|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 1277.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 2 AKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAKSGNIGVCIGTSGPAGT 81
Cdd:COG3960 1 ARMRAVDAAVAVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHVLARHVEGASHMAEGYTRAKAGNIGVCIGTSGPAGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 82 DMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHID 161
Cdd:COG3960 81 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVLEPAQVPRVFQQAFHLMRSGRPGPVLID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 162 LPFDVQMAEIEFDVDTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGW 241
Cdd:COG3960 161 LPIDVQMAEIEFDIDTYEPLPVYKPAATRAQIEKALDMLNAAERPLIVAGGGIINADASDLLVEFAELTGVPVIPTLMGW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 242 GAIPDDHPLMAGMAGLQTSQMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIVSD 321
Cdd:COG3960 241 GSIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRWANRHTGSLDVYTKGRKFVHVDIEPTQIGRVFAPDLGIVSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 322 AGAALKLMVEVARELRQAGKLPDYGEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAAA 401
Cdd:COG3960 321 AKAALELFVEVARERKAAGKLPDRSAWAAECQERKRTMLRKTHFDNVPIKPQRVYEEMNKAFGRDTRYVSTIGLSQIAAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 402 QFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQ 481
Cdd:COG3960 401 QFLHVYKPRHWINCGQAGPLGWTIPAALGVVAADPDRPVVALSGDYDFQFMIEELAVGAQFKLPYIHVVVNNSYLGLIRQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 482 SQRGFEMDYQVQLAFDNINNPDLNGYGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQKFQVPVVLEVILERVTNI 561
Cdd:COG3960 481 AQRGFDMDYCVQLAFENINAPELGGYGVDHVKVAEGLGCKAIRVTDPEEIAPAFEEAKALMAEHRVPVVVEVILERVTNI 560
|
570 580
....*....|....*....|....*...
gi 730604155 562 SMGTELDNVVEFEELADAREDAPTAIAM 589
Cdd:COG3960 561 SMGTEIDNVNEFEELAESPADAPTAIAL 588
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-591 |
0e+00 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 1267.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAKSGNIGVCIGTSGPAG 80
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIGVCIGTSGPAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 81 TDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHI 160
Cdd:PRK11269 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 161 DLPFDVQMAEIEFDVDTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMG 240
Cdd:PRK11269 161 DLPFDVQVAEIEFDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 241 WGAIPDDHPLMAGMAGLQTSQMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIVS 320
Cdd:PRK11269 241 WGAIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 321 DAGAALKLMVEVARELRQAGKLPDYGEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAA 400
Cdd:PRK11269 321 DAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQIAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 401 AQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIR 480
Cdd:PRK11269 401 AQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 481 QSQRGFEMDYQVQLAFDNINNPDLNGYGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQKFQVPVVLEVILERVTN 560
Cdd:PRK11269 481 QAQRAFDMDYCVQLAFENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALEQAKALMAEFRVPVVVEVILERVTN 560
|
570 580 590
....*....|....*....|....*....|.
gi 730604155 561 ISMGTELDNVVEFEELADAREDAPTAIAMLD 591
Cdd:PRK11269 561 ISMGTEIDAVNEFEELADNAADAPTAIMLLD 591
|
|
| 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: 1066.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 2 AKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAKSGNIGVCIGTSGPAGT 81
Cdd:TIGR01504 1 ARMRAVDAAVYVLEKEGITTAFGVPGAAINPFYSALKAHGGIRHILARHVEGASHMAEGYTRATAGNIGVCIGTSGPAGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 82 DMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHID 161
Cdd:TIGR01504 81 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIAAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 162 LPFDVQMAEIEFDVDTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGW 241
Cdd:TIGR01504 161 LPFDVQVAEIEFDPDTYEPLPVYKPAATRAQIEKAVEMLNAAERPLIVAGGGVINADAADLLQEFAELTGVPVIPTLMGW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 242 GAIPDDHPLMAGMAGLQTSQMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIVSD 321
Cdd:TIGR01504 241 GCIPDDHELMAGMVGLQTSHRYGNATLLESDFVFGIGNRWANRHTGSVDVYTEGRKFVHVDIEPTQIGRVFAPDLGIVSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 322 AGAALKLMVEVARELRQAGKLPDYGEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAAA 401
Cdd:TIGR01504 321 AKAALKLLVEVAQELKKAGRLPDRSEWAADCQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAGA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 402 QFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQ 481
Cdd:TIGR01504 401 QMLHVYKPRHWINCGQAGPLGWTIPAALGVCAADPKRNVVALSGDYDFQFMIEELAVGAQHNIPYIHVLVNNAYLGLIRQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 482 SQRGFEMDYQVQLAFDNINNPDLNGYGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQKFQVPVVLEVILERVTNI 561
Cdd:TIGR01504 481 AQRAFDMDYCVQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEEIAPAFEQAKALMAEHRVPVVVEVILERVTNI 560
|
570 580
....*....|....*....|....*...
gi 730604155 562 SMGTELDNVVEFEELADAREDAPTAIAM 589
Cdd:TIGR01504 561 SMGSEIDNVVEFEDLADNAADAPTATCF 588
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
2-565 |
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: 536.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 2 AKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGT 81
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARA-TGKPGVCLVTSGPGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 82 DMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHID 161
Cdd:COG0028 80 NLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 162 LPFDVQMAEIEFDVDTYEaLPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLM 239
Cdd:COG0028 160 IPKDVQAAEAEEEPAPPE-LRGYRPrpAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 240 GWGAIPDDHPLMAGMAGLQTSQmYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIV 319
Cdd:COG0028 239 GKGAFPEDHPLYLGMLGMHGTP-AANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 320 SDAGAALKLMVEVARElrqagKLPDYGEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLSQIA 399
Cdd:COG0028 318 GDAKAVLAALLEALEP-----RADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 400 AAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLI 479
Cdd:COG0028 393 AARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 480 RQSQRGFEMDYQVQLAFDNInnpdlngygvDHVAVAEGLGCRAIRVTEPGKIKAGLEEAkeLAQKfqVPVVLEVILERVT 559
Cdd:COG0028 473 RQWQELFYGGRYSGTDLPNP----------DFAKLAEAFGAKGERVETPEELEAALEEA--LASD--GPALIDVRVDPEE 538
|
....*.
gi 730604155 560 NISMGT 565
Cdd:COG0028 539 NPPGAT 544
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
4-574 |
2.25e-165 |
|
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: 482.69 E-value: 2.25e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 4 MRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDM 83
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARA-SGKVGVVLVTSGPGATNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 84 ITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLP 163
Cdd:TIGR00118 80 VTGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 164 FDVQMAEIEFDVDTYEALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGW 241
Cdd:TIGR00118 160 KDVTTAEIEYPYPEKVNLPGYRPtvKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 242 GAIPDDHPLMAGMAGLQTSQmYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIVSD 321
Cdd:TIGR00118 240 GSFPEDHPLSLGMLGMHGTK-TANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 322 AGAALKLMVEVARELRQagklPDYGEWAEQCRE-RKRTMLRKTHYDnVPIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAA 400
Cdd:TIGR00118 319 ARNVLEELLKKLFELKE----RKESAWLEQINKwKKEYPLKMDYTE-EGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 401 AQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIR 480
Cdd:TIGR00118 394 AQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 481 QSQRGFemdYQVQLAFDNINNpdlngyGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQkfqvPVVLEVILERVTN 560
Cdd:TIGR00118 474 QWQELF---YEERYSHTHMGS------LPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNE----PVLLDVVVDKPEN 540
|
570
....*....|....*...
gi 730604155 561 I-SM---GTELDNVVEFE 574
Cdd:TIGR00118 541 VlPMvapGGGLDEMIGEK 558
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-575 |
1.35e-146 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 434.97 E-value: 1.35e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKlGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAG 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARA-TGKVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 81 TDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHI 160
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 161 DLPFDVQMAEIEFDVDTYEALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTL 238
Cdd:PRK06048 163 DLPKDVTTAEIDFDYPDKVELRGYKPtyKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 239 MGWGAIPDDHPLMAGMAGLQTSQmYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGI 318
Cdd:PRK06048 243 MGIGAIPTEHPLSLGMLGMHGTK-YANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 319 VSDAGAALKlmvevarELRQAGKLPDYGEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFgRDTVYVSTIGLSQI 398
Cdd:PRK06048 322 VGDAKQVLK-------SLIKYVQYCDRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELC-PDAIIVTEVGQHQM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 399 AAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGL 478
Cdd:PRK06048 394 WAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 479 IRQSQrgfemdyqvQLAFDNINNPDLNGYGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQkfqvPVVLEVILERV 558
Cdd:PRK06048 474 VRQWQ---------ELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDR----PVVIDFIVECE 540
|
570 580
....*....|....*....|.
gi 730604155 559 TNIS----MGTELDNVVEFEE 575
Cdd:PRK06048 541 ENVSpmvpAGAAINEILDLEE 561
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
4-571 |
3.25e-139 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 416.85 E-value: 3.25e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 4 MRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKlGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDM 83
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARA-SGKVGVCVATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 84 ITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLP 163
Cdd:PRK06276 79 VTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 164 FDVQMAEIEFDVDTYEA---LPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTL 238
Cdd:PRK06276 159 KDVQEGELDLEKYPIPAkidLPGYKPttFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 239 MGWGAIPDDHPLMAGMAGLQTSQMyGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGI 318
Cdd:PRK06276 239 MGKGAFPEDHPLALGMVGMHGTKA-ANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 319 VSDAGAALKLMVEVARELrqagKLPDYGEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSF-----GRDTVYVSTI 393
Cdd:PRK06276 318 VGDAKNVLRDLLAELMKK----EIKNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLreidpSKNTIITTDV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 394 GLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNN 473
Cdd:PRK06276 394 GQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDN 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 474 SYLGLIRQSQRGFEMDYQVQLAFDniNNPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQkfqvPVVLEV 553
Cdd:PRK06276 474 RTLGMVYQWQNLYYGKRQSEVHLG--ETPDF-------VKLAESYGVKADRVEKPDEIKEALKEAIKSGE----PYLLDI 540
|
570 580
....*....|....*....|.
gi 730604155 554 ILERVTNISM---GTELDNVV 571
Cdd:PRK06276 541 IIDPAEALPMvppGGNLTNIL 561
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
363-564 |
1.34e-132 |
|
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: 385.48 E-value: 1.34e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 363 THYDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVA 442
Cdd:cd02006 1 THFDDVPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 443 LSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQSQRGFEMDYQVQLAFDNINNPDLNGYGVDHVAVAEGLGCRA 522
Cdd:cd02006 81 LSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAFDMDYQVNLAFENINSSELGGYGVDHVKVAEGLGCKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 730604155 523 IRVTEPGKIKAGLEEAKELAQKFQVPVVLEVILERVTNISMG 564
Cdd:cd02006 161 IRVTKPEELAAAFEQAKKLMAEHRVPVVVEAILERVTNISMG 202
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
3-561 |
6.02e-132 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 397.16 E-value: 6.02e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 3 KMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTD 82
Cdd:PRK08527 2 KLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARA-SGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 83 MITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDL 162
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 163 PFDVQMAEIEFDVDTYEALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMG 240
Cdd:PRK08527 161 PKDVTATLGEFEYPKEISLKTYKPtyKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 241 WGAIPDDHPLMAGMAGlqtsqMYG----NATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDY 316
Cdd:PRK08527 241 RGVLRSDDPLLLGMLG-----MHGsyaaNMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 317 GIVSDAGAALKLMVEVARELRQAgklpDYGEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLS 396
Cdd:PRK08527 316 PIVGDLKNVLKEMLEELKEENPT----TYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 397 QIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYL 476
Cdd:PRK08527 392 QMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 477 GLIRQSQRGF------EMDYQVQlafdninnPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKELaqkfQVPVV 550
Cdd:PRK08527 472 GMVRQWQTFFyeerysETDLSTQ--------PDF-------VKLAESFGGIGFRVTTKEEFDKALKEALES----DKVAL 532
|
570
....*....|.
