|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
10-583 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 1219.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 10 VEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGAT 89
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 90 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 169
Cdd:PRK07979 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 170 LPKDILNPAKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSS 249
Cdd:PRK07979 161 LPKDILNPANKLPYVWPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 250 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPV 329
Cdd:PRK07979 241 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 330 VGDARLVLEQMLELLAQDAPSQPQDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQM 409
Cdd:PRK07979 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 410 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 489
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 490 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEHVRNNRLVFVDVTVDGSEHVYPMQIRG 569
Cdd:PRK07979 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRG 560
|
570
....*....|....
gi 1334564377 570 GGMDEMWLSKTERT 583
Cdd:PRK07979 561 GGMDEMWLSKTERT 574
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
10-583 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 1090.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 10 VEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGAT 89
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 90 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 169
Cdd:PRK08979 81 NTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 170 LPKDILNPAKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSS 249
Cdd:PRK08979 161 LPKDCLNPAILHPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 250 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPV 329
Cdd:PRK08979 241 LMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 330 VGDARLVLEQMLELLAQDAPSQPQDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQM 409
Cdd:PRK08979 321 VGSADKVLDSMLALLDESGETNDEAAIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 410 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 489
Cdd:PRK08979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 490 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEhvRNNRLVFVDVTVDGSEHVYPMQIRG 569
Cdd:PRK08979 481 VKQWQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALA--MKDRLVFVDINVDETEHVYPMQIRG 558
|
570
....*....|....
gi 1334564377 570 GGMDEMWLSKTERT 583
Cdd:PRK08979 559 GAMNEMWLSKTERT 572
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
13-579 |
0e+00 |
|
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: 1003.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 13 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAI 92
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 93 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 172
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 173 DILNPAKKMPYawPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMG 252
Cdd:TIGR00118 161 DVTTAEIEYPY--PEKVNLPGYRPTVKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 253 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVVGD 332
Cdd:TIGR00118 239 LGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 333 ARLVLEQMLELLAqdaPSQPQDDIrDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAA 412
Cdd:TIGR00118 319 ARNVLEELLKKLF---ELKERKES-AWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 413 LYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQ 492
Cdd:TIGR00118 395 QFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 493 WQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVDGSEHVYPMQIRGGGM 572
Cdd:TIGR00118 475 WQELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSS---NEPVLLDVVVDKPENVLPMVAPGGGL 551
|
....*..
gi 1334564377 573 DEMWLSK 579
Cdd:TIGR00118 552 DEMIGEK 558
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
13-583 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 989.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 13 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAI 92
Cdd:PRK06882 4 LSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 93 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 172
Cdd:PRK06882 84 TGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 173 DILNPAKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMG 252
Cdd:PRK06882 164 DMVNPANKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 253 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVVGD 332
Cdd:PRK06882 244 LGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPIVGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 333 ARLVLEQMLELLAQDAPSQPQDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAA 412
Cdd:PRK06882 324 AKNVLEEFLSLLEEENLAKSQTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQMFAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 413 LYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQ 492
Cdd:PRK06882 404 LHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGMVKQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 493 WQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEhvRNNRLVFVDVTVDGSEHVYPMQIRGGGM 572
Cdd:PRK06882 484 WQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFS--IKDKLVFVDVNVDETEHVYPMQIRGGAM 561
|
570
....*....|.
gi 1334564377 573 DEMWLSKTERT 583
Cdd:PRK06882 562 NEMILSKPEET 572
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
10-583 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 983.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 10 VEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGAT 89
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 90 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 169
Cdd:PRK06466 81 NAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 170 LPKDILNPAKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSS 249
Cdd:PRK06466 161 IPKDMTNPAEKFEYEYPKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 250 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPV 329
Cdd:PRK06466 241 LMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 330 VGDARLVLEQMLELLAQDAPSQPQDDIRDWWQQIEIWRARQCL-KYDAESES-IKPQAVIETLWRLTKGDAYVTSDVGQH 407
Cdd:PRK06466 321 VGPVESVLTEMLAILKEIGEKPDKEALAAWWKQIDEWRGRHGLfPYDKGDGGiIKPQQVVETLYEVTNGDAYVTSDVGQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 408 QMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYL 487
Cdd:PRK06466 401 QMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 488 GMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEhvRNNRLVFVDVTVDGSEHVYPMQI 567
Cdd:PRK06466 481 GMVRQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFA--MKDRLVFIDIYVDRSEHVYPMQI 558
|
570
....*....|....*.
gi 1334564377 568 RGGGMDEMWLSKTERT 583
Cdd:PRK06466 559 ADGSMRDMWLSKTERT 574
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
13-577 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 820.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 13 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAI 92
Cdd:PRK06965 21 SIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 93 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 172
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 173 DIlnPAKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMG 252
Cdd:PRK06965 181 DV--SKTPCEYEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 253 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNA-TVLHIDIDPTSISKTVNADIPVVG 331
Cdd:PRK06965 259 LGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRVKVDIPIVG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 332 DARLVLEQMLELLAQDAPSQPQDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMFA 411
Cdd:PRK06965 339 DVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMWA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 412 ALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVK 491
Cdd:PRK06965 419 AQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMVR 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 492 QWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEhvRNNRLVFVDVTVDGSEHVYPMQIRGGG 571
Cdd:PRK06965 499 QWQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALR--LKDRTVFLDFQTDPTENVWPMVQAGKG 576
|
....*.
gi 1334564377 572 MDEMWL 577
Cdd:PRK06965 577 ITEMLL 582
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
11-575 |
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: 772.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 11 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATN 90
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 91 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 170
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 171 PKDILnpAKKMPYAwPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSL 250
Cdd:COG0028 161 PKDVQ--AAEAEEE-PAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 251 MGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVV 330
Cdd:COG0028 238 MGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 331 GDARLVLEQMLELLAQDApsqpqDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 410
Cdd:COG0028 318 GDAKAVLAALLEALEPRA-----DDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 411 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMV 490
Cdd:COG0028 393 AARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 491 KQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVDGSEHvypmqIRGG 570
Cdd:COG0028 473 RQWQELFYGGRYSGTDLPN-PDFAKLAEAFGAKGERVETPEELEAALEEALAS---DGPALIDVRVDPEEN-----PPGA 543
|
....*
gi 1334564377 571 GMDEM 575
Cdd:COG0028 544 TLDEM 548
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
13-577 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 771.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 13 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAI 92
Cdd:PRK09107 11 MTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 93 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 172
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 173 DIlNPAKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAP--LRHIIEIFNLPVVSSL 250
Cdd:PRK09107 171 DV-QFATGTYTPPQKAPVHVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVINSGPEASrlLRELVELTGFPITSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 251 MGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVV 330
Cdd:PRK09107 250 MGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPII 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 331 GDARLVLEQMLELLAQDAPSQPQDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKG-DAYVTSDVGQHQM 409
Cdd:PRK09107 330 GDVGHVLEDMLRLWKARGKKPDKEALADWWGQIARWRARNSLAYTPSDDVIMPQYAIQRLYELTKGrDTYITTEVGQHQM 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 410 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 489
Cdd:PRK09107 410 WAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMGM 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 490 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVDGSEHVYPMQIRG 569
Cdd:PRK09107 490 VRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDV---DKPVIFDCRVANLENCFPMIPSG 566
|
....*...
