|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-587 |
0e+00 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 1313.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAAGNIGVCLGTSGPAG 80
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIGVCIGTSGPAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 81 TDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLV 160
Cdd:PRK11269 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 161 DLPFDVQVAEIEFDPDMYEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMG 240
Cdd:PRK11269 161 DLPFDVQVAEIEFDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 241 WGCIPDDHPLMAGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVS 320
Cdd:PRK11269 241 WGAIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 321 DAKAALTLLIDVAQEMQKAGRLPCRKTWVDECQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAA 400
Cdd:PRK11269 321 DAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQIAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 401 AQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIR 480
Cdd:PRK11269 401 AQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 481 QSQRAFDMDYCVQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPVVVEVILERVTN 560
Cdd:PRK11269 481 QAQRAFDMDYCVQLAFENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALEQAKALMAEFRVPVVVEVILERVTN 560
|
570 580
....*....|....*....|....*..
gi 261245799 561 ISMGSELDNVTEFEEVADSAKDAPTET 587
Cdd:PRK11269 561 ISMGTEIDAVNEFEELADNAADAPTAI 587
|
|
| Gcl |
COG3960 |
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism]; |
2-589 |
0e+00 |
|
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443160 [Multi-domain] Cd Length: 588 Bit Score: 1311.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 2 AKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAAGNIGVCLGTSGPAGT 81
Cdd:COG3960 1 ARMRAVDAAVAVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHVLARHVEGASHMAEGYTRAKAGNIGVCIGTSGPAGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 82 DMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVD 161
Cdd:COG3960 81 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVLEPAQVPRVFQQAFHLMRSGRPGPVLID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 162 LPFDVQVAEIEFDPDMYEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGW 241
Cdd:COG3960 161 LPIDVQMAEIEFDIDTYEPLPVYKPAATRAQIEKALDMLNAAERPLIVAGGGIINADASDLLVEFAELTGVPVIPTLMGW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 242 GCIPDDHPLMAGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSD 321
Cdd:COG3960 241 GSIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRWANRHTGSLDVYTKGRKFVHVDIEPTQIGRVFAPDLGIVSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 322 AKAALTLLIDVAQEMQKAGRLPCRKTWVDECQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAA 401
Cdd:COG3960 321 AKAALELFVEVARERKAAGKLPDRSAWAAECQERKRTMLRKTHFDNVPIKPQRVYEEMNKAFGRDTRYVSTIGLSQIAAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 402 QMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQ 481
Cdd:COG3960 401 QFLHVYKPRHWINCGQAGPLGWTIPAALGVVAADPDRPVVALSGDYDFQFMIEELAVGAQFKLPYIHVVVNNSYLGLIRQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 482 SQRAFDMDYCVQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPVVVEVILERVTNI 561
Cdd:COG3960 481 AQRGFDMDYCVQLAFENINAPELGGYGVDHVKVAEGLGCKAIRVTDPEEIAPAFEEAKALMAEHRVPVVVEVILERVTNI 560
|
570 580
....*....|....*....|....*...
gi 261245799 562 SMGSELDNVTEFEEVADSAKDAPTETCF 589
Cdd:COG3960 561 SMGTEIDNVNEFEELAESPADAPTAIAL 588
|
|
| 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: 1182.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 2 AKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAAGNIGVCLGTSGPAGT 81
Cdd:TIGR01504 1 ARMRAVDAAVYVLEKEGITTAFGVPGAAINPFYSALKAHGGIRHILARHVEGASHMAEGYTRATAGNIGVCIGTSGPAGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 82 DMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVD 161
Cdd:TIGR01504 81 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 162 LPFDVQVAEIEFDPDMYEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGW 241
Cdd:TIGR01504 161 LPFDVQVAEIEFDPDTYEPLPVYKPAATRAQIEKAVEMLNAAERPLIVAGGGVINADAADLLQEFAELTGVPVIPTLMGW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 242 GCIPDDHPLMAGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSD 321
Cdd:TIGR01504 241 GCIPDDHELMAGMVGLQTSHRYGNATLLESDFVFGIGNRWANRHTGSVDVYTEGRKFVHVDIEPTQIGRVFAPDLGIVSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 322 AKAALTLLIDVAQEMQKAGRLPCRKTWVDECQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAA 401
Cdd:TIGR01504 321 AKAALKLLVEVAQELKKAGRLPDRSEWAADCQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAGA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 402 QMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQ 481
Cdd:TIGR01504 401 QMLHVYKPRHWINCGQAGPLGWTIPAALGVCAADPKRNVVALSGDYDFQFMIEELAVGAQHNIPYIHVLVNNAYLGLIRQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 482 SQRAFDMDYCVQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPVVVEVILERVTNI 561
Cdd:TIGR01504 481 AQRAFDMDYCVQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEEIAPAFEQAKALMAEHRVPVVVEVILERVTNI 560
|
570 580
....*....|....*....|....*...
gi 261245799 562 SMGSELDNVTEFEEVADSAKDAPTETCF 589
Cdd:TIGR01504 561 SMGSEIDNVVEFEDLADNAADAPTATCF 588
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
2-570 |
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: 542.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 2 AKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGT 81
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARAT-GKPGVCLVTSGPGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 82 DMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVD 161
Cdd:COG0028 80 NLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 162 LPFDVQVAEIEFDPDMYEpLPVYKP--AASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLM 239
Cdd:COG0028 160 IPKDVQAAEAEEEPAPPE-LRGYRPrpAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 240 GWGCIPDDHPLMAGMVGLQtAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIV 319
Cdd:COG0028 239 GKGAFPEDHPLYLGMLGMH-GTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 320 SDAKAALTLLIDVAQEmqkagRLPCRKTWVDECQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIA 399
Cdd:COG0028 318 GDAKAVLAALLEALEP-----RADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 400 AAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLI 479
Cdd:COG0028 393 AARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 480 RQSQRAFDMDYCVQLAFENInssevngygvDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAlmaqYRVPVVVEVILERVT 559
Cdd:COG0028 473 RQWQELFYGGRYSGTDLPNP----------DFAKLAEAFGAKGERVETPEELEAALEEALA----SDGPALIDVRVDPEE 538
|
570
....*....|.
gi 261245799 560 NiSMGSELDNV 570
Cdd:COG0028 539 N-PPGATLDEM 548
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
4-561 |
6.73e-163 |
|
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: 476.52 E-value: 6.73e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 4 MRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDM 83
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARAS-GKVGVVLVTSGPGATNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 84 ITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLP 163
Cdd:TIGR00118 80 VTGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 164 FDVQVAEIEFDPDMYEPLPVYKPA--ASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGW 241
Cdd:TIGR00118 160 KDVTTAEIEYPYPEKVNLPGYRPTvkGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 242 GCIPDDHPLMAGMVGLQtAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSD 321
Cdd:TIGR00118 240 GSFPEDHPLSLGMLGMH-GTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 322 AKAALtllidvAQEMQKAGRLPCRK--TWVDECQQRKRTLLRKTHFDNVPVKPQRVYEEMNKaFGRDVCYVTT-IGLSQI 398
Cdd:TIGR00118 319 ARNVL------EELLKKLFELKERKesAWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSR-VTKDEAIVTTdVGQHQM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 399 AAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGL 478
Cdd:TIGR00118 392 WAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGM 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 479 IRQSQRAFdmdycvqlaFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAlmaqYRVPVVVEVILERV 558
Cdd:TIGR00118 472 VRQWQELF---------YEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALS----SNEPVLLDVVVDKP 538
|
...
gi 261245799 559 TNI 561
Cdd:TIGR00118 539 ENV 541
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
363-564 |
6.18e-157 |
|
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: 447.50 E-value: 6.18e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 363 THFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVA 442
Cdd:cd02006 1 THFDDVPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 443 ISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDMDYCVQLAFENINSSEVNGYGVDHVKVAEGLGCKA 522
Cdd:cd02006 81 LSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAFDMDYQVNLAFENINSSELGGYGVDHVKVAEGLGCKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 261245799 523 IRVFKPEDIAPAFEQAKALMAQYRVPVVVEVILERVTNISMG 564
Cdd:cd02006 161 IRVTKPEELAAAFEQAKKLMAEHRVPVVVEAILERVTNISMG 202
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-575 |
1.33e-156 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 460.40 E-value: 1.33e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAG 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARAT-GKVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 81 TDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLV 160
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 161 DLPFDVQVAEIEFD-PDMYEpLPVYKP--AASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPT 237
Cdd:PRK06048 163 DLPKDVTTAEIDFDyPDKVE-LRGYKPtyKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 238 LMGWGCIPDDHPLMAGMVGLQTAhRYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLG 317
Cdd:PRK06048 242 LMGIGAIPTEHPLSLGMLGMHGT-KYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 318 IVSDAKAALTLLIDVAQEMQkagrlpcRKTWVDECQQRKRTL-LRKTHFDNVpVKPQRVYEEMNKAFgRDVCYVTTIGLS 396
Cdd:PRK06048 321 IVGDAKQVLKSLIKYVQYCD-------RKEWLDKINQWKKEYpLKYKEREDV-IKPQYVIEQIYELC-PDAIIVTEVGQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 397 QIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYL 476
Cdd:PRK06048 392 QMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 477 GLIRQSQRAFdmdycvqlaFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAqyrvPVVVEVILE 556
Cdd:PRK06048 472 GMVRQWQELF---------YDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDR----PVVIDFIVE 538
|
570 580
....*....|....*....|...
gi 261245799 557 RVTNIS----MGSELDNVTEFEE 575
Cdd:PRK06048 539 CEENVSpmvpAGAAINEILDLEE 561
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
14-554 |
1.71e-137 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 413.22 E-value: 1.71e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTrAAAGNIGVCLGTSGPAGTDMITALYSASAD 93
Cdd:PRK07789 41 LEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYA-QATGRVGVCMATSGPGATNLVTPIADANMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 94 SIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIEF 173
Cdd:PRK07789 120 SVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPKDALQAQTTF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 174 D--PDMYepLPVYKP---AASRvQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGWGCIPDDH 248
Cdd:PRK07789 200 SwpPRMD--LPGYRPvtkPHGK-QIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTLMARGAFPDSH 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 249 PL---MAGMVGLQTAhrygNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSDAKAA 325
Cdd:PRK07789 277 PQhlgMPGMHGTVAA----VAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHADVPIVGDVKEV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 326 LTLLIDVAQEMQKAGRLPCRKTWVDECQQ-RKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQML 404
Cdd:PRK07789 353 IAELIAALRAEHAAGGKPDLTAWWAYLDGwRETYPLGYDEPSDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQFI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 405 HVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPyIHV-LVNNAYLGLIRQSQ 483
Cdd:PRK07789 433 DYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIP-IKVaLINNGNLGMVRQWQ 511
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245799 484 RAF-DMDYcvqlafENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAkalMAQYRVPVVVEVI 554
Cdd:PRK07789 512 TLFyEERY------SNTDLHTHSHRIPDFVKLAEAYGCVGLRCEREEDVDAVIEKA---RAINDRPVVIDFV 574
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
4-570 |
9.07e-137 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 410.68 E-value: 9.07e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 4 MRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRkHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDM 83
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALY-DSDLIHILTRHEQAAAHAADGYARAS-GKVGVCVATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 84 ITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLP 163
Cdd:PRK06276 79 VTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 164 FDVQVAEIEFDPDMYE---PLPVYKPA--ASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTL 238
Cdd:PRK06276 159 KDVQEGELDLEKYPIPakiDLPGYKPTtfGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 239 MGWGCIPDDHPLMAGMVGLQtAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGI 318
Cdd:PRK06276 239 MGKGAFPEDHPLALGMVGMH-GTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 319 VSDAKAALTLLIDVAQEMQKAGrlpcRKTWVDECQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAF-----GRDVCYVTTI 393
Cdd:PRK06276 318 VGDAKNVLRDLLAELMKKEIKN----KSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLreidpSKNTIITTDV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 394 GLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNN 473
Cdd:PRK06276 394 GQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDN 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 474 AYLGLIRQSQRAFdmdYcvqlafeNINSSEVN-GYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAkalmAQYRVPVVVE 552
Cdd:PRK06276 474 RTLGMVYQWQNLY---Y-------GKRQSEVHlGETPDFVKLAESYGVKADRVEKPDEIKEALKEA----IKSGEPYLLD 539
|
570 580
....*....|....*....|.