gi 730604155 551 LEVILERVTNI 561
Cdd:PRK08527 533 IDVKIDRFENV 543
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-554 |
1.02e-129 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 393.19 E-value: 1.02e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAG 80
Cdd:PRK07789 28 PERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQA-TGRVGVCMATSGPGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 81 TDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHI 160
Cdd:PRK07789 107 TNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 161 DLPFDVQMAEIEFDVDTYEALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTL 238
Cdd:PRK07789 187 DIPKDALQAQTTFSWPPRMDLPGYRPvtKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 239 MGWGAIPDDHPLMAGMAGlqtsqMYGN-ATVLA---SDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGP 314
Cdd:PRK07789 267 MARGAFPDSHPQHLGMPG-----MHGTvAAVAAlqrSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 315 DYGIVSDAGAALKLMVEVARELRQAGKLPDYGEWAEQCRE-RKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVSTI 393
Cdd:PRK07789 342 DVPIVGDVKEVIAELIAALRAEHAAGGKPDLTAWWAYLDGwRETYPLGYDEPSDGSLAPQYVIERLGEIAGPDAIYVAGV 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 394 GLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNN 473
Cdd:PRK07789 422 GQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 474 SYLGLIRQSQRGFemdYQvqlafDNINNPDLN---GYGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQKfqvPVV 550
Cdd:PRK07789 502 GNLGMVRQWQTLF---YE-----ERYSNTDLHthsHRIPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAINDR---PVV 570
|
....
gi 730604155 551 LEVI 554
Cdd:PRK07789 571 IDFV 574
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
8-560 |
6.39e-129 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 391.34 E-value: 6.39e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 8 EAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKL---GGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDMI 84
Cdd:PRK07418 23 YALMDSLKRHGVKHIFGYPGGAILPIYDELYKAeaeGWLKHILVRHEQGAAHAADGYARA-TGKVGVCFGTSGPGATNLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 85 TGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLPF 164
Cdd:PRK07418 102 TGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 165 DVqmAEIEFDVDTYEA----LPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTL 238
Cdd:PRK07418 182 DV--GQEEFDYVPVEPgsvkPPGYRPtvKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTTL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 239 MGWGAIPDDHPLMAGMAGLQTSQmYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGI 318
Cdd:PRK07418 260 MGKGAFDEHHPLSVGMLGMHGTA-YANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVPI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 319 VSDAGAALKLMVEVARELRQAgklPDYGEWAEQCRERKRTM-LRKTHYDNvPIKPQRVYEEmLKSFGRDTVYVSTIGLSQ 397
Cdd:PRK07418 339 VGDVRKVLVKLLERSLEPTTP---PRTQAWLERINRWKQDYpLVVPPYEG-EIYPQEVLLA-VRDLAPDAYYTTDVGQHQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 398 IAAAQFLHvYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLG 477
Cdd:PRK07418 414 MWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQG 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 478 LIRQSQRGFemdYQVQLAFDNINN--PDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAkeLAqkFQVPVVLEVIL 555
Cdd:PRK07418 493 MVRQWQESF---YGERYSASNMEPgmPDF-------VKLAEAFGVKGMVISERDQLKDAIAEA--LA--HDGPVLIDVHV 558
|
....*
gi 730604155 556 ERVTN 560
Cdd:PRK07418 559 RRDEN 563
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
8-557 |
2.74e-128 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 388.02 E-value: 2.74e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 8 EAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDMITGL 87
Cdd:PRK07282 14 DLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKS-TGKLGVAVVTSGPGATNAITGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 88 YAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLPFDVQ 167
Cdd:PRK07282 93 ADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKDVS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 168 MAEIEFDVDTYEALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGWGAIP 245
Cdd:PRK07282 173 ALETDFIYDPEVNLPSYQPtlEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQGTIA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 246 DDHPLMAGMAGLQTSqMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIVSDAGAA 325
Cdd:PRK07282 253 TSHPLFLGMGGMHGS-YAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKKA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 326 LKLMVEvARELRQagklpDYGEWAEQCRERKRTMlRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLH 405
Cdd:PRK07282 332 LQMLLA-EPTVHN-----NTEKWIEKVTKDKNRV-RSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 406 VYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQSQRG 485
Cdd:PRK07282 405 YQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQES 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730604155 486 FEMDYQVQLAFDNINNPDLngygvdhvaVAEGLGCRAIRVTEPGKIKAGLEEAKElaqkfQVPVVLEVILER 557
Cdd:PRK07282 485 FYEGRTSESVFDTLPDFQL---------MAQAYGIKHYKFDNPETLAQDLEVITE-----DVPMLIEVDISR 542
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
2-553 |
2.37e-125 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 380.64 E-value: 2.37e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 2 AKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKlGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGT 81
Cdd:PRK07710 14 KLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARI-SGKPGVVIATSGPGAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 82 DMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHID 161
Cdd:PRK07710 92 NVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 162 LPFDVQMAEIEFDVDTYEALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLM 239
Cdd:PRK07710 172 IPKDMVVEEGEFCYDVQMDLPGYQPnyEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 240 GWGAIPDDHPLMAGMAGLQTSQMyGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIV 319
Cdd:PRK07710 252 GLGGFPADHPLFLGMAGMHGTYT-ANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 320 SDAGAALKLMVEvarelrQAGKLPDYGEWAEQCRERKRTMlrKTHYDNVP--IKPQRVYeEMLKSFGRDTVYVST-IGLS 396
Cdd:PRK07710 331 ADAKQALQVLLQ------QEGKKENHHEWLSLLKNWKEKY--PLSYKRNSesIKPQKAI-EMLYEITKGEAIVTTdVGQH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 397 QIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYL 476
Cdd:PRK07710 402 QMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEAL 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730604155 477 GLIRQSQRGFemdYQVQLAFDNI-NNPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKELaqkfQVPVVLEV 553
Cdd:PRK07710 482 GMVRQWQEEF---YNQRYSHSLLsCQPDF-------VKLAEAYGIKGVRIDDELEAKEQLQHAIEL----QEPVVIDC 545
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
4-561 |
5.23e-122 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 371.99 E-value: 5.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 4 MRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKlGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDM 83
Cdd:PRK06725 15 VTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARA-SGKVGVVFATSGPGATNL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 84 ITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLP 163
Cdd:PRK06725 93 VTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 164 FDVQMAEIEFDVDTYEALPAYKPQ--ASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGW 241
Cdd:PRK06725 173 KDVQNEKVTSFYNEVVEIPGYKPEprPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 242 GAIPDDHPLMAGMAGLQTSqMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIVSD 321
Cdd:PRK06725 253 GAYPPGDPLFLGMLGMHGT-YAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVGD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 322 AGAALKLMVEVARELRQagklpdyGEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAAA 401
Cdd:PRK06725 332 VKKALHMLLHMSIHTQT-------DEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 402 QFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQ 481
Cdd:PRK06725 405 HFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQ 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 482 SQrgfEMDYQVQLAFDNINNPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAkeLAQKFqvPVVLEVILERVTNI 561
Cdd:PRK06725 485 WQ---EMFYENRLSESKIGSPDF-------VKVAEAYGVKGLRATNSTEAKQVMLEA--FAHEG--PVVVDFCVEEGENV 550
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
3-537 |
2.49e-115 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 355.55 E-value: 2.49e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 3 KMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTD 82
Cdd:PRK09107 10 QMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARS-TGKPGVVLVTSGPGATN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 83 MITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDL 162
Cdd:PRK09107 89 AVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 163 PFDVQMAEIEFDV-DTYEALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINA--DASDDLVTFAELTGIPVIPT 237
Cdd:PRK09107 169 PKDVQFATGTYTPpQKAPVHVSYQPkvKGDAEAITEAVELLANAKRPVIYSGGGVINSgpEASRLLRELVELTGFPITST 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 238 LMGWGAIPDDHPLMAGMAGlqtsqMYG----NATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFG 313
Cdd:PRK09107 249 LMGLGAYPASGKNWLGMLG-----MHGtyeaNMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 314 PDYGIVSDAGAALKLMVEVareLRQAGKLPDYGE----WAEQCRERKRTMLRKTHYDNVpIKPQ----RVYEemlKSFGR 385
Cdd:PRK09107 324 VDVPIIGDVGHVLEDMLRL---WKARGKKPDKEAladwWGQIARWRARNSLAYTPSDDV-IMPQyaiqRLYE---LTKGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 386 DTvYVST-IGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKL 464
Cdd:PRK09107 397 DT-YITTeVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNL 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730604155 465 PYVHVLVNNSYLGLIRQSQrgfemdyqvQLAFDNINNPDLNGYGVDHVAVAEGLGCRAIRVTEPGKIKAGLEE 537
Cdd:PRK09107 476 PVKIFILNNQYMGMVRQWQ---------QLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQE 539
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-544 |
5.25e-113 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 348.73 E-value: 5.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAG 80
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARA-TGKVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 81 TDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHI 160
Cdd:PRK08979 80 TNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 161 DLPFDVQMAEIEFDVDTYEALP--AYKPQAS--RAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIP 236
Cdd:PRK08979 160 DLPKDCLNPAILHPYEYPESIKmrSYNPTTSghKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 237 TLMGWGAIPDDHPLMAGMAGlqtsqMYG----NATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVF 312
Cdd:PRK08979 240 TLMGLGAFPGTHKNSLGMLG-----MHGryeaNMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 313 GPDYGIVSDAGAALKLMV---EVARELRQAGKLPDYGEWAEQCRERKRTMLRKThydNVPIKPQRVYEEMLKSFGRDTVY 389
Cdd:PRK08979 315 RVDIPIVGSADKVLDSMLallDESGETNDEAAIASWWNEIEVWRSRNCLAYDKS---SERIKPQQVIETLYKLTNGDAYV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 390 VSTIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHV 469
Cdd:PRK08979 392 ASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKII 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730604155 470 LVNNSYLGLIRQSQrgfEMDYQVQLAFDNINN-PDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAkeLAQK 544
Cdd:PRK08979 472 NLNNRFLGMVKQWQ---DMIYQGRHSHSYMDSvPDF-------AKIAEAYGHVGIRISDPDELESGLEKA--LAMK 535
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-545 |
1.71e-112 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 347.67 E-value: 1.71e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAG 80
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARS-TGKVGCVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 81 TDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHI 160
Cdd:PRK06882 80 TNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 161 DLPFDVQMAEIEFdvdTYE-----ALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIP 233
Cdd:PRK06882 160 DIPKDMVNPANKF---TYEypeevSLRSYNPtvQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 234 VIPTLMGWGAIPDDHPLMAGMAGLQTSQMYGNAtVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFG 313
Cdd:PRK06882 237 VTSSLMGLGAYPSTDKQFLGMLGMHGTYEANNA-MHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 314 PDYGIVSDAGAALKLMVEVARELRQAGKLPDYGEWAEQCRERK-RTMLRKTHYDNVpIKPQRVYEEMLKSFGRDTVYVST 392
Cdd:PRK06882 316 AYIPIVGSAKNVLEEFLSLLEEENLAKSQTDLTAWWQQINEWKaKKCLEFDRTSDV-IKPQQVVEAIYRLTNGDAYVASD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 393 IGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVN 472
Cdd:PRK06882 395 VGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLN 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730604155 473 NSYLGLIRQSQRGFEMDYQVQLAFDNInnPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQKF 545