gi 1334564377 570 GGMDEMWL 577
Cdd:PRK09107 567 KAHNEMLL 574
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
13-582 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 743.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 13 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAI 92
Cdd:PRK08527 3 LSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 93 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 172
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 173 DIlnPAKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMG 252
Cdd:PRK08527 163 DV--TATLGEFEYPKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 253 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVVGD 332
Cdd:PRK08527 241 RGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 333 ARLVLEQMLELLAQDAPSqpqdDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAA 412
Cdd:PRK08527 321 LKNVLKEMLEELKEENPT----TYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 413 LYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQ 492
Cdd:PRK08527 397 QFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 493 WQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEhvrNNRLVFVDVTVDGSEHVYPMQIRGGGM 572
Cdd:PRK08527 477 WQTFFYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALE---SDKVALIDVKIDRFENVLPMVPAGGAL 553
|
570
....*....|
gi 1334564377 573 DEMWLSKTER 582
Cdd:PRK08527 554 YNMILPKKKD 563
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
11-575 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 669.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 11 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATN 90
Cdd:PRK06048 6 EKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 91 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 170
Cdd:PRK06048 85 LVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 171 PKDILNpaKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSL 250
Cdd:PRK06048 165 PKDVTT--AEIDFDYPDKVELRGYKPTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 251 MGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVV 330
Cdd:PRK06048 243 MGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPIV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 331 GDARLVLEQMLELLAqdapsqpQDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKgDAYVTSDVGQHQMF 410
Cdd:PRK06048 323 GDAKQVLKSLIKYVQ-------YCDRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQMW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 411 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMV 490
Cdd:PRK06048 395 AAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 491 KQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEhvrNNRLVFVDVTVDGSEHVYPMQIRGG 570
Cdd:PRK06048 475 RQWQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVA---SDRPVVIDFIVECEENVSPMVPAGA 551
|
....*
gi 1334564377 571 GMDEM 575
Cdd:PRK06048 552 AINEI 556
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
8-565 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 668.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 8 QAVEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTV---GGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTS 84
Cdd:PRK07418 14 VTPQRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAeaeGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 85 GPGATNAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPG 164
Cdd:PRK07418 94 GPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 165 PVVVDLPKDI-LNPAKKMPYAwPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFN 243
Cdd:PRK07418 174 PVLIDIPKDVgQEEFDYVPVE-PGSVKPPGYRPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 244 LPVVSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTV 323
Cdd:PRK07418 253 IPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 324 NADIPVVGDARLVLEQMLElLAQDAPSQPQDdiRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKgDAYVTSD 403
Cdd:PRK07418 333 RPDVPIVGDVRKVLVKLLE-RSLEPTTPPRT--QAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAP-DAYYTTD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 404 VGQHQMFAALYYPfDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLN 483
Cdd:PRK07418 409 VGQHQMWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIIN 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 484 NRYLGMVKQWQDMIYSGRHSQSYMQ-SLPDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVDGSEHV 562
Cdd:PRK07418 488 NGWQGMVRQWQESFYGERYSASNMEpGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAH---DGPVLIDVHVRRDENC 564
|
...
gi 1334564377 563 YPM 565
Cdd:PRK07418 565 YPM 567
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
7-574 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 662.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 7 RQAVEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGP 86
Cdd:PRK07789 25 IVAPERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 87 GATNAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPV 166
Cdd:PRK07789 105 GATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 167 VVDLPKDILNpaKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPV 246
Cdd:PRK07789 185 LVDIPKDALQ--AQTTFSWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 247 VSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNAD 326
Cdd:PRK07789 263 VTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHAD 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 327 IPVVGDARLVLEQMLELLAQDAPSQPQDDIRDWWQQIEIWRARQCLKYDAESE-SIKPQAVIETLWRLTKGDAYVTSDVG 405
Cdd:PRK07789 343 VPIVGDVKEVIAELIAALRAEHAAGGKPDLTAWWAYLDGWRETYPLGYDEPSDgSLAPQYVIERLGEIAGPDAIYVAGVG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 406 QHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNR 485
Cdd:PRK07789 423 QHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNG 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 486 YLGMVKQWQDMIYSGRHSQSYMQS----LPDFVRLAEAYGHVGLQINRPDELESKLSEALEhvRNNRLVFVDVTVDGSEH 561
Cdd:PRK07789 503 NLGMVRQWQTLFYEERYSNTDLHThshrIPDFVKLAEAYGCVGLRCEREEDVDAVIEKARA--INDRPVVIDFVVGKDAM 580
|
570
....*....|...
gi 1334564377 562 VYPMQIRGGGMDE 574
Cdd:PRK07789 581 VWPMVAAGTSNDE 593
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
13-575 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 641.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 13 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAI 92
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 93 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 172
Cdd:PRK06276 80 TGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 173 DILNPAKKMP-YAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLM 251
Cdd:PRK06276 160 DVQEGELDLEkYPIPAKIDLPGYKPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 252 GLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVVG 331
Cdd:PRK06276 240 GKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 332 DARLVLEQMLELLAQDAPsqpqDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKG-----DAYVTSDVGQ 406
Cdd:PRK06276 320 DAKNVLRDLLAELMKKEI----KNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDVGQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 407 HQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRY 486
Cdd:PRK06276 396 NQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 487 LGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALehvRNNRLVFVDVTVDGSEhVYPMQ 566
Cdd:PRK06276 476 LGMVYQWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAI---KSGEPYLLDIIIDPAE-ALPMV 551
|
....*....
gi 1334564377 567 IRGGGMDEM 575
Cdd:PRK06276 552 PPGGNLTNI 560
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
11-575 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 633.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 11 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATN 90
Cdd:PRK07710 14 KLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 91 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 170
Cdd:PRK07710 93 VVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 171 PKDILnpAKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSL 250
Cdd:PRK07710 173 PKDMV--VEEGEFCYDVQMDLPGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 251 MGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVV 330
Cdd:PRK07710 251 LGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 331 GDARLVLEQMLEllaqdaPSQPQDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 410
Cdd:PRK07710 331 ADAKQALQVLLQ------QEGKKENHHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 411 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMV 490
Cdd:PRK07710 405 AAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 491 KQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEhvrNNRLVFVDVTVDGSEHVYPMQIRGG 570
Cdd:PRK07710 485 RQWQEEFYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIE---LQEPVVIDCRVLQSEKVMPMVAPGK 561
|
....*
gi 1334564377 571 GMDEM 575
Cdd:PRK07710 562 GLHEM 566
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
11-581 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 627.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 11 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATN 90
Cdd:PRK06725 13 EEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 91 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 170
Cdd:PRK06725 92 LVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 171 PKDILNpaKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSL 250
Cdd:PRK06725 172 PKDVQN--EKVTSFYNEVVEIPGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 251 MGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVV 330
Cdd:PRK06725 250 MGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 331 GDARLVLEQMLELlaqdaPSQPQDDirDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 410
Cdd:PRK06725 330 GDVKKALHMLLHM-----SIHTQTD--EWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMW 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 411 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMV 490
Cdd:PRK06725 403 AAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 491 KQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVDGSEHVYPMQIRGG 570
Cdd:PRK06725 483 RQWQEMFYENRLSESKIGS-PDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAH---EGPVVVDFCVEEGENVFPMVPPNK 558
|
570
....*....|.