gi 261245799 553 VILERVTNISM---GSELDNV 570
Cdd:PRK06276 540 IIIDPAEALPMvppGGNLTNI 560
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
8-560 |
5.62e-125 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 381.32 E-value: 5.62e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 8 DAAMYVLEKEGITTAFGVPGAAINPFYSAMRK---HGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMI 84
Cdd:PRK07418 23 YALMDSLKRHGVKHIFGYPGGAILPIYDELYKaeaEGWLKHILVRHEQGAAHAADGYARAT-GKVGVCFGTSGPGATNLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 85 TALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPF 164
Cdd:PRK07418 102 TGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 165 DVQVAEIEFDPdmYEP----LPVYKP--AASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTL 238
Cdd:PRK07418 182 DVGQEEFDYVP--VEPgsvkPPGYRPtvKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTTL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 239 MGWGCIPDDHPLMAGMVGLQ-TAhrYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLG 317
Cdd:PRK07418 260 MGKGAFDEHHPLSVGMLGMHgTA--YANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 318 IVSDAKAALTLLIDVAQEMQKAGRlpcRKTWVDECQQRKRtllrkTHFDNVPVKPQRVY-EEMNKAFGR---DVCYVTTI 393
Cdd:PRK07418 338 IVGDVRKVLVKLLERSLEPTTPPR---TQAWLERINRWKQ-----DYPLVVPPYEGEIYpQEVLLAVRDlapDAYYTTDV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 394 GLSQIAAAQMLhvfKD--RHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLV 471
Cdd:PRK07418 410 GQHQMWAAQFL---RNgpRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVII 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 472 NNAYLGLIRQSQRAF-DMDYCvqlafeniNSSEVNGYGvDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAlmaqYRVPVV 550
Cdd:PRK07418 487 NNGWQGMVRQWQESFyGERYS--------ASNMEPGMP-DFVKLAEAFGVKGMVISERDQLKDAIAEALA----HDGPVL 553
|
570
....*....|
gi 261245799 551 VEVILERVTN 560
Cdd:PRK07418 554 IDVHVRRDEN 563
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
14-557 |
1.10e-123 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 376.08 E-value: 1.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITALYSASAD 93
Cdd:PRK07282 20 LRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKST-GKLGVAVVTSGPGATNAITGIADAMSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 94 SIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIEF 173
Cdd:PRK07282 99 SVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKDVSALETDF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 174 DPDMYEPLPVYKPA--ASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGWGCIPDDHPLM 251
Cdd:PRK07282 179 IYDPEVNLPSYQPTlePNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 252 AGMVGLQTAHRyGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSDAKAALTLLID 331
Cdd:PRK07282 259 LGMGGMHGSYA-ANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKKALQMLLA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 332 vaqemqkagrLPCRKT----WVDECQQRKRTlLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVF 407
Cdd:PRK07282 338 ----------EPTVHNntekWIEKVTKDKNR-VRSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 408 KDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFd 487
Cdd:PRK07282 407 NERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESF- 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 488 mdycvqlaFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAlmaqyRVPVVVEVILER 557
Cdd:PRK07282 486 --------YEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLEVITE-----DVPMLIEVDISR 542
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
9-560 |
1.55e-121 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 371.73 E-value: 1.55e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 9 AAMYV--LEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITA 86
Cdd:PRK09107 14 AEMVVqaLKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARST-GKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 87 LYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDV 166
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 167 QVAEIEFDPDmyEPLPVYKPAASRV-----QIEKALEMLIQSERPVIVAGGGVINA--DAAPLLQQFAELTNVPVIPTLM 239
Cdd:PRK09107 173 QFATGTYTPP--QKAPVHVSYQPKVkgdaeAITEAVELLANAKRPVIYSGGGVINSgpEASRLLRELVELTGFPITSTLM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 240 GWGCIPDDHPLMAGMVGLQTAHRyGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIV 319
Cdd:PRK09107 251 GLGAYPASGKNWLGMLGMHGTYE-ANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPII 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 320 SDAKAALTLLIDVAQEMQKAGRLPCRKTWVDECQQ-RKRTLLRKTHFDNVpVKPQ----RVYeEMNKafGRDVcYVTT-I 393
Cdd:PRK09107 330 GDVGHVLEDMLRLWKARGKKPDKEALADWWGQIARwRARNSLAYTPSDDV-IMPQyaiqRLY-ELTK--GRDT-YITTeV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 394 GLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNN 473
Cdd:PRK09107 405 GQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 474 AYLGLIRQSQrafdmdycvQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQakalMAQYRVPVVVEV 553
Cdd:PRK09107 485 QYMGMVRQWQ---------QLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQE----MIDVDKPVIFDC 551
|
....*..
gi 261245799 554 ILERVTN 560
Cdd:PRK09107 552 RVANLEN 558
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-538 |
2.71e-121 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 370.19 E-value: 2.71e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAG 80
Cdd:PRK08155 10 RKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTT-GKPAVCMACSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 81 TDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLV 160
Cdd:PRK08155 89 TNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 161 DLPFDVQVAEIEFD--PDMYEPLPVykPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTL 238
Cdd:PRK08155 169 DIPKDVQTAVIELEalPAPAEKDAA--PAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 239 MGWGCIPDDHPLMAGMVGLQTAhRYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGI 318
Cdd:PRK08155 247 MALGMLPKAHPLSLGMLGMHGA-RSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 319 VSDAKAALTLLIDVAQEMQkagrlpcRKTW---VDECQQRKRTLLRKThfDNvPVKPQRVYEEMNKAFGRDVCYVTTIGL 395
Cdd:PRK08155 326 QADVDDVLAQLLPLVEAQP-------RAEWhqlVADLQREFPCPIPKA--DD-PLSHYGLINAVAACVDDNAIITTDVGQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 396 SQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAY 475
Cdd:PRK08155 396 HQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEA 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245799 476 LGLIRQSQ------RAFDMDYcvqlafeninssevnGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQA 538
Cdd:PRK08155 476 LGLVHQQQslfygqRVFAATY---------------PGKINFMQIAAGFGLETCDLNNEADPQAALQEA 529
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
14-561 |
1.49e-120 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 367.89 E-value: 1.49e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITALYSASAD 93
Cdd:PRK08527 13 LKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARAS-GKVGVAIVTSGPGFTNAVTGLATAYMD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 94 SIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIEF 173
Cdd:PRK08527 92 SIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPKDVTATLGEF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 174 D-PDMYEpLPVYKPA--ASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGWGCIPDDHPL 250
Cdd:PRK08527 172 EyPKEIS-LKTYKPTykGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMARGVLRSDDPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 251 MAGMVGLQTAHRyGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSDAKAALTLLI 330
Cdd:PRK08527 251 LLGMLGMHGSYA-ANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGDLKNVLKEML 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 331 DVAQEMQKAGrlpcRKTWVDECQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDR 410
Cdd:PRK08527 330 EELKEENPTT----YKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 411 HWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFdmdy 490
Cdd:PRK08527 406 QLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQWQTFF---- 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261245799 491 cvqlaFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAkalmAQYRVPVVVEVILERVTNI 561
Cdd:PRK08527 482 -----YEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEA----LESDKVALIDVKIDRFENV 543
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
14-561 |
2.33e-119 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 365.45 E-value: 2.33e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITALYSASAD 93
Cdd:PRK06725 25 LKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARAS-GKVGVVFATSGPGATNLVTGLADAYMD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 94 SIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIEF 173
Cdd:PRK06725 103 SIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVQNEKVTS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 174 DPDMYEPLPVYKP--AASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGWGCIPDDHPLM 251
Cdd:PRK06725 183 FYNEVVEIPGYKPepRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 252 AGMVGLQTAHRyGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSDAKAALTLLID 331
Cdd:PRK06725 263 LGMLGMHGTYA-ANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVGDVKKALHMLLH 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 332 VAQEMQKAGRLPCRKTWVDECQ---QRKRTLLrkthfdnvpvKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFK 408
Cdd:PRK06725 342 MSIHTQTDEWLQKVKTWKEEYPlsyKQKESEL----------KPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKN 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 409 DRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFdm 488
Cdd:PRK06725 412 PRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEMF-- 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261245799 489 dYCVQLAFENINSSevngygvDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAlmaqYRVPVVVEVILERVTNI 561
Cdd:PRK06725 490 -YENRLSESKIGSP-------DFVKVAEAYGVKGLRATNSTEAKQVMLEAFA----HEGPVVVDFCVEEGENV 550
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
2-553 |
1.89e-117 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 360.23 E-value: 1.89e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 2 AKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGT 81
Cdd:PRK07710 14 KLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARIS-GKPGVVIATSGPGAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 82 DMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVD 161
Cdd:PRK07710 92 NVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 162 LPFDVQVAEIEFDPDMYEPLPVYKPAA--SRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLM 239
Cdd:PRK07710 172 IPKDMVVEEGEFCYDVQMDLPGYQPNYepNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 240 GWGCIPDDHPL---MAGMVGLQTAhrygNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDL 316
Cdd:PRK07710 252 GLGGFPADHPLflgMAGMHGTYTA----NMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 317 GIVSDAKAALTLLIdvaqemQKAGRLPCRKTWVDECQQRKRTLlrKTHFDNVP--VKPQRVYEEMNKAFGRDVCYVTTIG 394