Cdd:PRK06882 475 NRFLGMVKQWQDLIYSGRHSQVYMNSL--PDF-------AKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKL 538
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
9-560 |
1.42e-111 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 345.53 E-value: 1.42e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 9 AAVEVLKKEGVDIAFGVPGAAINPLYA---AMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDMIT 85
Cdd:CHL00099 15 ALIDSLVRHGVKHIFGYPGGAILPIYDelyAWEKKGLIKHILVRHEQGAAHAADGYARS-TGKVGVCFATSGPGATNLVT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 86 GLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLPFD 165
Cdd:CHL00099 94 GIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 166 VQMAEIEF----DVDTYEALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLM 239
Cdd:CHL00099 174 VGLEKFDYyppePGNTIIKILGCRPiyKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 240 GWGAIPDDHPLMAGMAGLQTSqMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIV 319
Cdd:CHL00099 254 GKGIFDEDHPLCLGMLGMHGT-AYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 320 SDagaalklMVEVARELRQAGKLPDYGEWAEQCRE-RKRTMLRKTHY------DNVPIKPQRVYEEmLKSFGRDTVYVST 392
Cdd:CHL00099 333 GD-------VKKVLQELLELLKNSPNLLESEQTQAwRERINRWRKEYpllipkPSTSLSPQEVINE-ISQLAPDAYFTTD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 393 IGLSQIAAAQFLHVyGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVN 472
Cdd:CHL00099 405 VGQHQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIIN 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 473 NSYLGLIRQSQRGFemdYQVQLAFDNINN--PDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQkfqvPVV 550
Cdd:CHL00099 484 NKWQGMVRQWQQAF---YGERYSHSNMEEgaPDF-------VKLAEAYGIKGLRIKSRKDLKSSLKEALDYDG----PVL 549
|
570
....*....|
gi 730604155 551 LEVILERVTN 560
Cdd:CHL00099 550 IDCQVIEDEN 559
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
4-537 |
2.87e-111 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 343.40 E-value: 2.87e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 4 MRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKlGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDM 83
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARA-TGKVGVCIATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 84 ITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLP 163
Cdd:PRK08978 79 ITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 164 FDVQMAEIEFDVDTYEalPAYKPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGWGA 243
Cdd:PRK08978 159 KDIQLAEGELEPHLTT--VENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 244 IPDDHPLMAGMAGlqtsqMYG----NATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIV 319
Cdd:PRK08978 237 VEADHPYYLGMLG-----MHGtkaaNLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 320 SDAGAALklmvevaRELRQAgklPDYGEWAEQCRERKRTMlrKTHYDN--VPIKPQRVYEEMLKSFGRDTVYVSTIGLSQ 397
Cdd:PRK08978 312 GDLNALL-------PALQQP---LNIDAWRQHCAQLRAEH--AWRYDHpgEAIYAPALLKQLSDRKPADTVVTTDVGQHQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 398 IAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLG 477
Cdd:PRK08978 380 MWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLG 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730604155 478 LIRQSQrgfemdyqvQLAFDN-------INNPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEE 537
Cdd:PRK08978 460 MVRQWQ---------QLFFDErysetdlSDNPDF-------VMLASAFGIPGQTITRKDQVEAALDT 510
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-538 |
4.67e-109 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 338.22 E-value: 4.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAG 80
Cdd:PRK08155 10 RKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMART-TGKPAVCMACSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 81 TDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHI 160
Cdd:PRK08155 89 TNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 161 DLPFDVQMAEIEFDVDTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMG 240
Cdd:PRK08155 169 DIPKDVQTAVIELEALPAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 241 WGAIPDDHPLMAGMAGLQTSQmYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIVS 320
Cdd:PRK08155 249 LGMLPKAHPLSLGMLGMHGAR-STNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 321 DAGAAL-KLMVEVARELRQagklpdygEWAEQCRERKRTM-LRKTHYDNvPIKPQRVYEEMLKSFGRDTVYVSTIGLSQI 398
Cdd:PRK08155 328 DVDDVLaQLLPLVEAQPRA--------EWHQLVADLQREFpCPIPKADD-PLSHYGLINAVAACVDDNAIITTDVGQHQM 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 399 AAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGL 478
Cdd:PRK08155 399 WTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGL 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730604155 479 IRQSQ------RGFEMDYQvqlafdninnpdlngYGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEA 538
Cdd:PRK08155 479 VHQQQslfygqRVFAATYP---------------GKINFMQIAAGFGLETCDLNNEADPQAALQEA 529
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-557 |
6.25e-109 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 338.26 E-value: 6.25e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAG 80
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARA-TGKTGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 81 TDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHI 160
Cdd:PRK06466 80 TNAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 161 DLPFDVQMAEIEFDvdtYE-----ALPAYKPqASR---AQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGI 232
Cdd:PRK06466 160 DIPKDMTNPAEKFE---YEypkkvKLRSYSP-AVRghsGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 233 PVIPTLMGWGAIPDDHPLMAGMAGLQTSqMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVF 312
Cdd:PRK06466 236 PVTNTLMGLGGFPGTDRQFLGMLGMHGT-YEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 313 GPDYGIVSDAGAALKLMVEVARELRQAGKLPDYGEWAEQCRE-RKR-TMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYV 390
Cdd:PRK06466 315 KADIPIVGPVESVLTEMLAILKEIGEKPDKEALAAWWKQIDEwRGRhGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 391 STIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVL 470
Cdd:PRK06466 395 SDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIIN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 471 VNNSYLGLIRQSQrgfEMDYQVQLAFDNINN-PDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQKFqvpV 549
Cdd:PRK06466 475 LNNGALGMVRQWQ---DMQYEGRHSHSYMESlPDF-------VKLAEAYGHVGIRITDLKDLKPKLEEAFAMKDRL---V 541
|
....*...
gi 730604155 550 VLEVILER 557
Cdd:PRK06466 542 FIDIYVDR 549
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-540 |
4.14e-105 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 328.35 E-value: 4.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAG 80
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARA-TGEVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 81 TDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHI 160
Cdd:PRK07979 80 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 161 DLPFDVQMAEIEFDVDTYE--ALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIP 236
Cdd:PRK07979 160 DLPKDILNPANKLPYVWPEsvSMRSYNPttQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 237 TLMGWGAIPDDHPLMAGMAGLQTSqMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDY 316
Cdd:PRK07979 240 SLMGLGAFPATHRQSLGMLGMHGT-YEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 317 GIVSDAGAALKLMVEVARELRQAGKLPDYGEWAEQCRE-RKRTMLRkthYD--NVPIKPQRVYEEMLKSFGRDTVYVSTI 393
Cdd:PRK07979 319 PIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQwRARQCLK---YDthSEKIKPQAVIETLWRLTKGDAYVTSDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 394 GLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNN 473
Cdd:PRK07979 396 GQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNN 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730604155 474 SYLGLIRQSQRGFEMDYQVQLAFDNInnPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKE 540
Cdd:PRK07979 476 RYLGMVKQWQDMIYSGRHSQSYMQSL--PDF-------VRLAEAYGHVGIQISHPDELESKLSEALE 533
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
2-544 |
1.07e-104 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 327.92 E-value: 1.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 2 AKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGT 81
Cdd:PRK06965 19 ADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARA-TGKVGVALVTSGPGVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 82 DMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHID 161
Cdd:PRK06965 98 NAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 162 LPFDVQMAEIEFDVDTYEALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLM 239
Cdd:PRK06965 178 IPKDVSKTPCEYEYPKSVEMRSYNPvtKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 240 GWGAIPDDHPLMAGMAGLQTSqMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEG-RKFVHIDIEPTQIGRVFGPDYGI 318
Cdd:PRK06965 258 GLGAYPASDKKFLGMLGMHGT-YEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRpRKIIHIDIDPSSISKRVKVDIPI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 319 VSDAGAALKLMVEVARELRQAGKLPDYGEWAEQCRE-RKRTMLRKTHYDNVpIKPQRVYEEMLKSFGRDTVYVSTIGLSQ 397
Cdd:PRK06965 337 VGDVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGwRSRDCLKYDRESEI-IKPQYVVEKLWELTDGDAFVCSDVGQHQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 398 IAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLG 477
Cdd:PRK06965 416 MWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLG 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730604155 478 LIRQSQrgfEMDYQVQLAFDNINN-PDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQK 544
Cdd:PRK06965 496 MVRQWQ---EIEYSKRYSHSYMDAlPDF-------VKLAEAYGHVGMRIEKTSDVEPALREALRLKDR 553
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
11-554 |
3.43e-103 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 323.61 E-value: 3.43e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 11 VEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDMITGLYAA 90
Cdd:PLN02470 20 VEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKA-SGKVGVCIATSGPGATNLVTGLADA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 91 IADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLPFDVQMAE 170
Cdd:PLN02470 99 LLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDIQQQL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 171 IEFDVDTYEALPAY----KPQASRAQIEKSLELLFASERPLLVAGGGIINadASDDLVTFAELTGIPVIPTLMGWGAIPD 246
Cdd:PLN02470 179 AVPNWNQPMKLPGYlsrlPKPPEKSQLEQIVRLISESKRPVVYVGGGCLN--SSEELREFVELTGIPVASTLMGLGAFPA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 247 DHPL---MAGMAGlqtsQMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIVSDAG 323
Cdd:PLN02470 257 SDELslqMLGMHG----TVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADVK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 324 AALKLMVEVARElrQAGKLPDYGEWAEQCRERKRTM-LRKTHYDNVpIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQ 402
Cdd:PLN02470 333 LALQGLNKLLEE--RKAKRPDFSAWRAELDEQKEKFpLSYPTFGDA-IPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 403 FLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQS 482
Cdd:PLN02470 410 WYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQW 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730604155 483 QRGFemdYQVQLAFDNINNPDLNGYGV-DHVAVAEGLGCRAIRVTEpgkiKAGLEEAKELAQKFQVPVVLEVI 554
Cdd:PLN02470 490 EDRF---YKANRAHTYLGDPDAEAEIFpDFLKFAEGCKIPAARVTR----KSDLREAIQKMLDTPGPYLLDVI 555
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
11-557 |
3.06e-97 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 307.92 E-value: 3.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 11 VEVLKKEGVDIAFGVPGAAINPLYAAM---KKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDMITGL 87
Cdd:PRK06456 9 VDSLKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARA-SGVPGVCTATSGPGTTNLVTGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 88 YAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLPFDVQ 167
Cdd:PRK06456 88 ITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIPRDIF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 168 MAEIEfDVDTYEA--LPAYKP---QASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGWG 242
Cdd:PRK06456 168 YEKME-EIKWPEKplVKGYRDfptRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTFPGKT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 243 AIPDDHPLMAGMAGlqtsqMYGNA----TVLASDFVYGIGNRWANRHTGSVEKYTE-GRKFVHIDIEPTQIGRVFGPDYG 317
Cdd:PRK06456 247 AIPHDHPLYFGPMG-----YYGRAeasmAALESDAMLVVGARFSDRTFTSYDEMVEtRKKFIMVNIDPTDGEKAIKVDVG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 318 IVSDAGAALKLMVEVARELrqaGKLPDYGEWAEQCRERKRTMLRKTHYD-NVPIKPQRVYEEMLKSFGRDTVYVSTIGLS 396
Cdd:PRK06456 322 IYGNAKIILRELIKAITEL---GQKRDRSAWLKRVKEYKEYYSQFYYTEeNGKLKPWKIMKTIRQALPRDAIVTTGVGQH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 397 QIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYL 476
Cdd:PRK06456 399 QMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 477 GLIRQSQRGFEMDYQVQLAFdninnpdlnGYGVDHVAVAEGLGCRAIRVTEPGKIkaglEEAKELAQKFQVPVVLEVILE 556
Cdd:PRK06456 479 GLVRQVQDLFFGKRIVGVDY---------GPSPDFVKLAEAFGALGFNVTTYEDI----EKSLKSAIKEDIPAVIRVPVD 545
|
.