gi 1334564377 571 GMDEMWLSKTE 581
Cdd:PRK06725 559 GNNEMIMKRWE 569
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
14-565 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 616.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 14 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHT---VGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATN 90
Cdd:CHL00099 11 TGAFALIDSLVRHGVKHIFGYPGGAILPIYDELYAwekKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 91 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 170
Cdd:CHL00099 91 LVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 171 PKDIlnPAKKMPYAWPE----TVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPV 246
Cdd:CHL00099 171 PKDV--GLEKFDYYPPEpgntIIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 247 VSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNAD 326
Cdd:CHL00099 249 TTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 327 IPVVGDARLVLEQMLELLAQDAPSQPQDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLtKGDAYVTSDVGQ 406
Cdd:CHL00099 329 VAIVGDVKKVLQELLELLKNSPNLLESEQTQAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQL-APDAYFTTDVGQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 407 HQMFAALYYPFdKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRY 486
Cdd:CHL00099 408 HQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKW 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 487 LGMVKQWQDMIYSGRHSQSYMQS-LPDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVDGSEHVYPM 565
Cdd:CHL00099 487 QGMVRQWQQAFYGERYSHSNMEEgAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDY---DGPVLIDCQVIEDENCYPM 563
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
14-575 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 604.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 14 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAIT 93
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 94 GIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKD 173
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 174 IlnPAKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMGL 253
Cdd:PRK07282 171 V--SALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 254 GAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVVGDA 333
Cdd:PRK07282 249 GTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 334 RLVLEQMLELlaqdapSQPQDDIRDWWQQIEIWRARqCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAAL 413
Cdd:PRK07282 329 KKALQMLLAE------PTVHNNTEKWIEKVTKDKNR-VRSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 414 YYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQW 493
Cdd:PRK07282 402 YYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 494 QDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELEsklsEALEHVRNNRLVFVDVTVDGSEHVYPMQIRGGGMD 573
Cdd:PRK07282 482 QESFYEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLA----QDLEVITEDVPMLIEVDISRKEHVLPMVPAGKSNH 557
|
..
gi 1334564377 574 EM 575
Cdd:PRK07282 558 EM 559
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
15-575 |
0e+00 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 600.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 15 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITG 94
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 95 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 174
Cdd:PRK08978 82 LADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 175 -LNPAKKMPYAWPETvsmrsynPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMGL 253
Cdd:PRK08978 162 qLAEGELEPHLTTVE-------NEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 254 GAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVVGDa 333
Cdd:PRK08978 235 GAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGD- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 334 rlvLEQMLELLAQDApsqpqdDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAAL 413
Cdd:PRK08978 314 ---LNALLPALQQPL------NIDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 414 YYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQW 493
Cdd:PRK08978 385 HMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 494 QDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVDGSEHVYPMQIRGGGMD 573
Cdd:PRK08978 465 QQLFFDERYSETDLSDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNS---EGPYLLHVSIDELENVWPLVPPGASNS 541
|
..
gi 1334564377 574 EM 575
Cdd:PRK08978 542 EM 543
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
15-571 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 542.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 15 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITG 94
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 95 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 174
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 175 lNPAKKMPYaWPETVSMRSY-----NPTTSGHKGQIKRALQtlaSAKKPVVYVGGGAISAAcyAPLRHIIEIFNLPVVSS 249
Cdd:PLN02470 175 -QQQLAVPN-WNQPMKLPGYlsrlpKPPEKSQLEQIVRLIS---ESKRPVVYVGGGCLNSS--EELREFVELTGIPVAST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 250 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPV 329
Cdd:PLN02470 248 LMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 330 VGDARLVLEQMLELLAQDAPSQPqdDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQM 409
Cdd:PLN02470 328 CADVKLALQGLNKLLEERKAKRP--DFSAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVGQHQM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 410 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 489
Cdd:PLN02470 406 WAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGM 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 490 VKQWQDMIYSGRHSQSYMQS-------LPDFVRLAEAYGHVGLQINRPDELESKLSEALEHVRNNRLvfvDVTVDGSEHV 562
Cdd:PLN02470 486 VVQWEDRFYKANRAHTYLGDpdaeaeiFPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLL---DVIVPHQEHV 562
|
....*....
gi 1334564377 563 YPMqIRGGG 571
Cdd:PLN02470 563 LPM-IPGGG 570
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-575 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 538.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 1 MTGIKWRQAVEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVV 80
Cdd:PRK08155 1 MASSGTTSTRKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 81 LVTSGPGATNAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAAS 160
Cdd:PRK08155 81 MACSGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 161 GRPGPVVVDLPKDILNPAKKMPyAWPEtVSMRSYNPTTSGHkgQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIE 240
Cdd:PRK08155 161 GRPGPVWIDIPKDVQTAVIELE-ALPA-PAEKDAAPAFDEE--SIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 241 IFNLPVVSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSIS 320
Cdd:PRK08155 237 KAQLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 321 KTVNADIPVVGDARLVLEQMLELLAqdapSQPQDdirDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYV 400
Cdd:PRK08155 317 KIKQPHVAIQADVDDVLAQLLPLVE----AQPRA---EWHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAII 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 401 TSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVL 480
Cdd:PRK08155 390 TTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKII 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 481 NLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALehvrnNRL--VFVDVTVDG 558
Cdd:PRK08155 470 LMNNEALGLVHQQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAI-----NRPgpALIHVRIDA 544
|
570
....*....|....*..
gi 1334564377 559 SEHVYPMQIRGGGMDEM 575
Cdd:PRK08155 545 EEKVYPMVPPGAANTEM 561
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
12-578 |
2.29e-141 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 421.55 E-value: 2.29e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 12 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDAL---HTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGA 88
Cdd:PRK06456 1 MPTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 89 TNAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 168
Cdd:PRK06456 81 TNLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 169 DLPKDILNpAKKMPYAWPETVSMRSYNP-TTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVV 247
Cdd:PRK06456 161 DIPRDIFY-EKMEEIKWPEKPLVKGYRDfPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 248 SSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPN-ATVLHIDIDPTSISKTVNAD 326
Cdd:PRK06456 240 STFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVNIDPTDGEKAIKVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 327 IPVVGDARLVLEQMLELLAQDApsqPQDDIRDWWQQIEIWRA-RQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVG 405
Cdd:PRK06456 320 VGIYGNAKIILRELIKAITELG---QKRDRSAWLKRVKEYKEyYSQFYYTEENGKLKPWKIMKTIRQALPRDAIVTTGVG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 406 QHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNR 485
Cdd:PRK06456 397 QHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 486 YLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEAlehVRNNRLVFVDVTVDGSEHVYPM 565
Cdd:PRK06456 477 TLGLVRQVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSA---IKEDIPAVIRVPVDKEELALPT 553
|
570
....*....|...
