITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLP 163
Cdd:PRK08322 79 VTGVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 164 VDVqlAEIEFDPETYEPLSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGV 243
Cdd:PRK08322 159 EDI--AAEETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 244 IPDDHPLMAGMCGLQtSHRYGNATLLASDFVFGIGN--------RWaNRHTgniptyteGRKFIHVDIEPTQIGRVFAPD 315
Cdd:PRK08322 237 IPETHPLSLGTAGLS-QGDYVHCAIEHADLIINVGHdviekppfFM-NPNG--------DKKVIHINFLPAEVDPVYFPQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 316 FGIVSDAGAALKLFLDVatewktAGKLRDWS-AWAEECRERKRSMLRKTHFDQT-PLKPQRVYEEMNKILGRDTCYVSTI 393
Cdd:PRK08322 307 VEVVGDIANSLWQLKER------LADQPHWDfPRFLKIREAIEAHLEEGADDDRfPMKPQRIVADLRKVMPDDDIVILDN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 394 GLSQIAGAQFLHVYKPrN--WINCGQAGpLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVV 471
Cdd:PRK08322 381 GAYKIWFARNYRAYEP-NtcLLDNALAT-MGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLIL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 472 NNSYLGLIRQAQRgfNMDFEVS-LAFENinadgdaekgygVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQALmeehQVP 550
Cdd:PRK08322 459 NDNAYGMIRWKQE--NMGFEDFgLDFGN------------PDFVKYAESYGAKGYRVESADDLLPTLEEALAQ----PGV 520
|
....
gi 429555433 551 VVIE 554
Cdd:PRK08322 521 HVID 524
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-553 |
2.83e-86 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 279.58 E-value: 2.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALR-ARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPA 79
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRkEQDKIKFIQVRHEEVAALAAAAYAKLT-GKIGVCLSIGGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 80 GTDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVL 159
Cdd:PRK08611 80 AIHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 160 I---DLPVDVQLAEIEFDPETYEPLsayKPAATRAQAEKALAMLNEAERPLIVAGGGIINAdaSDLLTEFAEITGVPVVP 236
Cdd:PRK08611 160 TipdDLPAQKIKDTTNKTVDTFRPT---VPSPKPKDIKKAAKLINKAKKPVILAGLGAKHA--KEELLAFAEKAKIPIIH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 237 TLMGWGVIPDDHPLMAGMCG-LQTSHRYgnATLLASDFVFGIGNRWAnrHTGNIPtytEGRKFIHVDIEPTQIGRVFAPD 315
Cdd:PRK08611 235 TLPAKGIIPDDHPYSLGNLGkIGTKPAY--EAMQEADLLIMVGTNYP--YVDYLP---KKAKAIQIDTDPANIGKRYPVN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 316 FGIVSDAGAALklfldvaTEWKTAGKLRDWSAWAEECRERKRS----MLRKTHFDQTPLKPQRVYEEMNKILGRDTCYVS 391
Cdd:PRK08611 308 VGLVGDAKKAL-------HQLTENIKHVEDRRFLEACQENMAKwwkwMEEDENNASTPIKPERVMAAIQKIADDDAVLSV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 392 TIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVV 471
Cdd:PRK08611 381 DVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 472 NNSYLGLIR--QAQRGfNMDFEVSLAfeninadgdaekgyGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlmeeHQV 549
Cdd:PRK08611 461 NNQQLAFIKyeQQAAG-ELEYAIDLS--------------DMDYAKFAEACGGKGYRVEKAEELDPAFEEALA----QDK 521
|
....
gi 429555433 550 PVVI 553
Cdd:PRK08611 522 PVII 525
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
7-554 |
7.94e-85 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 275.22 E-value: 7.94e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 7 VDAavyvLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMITG 86
Cdd:PRK08199 15 VDA----LRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLT-GRPGICFVTRGPGATNASIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 87 LYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLPVDV 166
Cdd:PRK08199 90 VHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPEDV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 167 QLAEIEF-DPETYEPLsayKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGVIP 245
Cdd:PRK08199 170 LSETAEVpDAPPYRRV---AAAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDLFD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 246 DDHPLMAGMCGLQTshrygNATLLA----SDFVFGIGNRwanrhTGNIPT--YT------EGRKFIHVDIEPTQIGRVFA 313
Cdd:PRK08199 247 NRHPNYAGDLGLGI-----NPALAArireADLVLAVGTR-----LGEVTTqgYTlldipvPRQTLVHVHPDAEELGRVYR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 314 PDFGIVSDAGAALKLFLDVAtewktAGKLRDWSAWAEEcrerkrsmLRKTHFDQTPLKPQ-------RVYEEMNKILGRD 386
Cdd:PRK08199 317 PDLAIVADPAAFAAALAALE-----PPASPAWAEWTAA--------AHADYLAWSAPLPGpgavqlgEVMAWLRERLPAD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 387 TCYvsTIGlsqiAG--AQFLHVYKPRNWINcGQAGP----LGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGA 460
Cdd:PRK08199 384 AII--TNG----AGnyATWLHRFFRFRRYR-TQLAPtsgsMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 461 QHKLPYLHVVVNNSYLGLIRQAQRgfnMDFE---VSLAFENinadgdaekgygVDHVAVAEGLGCKAIRVRSPNEFADAF 537
Cdd:PRK08199 457 QYGLPIIVIVVNNGMYGTIRMHQE---REYPgrvSGTDLTN------------PDFAALARAYGGHGETVERTEDFAPAF 521
|
570
....*....|....*..