Cdd:PRK07710 328 PIVADAKQALQVLL------QQEGKKENHHEWLSLLKNWKEKY--PLSYKRNSesIKPQKAIEMLYEITKGEAIVTTDVG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 395 LSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNA 474
Cdd:PRK07710 400 QHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNE 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245799 475 YLGLIRQSQRAFdmdycvqlaFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALmaqyRVPVVVEV 553
Cdd:PRK07710 480 ALGMVRQWQEEF---------YNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIEL----QEPVVIDC 545
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
14-560 |
4.77e-115 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 354.39 E-value: 4.77e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYS---AMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITALYSA 90
Cdd:CHL00099 20 LVRHGVKHIFGYPGGAILPIYDelyAWEKKGLIKHILVRHEQGAAHAADGYARST-GKVGVCFATSGPGATNLVTGIATA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 91 SADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAE 170
Cdd:CHL00099 99 QMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVGLEK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 171 IefdpDMYEPLPV----------YKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMG 240
Cdd:CHL00099 179 F----DYYPPEPGntiikilgcrPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLMG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 241 WGCIPDDHPLMAGMVGLQ-TAhrYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIV 319
Cdd:CHL00099 255 KGIFDEDHPLCLGMLGMHgTA--YANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 320 SDAKAALTLLIDVaqeMQKAGRLPCRK---TWvdecqqRKRT-LLRKTHFDNVPVK-----PQRVYEEMNKaFGRDVCYV 390
Cdd:CHL00099 333 GDVKKVLQELLEL---LKNSPNLLESEqtqAW------RERInRWRKEYPLLIPKPstslsPQEVINEISQ-LAPDAYFT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 391 TTIGLSQIAAAQMLHVfKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVL 470
Cdd:CHL00099 403 TDVGQHQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIII 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 471 VNNAYLGLIRQSQRAFdmdYCVQLAFENINSSEVNgygvdHVKVAEGLGCKAIRVFKPEDIAPAFEQAkalmAQYRVPVV 550
Cdd:CHL00099 482 INNKWQGMVRQWQQAF---YGERYSHSNMEEGAPD-----FVKLAEAYGIKGLRIKSRKDLKSSLKEA----LDYDGPVL 549
|
570
....*....|
gi 261245799 551 VEVILERVTN 560
Cdd:CHL00099 550 IDCQVIEDEN 559
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-541 |
6.02e-114 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 351.35 E-value: 6.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAG 80
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARAT-GKTGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 81 TDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLV 160
Cdd:PRK06466 80 TNAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 161 DLPFDVQVAEIEFDPDMYEPLPV--YKPAAS--RVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIP 236
Cdd:PRK06466 160 DIPKDMTNPAEKFEYEYPKKVKLrsYSPAVRghSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 237 TLMGWGCIPDDHPLMAGMVGLQTAHRyGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDL 316
Cdd:PRK06466 240 TLMGLGGFPGTDRQFLGMLGMHGTYE-ANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 317 GIVSDAKAALTLLIDVAQEMQKAGRLPCRKTW---VDECQQRkRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVcYVTT- 392
Cdd:PRK06466 319 PIVGPVESVLTEMLAILKEIGEKPDKEALAAWwkqIDEWRGR-HGLFPYDKGDGGIIKPQQVVETLYEVTNGDA-YVTSd 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 393 IGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVN 472
Cdd:PRK06466 397 VGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLN 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245799 473 NAYLGLIRQSQrafDMDYCVQLAFENINSSEvngygvDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAL 541
Cdd:PRK06466 477 NGALGMVRQWQ---DMQYEGRHSHSYMESLP------DFVKLAEAYGHVGIRITDLKDLKPKLEEAFAM 536
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-541 |
6.28e-112 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 346.04 E-value: 6.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAG 80
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARAT-GKVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 81 TDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLV 160
Cdd:PRK08979 80 TNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 161 DLPFDVQVAEIEFDPDMYEPLPV--YKPAAS--RVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIP 236
Cdd:PRK08979 160 DLPKDCLNPAILHPYEYPESIKMrsYNPTTSghKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 237 TLMGWGCIPDDHPLMAGMVGLQTAHRyGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDL 316
Cdd:PRK08979 240 TLMGLGAFPGTHKNSLGMLGMHGRYE-ANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 317 GIVSDAKAALTLLIDVAQEMQKAGRLPCRKTWVDECQQ-RKRTLLRkthFDNVP--VKPQRVYEEMNKAFGRDVCYVTTI 393
Cdd:PRK08979 319 PIVGSADKVLDSMLALLDESGETNDEAAIASWWNEIEVwRSRNCLA---YDKSSerIKPQQVIETLYKLTNGDAYVASDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 394 GLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNN 473
Cdd:PRK08979 396 GQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNN 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245799 474 AYLGLIRQSQrafDMDYCVQLAFENINSSEvngygvDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAL 541
Cdd:PRK08979 476 RFLGMVKQWQ---DMIYQGRHSHSYMDSVP------DFAKIAEAYGHVGIRISDPDELESGLEKALAM 534
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
9-556 |
3.04e-110 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 341.83 E-value: 3.04e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 9 AAMYV--LEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITA 86
Cdd:PRK07979 7 AEMVVrsLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARAT-GEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 87 LYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDV 166
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 167 QVAEIEFdPDMYePLPV----YKPAAS--RVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMG 240
Cdd:PRK07979 166 LNPANKL-PYVW-PESVsmrsYNPTTQghKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 241 WGCIPDDHPLMAGMVGLQTAHRyGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVS 320
Cdd:PRK07979 244 LGAFPATHRQSLGMLGMHGTYE-ANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 321 DAKAALTLLIDVAQEMQKAGRLPCRKTWVDECQQ-RKRTLLrKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIA 399
Cdd:PRK07979 323 DARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQwRARQCL-KYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 400 AAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLI 479
Cdd:PRK07979 402 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMV 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261245799 480 RQSQrafDMDYCVQLAFENINSSEvngygvDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVpVVVEVILE 556
Cdd:PRK07979 482 KQWQ---DMIYSGRHSQSYMQSLP------DFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNNRL-VFVDVTVD 548
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-561 |
3.11e-110 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 341.89 E-value: 3.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAG 80
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARST-GKVGCVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 81 TDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLV 160
Cdd:PRK06882 80 TNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 161 DLPFDVQVAEIEFD---PDMYEpLPVYKPAAS--RVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVI 235
Cdd:PRK06882 160 DIPKDMVNPANKFTyeyPEEVS-LRSYNPTVQghKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 236 PTLMGWGCIPDDHPLMAGMVGLQTAHRYGNAtLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPD 315
Cdd:PRK06882 239 SSLMGLGAYPSTDKQFLGMLGMHGTYEANNA-MHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 316 LGIVSDAKAALTLLIDVAQEMQKAGRLPCRKTWVDECQQRK-RTLLRKTHFDNVpVKPQRVYEEMNKAFGRDVCYVTTIG 394
Cdd:PRK06882 318 IPIVGSAKNVLEEFLSLLEEENLAKSQTDLTAWWQQINEWKaKKCLEFDRTSDV-IKPQQVVEAIYRLTNGDAYVASDVG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 395 LSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNA 474
Cdd:PRK06882 397 QHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 475 YLGLIRQSQrafDMDYCVQLAFENINSSEvngygvDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYrvpVVVEVI 554
Cdd:PRK06882 477 FLGMVKQWQ---DLIYSGRHSQVYMNSLP------DFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKL---VFVDVN 544
|
....*..
gi 261245799 555 LERVTNI 561
Cdd:PRK06882 545 VDETEHV 551
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
2-541 |
1.84e-108 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 337.55 E-value: 1.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 2 AKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGT 81
Cdd:PRK06965 19 ADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARAT-GKVGVALVTSGPGVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 82 DMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVD 161
Cdd:PRK06965 98 NAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 162 LPFDVQVAEIEFDP----DMYEPLPVYKPAASrvQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPT 237
Cdd:PRK06965 178 IPKDVSKTPCEYEYpksvEMRSYNPVTKGHSG--QIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 238 LMGWGCIPDDHPLMAGMVGLQTAHRYGNAtLLASDMVFGIGNRFANRHTGSVEKYTQG-RKIIHIDIEPTQIGRVLCPDL 316
Cdd:PRK06965 256 LMGLGAYPASDKKFLGMLGMHGTYEANMA-MQHCDVLIAIGARFDDRVIGNPAHFASRpRKIIHIDIDPSSISKRVKVDI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 317 GIVSDAKAALTLLIDVAQEMQKAGRLPCRKTWVDECQQ-RKRTLLRKTHFDNVpVKPQRVYEEMNKAFGRDVCYVTTIGL 395
Cdd:PRK06965 335 PIVGDVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGwRSRDCLKYDRESEI-IKPQYVVEKLWELTDGDAFVCSDVGQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 396 SQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAY 475
Cdd:PRK06965 414 HQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRY 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261245799 476 LGLIRQSQrafdmdycvQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAL 541
Cdd:PRK06965 494 LGMVRQWQ---------EIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRL 550
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
4-536 |
8.54e-108 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 334.54 E-value: 8.54e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 4 MRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDM 83
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARAT-GKVGVCIATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 84 ITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLP 163
Cdd:PRK08978 79 ITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 164 FDVQVAEIEFDPDMYEPLPvyKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGWGC 243
Cdd:PRK08978 159 KDIQLAEGELEPHLTTVEN--EPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 244 IPDDHPL---MAGMVGLQTAhrygNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVS 320
Cdd:PRK08978 237 VEADHPYylgMLGMHGTKAA----NLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 321 DAKAALTLLidvAQEMQKAGrlpcrktWVDECQQRKRTLlrKTHFDN--VPVKPQRVYEEMNKAFGRDVCYVTTIGLSQI 398