gi 730604155 557 R 557
Cdd:PRK06456 546 K 546
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-557 |
9.62e-93 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 295.38 E-value: 9.62e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGG-IEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPA 79
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARS-TGRPGVCSVVPGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 80 GTDMITGLYAAIADSVPILCITGQAPRARLYK---EDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPG 156
Cdd:PRK08266 80 VLNAGAALLTAYGCNSPVLCLTGQIPSALIGKgrgHLHEMPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 157 PVHIDLPFDVQMAEIEfDVDTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIinADASDDLVTFAELTGIPVIP 236
Cdd:PRK08266 160 PVALEMPWDVFGQRAP-VAAAPPLRPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEMLQAPVVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 237 TLMGWGAIPDDHPLMAGMAGlqtsqmyGNATVLASDFVYGIGNR-------WANRhtgsvekyTEGRKFVHIDIEPTQIG 309
Cdd:PRK08266 237 FRSGRGIVSDRHPLGLNFAA-------AYELWPQTDVVIGIGSRlelptfrWPWR--------PDGLKVIRIDIDPTEMR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 310 RvFGPDYGIVSDAGAALKLMVEvarelrqagKLPDYGEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLK-SFGRDTV 388
Cdd:PRK08266 302 R-LKPDVAIVADAKAGTAALLD---------ALSKAGSKRPSRRAELRELKAAARQRIQAVQPQASYLRAIReALPDDGI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 389 YVSTigLSQIAAAQFLH--VYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPY 466
Cdd:PRK08266 372 FVDE--LSQVGFASWFAfpVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 467 VHVLVNNSYLGLIRQSQRgfEMDYQVQLAFDnINNPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQkfq 546
Cdd:PRK08266 450 VTVVFNNNAYGNVRRDQK--RRFGGRVVASD-LVNPDF-------VKLAESFGVAAFRVDSPEELRAALEAALAHGG--- 516
|
570
....*....|.
gi 730604155 547 vPVVLEVILER 557
Cdd:PRK08266 517 -PVLIEVPVPR 526
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
4-553 |
2.56e-84 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 273.24 E-value: 2.56e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 4 MRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKlGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDM 83
Cdd:PRK08322 1 MKAADLFVKCLENEGVEYIFGIPGEENLDLLEALRD-SSIKLILTRHEQGAAFMAATYGRL-TGKAGVCLSTLGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 84 ITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLP 163
Cdd:PRK08322 79 VTGVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 164 FDVqmAEIEFDVDTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGWGA 243
Cdd:PRK08322 159 EDI--AAEETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 244 IPDDHPLMAGMAGLQtSQMYGNATVLASDFVYGIGN--------RWaNRHTgsvekyteGRKFVHIDIEPTQIGRVFGPD 315
Cdd:PRK08322 237 IPETHPLSLGTAGLS-QGDYVHCAIEHADLIINVGHdviekppfFM-NPNG--------DKKVIHINFLPAEVDPVYFPQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 316 YGIVSDAGAALKLMVEvaRELRQAGKLPDYgewAEQCRERKRTMLRKTHYDN-VPIKPQRVYEEMLKSFGRDTVYVSTIG 394
Cdd:PRK08322 307 VEVVGDIANSLWQLKE--RLADQPHWDFPR---FLKIREAIEAHLEEGADDDrFPMKPQRIVADLRKVMPDDDIVILDNG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 395 LSQIAAAQFLHVYGPRQWI--NAGQAgpLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVN 472
Cdd:PRK08322 382 AYKIWFARNYRAYEPNTCLldNALAT--MGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 473 NSYLGLIR--QSQRGFE---MDYQvqlafdninNPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAkeLAQKfqV 547
Cdd:PRK08322 460 DNAYGMIRwkQENMGFEdfgLDFG---------NPDF-------VKYAESYGAKGYRVESADDLLPTLEEA--LAQP--G 519
|
....*.
gi 730604155 548 PVVLEV 553
Cdd:PRK08322 520 VHVIDC 525
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
4-556 |
2.94e-76 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 253.14 E-value: 2.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 4 MRAIEAAVEVLKKEGVDIAFG--VPGAainpLYAAMKKLGgIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGT 81
Cdd:PRK06112 14 GTVAHAIARALKRHGVEQIFGqsLPSA----LFLAAEAIG-IRQIAYRTENAGGAMADGYARV-SGKVAVVTAQNGPAAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 82 DMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHID 161
Cdd:PRK06112 88 LLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 162 LPFDVQMAEIEF----DVDTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPT 237
Cdd:PRK06112 168 LPADLLTAAAAApaapRSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 238 LMGWGAIPDDHPLMAGMAGL----QTSQMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIGRVFG 313
Cdd:PRK06112 248 NMGKGAVDETHPLSLGVVGSlmgpRSPGRHLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGRNYE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 314 PdYGIVSDAGAALKLMVEVARELRQAGKLPDYGEWAE---QCRERKRT-MLRKTHYDNVPIKPQRVYEEMLKSFGRDTVY 389
Cdd:PRK06112 328 A-LRLVGDARLTLAALTDALRGRDLAARAGRRAALEPaiaAGREAHREdSAPVALSDASPIRPERIMAELQAVLTGDTIV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 390 VSTIGLSQIAAAQFLHVYGPRQWINA--GQAGpLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYV 467
Cdd:PRK06112 407 VADASYSSIWVANFLTARRAGMRFLTprGLAG-LGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVT 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 468 HVLVNNSYLGLIRQSQRGFEMDYQVQLAFDninnpdlngyGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKelaqKFQV 547
Cdd:PRK06112 486 IVVLNNGILGFQKHAETVKFGTHTDACHFA----------AVDHAAIARACGCDGVRVEDPAELAQALAAAM----AAPG 551
|
....*....
gi 730604155 548 PVVLEVILE 556
Cdd:PRK06112 552 PTLIEVITD 560
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
4-562 |
1.06e-75 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 251.27 E-value: 1.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 4 MRAIEAAVEVLKKEGVDIAFGVPgaaINPLYAAMKKLGgIEHILARHVEGASHMADGYTRAKSG-NIGVCIGTSGPAGTD 82
Cdd:PRK06154 20 MKVAEAVAEILKEEGVELLFGFP---VNELFDAAAAAG-IRPVIARTERVAVHMADGYARATSGeRVGVFAVQYGPGAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 83 MITGLYAAIADSVPILCITGQAPRARlykedfQAVD--IESIA--KPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPV 158
Cdd:PRK06154 96 AFGGVAQAYGDSVPVLFLPTGYPRGS------TDVApnFESLRnyRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 159 HIDLPFDVQMAEIEFDVDTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTL 238
Cdd:PRK06154 170 VLELPVDVLAEELDELPLDHRPSRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 239 MGWGAIPDDHPLMAGMAGLQTSqmygnATVL----ASDFVYGIGNRWANRHTGSveKYTEGRKFVHIDIEPTQIGRVFGP 314
Cdd:PRK06154 250 NGKSAFPEDHPLALGSGGRARP-----ATVAhflrEADVLFGIGCSLTRSYYGL--PMPEGKTIIHSTLDDADLNKDYPI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 315 DYGIVSDAGAALKLMVEVARE--LRQAGKLPDY-GEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVS 391
Cdd:PRK06154 323 DHGLVGDAALVLKQMIEELRRrvGPDRGRAQQVaAEIEAVRAAWLAKWMPKLTSDSTPINPYRVVWELQHAVDIKTVIIT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 392 -TIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVL 470
Cdd:PRK06154 403 hDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTIL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 471 VNNSYLGLirqsqrgfeMDYQVQLAFDNINNPDLNGygvDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAqKFQVPVV 550
Cdd:PRK06154 483 LNNFSMGG---------YDKVMPVSTTKYRATDISG---DYAAIARALGGYGERVEDPEMLVPALLRALRKV-KEGTPAL 549
|
570
....*....|..
gi 730604155 551 LEVILERVTNIS 562
Cdd:PRK06154 550 LEVITSEETALS 561
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
8-556 |
5.01e-75 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 249.02 E-value: 5.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 8 EAAVEVLKKEGVDIAFGVPG----AAINPLYAAmkklGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDM 83
Cdd:PRK08199 12 QILVDALRANGVERVFCVPGesylAVLDALHDE----TDIRVIVCRQEGGAAMMAEAYGKL-TGRPGICFVTRGPGATNA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 84 ITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLP 163
Cdd:PRK08199 87 SIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 164 FDVQmaeieFDVDTYEALPAYKPQA---SRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMG 240
Cdd:PRK08199 167 EDVL-----SETAEVPDAPPYRRVAaapGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 241 WGAIPDDHPLMAGMAGLQTSQMYGnATVLASDFVYGIGNRWANRHTGSvekYT------EGRKFVHIDIEPTQIGRVFGP 314
Cdd:PRK08199 242 QDLFDNRHPNYAGDLGLGINPALA-ARIREADLVLAVGTRLGEVTTQG---YTlldipvPRQTLVHVHPDAEELGRVYRP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 315 DYGIVSDagaalklMVEVAREL--RQAGKLPDYGEWAEQcrerkrtmLRKTHYDNVPIKPQ-------RVYEEMLKSFGR 385
Cdd:PRK08199 318 DLAIVAD-------PAAFAAALaaLEPPASPAWAEWTAA--------AHADYLAWSAPLPGpgavqlgEVMAWLRERLPA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 386 DTVYVSTIGlsqiAAAQFLHVYGP-RQWinAGQAGP----LGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGA 460
Cdd:PRK08199 383 DAIITNGAG----NYATWLHRFFRfRRY--RTQLAPtsgsMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 461 QFKLPYVHVLVNNSYLGLIRQSQrgfEMDYQVQLAFDNINNPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKE 540
Cdd:PRK08199 457 QYGLPIIVIVVNNGMYGTIRMHQ---EREYPGRVSGTDLTNPDF-------AALARAYGGHGETVERTEDFAPAFERALA 526
|
570
....*....|....*.