gi 1334564377 566 QIRGGGMDEMWLS 578
Cdd:PRK06456 554 LPPGGRLKQVILR 566
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
16-540 |
6.08e-125 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 380.09 E-value: 6.08e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 16 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARAT-GDVGVVLVTSGPGATNAITG 94
Cdd:PRK11269 7 VDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 95 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 174
Cdd:PRK11269 87 LYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 175 lnpaKKMPYAW-PETVS-MRSYNPTTsgHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMG 252
Cdd:PRK11269 167 ----QVAEIEFdPDTYEpLPVYKPAA--TRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 253 LGAFPATHRQSLGMLGMHGTYE-ANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVVG 331
Cdd:PRK11269 241 WGAIPDDHPLMAGMVGLQTSHRyGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 332 DARLVLEQMLELLAQDAPSQPQDDIRDWWQQIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMFA 411
Cdd:PRK11269 321 DAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTIGLSQIAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 412 ALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELP-VLVLnLNNRYLGMV 490
Cdd:PRK11269 401 AQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPyIHVL-VNNAYLGLI 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1334564377 491 KQWQ---DMIY------SGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEA 540
Cdd:PRK11269 480 RQAQrafDMDYcvqlafENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALEQA 538
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
15-560 |
2.83e-110 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 340.65 E-value: 2.83e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 15 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITG 94
Cdd:PRK08322 3 AADLFVKCLENEGVEYIFGIPGEENLDLLEALRD-SSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 95 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 174
Cdd:PRK08322 82 VAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 175 lnpaKKMPYawPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMGLG 254
Cdd:PRK08322 162 ----AAEET--DGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 255 AFPATHRQSLGMLGMH-GTYEaNMTMHNADVIFAVG---VRFDDRTTNnlakycPNA--TVLHIDIDPTSISKTVNADIP 328
Cdd:PRK08322 236 VIPETHPLSLGTAGLSqGDYV-HCAIEHADLIINVGhdvIEKPPFFMN------PNGdkKVIHINFLPAEVDPVYFPQVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 329 VVGDARLVLEQMLELLAqDAPSQPQDDIRDWWQQIeiwRARqcLKYDAESES--IKPQAVIETLWRLTKGDAYVTSDVGQ 406
Cdd:PRK08322 309 VVGDIANSLWQLKERLA-DQPHWDFPRFLKIREAI---EAH--LEEGADDDRfpMKPQRIVADLRKVMPDDDIVILDNGA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 407 HQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRY 486
Cdd:PRK08322 383 YKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNA 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1334564377 487 LGMVKqWQDMIYSGRHsqSYMQ-SLPDFVRLAEAYGHVGLQINRPDELESKLSEALE----HVrnnrlvfVDVTVDGSE 560
Cdd:PRK08322 463 YGMIR-WKQENMGFED--FGLDfGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAqpgvHV-------IDCPVDYSE 531
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
8-543 |
3.36e-107 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 333.00 E-value: 3.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 8 QAVEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPG 87
Cdd:PRK08199 3 STPRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 88 ATNAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVV 167
Cdd:PRK08199 83 ATNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 168 VDLPKDIL----NPAKKMPYAWPEtvsmrsynptTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFN 243
Cdd:PRK08199 163 LALPEDVLsetaEVPDAPPYRRVA----------AAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 244 LPVVSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNN---LAKYCPNATVLHIDIDPTSIS 320
Cdd:PRK08199 233 LPVACAFRRQDLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 321 KTVNADIPVVGDARLVLEQMLELlaqDAPSQPQddirdwWQQieiWRARQCLKYDAESESI-KPQA-----VIETLWRLT 394
Cdd:PRK08199 313 RVYRPDLAIVADPAAFAAALAAL---EPPASPA------WAE---WTAAAHADYLAWSAPLpGPGAvqlgeVMAWLRERL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 395 KGDAYVTSDVGQHQMFAALYYPFDKPRRWI--NSgglGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQ 472
Cdd:PRK08199 381 PADAIITNGAGNYATWLHRFFRFRRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQ 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334564377 473 YELPVLVLNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGLQINRPDELESKLSEALEH 543
Cdd:PRK08199 458 YGLPIIVIVVNNGMYGTIRMHQEREYPGRVSGTDLTN-PDFAALARAYGGHGETVERTEDFAPAFERALAS 527
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
381-565 |
1.87e-106 |
|
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: 317.52 E-value: 1.87e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 381 IKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSI 460
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 461 QMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEA 540
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|....*
gi 1334564377 541 LEHvrnNRLVFVDVTVDGSEHVYPM 565
Cdd:cd02015 161 LAS---DGPVLLDVLVDPEENVLPM 182
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
13-560 |
8.50e-102 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 318.49 E-value: 8.50e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 13 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLV-RHEQAAVHMADGLARATGDVGVVLVTSGPGATNA 91
Cdd:PRK08266 4 MTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHtRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 92 ITGIATAYMDSIPLVILSGQVATSLI--GYDAFQEC-DMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 168
Cdd:PRK08266 84 GAALLTAYGCNSPVLCLTGQIPSALIgkGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 169 DLPKDILnpAKKMPYAwPETVSMRSYNPttSGHKGQIKRALQTLASAKKPVVYVGGGAISAAcyAPLRHIIEIFNLPVVS 248
Cdd:PRK08266 164 EMPWDVF--GQRAPVA-AAPPLRPAPPP--APDPDAIAAAAALIAAAKNPMIFVGGGAAGAG--EEIRELAEMLQAPVVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 249 SLMGLGAFPATHRQSLGMLGmhgtyeANMTMHNADVIFAVGVRFDDRTTNnlAKYCP-NATVLHIDIDPTSISKTvNADI 327
Cdd:PRK08266 237 FRSGRGIVSDRHPLGLNFAA------AYELWPQTDVVIGIGSRLELPTFR--WPWRPdGLKVIRIDIDPTEMRRL-KPDV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 328 PVVGDARLVLEQMLELLAQDAPSQP--QDDIRD---WWQQieiwrarqclkydaESESIKPQ-----AVIETLWRltkgD 397
Cdd:PRK08266 308 AIVADAKAGTAALLDALSKAGSKRPsrRAELRElkaAARQ--------------RIQAVQPQasylrAIREALPD----D 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 398 AYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPV 477
Cdd:PRK08266 370 GIFVDELSQVGFASWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 478 LVLNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTV- 556
Cdd:PRK08266 450 VTVVFNNNAYGNVRRDQKRRFGGRVVASDLVN-PDFVKLAESFGVAAFRVDSPEELRAALEAALAH---GGPVLIEVPVp 525
|
....