Cdd:PRK08978 313 DLNALLPAL---QQPLNIDA-------WRQHCAQLRAEH--AWRYDHpgEAIYAPALLKQLSDRKPADTVVTTDVGQHQM 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 399 AAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGL 478
Cdd:PRK08978 381 WVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGM 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 261245799 479 IRQSQrafdmdycvQLAFENiNSSEVNGY-GVDHVKVAEGLGCKAIRVFKPEDIAPAFE 536
Cdd:PRK08978 461 VRQWQ---------QLFFDE-RYSETDLSdNPDFVMLASAFGIPGQTITRKDQVEAALD 509
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
14-554 |
3.14e-97 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 308.20 E-value: 3.14e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITALYSASAD 93
Cdd:PLN02470 23 LEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKAS-GKVGVCIATSGPGATNLVTGLADALLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 94 SIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQ--VAEI 171
Cdd:PLN02470 102 SVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDIQqqLAVP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 172 EFDPDMyePLPVY----KPAASRVQIEKALEMLIQSERPVIVAGGGVINadAAPLLQQFAELTNVPVIPTLMGWGCIPDD 247
Cdd:PLN02470 182 NWNQPM--KLPGYlsrlPKPPEKSQLEQIVRLISESKRPVVYVGGGCLN--SSEELREFVELTGIPVASTLMGLGAFPAS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 248 HPLMAGMVGLQTAhRYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSDAKAALT 327
Cdd:PLN02470 258 DELSLQMLGMHGT-VYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADVKLALQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 328 LLIDVAQEmqKAGRLPCRKTWVDEC-QQRKRTLLRKTHFDNVpVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHV 406
Cdd:PLN02470 337 GLNKLLEE--RKAKRPDFSAWRAELdEQKEKFPLSYPTFGDA-IPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 407 FKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAF 486
Cdd:PLN02470 414 KEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQWEDRF 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245799 487 dmdYCVQLAFENINSSEVNGYGV-DHVKVAEGLGCKAIRVFKPEDIAPAFEQakalMAQYRVPVVVEVI 554
Cdd:PLN02470 494 ---YKANRAHTYLGDPDAEAEIFpDFLKFAEGCKIPAARVTRKSDLREAIQK----MLDTPGPYLLDVI 555
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
14-549 |
4.84e-95 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 302.14 E-value: 4.84e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAM---RKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITALYSA 90
Cdd:PRK06456 12 LKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARAS-GVPGVCTATSGPGTTNLVTGLITA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 91 SADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAE 170
Cdd:PRK06456 91 YWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIPRDIFYEK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 171 IEFDPDMYEPL-PVYKPAASRV---QIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGWGCIPD 246
Cdd:PRK06456 171 MEEIKWPEKPLvKGYRDFPTRIdrlALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTFPGKTAIPH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 247 DHPLMAGMVGLqtahrYGNA----TLLASDMVFGIGNRFANRHTGSVEKYTQ-GRKIIHIDIEPTQIGRVLCPDLGIVSD 321
Cdd:PRK06456 251 DHPLYFGPMGY-----YGRAeasmAALESDAMLVVGARFSDRTFTSYDEMVEtRKKFIMVNIDPTDGEKAIKVDVGIYGN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 322 AKAALTLLIDVAQEMqkaGRLPCRKTWVDECQQRKRTLLRKTHFD-NVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAA 400
Cdd:PRK06456 326 AKIILRELIKAITEL---GQKRDRSAWLKRVKEYKEYYSQFYYTEeNGKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 401 AQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIR 480
Cdd:PRK06456 403 EVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLVR 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261245799 481 QSQRAFDMDYCVQLAFeninssevnGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQA--KALMAQYRVPV 549
Cdd:PRK06456 483 QVQDLFFGKRIVGVDY---------GPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAikEDIPAVIRVPV 544
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-557 |
1.64e-91 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 291.92 E-value: 1.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGG-IRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPA 79
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARST-GRPGVCSVVPGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 80 GTDMITALYSASADSIPILCITGQAP-------RARLHKEDFQAvdieAIAKPVSKMAVTVREAALVPRVLQQAFHLMRS 152
Cdd:PRK08266 80 VLNAGAALLTAYGCNSPVLCLTGQIPsaligkgRGHLHEMPDQL----ATLRSFTKWAERIEHPSEAPALVAEAFQQMLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 153 GRPGPVLVDLPFDV--QVAEIEFDPdmyePL-PVYKPAASRVQIEKALEMLIQSERPVIVAGGGVinADAAPLLQQFAEL 229
Cdd:PRK08266 156 GRPRPVALEMPWDVfgQRAPVAAAP----PLrPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 230 TNVPVIPTLMGWGCIPDDHPLMAGMVGlqtahryGNATLLASDMVFGIGNRFANRhTGSVEKYTQGRKIIHIDIEPTQIG 309
Cdd:PRK08266 230 LQAPVVAFRSGRGIVSDRHPLGLNFAA-------AYELWPQTDVVIGIGSRLELP-TFRWPWRPDGLKVIRIDIDPTEMR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 310 RvLCPDLGIVSDAKAALTLLIDvaqEMQKAG-RLPCRKTWVDECQQRKRTLLRKthfdnvpVKPQRVY-EEMNKAFGRDV 387
Cdd:PRK08266 302 R-LKPDVAIVADAKAGTAALLD---ALSKAGsKRPSRRAELRELKAAARQRIQA-------VQPQASYlRAIREALPDDG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 388 CYVTTigLSQI--AAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIP 465
Cdd:PRK08266 371 IFVDE--LSQVgfASWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 466 YIHVLVNNAYLGLIRQSQ-RAFDMDYcvqlafenINSSEVNGygvDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALmaq 544
Cdd:PRK08266 449 VVTVVFNNNAYGNVRRDQkRRFGGRV--------VASDLVNP---DFVKLAESFGVAAFRVDSPEELRAALEAALAH--- 514
|
570
....*....|...
gi 261245799 545 yRVPVVVEVILER 557
Cdd:PRK08266 515 -GGPVLIEVPVPR 526
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-554 |
6.34e-83 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 270.72 E-value: 6.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKH-GGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPA 79
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKLT-GKIGVCLSIGGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 80 GTDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAfhlMRSG--RPGP 157
Cdd:PRK08611 80 AIHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQA---IRTAyeKKGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 158 VLVDLPFDVQVAEIEFDPDmyEPLPVYKPAASRV---QIEKALEMLIQSERPVIVAGGGVINAdaAPLLQQFAELTNVPV 234
Cdd:PRK08611 157 AVLTIPDDLPAQKIKDTTN--KTVDTFRPTVPSPkpkDIKKAAKLINKAKKPVILAGLGAKHA--KEELLAFAEKAKIPI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 235 IPTLMGWGCIPDDHPLM---AGMVGLQTAHRygnaTLLASDMVFGIGNRFAnrHTGSVEKYTqgrKIIHIDIEPTQIGRV 311
Cdd:PRK08611 233 IHTLPAKGIIPDDHPYSlgnLGKIGTKPAYE----AMQEADLLIMVGTNYP--YVDYLPKKA---KAIQIDTDPANIGKR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 312 LCPDLGIVSDAKAALTLLIDvaqemqKAGRLPCRKtWVDECQQRKRT----LLRKTHFDNVPVKPQRVYEEMNKAFGRDV 387
Cdd:PRK08611 304 YPVNVGLVGDAKKALHQLTE------NIKHVEDRR-FLEACQENMAKwwkwMEEDENNASTPIKPERVMAAIQKIADDDA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 388 CYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYI 467
Cdd:PRK08611 377 VLSVDVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 468 HVLVNNAYLGLIRQSQRAF-DMDYCVQLAfeninssevngyGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAkalmAQYR 546
Cdd:PRK08611 457 VVVLNNQQLAFIKYEQQAAgELEYAIDLS------------DMDYAKFAEACGGKGYRVEKAEELDPAFEEA----LAQD 520
|
....*...
gi 261245799 547 VPVVVEVI 554
Cdd:PRK08611 521 KPVIIDVY 528
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
14-538 |
1.34e-80 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 263.61 E-value: 1.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRkHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITALYSASAD 93
Cdd:PRK08322 11 LENEGVEYIFGIPGEENLDLLEALR-DSSIKLILTRHEQGAAFMAATYGRLT-GKAGVCLSTLGPGATNLVTGVAYAQLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 94 SIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDvqVAEIEF 173
Cdd:PRK08322 89 GMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPED--IAAEET 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 174 DPDMYEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGWGCIPDDHPLMAG 253
Cdd:PRK08322 167 DGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVIPETHPLSLG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 254 MVGLQtAHRYGNATLLASDMVFGIGN-------RFANRHTgsvekytqGRKIIHIDIEPTQIGRVLCPDLGIVSDAKAAL 326
Cdd:PRK08322 247 TAGLS-QGDYVHCAIEHADLIINVGHdviekppFFMNPNG--------DKKVIHINFLPAEVDPVYFPQVEVVGDIANSL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 327 TLLIDvaqemqkagRLPCRKTWVDECQQRKRTLLRK-----THFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAA 401
Cdd:PRK08322 318 WQLKE---------RLADQPHWDFPRFLKIREAIEAhleegADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIWFA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 402 qmlhvfkdRHWiNCGQAGPL---------GWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVN 472
Cdd:PRK08322 389 --------RNY-RAYEPNTClldnalatmGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILN 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245799 473 -NAYlGLIRQSQ-----RAFDMDycvqlaFENinssevngygVDHVKVAEGLGCKAIRVFKPEDIAPAFEQA 538
Cdd:PRK08322 460 dNAY-GMIRWKQenmgfEDFGLD------FGN----------PDFVKYAESYGAKGYRVESADDLLPTLEEA 514
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
7-556 |
1.41e-77 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 255.96 E-value: 1.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 7 VDAamyvLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITA 86
Cdd:PRK08199 15 VDA----LRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLT-GRPGICFVTRGPGATNASIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 87 LYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDV 166
Cdd:PRK08199 90 VHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPEDV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 167 QVAEIEFdPDMyEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGWGCIPD 246
Cdd:PRK08199 170 LSETAEV-PDA-PPYRRVAAAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDLFDN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 247 DHPLMAGMVGLQTahrygNATLLA----SDMVFGIGNRFAnrhtgsvEKYTQG----------RKIIHIDIEPTQIGRVL 312
Cdd:PRK08199 248 RHPNYAGDLGLGI-----NPALAArireADLVLAVGTRLG-------EVTTQGytlldipvprQTLVHVHPDAEELGRVY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 313 CPDLGIVSDAKAALTLLIDVAqemqkAGRLPCRKTWVDEcqqrkrtlLRKTHFDNVPVKPQ-------RVYEEMNKAFGR 385
Cdd:PRK08199 316 RPDLAIVADPAAFAAALAALE-----PPASPAWAEWTAA--------AHADYLAWSAPLPGpgavqlgEVMAWLRERLPA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 386 DVCYvtTIGLSQIAA-AQMLHVFKDRHwincGQAGP----LGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGA 460
Cdd:PRK08199 383 DAII--TNGAGNYATwLHRFFRFRRYR----TQLAPtsgsMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 461 QFNIPYIHVLVNNAYLGLIRQSQrafdmdycvqlafENINSSEVNGYG---VDHVKVAEGLGCKAIRVFKPEDIAPAFEQ 537
Cdd:PRK08199 457 QYGLPIIVIVVNNGMYGTIRMHQ-------------EREYPGRVSGTDltnPDFAALARAYGGHGETVERTEDFAPAFER 523
|
570
....*....|....*....