gi 730604155 541 lAQKfqvPVVLEVILE 556
Cdd:PRK08199 527 -SGK---PALIEIRID 538
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
8-557 |
7.64e-75 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 247.97 E-value: 7.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 8 EAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKlGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDMITGL 87
Cdd:PRK07524 6 EALVRLLEAYGVETVFGIPGVHTVELYRGLAG-SGIRHVTPRHEQGAGFMADGYARV-SGKPGVCFIITGPGMTNIATAM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 88 YAAIADSVPILCITGQAPRARLYKED---FQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLPF 164
Cdd:PRK07524 84 GQAYADSIPMLVISSVNRRASLGKGRgklHELPDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 165 DVQMAEIEFDVdTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIInaDASDDLVTFAELTGIPVIPTLMGWGAI 244
Cdd:PRK07524 164 DVLAAPADHLL-PAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGAL--AAAAALRALAERLDAPVALTINAKGLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 245 PDDHPLMAGmaGLQTSQMyGNATVLASDFVYGIGNRWANRHTGSV--EKYTEGRKFVHIDIEPTQIGRVFGPDYGIVSDA 322
Cdd:PRK07524 241 PAGHPLLLG--ASQSLPA-VRALIAEADVVLAVGTELGETDYDVYfdGGFPLPGELIRIDIDPDQLARNYPPALALVGDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 323 GAALklmvevARELRQAGKLPDYGEWAEQCRERKRTMLRKTHYDnvPIKPQRVYEEMLKSFGRDTVYVstiGLSQIAAAQ 402
Cdd:PRK07524 318 RAAL------EALLARLPGQAAAADWGAARVAALRQALRAEWDP--LTAAQVALLDTILAALPDAIFV---GDSTQPVYA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 403 FLHVY---GPRQWINAGQA-GPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGL 478
Cdd:PRK07524 387 GNLYFdadAPRRWFNASTGyGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 479 IRqsqrgfemDYQVQLAFD----NINNPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQkfqvPVVLEVI 554
Cdd:PRK07524 467 IR--------RYMVARDIEpvgvDPYTPDF-------IALARAFGCAAERVADLEQLQAALRAAFARPG----PTLIEVD 527
|
...
gi 730604155 555 LER 557
Cdd:PRK07524 528 QAC 530
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-554 |
4.19e-73 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 244.53 E-value: 4.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKL-GGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPA 79
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKL-TGKIGVCLSIGGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 80 GTDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRpGPVH 159
Cdd:PRK08611 80 AIHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 160 IDLPFDVQMAEIEfdVDTYEALPAYKPQA---SRAQIEKSLELLFASERPLLVAGGGIINAdaSDDLVTFAELTGIPVIP 236
Cdd:PRK08611 159 LTIPDDLPAQKIK--DTTNKTVDTFRPTVpspKPKDIKKAAKLINKAKKPVILAGLGAKHA--KEELLAFAEKAKIPIIH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 237 TLMGWGAIPDDHPLMAGMAG-LQTSQMYgnATVLASDFVYGIGNRWAnrhtgSVEKYTEGRKFVHIDIEPTQIGRVFGPD 315
Cdd:PRK08611 235 TLPAKGIIPDDHPYSLGNLGkIGTKPAY--EAMQEADLLIMVGTNYP-----YVDYLPKKAKAIQIDTDPANIGKRYPVN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 316 YGIVSDAGAALKlmvevarELRQAGKLPDYGEWAEQCRERKRT----MLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVS 391
Cdd:PRK08611 308 VGLVGDAKKALH-------QLTENIKHVEDRRFLEACQENMAKwwkwMEEDENNASTPIKPERVMAAIQKIADDDAVLSV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 392 TIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLV 471
Cdd:PRK08611 381 DVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 472 NNSYLGLIRQSQRGF-EMDYQVQLAfdninnpdlngyGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKelaqKFQVPVV 550
Cdd:PRK08611 461 NNQQLAFIKYEQQAAgELEYAIDLS------------DMDYAKFAEACGGKGYRVEKAEELDPAFEEAL----AQDKPVI 524
|
....
gi 730604155 551 LEVI 554
Cdd:PRK08611 525 IDVY 528
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-558 |
1.17e-60 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 211.39 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAAVEVLKKEGVDIAFGVPGAAINP---LYAAmkklGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSG 77
Cdd:PRK07525 3 KMKMTPSEAFVETLQAHGITHAFGIIGSAFMDasdLFPP----AGIRFIDVAHEQNAGHMADGYTRV-TGRMGMVIGQNG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 78 PAGTDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRpGP 157
Cdd:PRK07525 78 PGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 158 VHIDLPFDVQMAEIefDVDTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPT 237
Cdd:PRK07525 157 AQINIPRDYFYGVI--DVEIPQPVRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 238 LMGWGAIPDDHPLMAGMAGLQTSQMyGNATVLASDFVYGIGNRWANRHT---GSVEKYTEGRKFVHIDIEPTQIGRVFGP 314
Cdd:PRK07525 235 YLHNDAFPGSHPLWVGPLGYNGSKA-AMELIAKADVVLALGTRLNPFGTlpqYGIDYWPKDAKIIQVDINPDRIGLTKKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 315 DYGIVSDAGaalklmvEVAREL--RQAGKLP-------------------------------DYG-EWAEQCRERKRTml 360
Cdd:PRK07525 314 SVGICGDAK-------AVARELlaRLAERLAgdagreerkaliaaeksaweqelsswdheddDPGtDWNEEARARKPD-- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 361 rkthydnvPIKPQRVYEEMLKSFGRDTVYVSTIG-LSQIAAAqFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKT 439
Cdd:PRK07525 385 --------YMHPRQALREIQKALPEDAIVSTDIGnNCSIANS-YLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRP 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 440 VVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNsylglirqSQRGFEMDYQVQLAFDNINNPDLNGyGVDHVAVAEGLG 519
Cdd:PRK07525 456 VVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRN--------YQWGAEKKNQVDFYNNRFVGTELDN-NVSYAGIAEAMG 526
|
570 580 590
....*....|....*....|....*....|....*....
gi 730604155 520 CRAIRVTEPGKIKAGLEEAKElAQKFQVPVVLEVILERV 558
Cdd:PRK07525 527 AEGVVVDTQEELGPALKRAID-AQNEGKTTVIEIMCNQE 564
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-163 |
9.07e-60 |
|
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: 195.83 E-value: 9.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 8 EAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKlGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDMITGL 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARA-TGKPGVVLVTSGPGLTNAVTGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730604155 88 YAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLP 163
Cdd:cd07035 79 ANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLP 154
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
8-556 |
2.45e-58 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 204.29 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 8 EAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKlGGIEHILARHVEGAShMADGYTRAKSGNIGVCIGTSGPAGTDMITGL 87
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRK-SKVKYVQVRHEEGAA-LAASVEAKITGKPSACMGTSGPGSIHLLNGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 88 YAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRpGPVHIDLPFDVQ 167
Cdd:PRK06457 84 YDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 168 MAEIEFDVDTYEALPA--YKPQASRAQiekslELLFASERPLLVAGGGIInaDASDDLVTFAELTGIPVIPTLMGWGAIP 245
Cdd:PRK06457 163 RKSSEYKGSKNTEVGKvkYSIDFSRAK-----ELIKESEKPVLLIGGGTR--GLGKEINRFAEKIGAPIIYTLNGKGILP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 246 DDHPLMAGMAGLQTSQMYGNA-------TVLASDFVYgignrwanrhtgsVEKYTEGRKFVHIDIEPTQIGRVFGPDYGI 318
Cdd:PRK06457 236 DLDPKVMGGIGLLGTKPSIEAmdkadllIMLGTSFPY-------------VNFLNKSAKVIQVDIDNSNIGKRLDVDLSY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 319 VSDAGAALKLMVEVARElrqagKLpdYGEWAEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLSQI 398
Cdd:PRK06457 303 PIPVAEFLNIDIEEKSD-----KF--YEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTM 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 399 AAAQFLHVYGPRQWINAGQAGPLGWTLPAALGV-VAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLG 477
Cdd:PRK06457 376 WTARHFRASGEQTFIFSAWLGSMGIGVPGSVGAsFAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLG 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 478 LIRQSQR--GFEmDYQVQLAfdninNPDLNgygvdhvAVAEGLGCRAIRVTEPGKIKAGLEEAKElaqkFQVPVVLEVIL 555
Cdd:PRK06457 456 MIKFEQEvmGYP-EWGVDLY-----NPDFT-------KIAESIGFKGFRLEEPKEAEEIIEEFLN----TKGPAVLDAIV 518
|
.
gi 730604155 556 E 556
Cdd:PRK06457 519 D 519
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
3-568 |
8.85e-57 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 200.08 E-value: 8.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 3 KMRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKlGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTD 82
Cdd:PRK08617 4 KKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALED-SGPELIVTRHEQNAAFMAAAIGRL-TGKPGVVLVTSGPGVSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 83 MITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDL 162
Cdd:PRK08617 82 LATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 163 PFDVQMAEIefdvdTYEALPAY-KPQ---ASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTL 238
Cdd:PRK08617 162 PQDVVDAPV-----TSKAIAPLsKPKlgpASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 239 MGWGAIPDDH-PLMAGMAGLQTSQMyGNATVLASDFVYGIGnrwanrhTGSVEkY------TEG-RKFVHIDIEPTQIGR 310
Cdd:PRK08617 237 QAAGVISRELeDHFFGRVGLFRNQP-GDELLKKADLVITIG-------YDPIE-YeprnwnSEGdATIIHIDVLPAEIDN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 311 VFGPDYGIVSDAGAALKLMVEVARELRQAGKLPDYGEwaEQCRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYV 390
Cdd:PRK08617 308 YYQPERELIGDIAATLDLLAEKLDGLSLSPQSLEILE--ELRAQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 391 STIGLSQIAAAQFLHVYGPRQW-INAGQAgPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHV 469
Cdd:PRK08617 386 VDVGSHYIWMARYFRSYEPRHLlFSNGMQ-TLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 470 LVNNSYLGLIRQSQrgfEMDYQ----VQLAfdninnpdlngyGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAkeLAQkf 545
Cdd:PRK08617 465 IWNDGHYNMVEFQE---EMKYGrssgVDFG------------PVDFVKYAESFGAKGLRVTSPDELEPVLREA--LAT-- 525
|
570 580
....*....|....*....|...
gi 730604155 546 QVPVVLEVILERVTNISMGTELD 568
Cdd:PRK08617 526 DGPVVIDIPVDYSDNIKLMEQLL 548
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
8-172 |
1.25e-54 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 182.82 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 8 EAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDMITGL 87
Cdd:pfam02776 3 EALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARA-TGKPGVVLVTSGPGATNALTGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 88 YAAIADSVPILCITGQAPRARLYKEDFQA-VDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLPFDV 166
Cdd:pfam02776 82 ANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLDV 161
|
....*.