gi 1334564377 557 DGSE 560
Cdd:PRK08266 526 RGSE 529
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
16-558 |
9.79e-96 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 304.09 E-value: 9.79e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 16 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDaLHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITGI 95
Cdd:TIGR03457 5 SEAFVEVLVANGVTHAFGIMGSAFMDAMD-LFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 96 ATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKDIL 175
Cdd:TIGR03457 84 AAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRDYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 176 npAKKMPYAWPETVSMRSynptTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMGLGA 255
Cdd:TIGR03457 163 --YGEIDVEIPRPVRLDR----GAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 256 FPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTT--NNLAKYCP-NATVLHIDIDPTSISKTVNADIPVVGD 332
Cdd:TIGR03457 237 FPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLGPFGTlpQYGIDYWPkNAKIIQVDANAKMIGLVKKVTVGICGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 333 ARLVLEQMLELLAQDA--------PSQPQDDIRDWWQQIEIW---RARQCLKYDAESES-----IKPQAVIETLWRLTKG 396
Cdd:TIGR03457 317 AKAAAAEILQRLAGKAgdanraerKAKIQAERSAWEQELSEMtheRDPFSLDMIVEQRQeegnwLHPRQVLRELEKAMPE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 397 DAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELP 476
Cdd:TIGR03457 397 DAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 477 VLVLNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEHVRNNRLVFVDVTV 556
Cdd:TIGR03457 477 VTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQAEGKTTVIEIVC 556
|
..
gi 1334564377 557 DG 558
Cdd:TIGR03457 557 TR 558
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
15-570 |
2.66e-93 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 297.30 E-value: 2.66e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 15 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTV-GGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAIT 93
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 94 GIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKD 173
Cdd:PRK08611 86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVLTIPDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 174 IlnPAKKMPYAWPETVSMRSYNPTTSgHKGQIKRALQTLASAKKPVVYVGGGAISAAcyAPLRHIIEIFNLPVVSSLMGL 253
Cdd:PRK08611 165 L--PAQKIKDTTNKTVDTFRPTVPSP-KPKDIKKAAKLINKAKKPVILAGLGAKHAK--EELLAFAEKAKIPIIHTLPAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 254 GAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRttnnlaKYCPN-ATVLHIDIDPTSISKTVNADIPVVGD 332
Cdd:PRK08611 240 GIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPKkAKAIQIDTDPANIGKRYPVNVGLVGD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 333 ARLVLEQMLELLA--QDAP--SQPQDDIRDWWQQIEIWRARqclkydaESESIKPQAVIETLWRLTKGDAYVTSDVGQHQ 408
Cdd:PRK08611 314 AKKALHQLTENIKhvEDRRflEACQENMAKWWKWMEEDENN-------ASTPIKPERVMAAIQKIADDDAVLSVDVGTVT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 409 MFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLG 488
Cdd:PRK08611 387 VWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 489 MVKQWQdmiysgrhsQS-----YMQSL--PDFVRLAEAYGHVGLQINRPDELESKLSEALehvRNNRLVFVDVTVDGSEH 561
Cdd:PRK08611 467 FIKYEQ---------QAageleYAIDLsdMDYAKFAEACGGKGYRVEKAEELDPAFEEAL---AQDKPVIIDVYVDPNAA 534
|
....*....
gi 1334564377 562 VYPMQIRGG 570
Cdd:PRK08611 535 PLPGKIVND 543
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
12-562 |
1.65e-90 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 288.80 E-value: 1.65e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 12 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNA 91
Cdd:PRK07524 1 MTTCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAG-SGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 92 ITGIATAYMDSIP-LVILSGQVATSL-IGYDAFQEC-DMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 168
Cdd:PRK07524 80 ATAMGQAYADSIPmLVISSVNRRASLgKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 169 DLPKDILnpAKKMPYAWPETVSmRSYNPTTsgHKGQIKRALQTLASAKKPVVYVGGGAISAAcyAPLRHIIEIFNLPVVS 248
Cdd:PRK07524 160 EIPLDVL--AAPADHLLPAPPT-RPARPGP--APAALAQAAERLAAARRPLILAGGGALAAA--AALRALAERLDAPVAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 249 SLMGLGAFPATHRQSLGmlgmhgtyeANMT-------MHNADVIFAVG---------VRFDDRttnnlakYCPNATVLHI 312
Cdd:PRK07524 233 TINAKGLLPAGHPLLLG---------ASQSlpavralIAEADVVLAVGtelgetdydVYFDGG-------FPLPGELIRI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 313 DIDPTSISKTVNADIPVVGDARLVLEQMLELLAQDAPSQPqddirdwWQQIEIWRARQCLKYDAESESIKPQAVIETLwR 392
Cdd:PRK07524 297 DIDPDQLARNYPPALALVGDARAALEALLARLPGQAAAAD-------WGAARVAALRQALRAEWDPLTAAQVALLDTI-L 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 393 LTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSG-GLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTAL 471
Cdd:PRK07524 369 AALPDAIFVGDSTQPVYAGNLYFDADAPRRWFNAStGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 472 QYELPVLVLNLNNRYLGMVKqwqdmiysgrhsqSYMQSL-----------PDFVRLAEAYGHVGLQINRPDELESKLSEA 540
Cdd:PRK07524 449 EADLPLIVLLWNNDGYGEIR-------------RYMVARdiepvgvdpytPDFIALARAFGCAAERVADLEQLQAALRAA 515
|
570 580
....*....|....*....|..
gi 1334564377 541 LEHvrnNRLVFVDVTVDGSEHV 562
Cdd:PRK07524 516 FAR---PGPTLIEVDQACWFAA 534
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
15-566 |
3.24e-90 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 288.19 E-value: 3.24e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 15 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITG 94
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALED-KGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 95 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 174
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 175 LNpakkmpyawpETVSMRSYNPTTSGHKG-----QIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSS 249
Cdd:TIGR02418 160 VD----------SPVSVKAIPASYAPKLGaapddAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 250 LMGLGAFPAT-HRQSLGMLGMHGTYEANMTMHNADVIFAVG---VRFDDRTTNNLAkycpNATVLHIDIDPTSISKTVNA 325
Cdd:TIGR02418 230 FQGAGAVSRElEDHFFGRVGLFRNQPGDRLLKQADLVITIGydpIEYEPRNWNSEN----DATIVHIDVEPAQIDNNYQP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 326 DIPVVGDarlvLEQMLELLAQDA-----PSQPQDDIRDWWQQIEIWRARqclKYDAESESIKPQAVIETLWRLTKGDAYV 400
Cdd:TIGR02418 306 DLELVGD----IASTLDLLAERIpgyelPPDALAILEDLKQQREALDRV---PATLKQAHLHPLEIIKAMQAIVTDDVTV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 401 TSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVL 480
Cdd:TIGR02418 379 TVDMGSHYIWMARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 481 NLNNRYLGMVKQWQDMIYsgrHSQSYMQSLP-DFVRLAEAYGHVGLQINRPDELESKLSEALEhvrNNRLVFVDVTVDGS 559
Cdd:TIGR02418 459 IWNDNGYNMVEFQEEMKY---QRSSGVDFGPiDFVKYAESFGAKGLRVESPDQLEPTLRQAME---VEGPVVVDIPVDYS 532
|
....*..