gi 261245799 538 AKAlmaqYRVPVVVEVILE 556
Cdd:PRK08199 524 ALA----SGKPALIEIRID 538
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
14-557 |
2.19e-73 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 244.11 E-value: 2.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITALYSASAD 93
Cdd:PRK07524 12 LEAYGVETVFGIPGVHTVELYRGLAG-SGIRHVTPRHEQGAGFMADGYARVS-GKPGVCFIITGPGMTNIATAMGQAYAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 94 SIPILCITGQAPRARLHKED---FQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAE 170
Cdd:PRK07524 90 SIPMLVISSVNRRASLGKGRgklHELPDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLDVLAAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 171 IEFDPDMyEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVInaDAAPLLQQFAELTNVPVIPTLMGWGCIPDDHPL 250
Cdd:PRK07524 170 ADHLLPA-PPTRPARPGPAPAALAQAAERLAAARRPLILAGGGAL--AAAAALRALAERLDAPVALTINAKGLLPAGHPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 251 MAGMVGLQTAHRygnATLLASDMVFGIGNRFANRHTGSV--EKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSDAKAALTL 328
Cdd:PRK07524 247 LLGASQSLPAVR---ALIAEADVVLAVGTELGETDYDVYfdGGFPLPGELIRIDIDPDQLARNYPPALALVGDARAALEA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 329 LIDVAQEmqkagrLPCRKTWVDECQQRKRTLLRKTHFDnvpvkPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVF- 407
Cdd:PRK07524 324 LLARLPG------QAAAADWGAARVAALRQALRAEWDP-----LTAAQVALLDTILAALPDAIFVGDSTQPVYAGNLYFd 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 408 --KDRHWINCGQA-GPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRqsqr 484
Cdd:PRK07524 393 adAPRRWFNASTGyGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIR---- 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261245799 485 afdmDYCVQLAFENINsseVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALmaqyRVPVVVEVILER 557
Cdd:PRK07524 469 ----RYMVARDIEPVG---VDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFAR----PGPTLIEVDQAC 530
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
4-562 |
3.70e-69 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 233.94 E-value: 3.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 4 MRAVDAAMYVLEKEGITTAFGVPgaaINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRAAAG-NIGVCLGTSGPAGTD 82
Cdd:PRK06154 20 MKVAEAVAEILKEEGVELLFGFP---VNELFDAAAA-AGIRPVIARTERVAVHMADGYARATSGeRVGVFAVQYGPGAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 83 MITALYSASADSIPILCITGQAPRARLHKE-DFQAVdieAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVD 161
Cdd:PRK06154 96 AFGGVAQAYGDSVPVLFLPTGYPRGSTDVApNFESL---RNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 162 LPFDVQVAEIEFDPDMYEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGW 241
Cdd:PRK06154 173 LPVDVLAEELDELPLDHRPSRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 242 GCIPDDHPLMAGMVGL----QTAHrygnaTLLASDMVFGIGNRFANRHTGSveKYTQGRKIIHIDIEPTQIGRVLCPDLG 317
Cdd:PRK06154 253 SAFPEDHPLALGSGGRarpaTVAH-----FLREADVLFGIGCSLTRSYYGL--PMPEGKTIIHSTLDDADLNKDYPIDHG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 318 IVSDAKAALTLLIDVAQEmqKAGRLPCRKTWV-DECQQRKRTLLRKTH----FDNVPVKPQRVYEEMNKAFGRDVCYVT- 391
Cdd:PRK06154 326 LVGDAALVLKQMIEELRR--RVGPDRGRAQQVaAEIEAVRAAWLAKWMpkltSDSTPINPYRVVWELQHAVDIKTVIITh 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 392 TIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLV 471
Cdd:PRK06154 404 DAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 472 NNAYLGLirqsqrafdMDYCVQLAFENINSSEVNGygvDHVKVAEGLGCKAIRVFKPEDIAPAFEQAkALMAQYRVPVVV 551
Cdd:PRK06154 484 NNFSMGG---------YDKVMPVSTTKYRATDISG---DYAAIARALGGYGERVEDPEMLVPALLRA-LRKVKEGTPALL 550
|
570
....*....|.
gi 261245799 552 EVILERVTNIS 562
Cdd:PRK06154 551 EVITSEETALS 561
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
4-556 |
5.44e-67 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 228.49 E-value: 5.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 4 MRAVDAAMYVLEKEGITTAFG--VPGAAinpFYSAmrKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGT 81
Cdd:PRK06112 14 GTVAHAIARALKRHGVEQIFGqsLPSAL---FLAA--EAIGIRQIAYRTENAGGAMADGYARVS-GKVAVVTAQNGPAAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 82 DMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVD 161
Cdd:PRK06112 88 LLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 162 LPFDVQVAEIEF----DPDMYEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPT 237
Cdd:PRK06112 168 LPADLLTAAAAApaapRSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 238 LMGWGCIPDDHPLMAGMVGL----QTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLc 313
Cdd:PRK06112 248 NMGKGAVDETHPLSLGVVGSlmgpRSPGRHLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGRNY- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 314 PDLGIVSDAKAALTLLIDVAQEMQKAGRLPCRKTWVD---ECQQRKRTLLRKTHF-DNVPVKPQRVYEEMNKAFGRDVCY 389
Cdd:PRK06112 327 EALRLVGDARLTLAALTDALRGRDLAARAGRRAALEPaiaAGREAHREDSAPVALsDASPIRPERIMAELQAVLTGDTIV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 390 VTTIGLSQIAAAQMLHVFKD--RHWINCGQAGpLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYI 467
Cdd:PRK06112 407 VADASYSSIWVANFLTARRAgmRFLTPRGLAG-LGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVT 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 468 HVLVNNAYLGLIRQSQRAFDMDYCVQLAFEninssevngyGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAlmaqYRV 547
Cdd:PRK06112 486 IVVLNNGILGFQKHAETVKFGTHTDACHFA----------AVDHAAIARACGCDGVRVEDPAELAQALAAAMA----APG 551
|
....*....
gi 261245799 548 PVVVEVILE 556
Cdd:PRK06112 552 PTLIEVITD 560
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-558 |
6.77e-64 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 220.25 E-value: 6.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLEKEGITTAFGVPGAAINP----FYSAmrkhgGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTS 76
Cdd:PRK07525 3 KMKMTPSEAFVETLQAHGITHAFGIIGSAFMDasdlFPPA-----GIRFIDVAHEQNAGHMADGYTRVT-GRMGMVIGQN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 77 GPAGTDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRpG 156
Cdd:PRK07525 77 GPGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-G 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 157 PVLVDLPFDVQVAEIefDPDMYEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIP 236
Cdd:PRK07525 156 PAQINIPRDYFYGVI--DVEIPQPVRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVAC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 237 TLMGWGCIPDDHPLMAGMVGLQTAhRYGNATLLASDMVFGIGNR---FANRHTGSVEKYTQGRKIIHIDIEPTQIGRVLC 313
Cdd:PRK07525 234 GYLHNDAFPGSHPLWVGPLGYNGS-KAAMELIAKADVVLALGTRlnpFGTLPQYGIDYWPKDAKIIQVDINPDRIGLTKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 314 PDLGIVSDAKAaltllidVAQEM--QKAGRLPC---RKTWVDECQQRK----RTLLRKTHFDNVP--------------- 369
Cdd:PRK07525 313 VSVGICGDAKA-------VARELlaRLAERLAGdagREERKALIAAEKsaweQELSSWDHEDDDPgtdwneeararkpdy 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 370 VKPQRVYEEMNKAFGRDVCYVTTIG-LSQIAAAqMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFD 448
Cdd:PRK07525 386 MHPRQALREIQKALPEDAIVSTDIGnNCSIANS-YLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 449 FQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDMDYCVQLAFENinssevngyGVDHVKVAEGLGCKAIRVFKP 528
Cdd:PRK07525 465 WGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDN---------NVSYAGIAEAMGAEGVVVDTQ 535
|
570 580 590
....*....|....*....|....*....|
gi 261245799 529 EDIAPAFEQAKALMAQyRVPVVVEVILERV 558
Cdd:PRK07525 536 EELGPALKRAIDAQNE-GKTTVIEIMCNQE 564
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
3-568 |
6.90e-62 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 213.95 E-value: 6.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 3 KMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTD 82
Cdd:PRK08617 4 KKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSG-PELIVTRHEQNAAFMAAAIGRLT-GKPGVVLVTSGPGVSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 83 MITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDL 162
Cdd:PRK08617 82 LATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 163 PFDVQVAEIEFDPdmYEPLPVYKP-AASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGW 241
Cdd:PRK08617 162 PQDVVDAPVTSKA--IAPLSKPKLgPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 242 GCIPDDH-PLMAGMVGL---QTahryGNATLLASDMVFGIG-------NRFANRHtgsvekytQGRKIIHIDIEPTQIGR 310
Cdd:PRK08617 240 GVISRELeDHFFGRVGLfrnQP----GDELLKKADLVITIGydpieyePRNWNSE--------GDATIIHIDVLPAEIDN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 311 VLCPDLGIVSDAKAALTLLIDVAQEMQKAGRLpcRKTWVDECQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYV 390
Cdd:PRK08617 308 YYQPERELIGDIAATLDLLAEKLDGLSLSPQS--LEILEELRAQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 391 TTIGLSQIAAAQMLHVFKDRHW-INCGQ-----AGPlgWTIPAALgvcaADPQRNVVAISGDFDFQFLIEELAVGAQFNI 464
Cdd:PRK08617 386 VDVGSHYIWMARYFRSYEPRHLlFSNGMqtlgvALP--WAIAAAL----VRPGKKVVSVSGDGGFLFSAMELETAVRLKL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 465 PYIHVL-VNNAYlglirqsqrafDMdycvqLAFENIN----SSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAk 539
Cdd:PRK08617 460 NIVHIIwNDGHY-----------NM-----VEFQEEMkygrSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREA- 522
|
570 580
....*....|....*....|....*....