gi 730604155 167 QMAEIE 172
Cdd:pfam02776 162 LLEEVD 167
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
8-553 |
9.65e-54 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 191.74 E-value: 9.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 8 EAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDMITGL 87
Cdd:PRK07064 7 ELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARV-SGGLGVALTSTGTGAGNAAGAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 88 YAAIADSVPILCITGQAPRARLYKED---FQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLPF 164
Cdd:PRK07064 86 VEALTAGTPLLHITGQIETPYLDQDLgyiHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 165 DVQMAEIEFDVDTyEALPAYKPQASRAQIEKSLELLFASERPLLVAGGGIINADASddLVTFAELtGIPVIPTLMGWGAI 244
Cdd:PRK07064 166 DIQAAEIELPDDL-APVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAE--VKRLVDL-GFGVVTSTQGRGVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 245 PDDHPLMAGMAGLQTSqmyGNATVLASDFVYGIGNRWANRHTGsveKYTEG--RKFVHIDIEPTQIGRVFGPDYGIVSDA 322
Cdd:PRK07064 242 PEDHPASLGAFNNSAA---VEALYKTCDLLLVVGSRLRGNETL---KYSLAlpRPLIRVDADAAADGRGYPNDLFVHGDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 323 GAALKLMVEvarelRQAGKLPDYGEWAEQCRERK---RTMLRKThydnvpIKPQRVYEEML-KSFGRDTVYVSTIGLSQI 398
Cdd:PRK07064 316 ARVLARLAD-----RLEGRLSVDPAFAADLRAAReaaVADLRKG------LGPYAKLVDALrAALPRDGNWVRDVTISNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 399 A-AAQFLHVYGPRQWINAgQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLG 477
Cdd:PRK07064 385 TwGNRLLPIFEPRANVHA-LGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYG 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730604155 478 LIRQSQRGFemdYQVQLAFDNINNPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAkeLAqkFQVPVVLEV 553
Cdd:PRK07064 464 VIRNIQDAQ---YGGRRYYVELHTPDF-------ALLAASLGLPHWRVTSADDFEAVLREA--LA--KEGPVLVEV 525
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
11-557 |
2.63e-47 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 174.41 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 11 VEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGAShMADGYTRAKSGNIGVCIGTSGPAGTDMITGLYAA 90
Cdd:PRK09124 10 AKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAA-FAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 91 IADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAfhvMRS--GRPGPVHIDLPFDVQM 168
Cdd:PRK09124 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIA---MRKaiLNRGVAVVVLPGDVAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 169 AEIEFDVdTYEALPAYKP--QASRAQIEKSLELLFASERPLLVAGGGIinADASDDLVTFAELTGIPVIPTLMGWGAIPD 246
Cdd:PRK09124 166 KPAPERA-TPHWYHAPQPvvTPAEEELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALRGKEHVEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 247 DHPLMAGMAGLQ--TSqmyGNATVLASDFVYGIGNRWANRhtgsvEKYTEGRKFVHIDIEPTQIGRVFGPDYGIVSDAGA 324
Cdd:PRK09124 243 DNPYDVGMTGLIgfSS---GYHAMMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 325 ALKLMVEVARELRQAGKLpdygewaEQCRERKRTM------LRKTHYDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLSQI 398
Cdd:PRK09124 315 TLAALLPLLEEKTDRKFL-------DKALEHYRKArkglddLAVPSDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 399 AAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGL 478
Cdd:PRK09124 388 WAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 479 IRQSQR--GFeMDYQVQLafdniNNPDLngygvdhVAVAEGLGCRAIRVTEPGKIKAGLEEAkeLAQkfQVPVVLEVILE 556
Cdd:PRK09124 468 VAMEMKagGY-LTDGTDL-----HNPDF-------AAIAEACGITGIRVEKASELDGALQRA--FAH--DGPALVDVVTA 530
|
.
gi 730604155 557 R 557
Cdd:PRK09124 531 K 531
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
10-538 |
6.54e-47 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 172.98 E-value: 6.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 10 AVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGgIEHILARHVEGASHMADGYTRAKSgNIGVCIGTSGPAGTDMITGLYA 89
Cdd:PRK05858 11 AARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTR-VPGVAVLTAGPGVTNGMSAMAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 90 AIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLPFDVQMA 169
Cdd:PRK05858 89 AQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDHAFS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 170 EIEFDVDTYEALPAYK-PQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGWGAIPDDH 248
Cdd:PRK05858 169 MADDDGRPGALTELPAgPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVVPADH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 249 PLMAGMAglqTSQMYGNATVLAS-----DFVYGIGnrWANRHTgsvekytegrKFVHIDIEPTQIGRVFGPDYGIVSDAG 323
Cdd:PRK05858 249 PLAFSRA---RGKALGEADVVLVvgvpmDFRLGFG--VFGGTA----------QLVHVDDAPPQRAHHRPVAAGLYGDLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 324 AALKLMVEvarelrQAGKLPDYGEW-------AEQCRERKRTMLRKthyDNVPIKPQRVYEEMLKSFGRDTVYVSTIGLS 396
Cdd:PRK05858 314 AILSALAG------AGGDRTDHQGWieelrtaETAARARDAAELAD---DRDPIHPMRVYGELAPLLDRDAIVIGDGGDF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 397 QIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYL 476
Cdd:PRK05858 385 VSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIW 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730604155 477 GLIRQSQR---GFEM--DYQVQLAFDNinnpdlngygvdhvaVAEGLGCRAIRVTEPGKIKAGLEEA 538
Cdd:PRK05858 465 GLEKHPMEalyGYDVaaDLRPGTRYDE---------------VVRALGGHGELVTVPAELGPALERA 516
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-554 |
3.65e-45 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 168.63 E-value: 3.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAiEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHvEGASHMADGYTRAKSGNIGVCIGTSGPAG 80
Cdd:PRK06546 1 MAKTVA-EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRH-EEAAAFAAAAEAQLTGKLAVCAGSCGPGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 81 TDMITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAF-HVMrsGRPGPVH 159
Cdd:PRK06546 79 LHLINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIqHAV--AGGGVSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 160 IDLPFDVQMAEIEfDVDTYEALPAYKPQA--SRAQIEKSLELLFASERPLLVAGGGIinADASDDLVTFAELTGIPVIPT 237
Cdd:PRK06546 157 VTLPGDIADEPAP-EGFAPSVISPRRPTVvpDPAEVRALADAINEAKKVTLFAGAGV--RGAHAEVLALAEKIKAPVGHS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 238 LMGWGAIPDDHPLMAGMAGLQTsqmYGNAT----------VLASDFVYgignrwanrhtgsvEKYTEGRKFVHIDIEPTQ 307
Cdd:PRK06546 234 LRGKEWIQYDNPFDVGMSGLLG---YGAAHeamheadlliLLGTDFPY--------------DQFLPDVRTAQVDIDPEH 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 308 IGRVFGPDYGIVSDAGAALklmvevaRELrqagkLPDygewAEQCRERK--RTMLRKtHYDN---------------VPI 370
Cdd:PRK06546 297 LGRRTRVDLAVHGDVAETI-------RAL-----LPL----VKEKTDRRflDRMLKK-HARKlekvvgaytrkvekhTPI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 371 KPQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQ 450
Cdd:PRK06546 360 HPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLS 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 451 FMIEELAVGAQFKLPYVHVLVNNSYLGLIRqsqrgFEM------DYQVqlafdniNNPDlngygVDHVAVAEGLGCRAIR 524
Cdd:PRK06546 440 MLLGELLTVKLYDLPVKVVVFNNSTLGMVK-----LEMlvdglpDFGT-------DHPP-----VDYAAIAAALGIHAVR 502
|
570 580 590
....*....|....*....|....*....|
gi 730604155 525 VTEPGKIKAGLEEAkeLAQKFqvPVVLEVI 554
Cdd:PRK06546 503 VEDPKDVRGALREA--FAHPG--PALVDVV 528
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-558 |
7.01e-44 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 164.79 E-value: 7.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 1 MAKMRAIEAA---VEVLKKEGVDIAFGVPGAAINPLYAAMKKLG--GIEH---ILARHVEGASHMADGYTRAkSGNIG-- 70
Cdd:PRK08327 1 SMALTMYTAAelfLELLKELGVDYIFINSGTDYPPIIEAKARARaaGRPLpefVICPHEIVAISMAHGYALV-TGKPQav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 71 ---VCIGTSGPAGtdmitGLYAAIADSVPILCITGQAPrarlYKEDF-------------QAVDIESIAKPVTKWAVTVR 134
Cdd:PRK08327 80 mvhVDVGTANALG-----GVHNAARSRIPVLVFAGRSP----YTEEGelgsrntrihwtqEMRDQGGLVREYVKWDYEIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 135 EPALVPRVFQQAFHVMRSGRPGPVHIDLPFDVQMAEIE-FDVDTYEALPAYKPQASRAQIEKSLELLFASERPLLVAGGG 213
Cdd:PRK08327 151 RGDQIGEVVARAIQIAMSEPKGPVYLTLPREVLAEEVPeVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITWRA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 214 IINADASDDLVTFAELTGIPVI---PTLMgwgAIPDDHPLMAGMAGlqtsqmygNATVLASDFVYGIGNR--WANRHTGS 288
Cdd:PRK08327 231 GRTAEGFASLRRLAEELAIPVVeyaGEVV---NYPSDHPLHLGPDP--------RADLAEADLVLVVDSDvpWIPKKIRP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 289 vekyTEGRKFVHIDIEP--TQIG-RVFGPDYGIVSDAGAALKLMVEVAREL---RQAGKLPDYGEWAE-QCRERKRTMLR 361
Cdd:PRK08327 300 ----DADARVIQIDVDPlkSRIPlWGFPCDLCIQADTSTALDQLEERLKSLasaERRRARRRRAAVRElRIRQEAAKRAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 362 KTHY-DNVPIKPQRVYEEMLKSFGRDTVYVSTIGlsqiAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTV 440
Cdd:PRK08327 376 IERLkDRGPITPAYLSYCLGEVADEYDAIVTEYP----FVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 441 VALSGDYDFQFMIEE--LAVGAQFKLPYVHVLVNNSYLGLIRQSQRGF-------EMDYQVQLAFDninnPDlngygVDH 511
Cdd:PRK08327 452 IATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVypegyaaRKGTFPGTDFD----PR-----PDF 522
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 730604155 512 VAVAEGLGCRAIRVTEPGKIKAGLEEAKELAQKFQVPVVLEVILERV 558
Cdd:PRK08327 523 AKIAEAFGGYGERVEDPEELKGALRRALAAVRKGRRSAVLDVIVDRV 569
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
393-553 |
1.37e-40 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 144.26 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 393 IGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVN 472
Cdd:pfam02775 2 IGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 473 NSYLGLIRQSQRGFEMDYQVQLAFDNINNPdlngygvDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKElaqkFQVPVVLE 552
Cdd:pfam02775 82 NGGYGMTRGQQTPFGGGRYSGPSGKILPPV-------DFAKLAEAYGAKGARVESPEELEEALKEALE----HDGPALID 150
|
.