gi 429555433 538 DRAQAlmeeHQVPVVIE 554
Cdd:PRK08199 522 ERALA----SGKPALIE 534
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
9-554 |
1.75e-76 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 252.59 E-value: 1.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 9 AAVYVLEKEGIDCAFGVPGAAINPFYSALrARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMITGLY 88
Cdd:PRK07524 7 ALVRLLEAYGVETVFGIPGVHTVELYRGL-AGSGIRHVTPRHEQGAGFMADGYARVS-GKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 89 SASADSIPILCITGQAPRARLDKE--------DFQAVdiakiAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLI 160
Cdd:PRK07524 85 QAYADSIPMLVISSVNRRASLGKGrgklhelpDQRAM-----VAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIEFDPeTYEPLSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIInaDASDLLTEFAEITGVPVVPTLMG 240
Cdd:PRK07524 160 EIPLDVLAAPADHLL-PAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGAL--AAAAALRALAERLDAPVALTINA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 241 WGVIPDDHPLMAGMCglqTSHRYGNATLLASDFVFGIGNRWANrhTGNIPTYTEG----RKFIHVDIEPTQIGRVFAPDF 316
Cdd:PRK07524 237 KGLLPAGHPLLLGAS---QSLPAVRALIAEADVVLAVGTELGE--TDYDVYFDGGfplpGELIRIDIDPDQLARNYPPAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 317 GIVSDAGAALKLFLDvatewKTAGKLRDwSAWAEECRERKRSMLRKTHfDQTPLKPQRVYEEMNKILgRDTCYVSTIGLS 396
Cdd:PRK07524 312 ALVGDARAALEALLA-----RLPGQAAA-ADWGAARVAALRQALRAEW-DPLTAAQVALLDTILAAL-PDAIFVGDSTQP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 397 QIAGAQFLHVYKPRNWINCGQA-GPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSY 475
Cdd:PRK07524 384 VYAGNLYFDADAPRRWFNASTGyGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDG 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429555433 476 LGLIRqaqrgfnmDFEVSLAFENINADgdaekGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlmeeHQVPVVIE 554
Cdd:PRK07524 464 YGEIR--------RYMVARDIEPVGVD-----PYTPDFIALARAFGCAAERVADLEQLQAALRAAFA----RPGPTLIE 525
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
4-558 |
3.08e-74 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 247.75 E-value: 3.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 4 MRAVDAAVYVLEKEGIDCAFG--VPGAainpFYSALRARGsIRHILARHVEGASHMAEGYTRaRHGNIGVCIGTSGPAGT 81
Cdd:PRK06112 14 GTVAHAIARALKRHGVEQIFGqsLPSA----LFLAAEAIG-IRQIAYRTENAGGAMADGYAR-VSGKVAVVTAQNGPAAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 82 DMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLID 161
Cdd:PRK06112 88 LLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 162 LPVDVQLAEIEFD--PETYE----PLSAYKPAATR-AQAEKALAmlnEAERPLIVAGGGIINADASDLLTEFAEITGVPV 234
Cdd:PRK06112 168 LPADLLTAAAAAPaaPRSNSlghfPLDRTVPAPQRlAEAASLLA---QAQRPVVVAGGGVHISGASAALAALQSLAGLPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 235 VPTLMGWGVIPDDHPLMAGMCGL----QTSHRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGR 310
Cdd:PRK06112 245 ATTNMGKGAVDETHPLSLGVVGSlmgpRSPGRHLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 311 VFAPdFGIVSDAGAALKLFLDVATEWKTAGKLRDWSAWAE---ECRERKR-SMLRKTHFDQTPLKPQRVYEEMNKILGRD 386
Cdd:PRK06112 325 NYEA-LRLVGDARLTLAALTDALRGRDLAARAGRRAALEPaiaAGREAHReDSAPVALSDASPIRPERIMAELQAVLTGD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 387 TCYVSTIGLSQIAGAQFLHVYKP--RNWINCGQAGpLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKL 464
Cdd:PRK06112 404 TIVVADASYSSIWVANFLTARRAgmRFLTPRGLAG-LGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 465 PYLHVVVNNSYLGLIRQAQRGFNMDFEVSLAFEninadgdaekgyGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlm 544
Cdd:PRK06112 483 PVTIVVLNNGILGFQKHAETVKFGTHTDACHFA------------AVDHAAIARACGCDGVRVEDPAELAQALAAAMA-- 548
|
570
....*....|....
gi 429555433 545 eeHQVPVVIEFILE 558
Cdd:PRK06112 549 --APGPTLIEVITD 560
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
4-564 |
2.74e-72 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 242.02 E-value: 2.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 4 MRAVDAAVYVLEKEGIDCAFGVPgaaINPFYSAlRARGSIRHILARHVEGASHMAEGYTRARHG-NIGVCIGTSGPAGTD 82
Cdd:PRK06154 20 MKVAEAVAEILKEEGVELLFGFP---VNELFDA-AAAAGIRPVIARTERVAVHMADGYARATSGeRVGVFAVQYGPGAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 83 MITGLYSASADSIPILCITGQAPRARLDKE-DFQAvdiAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLID 161
Cdd:PRK06154 96 AFGGVAQAYGDSVPVLFLPTGYPRGSTDVApNFES---LRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 162 LPVDVQLAEIEFDPETYEPLSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGW 241
Cdd:PRK06154 173 LPVDVLAEELDELPLDHRPSRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 242 GVIPDDHPLMAGMCGL----QTSHrygnaTLLASDFVFGIGNRWAnrHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFG 317
Cdd:PRK06154 253 SAFPEDHPLALGSGGRarpaTVAH-----FLREADVLFGIGCSLT--RSYYGLPMPEGKTIIHSTLDDADLNKDYPIDHG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 318 IVSDAGAALKLFLDVATEwKTAGKLRDWSAWAEECRERKRSMLRKTH----FDQTPLKPQRV-YEEMNKILGRDTCYVST 392
Cdd:PRK06154 326 LVGDAALVLKQMIEELRR-RVGPDRGRAQQVAAEIEAVRAAWLAKWMpkltSDSTPINPYRVvWELQHAVDIKTVIITHD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 393 IGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVN 472
Cdd:PRK06154 405 AGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLN 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 473 NSYLGLirqaqrgfnMDFEVSLAFENINAdgdaeKGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQALMEEHQvPVV 552
Cdd:PRK06154 485 NFSMGG---------YDKVMPVSTTKYRA-----TDISGDYAAIARALGGYGERVEDPEMLVPALLRALRKVKEGT-PAL 549
|
570
....*....|..
gi 429555433 553 IEFILERVTNIA 564
Cdd:PRK06154 550 LEVITSEETALS 561
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-560 |
1.38e-65 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 224.88 E-value: 1.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFySALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAG 80
Cdd:PRK07525 3 KMKMTPSEAFVETLQAHGITHAFGIIGSAFMDA-SDLFPPAGIRFIDVAHEQNAGHMADGYTRVT-GRMGMVIGQNGPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRpGPVLI 160
Cdd:PRK07525 81 TNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIefDPETYEPLSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMG 240
Cdd:PRK07525 160 NIPRDYFYGVI--DVEIPQPVRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 241 WGVIPDDHPLMAGMCGLQTShRYGNATLLASDFVFGIGNRWAnrHTGNIPTY-----TEGRKFIHVDIEPTQIGRVFAPD 315
Cdd:PRK07525 238 NDAFPGSHPLWVGPLGYNGS-KAAMELIAKADVVLALGTRLN--PFGTLPQYgidywPKDAKIIQVDINPDRIGLTKKVS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 316 FGIVSDAGAALKLFLDVATEwKTAGK-------------LRDW----SAWAEECRERKRSML-RKTHFDQTPLKPQRVYE 377
Cdd:PRK07525 315 VGICGDAKAVARELLARLAE-RLAGDagreerkaliaaeKSAWeqelSSWDHEDDDPGTDWNeEARARKPDYMHPRQALR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 378 EMNKILGRDTCYVSTIG-LSQIAGAqFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEEL 456
Cdd:PRK07525 394 EIQKALPEDAIVSTDIGnNCSIANS-YLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 457 AVGAQHKLPYLHVVVNNSYLGlirqAQRGFNMDFevslaFEN--INADGDAEKGYgvdhVAVAEGLGCKAIRVRSPNEFA 534
Cdd:PRK07525 473 MTAVRHNWPVTAVVFRNYQWG----AEKKNQVDF-----YNNrfVGTELDNNVSY----AGIAEAMGAEGVVVDTQEELG 539
|
570 580
....*....|....*....|....*.