gi 261245799 540 alMAQyRVPVVVEVILERVTNISMGSELD 568
Cdd:PRK08617 523 --LAT-DGPVVIDIPVDYSDNIKLMEQLL 548
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-163 |
1.27e-56 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 187.74 E-value: 1.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 8 DAAMYVLEKEGITTAFGVPGAAINPFYSAMRkHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITAL 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALA-RSGIRYILVRHEQGAVGMADGYARAT-GKPGVVLVTSGPGLTNAVTGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261245799 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLP 163
Cdd:cd07035 79 ANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLP 154
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
13-556 |
1.89e-56 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 199.29 E-value: 1.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 13 VLEKEGITTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGAShMAEGYTRAAAGNIGVCLGTSGPAGTDMITALYSASA 92
Cdd:PRK06457 11 VLEDNGIQRIYGIPGDSIDPLVDAIRKSK-VKYVQVRHEEGAA-LAASVEAKITGKPSACMGTSGPGSIHLLNGLYDAKM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 93 DSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRpGPVLVDLPFDVQVAEIE 172
Cdd:PRK06457 89 DHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDILRKSSE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 173 FDPDMYEPLPVYKpaaSRVQIEKALEMLIQSERPVIVAGGGVInaDAAPLLQQFAELTNVPVIPTLMGWGCIPDDHPLMA 252
Cdd:PRK06457 168 YKGSKNTEVGKVK---YSIDFSRAKELIKESEKPVLLIGGGTR--GLGKEINRFAEKIGAPIIYTLNGKGILPDLDPKVM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 253 GMVGLqTAHRYGNATLLASDMVFGIGNRFAnrhtgSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSDAKAALTLLID- 331
Cdd:PRK06457 243 GGIGL-LGTKPSIEAMDKADLLIMLGTSFP-----YVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLNIDIEe 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 332 ----VAQEMQKAgrlpcRKTWVDECQQRKRTLlrkthfdNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVF 407
Cdd:PRK06457 317 ksdkFYEELKGK-----KEDWLDSISKQENSL-------DKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRAS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 408 KDRHWINCGQAGPLGWTIPAALGVC-AADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRqsqraf 486
Cdd:PRK06457 385 GEQTFIFSAWLGSMGIGVPGSVGASfAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIK------ 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245799 487 dmdycvqlaFEninsSEVNGY---GV-----DHVKVAEGLGCKAIRVFKPEDIAPAFEQakalMAQYRVPVVVEVILE 556
Cdd:PRK06457 459 ---------FE----QEVMGYpewGVdlynpDFTKIAESIGFKGFRLEEPKEAEEIIEE----FLNTKGPAVLDAIVD 519
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
8-553 |
6.53e-55 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 194.82 E-value: 6.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 8 DAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITAL 87
Cdd:PRK07064 7 ELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVS-GGLGVALTSTGTGAGNAAGAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 88 YSASADSIPILCITGQAPRARLHKED---FQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPF 164
Cdd:PRK07064 86 VEALTAGTPLLHITGQIETPYLDQDLgyiHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 165 DVQVAEIEFdPDMYEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAplLQQFAELtNVPVIPTLMGWGCI 244
Cdd:PRK07064 166 DIQAAEIEL-PDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAE--VKRLVDL-GFGVVTSTQGRGVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 245 PDDHPLMAGMVGLQTAhryGNATLLASDMVFGIGNRFANRHTGsveKYTQG--RKIIHIDIEPTQIGRVLCPDLGIVSDA 322
Cdd:PRK07064 242 PEDHPASLGAFNNSAA---VEALYKTCDLLLVVGSRLRGNETL---KYSLAlpRPLIRVDADAAADGRGYPNDLFVHGDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 323 KAALTLLIDvaqemQKAGRLPCRKTWVDECQQRK---RTLLRKThfdnvpVKPQRVY-EEMNKAFGRDVCYVTTIGLSQI 398
Cdd:PRK07064 316 ARVLARLAD-----RLEGRLSVDPAFAADLRAAReaaVADLRKG------LGPYAKLvDALRAALPRDGNWVRDVTISNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 399 A-AAQMLHVFKDRHWINcGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLG 477
Cdd:PRK07064 385 TwGNRLLPIFEPRANVH-ALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYG 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245799 478 LIRQSQRA-FDMDYC-VQLafeninssevngYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAlmaqYRVPVVVEV 553
Cdd:PRK07064 464 VIRNIQDAqYGGRRYyVEL------------HTPDFALLAASLGLPHWRVTSADDFEAVLREALA----KEGPVLVEV 525
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
6-172 |
1.44e-51 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 174.73 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 6 AVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRaAAGNIGVCLGTSGPAGTDMIT 85
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYAR-ATGKPGVVLVTSGPGATNALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 86 ALYSASADSIPILCITGQAPRARLHKEDFQA-VDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPF 164
Cdd:pfam02776 80 GLANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPL 159
|
....*...
gi 261245799 165 DVQVAEIE 172
Cdd:pfam02776 160 DVLLEEVD 167
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
4-554 |
3.57e-47 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 173.75 E-value: 3.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 4 MRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRkHGGIRHILARHVEGASHMAEGY---TRAAagniGVCLGTSGPAG 80
Cdd:PRK05858 5 GHAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAR-EEGIRLIDVRHEQTAAFAAEAWaklTRVP----GVAVLTAGPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 81 TDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLV 160
Cdd:PRK05858 80 TNGMSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 161 DLPFDV--QVAEIEFDPDMYEPLPVyKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTL 238
Cdd:PRK05858 160 DFPMDHafSMADDDGRPGALTELPA-GPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 239 MGWGCIPDDHPLMAGmvglqtahRYGNATLLASDMVFGIGNRFANR-HTGSVEKYTQgrkIIHIDIEPTQIGRVLCPDLG 317
Cdd:PRK05858 239 MGRGVVPADHPLAFS--------RARGKALGEADVVLVVGVPMDFRlGFGVFGGTAQ---LVHVDDAPPQRAHHRPVAAG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 318 IVSDAKAALTLLIDVaqemqkAGRLPCRKTWVDECQQ-------RKRTLLRKthfDNVPVKPQRVYEEMNKAFGRDVCYV 390
Cdd:PRK05858 308 LYGDLSAILSALAGA------GGDRTDHQGWIEELRTaetaaraRDAAELAD---DRDPIHPMRVYGELAPLLDRDAIVI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 391 TTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVL 470
Cdd:PRK05858 379 GDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 471 VNNAYLGLIRQSQRAFdmdycvqlafeninssevngYGVDHV----------KVAEGLGCKAIRVFKPEDIAPAFEQAKA 540
Cdd:PRK05858 459 GNNGIWGLEKHPMEAL--------------------YGYDVAadlrpgtrydEVVRALGGHGELVTVPAELGPALERAFA 518
|
570
....*....|....
gi 261245799 541 lmaqYRVPVVVEVI 554
Cdd:PRK05858 519 ----SGVPYLVNVL 528
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
14-557 |
3.88e-47 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 174.02 E-value: 3.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGAShMAEGYTRAAAGNIGVCLGTSGPAGTDMITALYSASAD 93
Cdd:PRK09124 13 LEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAA-FAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDCHRN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 94 SIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAfhlMRS--GRPGPVLVDLPFDVQVAEI 171
Cdd:PRK09124 92 HVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIA---MRKaiLNRGVAVVVLPGDVALKPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 172 EFD--PDMYEP-LPVYKPAASrvQIEKALEMLIQSERPVIVAGGGVinADAAPLLQQFAELTNVPVIPTLMGWGCIPDDH 248
Cdd:PRK09124 169 PERatPHWYHApQPVVTPAEE--ELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALRGKEHVEYDN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 249 PLMAGMVGLqTAHRYGNATLLASDMVFGIGNRFANRhtgsvEKYTQGRKIIHIDIEPTQIGRvLCP-DLGIVSDAKAALT 327
Cdd:PRK09124 245 PYDVGMTGL-IGFSSGYHAMMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGR-RSPvDLGLVGDVKATLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 328 LLIDVAQEMQKAGRL-PCRKTWVDecqQRKR--TLLRKTHfDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQML 404
Cdd:PRK09124 318 ALLPLLEEKTDRKFLdKALEHYRK---ARKGldDLAVPSD-GGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 405 HVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQR 484
Cdd:PRK09124 394 KMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMK 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261245799 485 AFD-MDYCVQLafENinssevngygVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAlmaqYRVPVVVEVILER 557
Cdd:PRK09124 474 AGGyLTDGTDL--HN----------PDFAAIAEACGITGIRVEKASELDGALQRAFA----HDGPALVDVVTAK 531
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
393-553 |
1.20e-43 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 152.74 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 393 IGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVN 472
Cdd:pfam02775 2 IGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 473 NAYLGLIRQSQRAFDMDYCVQLAFEninssevNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAlmaqYRVPVVVE 552
Cdd:pfam02775 82 NGGYGMTRGQQTPFGGGRYSGPSGK-------ILPPVDFAKLAEAYGAKGARVESPEELEEALKEALE----HDGPALID 150
|
.
gi 261245799 553 V 553
Cdd:pfam02775 151 V 151
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
193-329 |
1.20e-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: 152.33 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 193 IEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGWGCIPDDHPLMAGMVGLqTAHRYGNATLLASD 272
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGM-HGTPAANEALEEAD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 261245799 273 MVFGIGNRFA-NRHTGSVEKYTQGRKIIHIDIEPTQIGRVLCPDLGIVSDAKAALTLL 329
Cdd:pfam00205 80 LVLAVGARFDdIRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
2-556 |
6.33e-41 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 155.88 E-value: 6.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 2 AKMRAVDAAMY-VLEKEGITTAFGVPGAAINPFYSAMRkhGGIRHILARHVEGASHMAEGYTRAAaGNIG-VCLGTSGPA 79
Cdd:PRK07092 9 AAMTTVRDATIdLLRRFGITTVFGNPGSTELPFLRDFP--DDFRYVLGLQEAVVVGMADGYAQAT-GNAAfVNLHSAAGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 80 GTDMiTALYSASADSIPILCITGQAPRARLHKEDF-QAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPV 158
Cdd:PRK07092 86 GNAM-GNLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 159 LVDLPFDvqvaeiEFDPDMyEPLPVYKPAA----SRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPV 234
Cdd:PRK07092 165 FVSIPYD------DWDQPA-EPLPARTVSSavrpDPAALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 235 IPTLMGWGC-IPDDHPLMAGMVglqTAHRYG-NATLLASDMVFGIGnrfanrhtGSVEKYTQ---------GRKIIHIDI 303
Cdd:PRK07092 238 WVAPMSGRCsFPEDHPLFAGFL---PASREKiSALLDGHDLVLVIG--------APVFTYHVegpgphlpeGAELVQLTD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 304 EPTQIGRVLCPDlGIVSDAKAALTLLIDVAQEMQKAgrlpcrktwvdecQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAF 383
Cdd:PRK07092 307 DPGEAAWAPMGD-AIVGDIRLALRDLLALLPPSARP-------------APPARPMPPPAPAPGEPLSVAFVLQTLAALR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 384 GRDVCYV----TTIGLSQiAAAQMLHvfKDRHWINCgqAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVG 459
Cdd:PRK07092 373 PADAIVVeeapSTRPAMQ-EHLPMRR--QGSFYTMA--SGGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 460 AQFNIPYIHVLVNNAYLGLIRQSQRAFDmdycvqlaFENINSSEVNgyGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAK 539
Cdd:PRK07092 448 AQLKLPVTFVILNNGRYGALRWFAPVFG--------VRDVPGLDLP--GLDFVALARGYGCEAVRVSDAAELADALARAL 517
|
570
....*....|....*..
gi 261245799 540 AlmaqYRVPVVVEVILE 556
Cdd:PRK07092 518 A----ADGPVLVEVEVA 530
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
13-554 |
7.55e-41 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 156.30 E-value: 7.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 13 VLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHvEGASHMAEGYTRAAAGNIGVCLGTSGPAGTDMITALYSASA 92
Cdd:PRK06546 12 QLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRH-EEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLYDAHR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 93 DSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAF-HLMrsGRPGPVLVDLPFDVqvAEI 171
Cdd:PRK06546 91 SGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIqHAV--AGGGVSVVTLPGDI--ADE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 172 EFDPDMYEPLPVYKPAA---SRVQIEKALEMLIQSERPVIVAGGGVINADAAPLlqQFAELTNVPVIPTLMGWGCIPDDH 248
Cdd:PRK06546 167 PAPEGFAPSVISPRRPTvvpDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVL--ALAEKIKAPVGHSLRGKEWIQYDN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 249 PLMAGMVGLQTahrYGNAT--LLASDMVFGIGNRFAnrhtgsvekYTQ---GRKIIHIDIEPTQIGRVLCPDLGIVSDAK 323
Cdd:PRK06546 245 PFDVGMSGLLG---YGAAHeaMHEADLLILLGTDFP---------YDQflpDVRTAQVDIDPEHLGRRTRVDLAVHGDVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 324 AALTLLIDVAQEmqKAGRlpcrkTWVDECQQRKRTLLRK---THFDNV----PVKPQRVYEEMNKAFGRDVCYVTTIGLS 396
Cdd:PRK06546 313 ETIRALLPLVKE--KTDR-----RFLDRMLKKHARKLEKvvgAYTRKVekhtPIHPEYVASILDELAADDAVFTVDTGMC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 397 QIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYL 476
Cdd:PRK06546 386 NVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261245799 477 GLIRqsqrafdmdycVQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKAlmaqYRVPVVVEVI 554
Cdd:PRK06546 466 GMVK-----------LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFA----HPGPALVDVV 528
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
374-554 |
1.20e-40 |
|
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: 145.09 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 374 RVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLI 453
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 454 EELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDmdycvqlafeNINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAP 533
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFY----------GGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEA 150
|
170 180
....*....|....*....|.