gi 1334564377 560 EHVYPMQ 566
Cdd:TIGR02418 533 DNPKLMS 539
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
17-554 |
7.51e-90 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 288.82 E-value: 7.51e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 17 EMVVRSLIDQGVKQVFGYPGGAVLDIYDaLHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITGIA 96
Cdd:PRK07525 10 EAFVETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 97 TAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKDIln 176
Cdd:PRK07525 89 TAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRDY-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 177 pakkmpyaWPETVSMRSYNPTT----SGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMG 252
Cdd:PRK07525 166 --------FYGVIDVEIPQPVRlergAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 253 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTnnLAK----YCP-NATVLHIDIDPTSISKTVNADI 327
Cdd:PRK07525 238 NDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPFGT--LPQygidYWPkDAKIIQVDINPDRIGLTKKVSV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 328 PVVGDARLVLEQMLELLAQDAPSQPQDDIR---------DWWQQIEIW-------------RARqclkyDAESESIKPQA 385
Cdd:PRK07525 316 GICGDAKAVARELLARLAERLAGDAGREERkaliaaeksAWEQELSSWdhedddpgtdwneEAR-----ARKPDYMHPRQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 386 VIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQ 465
Cdd:PRK07525 391 ALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 466 ELSTALQYELPVLVLNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEHVR 545
Cdd:PRK07525 471 EVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDAQN 550
|
....*....
gi 1334564377 546 NNRLVFVDV 554
Cdd:PRK07525 551 EGKTTVIEI 559
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
14-566 |
1.47e-89 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 286.75 E-value: 1.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 14 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAIT 93
Cdd:PRK08617 6 YGADLVVDSLINQGVKYVFGIPGAKIDRVFDALED-SGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 94 GIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKD 173
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 174 ILN-PAKKMPYAWPETVSMRSYNPttsghkGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMG 252
Cdd:PRK08617 165 VVDaPVTSKAIAPLSKPKLGPASP------EDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 253 LGAFPATH-RQSLGMLGMHGTYEANMTMHNADVIFAVG---VRFDDRTTNNLakycPNATVLHIDIDPTSISKTVNADIP 328
Cdd:PRK08617 239 AGVISRELeDHFFGRVGLFRNQPGDELLKKADLVITIGydpIEYEPRNWNSE----GDATIIHIDVLPAEIDNYYQPERE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 329 VVGDarlvLEQMLELLAQDA-----PSQPQDDIRDWWQQIEiwrARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSD 403
Cdd:PRK08617 315 LIGD----IAATLDLLAEKLdglslSPQSLEILEELRAQLE---ELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 404 VGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLN 483
Cdd:PRK08617 388 VGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 484 NRYLGMVKQWQDMIY---SGRHSQSYmqslpDFVRLAEAYGHVGLQINRPDELESKLSEALEhvrNNRLVFVDVTVDGSE 560
Cdd:PRK08617 468 DGHYNMVEFQEEMKYgrsSGVDFGPV-----DFVKYAESFGAKGLRVTSPDELEPVLREALA---TDGPVVIDIPVDYSD 539
|
....*.
gi 1334564377 561 HVYPMQ 566
Cdd:PRK08617 540 NIKLME 545
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
11-554 |
5.05e-82 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 267.45 E-value: 5.05e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 11 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALhtvgGIDHVLVRHEQAAVHMADGLARATG--DVGVVLVTSGPGA 88
Cdd:PRK06154 18 KTMKVAEAVAEILKEEGVELLFGFPVNELFDAAAAA----GIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 89 TNAITGIATAYMDSIPLVILSGQVATSLIGYDA-FQECDMVgisRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVV 167
Cdd:PRK06154 94 ENAFGGVAQAYGDSVPVLFLPTGYPRGSTDVAPnFESLRNY---RHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 168 VDLPKDILN---PAKKMPYAwPETVSMRSYNPTTsghkgqIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNL 244
Cdd:PRK06154 171 LELPVDVLAeelDELPLDHR-PSRRSRPGADPVE------VVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 245 PVVSSLMGLGAFPATHRQSLGMLGMhgTYEANMT--MHNADVIFAVGVRFddrTTNNLAKYCP-NATVLHIDIDPTSISK 321
Cdd:PRK06154 244 PVMTTLNGKSAFPEDHPLALGSGGR--ARPATVAhfLREADVLFGIGCSL---TRSYYGLPMPeGKTIIHSTLDDADLNK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 322 TVNADIPVVGDARLVLEQMLELLAQDAPSQPQD---------DIRDWWqqIEIWRArqclKYDAESESIKPQAVI-ETLW 391
Cdd:PRK06154 319 DYPIDHGLVGDAALVLKQMIEELRRRVGPDRGRaqqvaaeieAVRAAW--LAKWMP----KLTSDSTPINPYRVVwELQH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 392 RLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTAL 471
Cdd:PRK06154 393 AVDIKTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 472 QYELPVLVLNLNNRYLGmvkqwqdmiysgrhsqSYMQSLP-------------DFVRLAEAYGHVGLQINRPDELESKLS 538
Cdd:PRK06154 473 RERIPILTILLNNFSMG----------------GYDKVMPvsttkyratdisgDYAAIARALGGYGERVEDPEMLVPALL 536
|
570
....*....|....*.