gi 429555433 535 DAFDRAQAlMEEHQVPVVIEFILERV 560
Cdd:PRK07525 540 PALKRAID-AQNEGKTTVIEIMCNQE 564
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
3-554 |
1.43e-62 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 215.87 E-value: 1.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 3 KMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGsIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTD 82
Cdd:PRK08617 4 KKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSG-PELIVTRHEQNAAFMAAAIGRLT-GKPGVVLVTSGPGVSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 83 MITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDL 162
Cdd:PRK08617 82 LATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 163 PVDVQLAEIEFDPetYEPLSAYKP-AATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGW 241
Cdd:PRK08617 162 PQDVVDAPVTSKA--IAPLSKPKLgPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 242 GVIPDDH-PLMAGMCGL---QTshryGNATLLASDFVFGIG--------NRWANRHTGNIptytegrkfIHVDIEPTQIG 309
Cdd:PRK08617 240 GVISRELeDHFFGRVGLfrnQP----GDELLKKADLVITIGydpieyepRNWNSEGDATI---------IHIDVLPAEID 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 310 RVFAPDFGIVSDAGAALKLFLDVATEWKTAGKLRDwsAWAEECRERKRSMLRKTHFDQTPLKPQRVYEEMNKILGRDTCY 389
Cdd:PRK08617 307 NYYQPERELIGDIAATLDLLAEKLDGLSLSPQSLE--ILEELRAQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 390 VSTIGLSQIAGAQFLHVYKPRNW-INCGQAgPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLH 468
Cdd:PRK08617 385 TVDVGSHYIWMARYFRSYEPRHLlFSNGMQ-TLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVH 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 469 VV-VNNSYlglirqaqrgfNMdfevsLAFENinadgdaEKGYG---------VDHVAVAEGLGCKAIRVRSPNEFADAFD 538
Cdd:PRK08617 464 IIwNDGHY-----------NM-----VEFQE-------EMKYGrssgvdfgpVDFVKYAESFGAKGLRVTSPDELEPVLR 520
|
570
....*....|....*.
gi 429555433 539 RAqalMEEhQVPVVIE 554
Cdd:PRK08617 521 EA---LAT-DGPVVID 532
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
8-558 |
6.47e-61 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 211.23 E-value: 6.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 8 DAAVYVLEKEGIDCAFGVPGAAINPFYSALRaRGSIRHILARHVEGAShMAEGYTRARHGNIGVCIGTSGPAGTDMITGL 87
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIR-KSKVKYVQVRHEEGAA-LAASVEAKITGKPSACMGTSGPGSIHLLNGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 88 YSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRpGPVLIDLPVDVQ 167
Cdd:PRK06457 84 YDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 168 LAEIEFDPETYEPLSAYKPAATRAQAEKalaMLNEAERPLIVAGGGIInaDASDLLTEFAEITGVPVVPTLMGWGVIPDD 247
Cdd:PRK06457 163 RKSSEYKGSKNTEVGKVKYSIDFSRAKE---LIKESEKPVLLIGGGTR--GLGKEINRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 248 HPLMAGMCGLQTSHRYGNAtLLASDFVFGIGNRWANRHTGNiptytEGRKFIHVDIEPTQIGRVFAPDFGIVSDAGAALK 327
Cdd:PRK06457 238 DPKVMGGIGLLGTKPSIEA-MDKADLLIMLGTSFPYVNFLN-----KSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 328 LFLDVATE---WKTAGKLRDWSAWAEEcRERKRSmlrkthfdqTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFL 404
Cdd:PRK06457 312 IDIEEKSDkfyEELKGKKEDWLDSISK-QENSLD---------KPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 405 HVYKPRNWINCGQAGPLGWTLPAALGVR-AADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQAQ 483
Cdd:PRK06457 382 RASGEQTFIFSAWLGSMGIGVPGSVGASfAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQ 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429555433 484 rgfnmdfEVSlafeninadGDAEKG---YGVDHVAVAEGLGCKAIRVRSPNEFADAFDRaqalMEEHQVPVVIEFILE 558
Cdd:PRK06457 462 -------EVM---------GYPEWGvdlYNPDFTKIAESIGFKGFRLEEPKEAEEIIEE----FLNTKGPAVLDAIVD 519
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-164 |
1.15e-57 |
|
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: 190.44 E-value: 1.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 8 DAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGsIRHILARHVEGASHMAEGYTRArHGNIGVCIGTSGPAGTDMITGL 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSG-IRYILVRHEQGAVGMADGYARA-TGKPGVVLVTSGPGLTNAVTGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429555433 88 YSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLPV 164
Cdd:cd07035 79 ANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
6-172 |
1.32e-53 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 180.12 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 6 AVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRArHGNIGVCIGTSGPAGTDMIT 85
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARA-TGKPGVVLVTSGPGATNALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 86 GLYSASADSIPILCITGQAPRARLDKEDFQA-VDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLPV 164
Cdd:pfam02776 80 GLANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPL 159
|
....*...
gi 429555433 165 DVQLAEIE 172
Cdd:pfam02776 160 DVLLEEVD 167
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
4-478 |
1.02e-51 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 186.08 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 4 MRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGsIRHILARHVEGASHMAEGYTRARHgNIGVCIGTSGPAGTDM 83
Cdd:PRK05858 5 GHAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTR-VPGVAVLTAGPGVTNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 84 ITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLP 163
Cdd:PRK05858 83 MSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 164 VDV--QLAEIEFDPETYEPLSAyKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGW 241
Cdd:PRK05858 163 MDHafSMADDDGRPGALTELPA-GPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 242 GVIPDDHPLMAGmcglqtshRYGNATLLASDFVFGIGNRWANRHtgNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSD 321
Cdd:PRK05858 242 GVVPADHPLAFS--------RARGKALGEADVVLVVGVPMDFRL--GFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 322 AGAALKLFldvATEWKTAGKLRDW----SAWAEECRERKRSMLRKthfDQTPLKPQRVYEEMNKILGRDTCYVSTIG-LS 396
Cdd:PRK05858 312 LSAILSAL---AGAGGDRTDHQGWieelRTAETAARARDAAELAD---DRDPIHPMRVYGELAPLLDRDAIVIGDGGdFV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 397 QIAGaQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYL 476
Cdd:PRK05858 386 SYAG-RYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIW 464
|
..