gi 261245799 534 AFEQAKAlmaqYRVPVVVEVI 554
Cdd:cd00568 151 ALAEALA----AGGPALIEVK 167
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
41-540 |
2.36e-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: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 41 GGIRHILARHVEGASHMAEGYTRAAagN---IGVCLGTSGPAGTDMITALYSASADSIPILCITG-----QAPRARLHK- 111
Cdd:COG3962 56 DELPTYQGRNEQGMAHAAIAYAKQK--NrrrIMACTSSIGPGATNMVTAAALATANRLPVLLLPGdtfatRQPDPVLQQl 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 112 EDFQAVDIEA--IAKPVSKM--AVTvREAALVPrVLQQAFHLMRSgrP---GPVLVDLPFDVQVAEIEFDPDMYEP--LP 182
Cdd:COG3962 134 EHFHDPTISVndAFRPVSRYwdRIT-RPEQLMS-ALPRAMRVLTD--PaetGAVTLALPQDVQAEAYDYPESFFAKrvHR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 183 VYKPAASRVQIEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGWGCIPDDHPLMAGMVGLqTAHR 262
Cdd:COG3962 210 IRRPPPDPAELARAVELIRAAKRPLIIAGGGVRYSEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLGGIGV-TGTL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 263 YGNAtlLAS--DMVFGIGNRFANRHTGSVEKYT-QGRKIIHIDIEPtqigrvlcPD------LGIVSDAKAALTLLidvA 333
Cdd:COG3962 289 AANA--LAAeaDLVIGVGTRLQDFTTGSKTLFAnPDVRFVNINVAR--------FDaykhdaLPVVADAREGLEAL---T 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 334 QEMQKAGrlpCRKTWVDECQQRKR----TLLRKTHFDNVPVKPQ-RVYEEMNKAFGRD---VCyvttiglsqiAAAQM-- 403
Cdd:COG3962 356 EALAGWR---YPAAWTDEAAELKAewdaEVDRLYAPTNGGLPTQaQVIGAVNEAAGPDdivVC----------AAGSLpg 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 404 -LHvfkdRHWiNCGQAGP---------LGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNN 473
Cdd:COG3962 423 dLH----KLW-RTRDPGTyhveygyscMGYEIAGGLGVKLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKIIVVLLDN 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 474 AYLGLIRQSQRAFDMD-YCVQLAFENINSSEVNG--YGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKA 540
Cdd:COG3962 498 HGFGCINRLQMSTGSQsFGTELRDRDTETGRLDGglLPVDFAANAASLGAKAYRVTTIAELRAALERAKA 567
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
18-554 |
5.43e-39 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 151.22 E-value: 5.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 18 GITTAFGVPGAAINPFYSAM-RKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITALYSASADSIP 96
Cdd:PRK08273 17 GVRRVFGYPGDGINGLLGALgRADDKPEFVQARHEEMAAFMAVAHAKFT-GEVGVCLATSGPGAIHLLNGLYDAKLDHVP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 97 ILCITGQAPRARLHKEDFQAVDIEAIAKPV-SKMAVTVREAALVPRVLQQAFHLMRSGRpGPVLVDLPFDVQVAEiefdp 175
Cdd:PRK08273 96 VVAIVGQQARAALGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTALAER-TVTAVILPNDVQELE----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 176 dmYEPLP-----VY--------KPAASRVQIEKALEMLIQSERPVIVAGGGVinADAAPLLQQFAELTNVPVIPTLMGWG 242
Cdd:PRK08273 170 --YEPPPhahgtVHsgvgytrpRVVPYDEDLRRAAEVLNAGRKVAILVGAGA--LGATDEVIAVAERLGAGVAKALLGKA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 243 CIPDDHPLMAGMVG-LQTAHRY----GNATLLasdMVfgignrfanrhtGSVEKYT-------QGRKIiHIDIEPTQIGR 310
Cdd:PRK08273 246 ALPDDLPWVTGSIGlLGTKPSYelmrECDTLL---MV------------GSSFPYSeflpkegQARGV-QIDIDGRMLGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 311 VLCPDLGIVSDAKAALTLLIDVAQEMQKAGrlpCRKTWVDECQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYV 390
Cdd:PRK08273 310 RYPMEVNLVGDAAETLRALLPLLERKKDRS---WRERIEKWVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 391 TTIGLSQIAAAQMLHVfkdRHWINCGQAGPL---GWTIPAALGVCAADPQRNVVAISGDFDFQFL-IEELAVGA----QF 462
Cdd:PRK08273 387 ADSGSCANWYARDLRM---RRGMMASLSGTLatmGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAkywrQW 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 463 NIPYIHVLV-NNAYLGLIRQSQRAFDMDycvqLAFEniNSSEVNgyGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAkal 541
Cdd:PRK08273 464 SDPRLIVLVlNNRDLNQVTWEQRVMEGD----PKFE--ASQDLP--DVPYARFAELLGLKGIRVDDPEQLGAAWDEA--- 532
|
570
....*....|...
gi 261245799 542 MAQYRvPVVVEVI 554
Cdd:PRK08273 533 LAADR-PVVLEVK 544
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-558 |
5.57e-39 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 150.92 E-value: 5.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLE---KEGITTAFGVPGAAINPFYSAMRKHG--GIRH---ILARHVEGASHMAEGYTrAAAGNIGVC 72
Cdd:PRK08327 1 SMALTMYTAAELFLEllkELGVDYIFINSGTDYPPIIEAKARARaaGRPLpefVICPHEIVAISMAHGYA-LVTGKPQAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 73 L-----GTSGPAGtdmitALYSASADSIPILCITGQAP---RARL-HKEDF-----QAVDIEAIAKPVSKMAVTVREAAL 138
Cdd:PRK08327 80 MvhvdvGTANALG-----GVHNAARSRIPVLVFAGRSPyteEGELgSRNTRihwtqEMRDQGGLVREYVKWDYEIRRGDQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 139 VPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIE-FDPDMYEPLPVYKPAASRVQIEKALEMLIQSERPVIVAGGGVINA 217
Cdd:PRK08327 155 IGEVVARAIQIAMSEPKGPVYLTLPREVLAEEVPeVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITWRAGRTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 218 DAAPLLQQFAELTNVPVI---PTLMGwgcIPDDHPLMAGMVglqtahryGNATLLASDMVFGIGNR---FANRHTGSvek 291
Cdd:PRK08327 235 EGFASLRRLAEELAIPVVeyaGEVVN---YPSDHPLHLGPD--------PRADLAEADLVLVVDSDvpwIPKKIRPD--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 292 ytQGRKIIHIDIEPTQiGRVlcP------DLGIVSDAKAALTLLIDVAQEMQKAGRLPCRKTWVDECQQRKRT-LLRKTH 364
Cdd:PRK08327 301 --ADARVIQIDVDPLK-SRI--PlwgfpcDLCIQADTSTALDQLEERLKSLASAERRRARRRRAAVRELRIRQeAAKRAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 365 FDNV----PVKPQRVYEEMNKAFGRDVCYVTTIGlsqiAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNV 440
Cdd:PRK08327 376 IERLkdrgPITPAYLSYCLGEVADEYDAIVTEYP----FVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 441 VAISGDFDFQFLIEE--LAVGAQFNIPYIHVLVNNAYLGLIRQSQRAfdmdycvqlAFENINSSEVNGY-GVD------H 511
Cdd:PRK08327 452 IATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLE---------VYPEGYAARKGTFpGTDfdprpdF 522
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 261245799 512 VKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPVVVEVILERV 558
Cdd:PRK08327 523 AKIAEAFGGYGERVEDPEELKGALRRALAAVRKGRRSAVLDVIVDRV 569
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
370-563 |
2.71e-38 |
|
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: 139.56 E-value: 2.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 370 VKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDF 449
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 450 QFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFdmdycvqlaFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPE 529
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELF---------YEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPE 151
|
170 180 190
....*....|....*....|....*....|....
gi 261245799 530 DIAPAFEQAKAlmaqYRVPVVVEVILERVTNISM 563
Cdd:cd02015 152 ELEAALKEALA----SDGPVLLDVLVDPEENVLP 181
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
14-571 |
1.12e-37 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 147.05 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFySAMRKHGGIRHILARHVEGAshmaeGYTRAAAGNI----GVCLGTSGPAGTDMITALYS 89
Cdd:PRK09259 20 LKLNGIDTIYGVVGIPITDL-ARLAQAEGIRYIGFRHEQSA-----GNAAAAAGFLtqkpGVCLTVSAPGFLNGLTALAN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 90 ASADSIPILCITGQAPRA--RLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQ 167
Cdd:PRK09259 94 ATTNCFPMIMISGSSEREivDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 168 VAEIEFDP------DMYEPLPVYKPAASRVqiEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAELTNVPVIPTLMGW 241
Cdd:PRK09259 174 AQTMDADEaltslvKVVDPAPAQLPAPEAV--DRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSMAK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 242 GCIPDDHPLMAGmvglqtAHRygNATLLASDMVFGIGNRFaN---RHtGSVEKYTQGRKIIHIDIEPTQIG---RVLCPd 315
Cdd:PRK09259 252 GLLPDTHPQSAA------AAR--SLALANADVVLLVGARL-NwllSH-GKGKTWGADKKFIQIDIEPQEIDsnrPIAAP- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 316 lgIVSDAKAALTLLID-VAQEMQKAgrlpcRKTWVDECQQRKRTLLRKTHfdnvpVKPQRVYEEMN--KAFG--RDV--- 387
Cdd:PRK09259 321 --VVGDIGSVMQALLAgLKQNTFKA-----PAEWLDALAERKEKNAAKMA-----EKLSTDTQPMNfyNALGaiRDVlke 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 388 ---CYVTTIGLSQIAAAQ-MLHVFKDRHWINCGQAG----PLGWTIPAAlgVCAADPqrnVVAISGDFDFQFLIEELAVG 459
Cdd:PRK09259 389 npdIYLVNEGANTLDLARnIIDMYKPRHRLDCGTWGvmgiGMGYAIAAA--VETGKP---VVAIEGDSAFGFSGMEVETI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 460 AQFNIPYIHVLVNNA--YLGLIRQSQRAFDMdycvqlafeninSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQ 537
Cdd:PRK09259 464 CRYNLPVTVVIFNNGgiYRGDDVNLSGAGDP------------SPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTE 531
|
570 580 590
....*....|....*....|....*....|....