gi 730604155 553 V 553
Cdd:pfam02775 151 V 151
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
11-473 |
3.09e-40 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 154.37 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 11 VEVLKKEGVDIAFGVPGAAINPLyAAMKKLGGIEHILARHVEGASHMA--DGYTRAKSGnigVCIGTSGPAGTDMITGLY 88
Cdd:PRK09259 17 IDALKLNGIDTIYGVVGIPITDL-ARLAQAEGIRYIGFRHEQSAGNAAaaAGFLTQKPG---VCLTVSAPGFLNGLTALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 89 AAIADSVPILCITGQAPRA--RLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLPFDV 166
Cdd:PRK09259 93 NATTNCFPMIMISGSSEREivDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 167 QMAEIEFD------VDTYEALPAYKPqaSRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMG 240
Cdd:PRK09259 173 LAQTMDADealtslVKVVDPAPAQLP--APEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSMA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 241 WGAIPDDHPLMAGMAglqtsqmygNATVLA-SDFVYGIGNR--WANRHtGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYG 317
Cdd:PRK09259 251 KGLLPDTHPQSAAAA---------RSLALAnADVVLLVGARlnWLLSH-GKGKTWGADKKFIQIDIEPQEIDSNRPIAAP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 318 IVSDAGAALKLMVEvarELRQAGKLPDyGEWAEQCRERKRT----MLRKTHYDNVPIK---PQRVYEEMLKSfGRDTVYV 390
Cdd:PRK09259 321 VVGDIGSVMQALLA---GLKQNTFKAP-AEWLDALAERKEKnaakMAEKLSTDTQPMNfynALGAIRDVLKE-NPDIYLV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 391 S----TIGLsqiaAAQFLHVYGPRQWINAGQAGPLGWTLPAALGvVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPY 466
Cdd:PRK09259 396 NeganTLDL----ARNIIDMYKPRHRLDCGTWGVMGIGMGYAIA-AAVETGKPVVAIEGDSAFGFSGMEVETICRYNLPV 470
|
....*..
gi 730604155 467 VHVLVNN 473
Cdd:PRK09259 471 TVVIFNN 477
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
11-554 |
6.85e-40 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 153.91 E-value: 6.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 11 VEVLKKEGVDIAFGVPGAAINPLYAAMKKLGG-IEHILARHVEGASHMADGYtrAK-SGNIGVCIGTSGPAGTDMITGLY 88
Cdd:PRK08273 10 LERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAH--AKfTGEVGVCLATSGPGAIHLLNGLY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 89 AAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPV-TKWAVTVREPALVPRVFQQAFHVMRSGRpGPVHIDLPFDVQ 167
Cdd:PRK08273 88 DAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTALAER-TVTAVILPNDVQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 168 MAEiefdvdtYEALP-------------AYKPQASRAQIEKSLELLFASERPLLVAGGGIinADASDDLVTFAELTGIPV 234
Cdd:PRK08273 167 ELE-------YEPPPhahgtvhsgvgytRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGA--LGATDEVIAVAERLGAGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 235 IPTLMGWGAIPDDHPLMAGMAGLQTSQ-----MYGNATVLAsdfvygignrwanrhTGSVEKYTE-----GR-KFVHIDI 303
Cdd:PRK08273 238 AKALLGKAALPDDLPWVTGSIGLLGTKpsyelMRECDTLLM---------------VGSSFPYSEflpkeGQaRGVQIDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 304 EPTQIGRVFGPDYGIVSDAGAALklmvevaRELRQAGKLPDYGEWAEQC----RERKRTMLRKTHYDNVPIKPQRVYEEM 379
Cdd:PRK08273 303 DGRMLGLRYPMEVNLVGDAAETL-------RALLPLLERKKDRSWRERIekwvARWWETLEARAMVPADPVNPQRVFWEL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 380 LKSFGRDTVYVSTIGLSQIAAAQFLHVygpRQWINAGQAGPL---GWTLPAALGVVAADRSKTVVALSGDYDFQfM--IE 454
Cdd:PRK08273 376 SPRLPDNAILTADSGSCANWYARDLRM---RRGMMASLSGTLatmGPAVPYAIAAKFAHPDRPVIALVGDGAMQ-MngMA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 455 ELAVGA----QFKLPYVHVLV-NNSYLGLIRQSQRGFEMDYQVqLAFDNInnPDlngygVDHVAVAEGLGCRAIRVTEPG 529
Cdd:PRK08273 452 ELITVAkywrQWSDPRLIVLVlNNRDLNQVTWEQRVMEGDPKF-EASQDL--PD-----VPYARFAELLGLKGIRVDDPE 523
|
570 580
....*....|....*....|....*
gi 730604155 530 KIKAGLEEAkeLAQkfQVPVVLEVI 554
Cdd:PRK08273 524 QLGAAWDEA--LAA--DRPVVLEVK 544
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
193-327 |
1.68e-39 |
|
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: 140.78 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 193 IEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGWGAIPDDHPLMAGMAGLQTSQmYGNATVLASD 272
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTP-AANEALEEAD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 730604155 273 FVYGIGNRWA-NRHTGSVEKYTEGRKFVHIDIEPTQIGRVFGPDYGIVSDAGAALK 327
Cdd:pfam00205 80 LVLAVGARFDdIRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLE 135
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
8-556 |
1.27e-38 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 149.34 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 8 EAAVEVLKKEGVDIAFGVPGAAINPLYAAMKklGGIEHILARHVEGASHMADGYTRAkSGNIGVcIGTSGPAGTDMITG- 86
Cdd:PRK07092 16 DATIDLLRRFGITTVFGNPGSTELPFLRDFP--DDFRYVLGLQEAVVVGMADGYAQA-TGNAAF-VNLHSAAGVGNAMGn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 87 LYAAIADSVPILCITGQAPRARLYKEDF-QAVDIESIAKPVTKWAVtvrEPAL---VPRVFQQAFHVMRSGRPGPVHIDL 162
Cdd:PRK07092 92 LFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSI---EPARaedVPAAIARAYHIAMQPPRGPVFVSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 163 PFDVQMAEIEfDVDTYEALPAYKPqaSRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPV-IPTLMGW 241
Cdd:PRK07092 169 PYDDWDQPAE-PLPARTVSSAVRP--DPAALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPVwVAPMSGR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 242 GAIPDDHPLMAGMagLQTSQMYGNATVLASDFVYGIGNRWANRHT-GSVEKYTEGRKFVHIDIEPTQIGRVFGPDyGIVS 320
Cdd:PRK07092 246 CSFPEDHPLFAGF--LPASREKISALLDGHDLVLVIGAPVFTYHVeGPGPHLPEGAELVQLTDDPGEAAWAPMGD-AIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 321 DAGAALKLMVEVARELRQAgklpdygewaeqcRERKRTMLRKTHYDNVPIKPQRVYEEMLKSFGRDTVYV----STIGLS 396
Cdd:PRK07092 323 DIRLALRDLLALLPPSARP-------------APPARPMPPPAPAPGEPLSVAFVLQTLAALRPADAIVVeeapSTRPAM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 397 QiaaaQFLHVYGPRQWINAGqAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYL 476
Cdd:PRK07092 390 Q----EHLPMRRQGSFYTMA-SGGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRY 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 477 GLIRQSQRGFEMDyqvqlafdniNNPDLNGYGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAkeLAQKfqVPVVLEVILE 556
Cdd:PRK07092 465 GALRWFAPVFGVR----------DVPGLDLPGLDFVALARGYGCEAVRVSDAAELADALARA--LAAD--GPVLVEVEVA 530
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
8-170 |
1.62e-37 |
|
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: 136.53 E-value: 1.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 8 EAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYtrAK-SGNIGVCIGTSGPAGTDMITG 86
Cdd:cd07039 4 DVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAE--AKlTGKLGVCLGSSGPGAIHLLNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 87 LYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAfhvMRS--GRPGPVHIDLPF 164
Cdd:cd07039 82 LYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRA---IRTaiAKRGVAVLILPG 158
|
....*.
gi 730604155 165 DVQMAE 170
Cdd:cd07039 159 DVQDAP 164
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
370-563 |
8.53e-36 |
|
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: 132.62 E-value: 8.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 370 IKPQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDF 449
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 450 QFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQSQRGFemdyqvqlaFDNINNPDLNGYGVDHVAVAEGLGCRAIRVTEPG 529
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELF---------YEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPE 151
|
170 180 190
....*....|....*....|....*....|....
gi 730604155 530 KIKAGLEEAKElaqkFQVPVVLEVILERVTNISM 563
Cdd:cd02015 152 ELEAALKEALA----SDGPVLLDVLVDPEENVLP 181
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
374-554 |
4.17e-35 |
|
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: 130.07 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 374 RVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMI 453
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 454 EELAVGAQFKLPYVHVLVNNSYLGLIRQSQRgfemdyqvqlAFDNINNPDLNGYGVDHVAVAEGLGCRAIRVTEPGKIKA 533
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQE----------AFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEA 150
|
170 180
....*....|....*....|.
gi 730604155 534 GLEEAKElaqkFQVPVVLEVI 554
Cdd:cd00568 151 ALAEALA----AGGPALIEVK 167
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
41-540 |
3.98e-32 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 443162 [Multi-domain] Cd Length: 622 Bit Score: 131.40 E-value: 3.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 41 GGIEHILARHVEGASHMADGYTRAKsgN---IGVCIGTSGPAGTDMITGLYAAIADSVPILCITGQ--APRA------RL 109
Cdd:COG3962 56 DELPTYQGRNEQGMAHAAIAYAKQK--NrrrIMACTSSIGPGATNMVTAAALATANRLPVLLLPGDtfATRQpdpvlqQL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 110 ykEDFQAVDIeSIA---KPVTKWAVTVREPALVPRVFQQAFHVMRSgrP---GPVHIDLPFDVQmAEiEFDVdtyealPA 183
Cdd:COG3962 134 --EHFHDPTI-SVNdafRPVSRYWDRITRPEQLMSALPRAMRVLTD--PaetGAVTLALPQDVQ-AE-AYDY------PE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 184 Y----------KPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVIPTLMGWGAIPDDHPLMAG 253
Cdd:COG3962 201 SffakrvhrirRPPPDPAELARAVELIRAAKRPLIIAGGGVRYSEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 254 MAGLqTSQMYGNATVLASDFVYGIGNRWANRHTGSVEKYT-EGRKFVHIDIEPTQIGRVFGpdYGIVSDAGAALKlmvev 332
Cdd:COG3962 281 GIGV-TGTLAANALAAEADLVIGVGTRLQDFTTGSKTLFAnPDVRFVNINVARFDAYKHDA--LPVVADAREGLE----- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 333 arELRQAgkLPDYG---EWAEQCRERKRTML----RKTHYDNVPIKPQ-RVYEEMLKSFG-RDTVyvstiglsqIAAAQF 403
Cdd:COG3962 353 --ALTEA--LAGWRypaAWTDEAAELKAEWDaevdRLYAPTNGGLPTQaQVIGAVNEAAGpDDIV---------VCAAGS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 404 LhvygP----RQWiNAGQAGP---------LGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVL 470
Cdd:COG3962 420 L----PgdlhKLW-RTRDPGTyhveygyscMGYEIAGGLGVKLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKIIVVL 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730604155 471 VNNSYLGLIRQSQRGFEMD-YQVQLAFDNINNPDLNG--YGVDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKE 540
Cdd:COG3962 495 LDNHGFGCINRLQMSTGSQsFGTELRDRDTETGRLDGglLPVDFAANAASLGAKAYRVTTIAELRAALERAKA 567
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
14-557 |
1.10e-29 |
|
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: 123.34 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 14 LKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAKSgnIGVCIGTSGPAGTDMITGLYAAIAD 93
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNG--LGALVTTYGVGELSAINGIAGAYAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 94 SVPILCITGqAP--RARLYKE---------DFQAvDIEsIAKPVTKWAVTVRE---PALVPRVFQQAFHVMRsgrpgPVH 159
Cdd:COG3961 93 RVPVVHIVG-APgtRAQRRGPllhhtlgdgDFDH-FLR-MFEEVTVAQAVLTPenaAAEIDRVLAAALREKR-----PVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 160 IDLPFDVQMAEIEfdvDTYEALPAYKPQASRAQ----IEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTGIPVI 235
Cdd:COG3961 165 IELPRDVADAPIE---PPEAPLPLPPPASDPAAlaaaVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 236 PTLMGWGAIPDDHPLMAGM-AGlQTSQMYGNATVLASDFVYGIGNRWANRHTGSVEKYTEGRKFVHIDIEPTQIG-RVFG 313
Cdd:COG3961 242 TTLLGKSVLDESHPQFIGTyAG-AASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVGgHIYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 314 PDYgiVSDAGAALklmveVARELRQAGKLPDYGEWAEQCRERkrtmlrkthyDNVPIKPQRVYEEMLKSFGRDTVYVSTI 393
Cdd:COG3961 321 GVS--LADFLEAL-----AELLKKRSAPLPAPAPPPPPPPAA----------PDAPLTQDRLWQRLQAFLDPGDIVVADT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 394 GLSQIAAAqFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNN 473
Cdd:COG3961 384 GTSLFGAA-DLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNN 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 474 S-YLglirqSQRGFEMDYQvqlAFDNINNpdlngygVDHVAVAEGLGC---RAIRVTEPGKIKAGLEEAKELAQKfqvPV 549
Cdd:COG3961 463 DgYT-----IERAIHGPDG---PYNDIAN-------WDYAKLPEAFGGgnaLGFRVTTEGELEEALAAAEANTDR---LT 524
|
....*...