gi 429555433 477 GL 478
Cdd:PRK05858 465 GL 466
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
8-554 |
2.00e-50 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 182.50 E-value: 2.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 8 DAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMITGL 87
Cdd:PRK07064 7 ELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVS-GGLGVALTSTGTGAGNAAGAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 88 YSASADSIPILCITGQAPRARLDKedfqavDIAKI-AAP--------VTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPV 158
Cdd:PRK07064 86 VEALTAGTPLLHITGQIETPYLDQ------DLGYIhEAPdqltmlraVSKAAFRVRSAETALATIREAVRVALTAPTGPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 159 LIDLPVDVQLAEIEFdPETYEPLSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASdlLTEFAEItGVPVVPTL 238
Cdd:PRK07064 160 SVEIPIDIQAAEIEL-PDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAE--VKRLVDL-GFGVVTST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 239 MGWGVIPDDHPLMAGMCGLQTShryGNATLLASDFVFGIGNRWANRHTGN----IPtytegRKFIHVDIEPTQIGRVFAP 314
Cdd:PRK07064 236 QGRGVVPEDHPASLGAFNNSAA---VEALYKTCDLLLVVGSRLRGNETLKyslaLP-----RPLIRVDADAAADGRGYPN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 315 DFGIVSDAGAALKLFLDvatewKTAGKLRDWSAWAEECRERK---RSMLRKThfdqtpLKPQRVY-EEMNKILGRDTCYV 390
Cdd:PRK07064 308 DLFVHGDAARVLARLAD-----RLEGRLSVDPAFAADLRAAReaaVADLRKG------LGPYAKLvDALRAALPRDGNWV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 391 STIGLSQIA-GAQFLHVYKPRNWINcGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHV 469
Cdd:PRK07064 377 RDVTISNSTwGNRLLPIFEPRANVH-ALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 470 VVNNSYLGLIRqaqrgfnmdfevslafeNINADGDAEKGYGV-----DHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlm 544
Cdd:PRK07064 456 LMNDGGYGVIR-----------------NIQDAQYGGRRYYVelhtpDFALLAASLGLPHWRVTSADDFEAVLREALA-- 516
|
570
....*....|
gi 429555433 545 eeHQVPVVIE 554
Cdd:PRK07064 517 --KEGPVLVE 524
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
14-554 |
1.04e-48 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 178.64 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 14 LEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGAShMAEGYTRARHGNIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:PRK09124 13 LEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAA-FAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDCHRN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 94 SIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAfhlMRS--GRPGPVLIDLPVDVQLAEI 171
Cdd:PRK09124 92 HVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIA---MRKaiLNRGVAVVVLPGDVALKPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 172 EfDPETYEPLSAYKPAATRAQAE--KALAMLNEAERPLIVAGGGIinADASDLLTEFAEITGVPVVPTLMGWGVIPDDHP 249
Cdd:PRK09124 169 P-ERATPHWYHAPQPVVTPAEEElrKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALRGKEHVEYDNP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 250 LMAGMCGLqTSHRYGNATLLASDFVFGIGNRWANRhtgniPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSDAGAALKLF 329
Cdd:PRK09124 246 YDVGMTGL-IGFSSGYHAMMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKATLAAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 330 LDVATEWKTAGKLRDWSAWAEECRERKRSMLRKTHfDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKP 409
Cdd:PRK09124 320 LPLLEEKTDRKFLDKALEHYRKARKGLDDLAVPSD-GGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 410 RNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIrqaqrgfnmd 489
Cdd:PRK09124 399 RRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFV---------- 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429555433 490 fevslAFEnINADGDAEKGYGV---DHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlmeeHQVPVVIE 554
Cdd:PRK09124 469 -----AME-MKAGGYLTDGTDLhnpDFAAIAEACGITGIRVEKASELDGALQRAFA----HDGPALVD 526
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-560 |
8.97e-46 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 170.18 E-value: 8.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLE---KEGIDCAFGVPG---AAINPFYSALRARGSI--RHILARHVEGASHMAEGYTRARhGNIG-- 70
Cdd:PRK08327 1 SMALTMYTAAELFLEllkELGVDYIFINSGtdyPPIIEAKARARAAGRPlpEFVICPHEIVAISMAHGYALVT-GKPQav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 71 ---VCIGTSGPAGtdmitGLYSASADSIPILCITGQAP---RARLDKEDF------QAVDIAKIAAPVTKWAVTVMEPAL 138
Cdd:PRK08327 80 mvhVDVGTANALG-----GVHNAARSRIPVLVFAGRSPyteEGELGSRNTrihwtqEMRDQGGLVREYVKWDYEIRRGDQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 139 VPFVFQKAFHLMRSGRPGPVLIDLPVDVqLAEiEFDPETYEP---LSAYKPAATRAQAEKALAMLNEAERPLIVAGGGII 215
Cdd:PRK08327 155 IGEVVARAIQIAMSEPKGPVYLTLPREV-LAE-EVPEVKADAgrqMAPAPPAPDPEDIARAAEMLAAAERPVIITWRAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 216 NADASDLLTEFAEITGVPVV---PTLMgwgVIPDDHPLMAGmcglqtshRYGNATLLASDFVFGIGNR--WanrhtgnIP 290
Cdd:PRK08327 233 TAEGFASLRRLAEELAIPVVeyaGEVV---NYPSDHPLHLG--------PDPRADLAEADLVLVVDSDvpW-------IP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 291 TYT---EGRKFIHVDIEP--TQIG-RVFAPDFGIVSDAGAALKLFLDVATEWKTAGKLRDWSAWAEECRERKRSMLRK-- 362
Cdd:PRK08327 295 KKIrpdADARVIQIDVDPlkSRIPlWGFPCDLCIQADTSTALDQLEERLKSLASAERRRARRRRAAVRELRIRQEAAKra 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 363 ---THFDQTPLKPQRVYEEMNKILGRDTCYVSTIGLSQiagaQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQ 439
Cdd:PRK08327 375 eieRLKDRGPITPAYLSYCLGEVADEYDAIVTEYPFVP----RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 440 IVALSGDYDFQFLIEE--LAVGAQHKLPYLHVVVNNS-YL------------GLIRQAQRGFNMDFEVSLAFEninadgd 504
Cdd:PRK08327 451 VIATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGgWLavkeavlevypeGYAARKGTFPGTDFDPRPDFA------- 523
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 429555433 505 aekgygvdhvAVAEGLGCKAIRVRSPNEFADAFDRAQALMEEHQVPVVIEFILERV 560
Cdd:PRK08327 524 ----------KIAEAFGGYGERVEDPEELKGALRRALAAVRKGRRSAVLDVIVDRV 569
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
393-555 |
1.91e-43 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 152.35 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 393 IGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVN 472
Cdd:pfam02775 2 IGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 473 NSYLGLIRQAQRGFNMDFEVSLafeninadgDAEKGYGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQalmeEHQVPVV 552
Cdd:pfam02775 82 NGGYGMTRGQQTPFGGGRYSGP---------SGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEAL----EHDGPAL 148
|
...