gi 261245799 538 AkalMAQYRvPVVVEVILERvtniSMGSELDNVT 571
Cdd:PRK09259 532 A---IASGK-PTLINVVIDP----AAGTESGHIT 557
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
14-557 |
4.75e-35 |
|
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: 139.14 E-value: 4.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGnIGVCLGTSGPAGTDMITALYSASAD 93
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVN-G-LGALVTTYGVGELSAINGIAGAYAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 94 SIPILCITG------QAPRARLH----KEDFQAVdieaiakpvSKMA--VTVREAALVP--------RVLQQAFHLMRsg 153
Cdd:COG3961 93 RVPVVHIVGapgtraQRRGPLLHhtlgDGDFDHF---------LRMFeeVTVAQAVLTPenaaaeidRVLAAALREKR-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 154 rpgPVLVDLPFDVQVAEIEFDPdmyEPLPVYKPAASRVQ----IEKALEMLIQSERPVIVAGGGVINADAAPLLQQFAEL 229
Cdd:COG3961 162 ---PVYIELPRDVADAPIEPPE---APLPLPPPASDPAAlaaaVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 230 TNVPVIPTLMGWGCIPDDHPLMAGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSvekYTQ---GRKIIHIDIEPT 306
Cdd:COG3961 236 TGIPVATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGG---FTAqldPERTIDIQPDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 307 QIGRVLCPDLGIvsdaKAALTLLIDVAQEMQKAGRLPCRKtwvdecqqrkrtllrKTHFDNVPVKP---QRVYEEMNKAF 383
Cdd:COG3961 313 RVGGHIYPGVSL----ADFLEALAELLKKRSAPLPAPAPP---------------PPPPPAAPDAPltqDRLWQRLQAFL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 384 GRDVCYVTTIGLSQIAAAQM-LHvfKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQF 462
Cdd:COG3961 374 DPGDIVVADTGTSLFGAADLrLP--EGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 463 NIPYIHVLVNNaylglirqsqrafdmdycvqlafeninssevNGYGV-----------------DHVKVAEGLGCKAIRV 525
Cdd:COG3961 452 GLKPIIFVLNN-------------------------------DGYTIeraihgpdgpyndianwDYAKLPEAFGGGNALG 500
|
570 580 590
....*....|....*....|....*....|....*
gi 261245799 526 FK---PEDIAPAFEQAKALMAQyrvPVVVEVILER 557
Cdd:COG3961 501 FRvttEGELEEALAAAEANTDR---LTLIEVVLDK 532
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
8-170 |
1.03e-33 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 126.13 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 8 DAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITAL 87
Cdd:cd07039 4 DVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLT-GKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAfhlMRS--GRPGPVLVDLPFD 165
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRA---IRTaiAKRGVAVLILPGD 159
|
....*
gi 261245799 166 VQVAE 170
Cdd:cd07039 160 VQDAP 164
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
369-557 |
1.43e-29 |
|
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: 114.94 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 369 PVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFD 448
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 449 FQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAF-DMDYCVQLafeninssevngYGVDHVKVAEGLGCKAIRVFK 527
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMgQPEFGVDL------------PNPDFAKIAEAMGIKGIRVED 148
|
170 180 190
....*....|....*....|....*....|
gi 261245799 528 PEDIAPAFEQAKAlmaqYRVPVVVEVILER 557
Cdd:cd02014 149 PDELEAALDEALA----ADGPVVIDVVTDP 174
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
13-164 |
1.61e-24 |
|
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: 99.73 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 13 VLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYtrAAAGNIGVCLGTSGPAGTDMITALYSASA 92
Cdd:cd06586 6 VLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGY--ARAGGPPVVIVTSGTGLLNAINGLADAAA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261245799 93 DSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGrPGPVLVDLPF 164
Cdd:cd06586 84 EHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
372-556 |
2.31e-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: 91.44 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 372 PQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQF 451
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 452 LIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQrafdmdycvQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDI 531
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQ---------QLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEEL 151
|
170 180
....*....|....*....|....*
gi 261245799 532 APAFEQAKALmaqyRVPVVVEVILE 556
Cdd:cd02004 152 KPALKRALAS----GKPALINVIID 172
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
369-557 |
1.29e-20 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 89.88 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 369 PVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFD 448
Cdd:cd02013 3 PMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 449 FQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDMDYCVQLAFENINssevngygvdHVKVAEGLGCKAIRVFKP 528
Cdd:cd02013 83 WGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESES----------FAKIAEACGAKGITVDKP 152
|
170 180
....*....|....*....|....*....
gi 261245799 529 EDIAPAFEQAKALMAQYRvPVVVEVILER 557
Cdd:cd02013 153 EDVGPALQKAIAMMAEGK-TTVIEIVCDQ 180
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
372-555 |
5.10e-17 |
|
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: 79.18 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 372 PQRVYEEMNKAFGRDVCYVTTiGLSQIAAAQMLHVFKDRH-WINCGqAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQ 450
Cdd:cd02002 3 PEYLAAALAAALPEDAIIVDE-AVTNGLPLRDQLPLTRPGsYFTLR-GGGLGWGLPAAVGAALANPDRKVVAIIGDGSFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 451 FLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDMDYCVQLAFENINSSEVngyGVDHVKVAEGLGCKAIRVFKPED 530
Cdd:cd02002 81 YTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENAPDGLDLLDP---GIDFAAIAKAFGVEAERVETPEE 157
|
170 180
....*....|....*....|....*
gi 261245799 531 IAPAFEQAkalMAQYRvPVVVEVIL 555
Cdd:cd02002 158 LDEALREA---LAEGG-PALIEVVV 178
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
372-553 |
1.78e-15 |
|
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: 74.63 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 372 PQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRH-WINCGQAgPLGWTIPAALGVCAADPQRNVVAISGDFDFQ 450
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTcLISNGLA-TMGVALPGAIGAKLVYPDRKVVAVSGDGGFM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 451 FLIEELAVGAQFNIPYIH-VLVNNAYlGLIRQSQrafDMDYcvqlaFEninSSEVNGYGVDHVKVAEGLGCKAIRVFKPE 529
Cdd:cd02010 80 MNSQELETAVRLKIPLVVlIWNDNGY-GLIKWKQ---EKEY-----GR---DSGVDFGNPDFVKYAESFGAKGYRIESAD 147
|
170 180
....*....|....*....|....
gi 261245799 530 DIAPAFEQAkalMAQyRVPVVVEV 553
Cdd:cd02010 148 DLLPVLERA---LAA-DGVHVIDC 167
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
421-553 |
4.75e-12 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 65.40 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 421 LGWTIPAALGVCAADPQRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDMD-YCVQLAFENI 499
Cdd:cd02003 50 MGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGsFGTEFRDRDQ 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 261245799 500 NSSEVNG--YGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALmaqyRVPVVVEV 553
Cdd:cd02003 130 ESGQLDGalLPVDFAANARSLGARVEKVKTIEELKAALAKAKAS----DRTTVIVI 181
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
374-557 |
2.53e-10 |
|
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: 59.86 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 374 RVYEEMNKAF-GRDVCYVTTiGLSQIAAAQM-LHvfKDRHWINCGQAGPLGWTIPAALGVCAADPQRNVVAISGDFDFQF 451
Cdd:cd02005 6 RLWQQVQNFLkPNDILVAET-GTSWFGALDLkLP--KGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 452 LIEELAVGAQFNIPYIHVLVNNA-YLglirqSQRAF-DMDYcvqlAFENINSsevngygVDHVKVAEGLGC----KAIRV 525
Cdd:cd02005 83 TVQELSTMIRYGLNPIIFLINNDgYT-----IERAIhGPEA----SYNDIAN-------WNYTKLPEVFGGggggLSFRV 146
|
170 180 190
....*....|....*....|....*....|..
gi 261245799 526 FKPEDIAPAFEQAKalmAQYRVPVVVEVILER 557
Cdd:cd02005 147 KTEGELDEALKDAL---FNRDKLSLIEVILPK 175
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
14-156 |
4.36e-07 |
|
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: 49.80 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAAgnIGVCLGTSGPAGTDMITALYSASAD 93
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG--LGALVTTYGVGELSALNGIAGAYAE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261245799 94 SIPILCITG------QAPRARLH----KEDFQAvdIEAIAKPVSKMAVTVRE----AALVPRVLQQAfhlMRSGRPG 156
Cdd:cd07038 85 HVPVVHIVGapstkaQASGLLLHhtlgDGDFDV--FLKMFEEITCAAARLTDpenaAEEIDRVLRTA---LRESRPV 156
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
14-164 |
4.92e-07 |
|
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: 49.80 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 14 LEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILarHVE--GASHMAEGYTRAAaGNIGVCLGTSGPAGTDMITALYSAS 91
Cdd:cd07037 7 LKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHV--RVDerSAAFFALGLAKAS-GRPVAVVCTSGTAVANLLPAVVEAY 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245799 92 ADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVR------EAALVPRVLQQAFHLMRSGRPGPVLVDLPF 164
Cdd:cd07037 84 YSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddDLWYLLRLANRAVLEALSAPPGPVHLNLPF 162
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
4-219 |
1.51e-06 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 51.00 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 4 MRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHvEG-ASHMAEGYTRAAaGNIGVCLGTSGPAGTD 82
Cdd:PRK07586 1 MNGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLF-EGvATGAADGYARMA-GKPAATLLHLGPGLAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 83 MITALYSASADSIPILCITGQapRARLHKeDFQA---VDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVL 159
Cdd:PRK07586 79 GLANLHNARRARTPIVNIVGD--HATYHR-KYDApltSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVAT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 160 VDLPFDVQVAEIEFDPDMYEPLPVykPAASRVQIEKALEMLIQSERPVIVAGGGVINADA 219
Cdd:PRK07586 156 LILPADVAWSEGGPPAPPPPAPAP--AAVDPAAVEAAAAALRSGEPTVLLLGGRALRERG 213
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
1-194 |
2.86e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 46.79 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 1 MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAAaGNIGVCLGTSGPAG 80
Cdd:PRK12474 2 GQTMNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIA-GKPAVTLLHLGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245799 81 TDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLV 160
Cdd:PRK12474 81 ANGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATL 160
|
170 180 190
....*....|....*....|....*....|....
gi 261245799 161 DLPFDVQvaeieFDPDMYEPLPVYKPAASRVQIE 194
Cdd:PRK12474 161 IMPADVA-----WNEAAYAAQPLRGIGPAPVAAE 189
|
|
| |