gi 1334564377 539 EALEHVRNNRLVFVDV 554
Cdd:PRK06154 537 RALRKVKEGTPALLEV 552
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
12-565 |
1.79e-77 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 255.14 E-value: 1.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 12 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNA 91
Cdd:PRK06457 1 MPSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRK-SKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 92 ITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLP 171
Cdd:PRK06457 80 LNGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 172 KDILNPAKKMPYAWPETVSMRSYNPTTSGHKGQIKRalqtlasAKKPVVYVGGGAISAAcyAPLRHIIEIFNLPVVSSLM 251
Cdd:PRK06457 159 VDILRKSSEYKGSKNTEVGKVKYSIDFSRAKELIKE-------SEKPVLLIGGGTRGLG--KEINRFAEKIGAPIIYTLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 252 GLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNlakycPNATVLHIDIDPTSISKTVNADIPVVG 331
Cdd:PRK06457 230 GKGILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLN-----KSAKVIQVDIDNSNIGKRLDVDLSYPI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 332 DARLVLEQMLELLAQDAPSQPQDDIRDWWQQIEiwrarqclkyDAESES---IKPQAVIETLWRLTKGDAYVTSDVGQHQ 408
Cdd:PRK06457 305 PVAEFLNIDIEEKSDKFYEELKGKKEDWLDSIS----------KQENSLdkpMKPQRVAYIVSQKCKKDAVIVTDTGNVT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 409 MFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMAL-PKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYL 487
Cdd:PRK06457 375 MWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAVeNKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKL 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1334564377 488 GMVKQWQD-MIYSGRHSQSYMqslPDFVRLAEAYGHVGLQINRPDELESKLSEALehvRNNRLVFVDVTVDGSEHvyPM 565
Cdd:PRK06457 455 GMIKFEQEvMGYPEWGVDLYN---PDFTKIAESIGFKGFRLEEPKEAEEIIEEFL---NTKGPAVLDAIVDPNER--PM 525
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
7-561 |
3.55e-77 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 255.07 E-value: 3.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 7 RQAVEMLSGAEMVVRSLIDQGVKQVFGYpggavlDIYDALHTVG---GIDHVLVRHEQAAVHMADGLARATGDVGVVLVT 83
Cdd:PRK06112 8 PGFTLNGTVAHAIARALKRHGVEQIFGQ------SLPSALFLAAeaiGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 84 SGPGATNAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRP 163
Cdd:PRK06112 82 NGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 164 GPVVVDLPKDILNPAKKMPyAWPETVSMRSYnP--TTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEI 241
Cdd:PRK06112 162 GPVVLLLPADLLTAAAAAP-AAPRSNSLGHF-PldRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 242 FNLPVVSSLMGLGAFPATHRQSLGMLGM------HGTYEANMtMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDID 315
Cdd:PRK06112 240 AGLPVATTNMGKGAVDETHPLSLGVVGSlmgprsPGRHLRDL-VREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 316 PTSISKTVNAdIPVVGDARLVLEQMLELLAQDAPSQPQDD-------IRDWWQQIEIWRARQclkYDAESESIKPQAVIE 388
Cdd:PRK06112 319 GEEVGRNYEA-LRLVGDARLTLAALTDALRGRDLAARAGRraalepaIAAGREAHREDSAPV---ALSDASPIRPERIMA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 389 TLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPR-RWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQEL 467
Cdd:PRK06112 395 ELQAVLTGDTIVVADASYSSIWVANFLTARRAGmRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAEL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 468 STALQYELPVLVLNLNNRYLGMVKQWQDMIYsGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDEleskLSEALEHVRNN 547
Cdd:PRK06112 475 ETARRMGVPVTIVVLNNGILGFQKHAETVKF-GTHTDACHFAAVDHAAIARACGCDGVRVEDPAE----LAQALAAAMAA 549
|
570
....*....|....*
gi 1334564377 548 RLVFV-DVTVDGSEH 561
Cdd:PRK06112 550 PGPTLiEVITDPSAF 564
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
17-172 |
1.16e-71 |
|
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: 226.64 E-value: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 17 EMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITGIA 96
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1334564377 97 TAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 172
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
27-558 |
9.46e-69 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 232.80 E-value: 9.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 27 GVKQVFGYPGGAVLDIYDALHT-VGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITGIATAYMDSIPL 105
Cdd:TIGR02720 13 GVDHIYGIPGGSFNSTMDALSAeRDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYDAKEDHVPV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 106 VILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVVVDLPKDIlnPAKKMP--Y 183
Cdd:TIGR02720 93 LALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAI-RRAYAHNGVAVVTIPVDF--GWQEIPdnD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 184 AWPETVSMRSYN-PTTSGHkgQIKRALQTLASAKKPVVYVGGGAISAAcyAPLRHIIEIFNLPVVSSLMGLGAFPATHRQ 262
Cdd:TIGR02720 170 YYASSVSYQTPLlPAPDVE--AVTRAVQTLKAAERPVIYYGIGARKAG--EELEALSEKLKIPLISTGLAKGIIEDRYPA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 263 SLGMLGMHGTYEANMTMHNADVIFAVGVRFD----DRTTNNlAKYcpnatVLHIDIDPTSISKTVNADIPVVGDARLVLE 338
Cdd:TIGR02720 246 YLGSAYRVAQKPANEALFQADLVLFVGNNYPfaevSKAFKN-TKY-----FIQIDIDPAKLGKRHHTDIAVLADAKKALA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 339 QMLellaqdAPSQPQDDiRDWWQ----QIEIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALY 414
Cdd:TIGR02720 320 AIL------AQVEPRES-TPWWQanvaNVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 415 YPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQ 494
Cdd:TIGR02720 393 LKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQ 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1334564377 495 DmiysGRHSQSYMQSLP--DFVRLAEAYGHVGLQINRPDELESKLSEALEhVRNNRLVFVDVTVDG 558
Cdd:TIGR02720 473 E----DTNQPLIGVDFNdaDFAKIAEGVGAVGFRVNKIEQLPAVFEQAKA-IKQGKPVLIDAKITG 533
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
11-559 |
1.91e-66 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 225.64 E-value: 1.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 11 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATN 90
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 91 AITGIATAYMDSIPLVILSGQVATSLIGYDA--FQEC-DMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVV 167
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 168 VDLPKDIlnpaKKMPYAWPETVS-MRSYNPTTSGHkgQIKRALQTLASAKKPVVYVGGGAISAAcyAPLRHIIEIfNLPV 246
Cdd:PRK07064 161 VEIPIDI----QAAEIELPDDLApVHVAVPEPDAA--AVAELAERLAAARRPLLWLGGGARHAG--AEVKRLVDL-GFGV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 247 VSSLMGLGAFPATHRQSLGMLGMHGTYEAnmTMHNADVIFAVGVRFDDRTTNNLAKYCPnATVLHIDIDPTSISKTVNAD 326
Cdd:PRK07064 232 VTSTQGRGVVPEDHPASLGAFNNSAAVEA--LYKTCDLLLVVGSRLRGNETLKYSLALP-RPLIRVDADAAADGRGYPND 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 327 IPVVGDARLVLEQMLELLAQDAPSQPQ--DDIRDWWQQIEiwrarqclkyDAESESIKPQAVI-ETLWRLTKGDAYVTSD 403
Cdd:PRK07064 309 LFVHGDAARVLARLADRLEGRLSVDPAfaADLRAAREAAV----------ADLRKGLGPYAKLvDALRAALPRDGNWVRD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 404 VG-QHQMFAALYYPFDKPRRWINSGGlGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNL 482
Cdd:PRK07064 379 VTiSNSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLM 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1334564377 483 NNRYLGMVKQWQDMIYSGRHsqsYMQSL--PDFVRLAEAYGHVGLQINRPDELESKLSEALEHvRNNRLVFVDVTVDGS 559
Cdd:PRK07064 458 NDGGYGVIRNIQDAQYGGRR---YYVELhtPDFALLAASLGLPHWRVTSADDFEAVLREALAK-EGPVLVEVDMLSIGP 532
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
16-557 |
2.90e-65 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 224.02 E-value: 2.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 16 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGG-IDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITG 94
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 95 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVkHSFLVKQT--EDIPQVLKKAFWLAASGRpGPVVVDLPK 172
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVA-GAFVQMVTvpEQLRHLVDRAVRTALAER-TVTAVILPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 173 DILN-PAKKMPYAWPETVSMRSYN-PTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAAcyAPLRHIIEIFNLPVVSSL 250
Cdd:PRK08273 164 DVQElEYEPPPHAHGTVHSGVGYTrPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGAT--DEVIAVAERLGAGVAKAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 251 MGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDdrttnnLAKYCP---NATVLHIDIDPTSISKTVNADI 327
Cdd:PRK08273 242 LGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFP------YSEFLPkegQARGVQIDIDGRMLGLRYPMEV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 328 PVVGDARLVLEQMLELLAQDAPSQPQDDI----RDWWQQIEIwRARqclkydAESESIKPQAVIETLWRLTKGDAYVTSD 403
Cdd:PRK08273 316 NLVGDAAETLRALLPLLERKKDRSWRERIekwvARWWETLEA-RAM------VPADPVNPQRVFWELSPRLPDNAILTAD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 404 VGQhqmfAALYYPFD-KPRRWIN---SGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMN-IQELSTALQY----- 473
Cdd:PRK08273 389 SGS----CANWYARDlRMRRGMMaslSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKYwrqws 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 474 ELPVLVLNLNNRYLGMVkQWQDMIYSGRHSQSYMQSLPDF--VRLAEAYGHVGLQINRPDELESKLSEALEhvrNNRLVF 551
Cdd:PRK08273 465 DPRLIVLVLNNRDLNQV-TWEQRVMEGDPKFEASQDLPDVpyARFAELLGLKGIRVDDPEQLGAAWDEALA---ADRPVV 540
|
....*.