gi 429555433 553 IEF 555
Cdd:pfam02775 149 IDV 151
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-556 |
1.96e-43 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 163.62 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAvDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAG 80
Cdd:PRK06546 1 MAKTVA-EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLT-GKLAVCAGSCGPGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAF-HLMrsGRPGPVL 159
Cdd:PRK06546 79 LHLINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIqHAV--AGGGVSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 160 IDLPVDVQLAEIEfDPETYEPLSAYKPAATRAQAE-KALA-MLNEAERPLIVAGGGIinADASDLLTEFAEITGVPVVPT 237
Cdd:PRK06546 157 VTLPGDIADEPAP-EGFAPSVISPRRPTVVPDPAEvRALAdAINEAKKVTLFAGAGV--RGAHAEVLALAEKIKAPVGHS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 238 LMGWGVIPDDHPLMAGMCGLQTshrYGNAT----------LLASDFvfgignrwanrhtgnipTYTE---GRKFIHVDIE 304
Cdd:PRK06546 234 LRGKEWIQYDNPFDVGMSGLLG---YGAAHeamheadlliLLGTDF-----------------PYDQflpDVRTAQVDID 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 305 PTQIGRVFAPDFGIVSDAGAALKLFLDVATEwKTAGKLRDwsawaeecrerkrSMLRKtHFD---------------QTP 369
Cdd:PRK06546 294 PEHLGRRTRVDLAVHGDVAETIRALLPLVKE-KTDRRFLD-------------RMLKK-HARklekvvgaytrkvekHTP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 370 LKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDF 449
Cdd:PRK06546 359 IHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 450 QFLIEELAVGAQHKLPYLHVVVNNSYLGLIRqaqrgFNM------DFEVslafeninadgDAEKgygVDHVAVAEGLGCK 523
Cdd:PRK06546 439 SMLLGELLTVKLYDLPVKVVVFNNSTLGMVK-----LEMlvdglpDFGT-----------DHPP---VDYAAIAAALGIH 499
|
570 580 590
....*....|....*....|....*....|...
gi 429555433 524 AIRVRSPNEFADAFDRAQAlmeeHQVPVVIEFI 556
Cdd:PRK06546 500 AVRVEDPKDVRGALREAFA----HPGPALVDVV 528
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
194-327 |
9.06e-43 |
|
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: 150.02 E-value: 9.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 194 EKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGVIPDDHPLMAGMCGLqTSHRYGNATLLASDF 273
Cdd:pfam00205 2 EKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGM-HGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 429555433 274 VFGIGNRWA-NRHTGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSDAGAALK 327
Cdd:pfam00205 81 VLAVGARFDdIRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLE 135
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
2-554 |
1.65e-42 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 160.12 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 2 AKMRAVDAAVY-VLEKEGIDCAFGVPGAAINPFYSALRArgSIRHILARHVEGASHMAEGYTRARhGNIGVcIGTSGPAG 80
Cdd:PRK07092 9 AAMTTVRDATIdLLRRFGITTVFGNPGSTELPFLRDFPD--DFRYVLGLQEAVVVGMADGYAQAT-GNAAF-VNLHSAAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITG-LYSASADSIPILCITGQAPRARLDKEDF-QAVDIAKIAAPVTKWAVtvmEPAL---VPFVFQKAFHLMRSGRP 155
Cdd:PRK07092 85 VGNAMGnLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSI---EPARaedVPAAIARAYHIAMQPPR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 156 GPVLIDLPVDvqlaeiEFDPETyEPLSAYKPAATRAQAEKALA----MLNEAERPLIVAGGGIINADASDLLTEFAEITG 231
Cdd:PRK07092 162 GPVFVSIPYD------DWDQPA-EPLPARTVSSAVRPDPAALArlgdALDAARRPALVVGPAVDRAGAWDDAVRLAERHR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 232 VPV-VPTLMGWGVIPDDHPLMAGMcgLQTSHRYGNATLLASDFVFGIGNRWANRHT-GNIPTYTEGRKFIHVDIEPTQIG 309
Cdd:PRK07092 235 APVwVAPMSGRCSFPEDHPLFAGF--LPASREKISALLDGHDLVLVIGAPVFTYHVeGPGPHLPEGAELVQLTDDPGEAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 310 RvfAPdFG--IVSDAGAALKLFLDVATEWKTAgklrdwsawAEECRERKRSMLRkthfDQTPLKPQRVYEEMNKILGRDT 387
Cdd:PRK07092 313 W--AP-MGdaIVGDIRLALRDLLALLPPSARP---------APPARPMPPPAPA----PGEPLSVAFVLQTLAALRPADA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 388 CYV----STIGLSQiagaQFLHVYKPRNWINcGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHK 463
Cdd:PRK07092 377 IVVeeapSTRPAMQ----EHLPMRRQGSFYT-MASGGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 464 LPYLHVVVNNSYLGLIRQAQRGFNMDFEVSLAFEninadgdaekgyGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAl 543
Cdd:PRK07092 452 LPVTFVILNNGRYGALRWFAPVFGVRDVPGLDLP------------GLDFVALARGYGCEAVRVSDAAELADALARALA- 518
|
570
....*....|.
gi 429555433 544 meeHQVPVVIE 554
Cdd:PRK07092 519 ---ADGPVLVE 526
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
18-556 |
3.14e-42 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 160.46 E-value: 3.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 18 GIDCAFGVPGAAINPFYSAL-RARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMITGLYSASADSIP 96
Cdd:PRK08273 17 GVRRVFGYPGDGINGLLGALgRADDKPEFVQARHEEMAAFMAVAHAKFT-GEVGVCLATSGPGAIHLLNGLYDAKLDHVP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 97 ILCITGQAPRARLDKEDFQAVDIAKIAAPV-TKWAVTVMEPALVPFVFQKAFHLMRSGRpGPVLIDLPVDVQlaEIEFDP 175
Cdd:PRK08273 96 VVAIVGQQARAALGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTALAER-TVTAVILPNDVQ--ELEYEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 176 ETYE--------PLSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIinADASDLLTEFAEITGVPVVPTLMGWGVIPDD 247
Cdd:PRK08273 173 PPHAhgtvhsgvGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGA--LGATDEVIAVAERLGAGVAKALLGKAALPDD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 248 HPLMAGMCGL---QTSHRYGNA--TLLAsdfvfgIGNrwanrhtgNIPtYTE-----GR-KFIHVDIEPTQIGRVFAPDF 316
Cdd:PRK08273 251 LPWVTGSIGLlgtKPSYELMREcdTLLM------VGS--------SFP-YSEflpkeGQaRGVQIDIDGRMLGLRYPMEV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 317 GIVSDAGAALKLFLDVATEwktaGKLRDWSAWAEECRERKRSMLRK-THFDQTPLKPQRVYEEMNKILGRDTCYVSTIGL 395
Cdd:PRK08273 316 NLVGDAAETLRALLPLLER----KKDRSWRERIEKWVARWWETLEArAMVPADPVNPQRVFWELSPRLPDNAILTADSGS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 396 SQIAGAQFLhvyKPRNWINCGQAGPL---GWTLPAALGVRAADPNRQIVALSGDYDFQFL-IEELAVGAQH----KLPYL 467
Cdd:PRK08273 392 CANWYARDL---RMRRGMMASLSGTLatmGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKYwrqwSDPRL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 468 HVVV-NNSYLGLIRQAQRGFNMD--FEVSLAFENinadgdaekgygVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlm 544
Cdd:PRK08273 469 IVLVlNNRDLNQVTWEQRVMEGDpkFEASQDLPD------------VPYARFAELLGLKGIRVDDPEQLGAAWDEALA-- 534
|
570
....*....|..