gi 730604155 550 VLEVILER 557
Cdd:COG3961 525 LIEVVLDK 532
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
369-557 |
3.88e-26 |
|
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: 105.31 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 369 PIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYD 448
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 449 FQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQSQRGF-EMDYQVQLafdninnpdlngYGVDHVAVAEGLGCRAIRVTE 527
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMgQPEFGVDL------------PNPDFAKIAEAMGIKGIRVED 148
|
170 180 190
....*....|....*....|....*....|
gi 730604155 528 PGKIKAGLEEAKelaqKFQVPVVLEVILER 557
Cdd:cd02014 149 PDELEAALDEAL----AADGPVVIDVVTDP 174
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
9-164 |
4.91e-25 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 101.27 E-value: 4.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 9 AAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYtrAKSGNIGVCIGTSGPAGTDMITGLY 88
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGY--ARAGGPPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730604155 89 AAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGrPGPVHIDLPF 164
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
372-555 |
4.93e-21 |
|
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: 90.73 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 372 PQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLHVYGPRQWINAGqAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQF 451
Cdd:cd02002 3 PEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLR-GGGLGWGLPAAVGAALANPDRKVVAIIGDGSFMY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 452 MIEELAVGAQFKLP-YVHVLVNNSYLGLiRQSQRGFemdYQVQLAFDNINNPDLNGYGVDHVAVAEGLGCRAIRVTEPGK 530
Cdd:cd02002 82 TIQALWTAARYGLPvTVVILNNRGYGAL-RSFLKRV---GPEGPGENAPDGLDLLDPGIDFAAIAKAFGVEAERVETPEE 157
|
170 180
....*....|....*....|....*
gi 730604155 531 IKAGLEEAKElaqkFQVPVVLEVIL 555
Cdd:cd02002 158 LDEALREALA----EGGPALIEVVV 178
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
372-556 |
1.07e-20 |
|
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: 89.51 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 372 PQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYDFQF 451
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 452 MIEELAVGAQFKLPYVHVLVNNSYLGLIRQSQrgfemdyqvQLAFDNINNPDLNGYGVDHVAVAEGLGCRAIRVTEPGKI 531
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQ---------QLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEEL 151
|
170 180
....*....|....*....|....*
gi 730604155 532 KAGLEEAKELAQkfqvPVVLEVILE 556
Cdd:cd02004 152 KPALKRALASGK----PALINVIID 172
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
372-553 |
1.23e-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: 75.02 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 372 PQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLHVYGPRQ-WINAGQAgPLGWTLPAALGVVAADRSKTVVALSGDYDFQ 450
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTcLISNGLA-TMGVALPGAIGAKLVYPDRKVVAVSGDGGFM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 451 FMIEELAVGAQFKLPYVHVLVNNSYLGLIRQSQrgfEMDYQvQLAFDNINNPDLngygvdhVAVAEGLGCRAIRVTEPGK 530
Cdd:cd02010 80 MNSQELETAVRLKIPLVVLIWNDNGYGLIKWKQ---EKEYG-RDSGVDFGNPDF-------VKYAESFGAKGYRIESADD 148
|
170 180
....*....|....*....|...
gi 730604155 531 IKAGLEEAkeLAQKfqVPVVLEV 553
Cdd:cd02010 149 LLPVLERA--LAAD--GVHVIDC 167
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
369-557 |
6.89e-15 |
|
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: 73.31 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 369 PIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLHVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYD 448
Cdd:cd02013 3 PMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 449 FQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQSQRGFemdYQVQLAFDNINNPDLNGygvdhvaVAEGLGCRAIRVTEP 528
Cdd:cd02013 83 WGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDF---YNNRFVGTELESESFAK-------IAEACGAKGITVDKP 152
|
170 180
....*....|....*....|....*....
gi 730604155 529 GKIKAGLEEAKELAQKFQvPVVLEVILER 557
Cdd:cd02013 153 EDVGPALQKAIAMMAEGK-TTVIEIVCDQ 180
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
369-557 |
3.55e-12 |
|
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: 65.25 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 369 PIKPQRVYEEMLKSFGRDTVYVSTIGLSQIAAAQFLhVYGPRQWINAGQAGPLGWTLPAALGVVAADRSKTVVALSGDYD 448
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLK-LPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 449 FQFMIEELAVGAQFKLPYVHVLVNNsylglirqsqRGFEMDYQVQ---LAFDNINNpdlngygVDHVAVAEGLGC----R 521
Cdd:cd02005 80 FQMTVQELSTMIRYGLNPIIFLINN----------DGYTIERAIHgpeASYNDIAN-------WNYTKLPEVFGGggggL 142
|
170 180 190
....*....|....*....|....*....|....*.
gi 730604155 522 AIRVTEPGKIKAGLEEAKELAQKFQvpvVLEVILER 557
Cdd:cd02005 143 SFRVKTEGELDEALKDALFNRDKLS---LIEVILPK 175
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
11-164 |
8.77e-11 |
|
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: 60.59 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 11 VEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILarHVE--GASHMADGYTRAkSGNIGVCIGTSGPAGTDmitgLY 88
Cdd:cd07037 4 VEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHV--RVDerSAAFFALGLAKA-SGRPVAVVCTSGTAVAN----LL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 89 AAIA----DSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREP------ALVPRVFQQAFHVMRSGRPGPV 158
Cdd:cd07037 77 PAVVeayySGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPeddddlWYLLRLANRAVLEALSAPPGPV 156
|
....*.
gi 730604155 159 HIDLPF 164
Cdd:cd07037 157 HLNLPF 162
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
421-553 |
3.60e-09 |
|
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: 56.93 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 421 LGWTLPAALGVVAADRSKTVVALSGDYDFQFMIEELAVGAQFKLPYVHVLVNNSYLGLIRQSQ-----RGFEMDyqvqla 495
Cdd:cd02003 50 MGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQestgsGSFGTE------ 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730604155 496 FDNINNPDLNGYG----VDHVAVAEGLGCRAIRVTEPGKIKAGLEEAKELaqkfQVPVVLEV 553
Cdd:cd02003 124 FRDRDQESGQLDGallpVDFAANARSLGARVEKVKTIEELKAALAKAKAS----DRTTVIVI 181
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
14-163 |
3.87e-09 |
|
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: 55.96 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 14 LKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAKSgnIGVCIGTSGPAGTDMITGLYAAIAD 93
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG--LGALVTTYGVGELSALNGIAGAYAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 94 SVPILCITGQAPRAR----------LYKEDFQAvdIESIAKPVTKWAVTVREPALVPRVFQQAF-HVMRSGRpgPVHIDL 162
Cdd:cd07038 85 HVPVVHIVGAPSTKAqasglllhhtLGDGDFDV--FLKMFEEITCAAARLTDPENAAEEIDRVLrTALRESR--PVYIEI 160
|
.
gi 730604155 163 P 163
Cdd:cd07038 161 P 161
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
4-194 |
1.76e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 54.11 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 4 MRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAkSGNIGVCIGTSGPAGTDM 83
Cdd:PRK12474 5 MNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRI-AGKPAVTLLHLGPGLANG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 84 ITGLYAAIADSVPILCITGQAPRARLYKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMRSGRPGPVHIDLP 163
Cdd:PRK12474 84 LANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMP 163
|
170 180 190
....*....|....*....|....*....|.
gi 730604155 164 FDVQMAEiefdvDTYEALPAYKPQASRAQIE 194
Cdd:PRK12474 164 ADVAWNE-----AAYAAQPLRGIGPAPVAAE 189
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
4-538 |
2.11e-04 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 44.06 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 4 MRAIEAAVEVLKKEGVDIAFGVPGAAINPLYAAMKKLGGIEHILARHVEGASHMADGYTRAKsgnigvciGTsgPAGTDM 83
Cdd:PRK07586 1 MNGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMA--------GK--PAATLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 84 ITG---------LYAAIADSVPILCITGQAPRarlYKEDFQA---VDIESIAKPVTKWAVTVREPALVPRVFQQAFHVMR 151
Cdd:PRK07586 71 HLGpglanglanLHNARRARTPIVNIVGDHAT---YHRKYDApltSDIEALARPVSGWVRRSESAADVAADAAAAVAAAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 152 SGRPGPVHIDLPFDVQMAEIEFDVDTYEALPAykPQASRAQIEKSLELLFASERPLLVAGGGIINADASDDLVTFAELTG 231
Cdd:PRK07586 148 GAPGQVATLILPADVAWSEGGPPAPPPPAPAP--AAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAATG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 232 IPVI----PTLMGWGA---IPDDHPLMAGMAGLQ---TSQMygnatVLA------SDFVY-GIGNRWAnrhtgsvekyTE 294
Cdd:PRK07586 226 ARLLaetfPARMERGAgrpAVERLPYFAEQALAQlagVRHL-----VLVgakapvAFFAYpGKPSRLV----------PE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 295 GRKfVHIDIEPTQigrvfgpdygivsDAGAALKlmvEVARELrqaGKLPDYGEWAEQCRERKRTMlrkthydnvPIKPQR 374
Cdd:PRK07586 291 GCE-VHTLAGPGE-------------DAAAALE---ALADAL---GAKPAAPPLAAPARPPLPTG---------ALTPEA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 375 VYEEMLKSFGRDTVYVSTIGLSQIAAAQFLHVYGPRQWI-NAGqaGPLGWTLPAALG--VVAADRSktVVALSGDYDFQF 451
Cdd:PRK07586 342 IAQVIAALLPENAIVVDESITSGRGFFPATAGAAPHDWLtLTG--GAIGQGLPLATGaaVACPDRK--VLALQGDGSAMY 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730604155 452 MIEELAVGAQFKLPYVHVLVNNSYLGLIRQSQRGFEMDYQVQLAFD--NINNPDLngygvDHVAVAEGLGCRAIRVTEPG 529
Cdd:PRK07586 418 TIQALWTQARENLDVTTVIFANRAYAILRGELARVGAGNPGPRALDmlDLDDPDL-----DWVALAEGMGVPARRVTTAE 492
|
....*....
gi 730604155 530 KIKAGLEEA 538
Cdd:PRK07586 493 EFADALAAA 501
|
|
| |