gi 429555433 545 eeHQVPVVIEFI 556
Cdd:PRK08273 535 --ADRPVVLEVK 544
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
14-542 |
1.57e-41 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 158.23 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 14 LEKEGIDCAFGVPGAAINPFYSALRARGsIRHILARHVEGASHMA--EGYTRARHGnigVCIGTSGPAGTDMITGLYSAS 91
Cdd:PRK09259 20 LKLNGIDTIYGVVGIPITDLARLAQAEG-IRYIGFRHEQSAGNAAaaAGFLTQKPG---VCLTVSAPGFLNGLTALANAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 92 ADSIPILCITGQAPRARLD--KEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLIDLPVDVQLA 169
Cdd:PRK09259 96 TNCFPMIMISGSSEREIVDlqQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVLAQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 170 EIEFDPETYEPLSAYKPAA----TRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGVIP 245
Cdd:PRK09259 176 TMDADEALTSLVKVVDPAPaqlpAPEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSMAKGLLP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 246 DDHPLMAGMCglqtshrygNATLLA-SDFVFGIGNR--WANRHtGNIPTYTEGRKFIHVDIEPTQIGRVFAPDFGIVSDA 322
Cdd:PRK09259 256 DTHPQSAAAA---------RSLALAnADVVLLVGARlnWLLSH-GKGKTWGADKKFIQIDIEPQEIDSNRPIAAPVVGDI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 323 GAALKLFLD-VATEWKTAGklrdwSAWAEECRERKR----SMLRKTHFDQTPLKPQRVYEEMNKIL--GRDTCYVStigl 395
Cdd:PRK09259 326 GSVMQALLAgLKQNTFKAP-----AEWLDALAERKEknaaKMAEKLSTDTQPMNFYNALGAIRDVLkeNPDIYLVN---- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 396 sqiAGAQFLHV-------YKPRNWINCGQAGPLGWTLPAALGVrAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLH 468
Cdd:PRK09259 397 ---EGANTLDLarniidmYKPRHRLDCGTWGVMGIGMGYAIAA-AVETGKPVVAIEGDSAFGFSGMEVETICRYNLPVTV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 469 VVVNNS--YLGlirqaqrgfnmDFEvslafeniNADGDAEKG-----YGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQ 541
Cdd:PRK09259 473 VIFNNGgiYRG-----------DDV--------NLSGAGDPSptvlvHHARYDKMMEAFGGVGYNVTTPDELRHALTEAI 533
|
.
gi 429555433 542 A 542
Cdd:PRK09259 534 A 534
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
39-553 |
2.15e-39 |
|
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: 152.59 E-value: 2.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 39 ARGSIRHILARHVEGASHMAEGYTRARH-GNIGVCIGTSGPAGTDMITGLYSASADSIPILCITG-----QAPRARLDK- 111
Cdd:COG3962 54 DPDELPTYQGRNEQGMAHAAIAYAKQKNrRRIMACTSSIGPGATNMVTAAALATANRLPVLLLPGdtfatRQPDPVLQQl 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 112 EDFQAVDIAKIAA--PVTKWAVTVMEPALVPFVFQKAFHLMRSgrP---GPVLIDLPVDVQlAEiEFDpetYePLSAYK- 185
Cdd:COG3962 134 EHFHDPTISVNDAfrPVSRYWDRITRPEQLMSALPRAMRVLTD--PaetGAVTLALPQDVQ-AE-AYD---Y-PESFFAk 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 186 -------PAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGVIPDDHPLMAGMCGLq 258
Cdd:COG3962 206 rvhrirrPPPDPAELARAVELIRAAKRPLIIAGGGVRYSEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLGGIGV- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 259 TSHRYGNAtlLAS--DFVFGIGNR---------WANRHtgniptytEGRKFIHVDIEPTQIGRVFApdFGIVSDAGAALK 327
Cdd:COG3962 285 TGTLAANA--LAAeaDLVIGVGTRlqdfttgskTLFAN--------PDVRFVNINVARFDAYKHDA--LPVVADAREGLE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 328 LFLDVATEWKTAgklrdwSAWAEECRERKRSML----RKTHFDQTPLKPQ-RVYEEMNKILGRDTCYVSTIGlSQIAGaq 402
Cdd:COG3962 353 ALTEALAGWRYP------AAWTDEAAELKAEWDaevdRLYAPTNGGLPTQaQVIGAVNEAAGPDDIVVCAAG-SLPGD-- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 403 fLHvykpRNWiNCGQAGP---------LGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNN 473
Cdd:COG3962 424 -LH----KLW-RTRDPGTyhveygyscMGYEIAGGLGVKLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKIIVVLLDN 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 474 SYLGLIRQAQRGFNMDfevslAFENINADGDAEKGY------GVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlmeeH 547
Cdd:COG3962 498 HGFGCINRLQMSTGSQ-----SFGTELRDRDTETGRldggllPVDFAANAASLGAKAYRVTTIAELRAALERAKA----A 568
|
....*.
gi 429555433 548 QVPVVI 553
Cdd:COG3962 569 DRTTVI 574
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
374-554 |
5.45e-39 |
|
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: 140.85 E-value: 5.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 374 RVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLI 453
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 454 EELAVGAQHKLPYLHVVVNNSYLGLIRQAQRGFNMDFEVSLAFENInadgdaekgygvDHVAVAEGLGCKAIRVRSPNEF 533
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNP------------DFAALAEAYGAKGVRVEDPEDL 148
|
170 180
....*....|....*....|.
gi 429555433 534 ADAFDRAQAlmeeHQVPVVIE 554
Cdd:cd00568 149 EAALAEALA----AGGPALIE 165
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
14-559 |
7.30e-38 |
|
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: 147.23 E-value: 7.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 14 LEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGnIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVN-G-LGALVTTYGVGELSAINGIAGAYAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 94 SIPILCITGqAPRAR-----------LDKEDFQAVdiAKIAAPVTKwAVTVMEPALVPF----VFQKAFHLMRsgrpgPV 158
Cdd:COG3961 93 RVPVVHIVG-APGTRaqrrgpllhhtLGDGDFDHF--LRMFEEVTV-AQAVLTPENAAAeidrVLAAALREKR-----PV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 159 LIDLPVDVQLAEIEfdpETYEPLSAYKPAATRAQ----AEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPV 234
Cdd:COG3961 164 YIELPRDVADAPIE---PPEAPLPLPPPASDPAAlaaaVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 235 VPTLMGWGVIPDDHPLMAGMCGLQTSHRYGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIG-RVFA 313
Cdd:COG3961 241 ATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVGgHIYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 314 PdfgiVS--DAGAAL-KLFLDVATEWKTAGKLRDWSAWAeecrerkrsmlrkthfDQTPLKPQRVYEEMNKILGRDTCYV 390
Cdd:COG3961 321 G----VSlaDFLEALaELLKKRSAPLPAPAPPPPPPPAA----------------PDAPLTQDRLWQRLQAFLDPGDIVV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 391 STIGLSqIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVV 470
Cdd:COG3961 381 ADTGTS-LFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 471 VNNS-YlgLIRQAQRGFNMdfevslAFENINAdgdaekgygVDHVAVAEGLGCK---AIRVRSPNEFADAFDRAQAlmeE 546
Cdd:COG3961 460 LNNDgY--TIERAIHGPDG------PYNDIAN---------WDYAKLPEAFGGGnalGFRVTTEGELEEALAAAEA---N 519
|
570
....*....|...
gi 429555433 547 HQVPVVIEFILER 559
Cdd:COG3961 520 TDRLTLIEVVLDK 532
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
370-563 |
5.14e-37 |
|
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: 136.09 E-value: 5.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 370 LKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDF 449
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 450 QFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQAQRGFnmdFEvslafENINADgdaEKGYGVDHVAVAEGLGCKAIRVRS 529
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELF---YE-----GRYSHT---TLDSNPDFVKLAEAYGIKGLRVEK 149
|
170 180 190
....*....|....*....|....*....|....
gi 429555433 530 PNEFADAFDRAQalmeEHQVPVVIEFILERVTNI 563
Cdd:cd02015 150 PEELEAALKEAL----ASDGPVLLDVLVDPEENV 179
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
8-170 |
2.20e-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: 128.05 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 8 DAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAGTDMITGL 87
Cdd:cd07039 4 DVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLT-GKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 88 YSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAfhlMRS--GRPGPVLIDLPVD 165
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRA---IRTaiAKRGVAVLILPGD 159
|
....*
gi 429555433 166 VQLAE 170
Cdd:cd07039 160 VQDAP 164
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
369-559 |
9.91e-34 |
|
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: 126.49 E-value: 9.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 369 PLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYD 448
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 449 FQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQAQRGF-NMDFEVSLafeninadgdaekgYGVDHVAVAEGLGCKAIRV 527
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMgQPEFGVDL--------------PNPDFAKIAEAMGIKGIRV 146
|
170 180 190
....*....|....*....|....*....|..
gi 429555433 528 RSPNEFADAFDRAQAlmeeHQVPVVIEFILER 559
Cdd:cd02014 147 EDPDELEAALDEALA----ADGPVVIDVVTDP 174
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
8-164 |
2.79e-25 |
|
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: 102.04 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 8 DAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYtrARHGNIGVCIGTSGPAGTDMITGL 87
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGY--ARAGGPPVVIVTSGTGLLNAINGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429555433 88 YSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGrPGPVLIDLPV 164
Cdd:cd06586 79 ADAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
369-559 |
2.70e-21 |
|
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: 91.80 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 369 PLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYD 448
Cdd:cd02013 3 PMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 449 FQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQAQRGFNMDFEVSLAFENINADGdaekgygvdhvaVAEGLGCKAIRVR 528
Cdd:cd02013 83 WGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESESFAK------------IAEACGAKGITVD 150
|
170 180 190
....*....|....*....|....*....|.
gi 429555433 529 SPNEFADAFDRAQALMEEHQvPVVIEFILER 559
Cdd:cd02013 151 KPEDVGPALQKAIAMMAEGK-TTVIEIVCDQ 180
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
372-558 |
4.09e-21 |
|
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: 90.67 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 372 PQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQF 451
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 452 LIEELAVGAQHKLPYLHVVVNNSYLGLIRQAQRGfnmDFEVSLAFENINADGDAEKgygvdhvaVAEGLGCKAIRVRSPN 531
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQL---SYGLGLPVTTLLPDTRYDL--------VAEAFGGKGELVTTPE 149
|
170 180
....*....|....*....|....*..
gi 429555433 532 EFADAFDRAQAlmeeHQVPVVIEFILE 558
Cdd:cd02004 150 ELKPALKRALA----SGKPALINVIID 172
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
402-554 |
1.45e-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: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 402 QFLHVYKPRNWINCGqAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQ 481
Cdd:cd02002 33 DQLPLTRPGSYFTLR-GGGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALWTAARYGLPVTVVILNNRGYGALRS 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429555433 482 AQRGFNMDFEVSLAFENINADGDaekgyGVDHVAVAEGLGCKAIRVRSPNEFADAFDRAqalmEEHQVPVVIE 554
Cdd:cd02002 112 FLKRVGPEGPGENAPDGLDLLDP-----GIDFAAIAKAFGVEAERVETPEELDEALREA----LAEGGPALIE 175
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
372-554 |
6.71e-18 |
|
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: 81.57 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 372 PQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLHVYKPRN-WINCGQAgPLGWTLPAALGVRAADPNRQIVALSGDYDFQ 450
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTcLISNGLA-TMGVALPGAIGAKLVYPDRKVVAVSGDGGFM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 451 FLIEELAVGAQHKLPYLHVVVNNSYLGLIR-QAQRGFNMDFEVSlaFENInadgdaekgygvDHVAVAEGLGCKAIRVRS 529
Cdd:cd02010 80 MNSQELETAVRLKIPLVVLIWNDNGYGLIKwKQEKEYGRDSGVD--FGNP------------DFVKYAESFGAKGYRIES 145
|
170 180
....*....|....*....|....*
gi 429555433 530 PNEFADAFDRAQALmeehQVPVVIE 554
Cdd:cd02010 146 ADDLLPVLERALAA----DGVHVID 166
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
421-554 |
2.46e-14 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 71.95 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 421 LGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQAQRGFNMDfevslAFENIN 500
Cdd:cd02003 50 MGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSG-----SFGTEF 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 501 ADGDAEKGYG------VDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlmeeHQVPVVIE 554
Cdd:cd02003 125 RDRDQESGQLdgallpVDFAANARSLGARVEKVKTIEELKAALAKAKA----SDRTTVIV 180
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
369-559 |
1.06e-11 |
|
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: 63.71 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 369 PLKPQRVYEEMNKILGRDTCYVSTIGLSQIAGAQFLhVYKPRNWINCGQAGPLGWTLPAALGVRAADPNRQIVALSGDYD 448
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLK-LPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 449 FQFLIEELAVGAQHKLPYLHVVVNN---SYLGLIRQAQRGFNmdfevslafeNINadgdaekgyGVDHVAVAEGLGC--- 522
Cdd:cd02005 80 FQMTVQELSTMIRYGLNPIIFLINNdgyTIERAIHGPEASYN----------DIA---------NWNYTKLPEVFGGggg 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 429555433 523 -KAIRVRSPNEFADAFDRAQAlmeEHQVPVVIEFILER 559
Cdd:cd02005 141 gLSFRVKTEGELDEALKDALF---NRDKLSLIEVILPK 175
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
54-480 |
2.82e-08 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 56.63 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 54 ASHMAEGYTRARhgNIGVCIGTSGPAGTDMITGLYSASADSIPILCITG-----------------------QAPRArld 110
Cdd:PLN02573 66 AGYAADGYARAR--GVGACVVTFTVGGLSVLNAIAGAYSENLPVICIVGgpnsndygtnrilhhtiglpdfsQELRC--- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 111 kedFQAVDIAKIAapvtkwaVTVMEPA--LVPFVFQKAFHlmrsgRPGPVLIDlpVDVQLAEIEFDPETYEPL------S 182
Cdd:PLN02573 141 ---FQTVTCYQAV-------INNLEDAheLIDTAISTALK-----ESKPVYIS--VSCNLAAIPHPTFSREPVpffltpR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 183 AYKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVPTLMGWGVIPDDHPLMAGMCGLQTSHR 262
Cdd:PLN02573 204 LSNKMSLEAAVEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADASGYPVAVMPSAKGLVPEHHPHFIGTYWGAVSTP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 263 YGNATLLASDFVFGIGNRWANRHTGNIPTYTEGRKFIHVDIEPTQIGRvfAPDFGIVsdagaALKLFLDVatewkTAGKL 342
Cdd:PLN02573 284 FCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGN--GPAFGCV-----LMKDFLEA-----LAKRV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 343 RDWSAWAEecrERKRSMLRKTH-FDQTPLKPQRV---YEEMNKILGRDTCYVSTIGLSqiagaqFLHVYKPRNWINCG-- 416
Cdd:PLN02573 352 KKNTTAYE---NYKRIFVPEGEpLKSEPGEPLRVnvlFKHIQKMLSGDTAVIAETGDS------WFNCQKLKLPEGCGye 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 417 ---QAGPLGWTLPAALGVRAADPNRQIVALSGDYDFQ------------------FLIE------ELAVgaqHKLPYlHV 469
Cdd:PLN02573 423 fqmQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQvtaqdvstmircgqksiiFLINnggytiEVEI---HDGPY-NV 498
|
490
....*....|.
gi 429555433 470 VVNNSYLGLIR 480
Cdd:PLN02573 499 IKNWNYTGLVD 509
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
1-557 |
1.49e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 54.11 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 1 MAKMRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhGNIGVCIGTSGPAG 80
Cdd:PRK12474 2 GQTMNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIA-GKPAVTLLHLGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 81 TDMITGLYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSGRPGPVLI 160
Cdd:PRK12474 81 ANGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 161 DLPVDVQLAEIEFdpeTYEPLSAYKPAATRAQA-EKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGVPVVP--- 236
Cdd:PRK12474 161 IMPADVAWNEAAY---AAQPLRGIGPAPVAAETvERIAALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVRLYCdtf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 237 ---TLMGWGVIPddhplmagMCGLQTSHRYGNATLLASDFVFGIGNRwanrhtgniptytEGRKFIHVdiePTQIGRVFA 313
Cdd:PRK12474 238 aprIERGAGRVP--------IERIPYFHEQITAFLKDVEQLVLVGAK-------------PPVSFFAY---PGKPSWGAP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 314 PDFGIVSDAGAALKLfldvatewktAGKLRDWSAWAEECRERKrsmlrkthfdqtpLKPQRVYEEMNKilGRdtcyvsti 393
Cdd:PRK12474 294 PGCEIVYLAQPDEDL----------AQALQDLADAVDAPAEPA-------------ARTPLALPALPK--GA-------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 394 gLSQIAGAQFLHVYKPRNWINCGQA------------------------GPLGWTLPAALGVRAADPNRQIVALSGDYDF 449
Cdd:PRK12474 341 -LNSLGVAQLIAHRTPDQAIYADEAltsglffdmsydrarphthlpltgGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGA 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 450 QFLIEELAVGAQHKLPYLHVV-VNNSYLGLIRQAQRgfnmdfevslafenINADGDAEKGYG--------VDHVAVAEGL 520
Cdd:PRK12474 420 AYTMQALWTMARENLDVTVVIfANRSYAILNGELQR--------------VGAQGAGRNALSmldlhnpeLNWMKIAEGL 485
|
570 580 590
....*....|....*....|....*....|....*..
gi 429555433 521 GCKAIRVRSPNEFADAFDRAQAlmeeHQVPVVIEFIL 557
Cdd:PRK12474 486 GVEASRATTAEEFSAQYAAAMA----QRGPRLIEAMI 518
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
26-163 |
4.16e-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: 47.11 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 26 PGAAINPFYSALRARGSIRHILarHVE--GASHMAEGYTRARhGNIGVCIGTSGPAGTDMITGLYSASADSIPILCITGQ 103
Cdd:cd07037 19 PGSRSAPLALAAAEHPEFRLHV--RVDerSAAFFALGLAKAS-GRPVAVVCTSGTAVANLLPAVVEAYYSGVPLLVLTAD 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429555433 104 APRARLDKEDFQAVDIAKIAAPVTKWAVTV------MEPALVPFVFQKAFHLMRSGRPGPVLIDLP 163
Cdd:cd07037 96 RPPELRGTGANQTIDQVGLFGDYVRWSVDLpppeddDDLWYLLRLANRAVLEALSAPPGPVHLNLP 161
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
14-164 |
5.61e-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: 46.72 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 14 LEKEGIDCAFGVPGAAINPFYSALRARGSIRHILARHVEGASHMAEGYTRARhgNIGVCIGTSGPAGTDMITGLYSASAD 93
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVK--GLGALVTTYGVGELSALNGIAGAYAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 94 SIPILCITGQAPRAR----------LDKEDFQAvdIAKIAAPVTKWAVTVMEPALVPFVFQKAF-HLMRSGRpgPVLIDL 162
Cdd:cd07038 85 HVPVVHIVGAPSTKAqasglllhhtLGDGDFDV--FLKMFEEITCAAARLTDPENAAEEIDRVLrTALRESR--PVYIEI 160
|
..
gi 429555433 163 PV 164
Cdd:cd07038 161 PR 162
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
4-232 |
4.75e-05 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 46.38 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 4 MRAVDAAVYVLEKEGIDCAFGVPGAAINPFYSAL-RARGsIRHILARHVEGASHMAEGYTRArhgnigvcigTSGPAGTD 82
Cdd:PRK07586 1 MNGAESLVRTLVDGGVDVCFANPGTSEMHFVAALdRVPG-MRCVLGLFEGVATGAADGYARM----------AGKPAATL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 83 MITG---------LYSASADSIPILCITGQAPRARLDKEDFQAVDIAKIAAPVTKWAVTVMEPALVPFVFQKAFHLMRSG 153
Cdd:PRK07586 70 LHLGpglanglanLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429555433 154 RPGPVLIDLPVDVQLAEIefDPETYEPLSAYKPAATRAQAEKALAMLNEAERPLIVAGGGIINADASDLLTEFAEITGV 232
Cdd:PRK07586 150 PGQVATLILPADVAWSEG--GPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAATGA 226
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
409-554 |
5.51e-05 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 45.99 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429555433 409 PRNWI-NCGqaGPLGWTLPAALGVRAADPNRQIVALSGDYDFQFLIEELAVGAQHKLPYLHVVVNNSYLGLIRQAQRGFN 487
Cdd:PRK07586 376 PHDWLtLTG--GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGELARVG 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429555433 488 MDFEVSLAFENINADGDAekgygVDHVAVAEGLGCKAIRVRSPNEFADAFDRAQAlmeeHQVPVVIE 554
Cdd:PRK07586 454 AGNPGPRALDMLDLDDPD-----LDWVALAEGMGVPARRVTTAEEFADALAAALA----EPGPHLIE 511
|
|
| |