gi 1334564377 552 VDVTVD 557
Cdd:PRK08273 541 LEVKTD 546
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
403-554 |
1.20e-63 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 205.51 E-value: 1.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 403 DVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNL 482
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1334564377 483 NNRYLGMVKQWQDMIYSGRHSQSYMQSL--PDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDV 554
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGKILppVDFAKLAEAYGAKGARVESPEELEEALKEALEH---DGPALIDV 151
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
15-175 |
2.19e-63 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 205.55 E-value: 2.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 15 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITG 94
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 95 IATAYMDSIPLVILSGQVATSLIGYDAFQ-ECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKD 173
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 1334564377 174 IL 175
Cdd:pfam02776 161 VL 162
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
12-559 |
7.68e-62 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 214.09 E-value: 7.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 12 MLSGAEMVVRSLIDQGVKQVFGYPG---GAVLDIYDALHTVGGI--DHVLVRHEQAAVHMADGLARATGDVGVVLVTSGP 86
Cdd:PRK08327 6 MYTAAELFLELLKELGVDYIFINSGtdyPPIIEAKARARAAGRPlpEFVICPHEIVAISMAHGYALVTGKPQAVMVHVDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 87 GATNAITGIATAYMDSIPLVILSGQVATS----------LIGY--DAFqecDMVGISRPVVKHSFLVKQTEDIPQVLKKA 154
Cdd:PRK08327 86 GTANALGGVHNAARSRIPVLVFAGRSPYTeegelgsrntRIHWtqEMR---DQGGLVREYVKWDYEIRRGDQIGEVVARA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 155 FWLAASGRPGPVVVDLPKDILnpAKKMPYawpETVSMRSYNPTTSGH--KGQIKRALQTLASAKKPVVYVGGGAISAACY 232
Cdd:PRK08327 163 IQIAMSEPKGPVYLTLPREVL--AEEVPE---VKADAGRQMAPAPPApdPEDIARAAEMLAAAERPVIITWRAGRTAEGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 233 APLRHIIEIFNLPVVSSLMGLGAFPATHrqslgmlGMHGTYEANMTMHNADVIFAVGvrfddrttnNLAKYCP------- 305
Cdd:PRK08327 238 ASLRRLAEELAIPVVEYAGEVVNYPSDH-------PLHLGPDPRADLAEADLVLVVD---------SDVPWIPkkirpda 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 306 NATVLHIDIDPtsiSKT------VNADIPVVGDARLVLEQMLELLA--QDAPSQPQDDIRDWWQQIEI---WRARQCLKY 374
Cdd:PRK08327 302 DARVIQIDVDP---LKSriplwgFPCDLCIQADTSTALDQLEERLKslASAERRRARRRRAAVRELRIrqeAAKRAEIER 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 375 DAESESIKPQAVIETLWRLTKGDAYVTSDVGqhqmFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCV 454
Cdd:PRK08327 379 LKDRGPITPAYLSYCLGEVADEYDAIVTEYP----FVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIAT 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 455 TGDGSIQMNIQE--LSTALQYELPVLVLNLNNRYLGMVKQWQDMIYS---GRHSQSYMQS----LPDFVRLAEAYGHVGL 525
Cdd:PRK08327 455 VGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPegyAARKGTFPGTdfdpRPDFAKIAEAFGGYGE 534
|
570 580 590
....*....|....*....|....*....|....*
gi 1334564377 526 QINRPDELESKLSEALEHVRN-NRLVFVDVTVDGS 559
Cdd:PRK08327 535 RVEDPEELKGALRRALAAVRKgRRSAVLDVIVDRV 569
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
15-542 |
1.94e-61 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 212.27 E-value: 1.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 15 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITG 94
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGARE-EGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 95 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 174
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 175 L-NPAKKMPYAWPETVSMRSYNPTTSghkgQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMGL 253
Cdd:PRK05858 166 AfSMADDDGRPGALTELPAGPTPDPD----ALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 254 GAFPATHRQSLgmlgmhgTYEANMTMHNADVIFAVGVRFDDRTtnNLAKYCPNATVLHIDIDPTSISKTVNADIPVVGDA 333
Cdd:PRK05858 242 GVVPADHPLAF-------SRARGKALGEADVVLVVGVPMDFRL--GFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 334 RLVLEQMLEllaqdaPSQPQDDIRDWWQQI----EIWRARQCLKYDAESESIKPQAVIETLWRLTKGDAYVTSDVGQHQM 409
Cdd:PRK05858 313 SAILSALAG------AGGDRTDHQGWIEELrtaeTAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 410 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 489
Cdd:PRK05858 387 YAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGL 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1334564377 490 VKQWQDMIYsGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALE 542
Cdd:PRK05858 467 EKHPMEALY-GYDVAADLRPGTRYDEVVRALGGHGELVTVPAELGPALERAFA 518
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
26-557 |
2.31e-61 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 211.74 E-value: 2.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 26 QGVKQVFGYPGGAVLDIYDALHtvGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITGIATAYMDSIPL 105
Cdd:PRK07092 25 FGITTVFGNPGSTELPFLRDFP--DDFRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFTAFKNHTPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 106 VILSGQVATSLIGYDAF-QECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDILN-PAkkmpy 183
Cdd:PRK07092 103 VITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYDDWDqPA----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 184 awpETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPV-VSSLMGLGAFPATHRQ 262
Cdd:PRK07092 178 ---EPLPARTVSSAVRPDPAALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPVwVAPMSGRCSFPEDHPL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 263 SLGML-GMHGTYEANMTMHnaDVIFAVGV---RFDDRTTnnlAKYCP-NATVLHIDIDPTSISKTVNADiPVVGDARLVL 337
Cdd:PRK07092 255 FAGFLpASREKISALLDGH--DLVLVIGApvfTYHVEGP---GPHLPeGAELVQLTDDPGEAAWAPMGD-AIVGDIRLAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 338 EQMLELLAQDAPSQPQddirdwwqqieiwrARQCLK-YDAESESIKPQAVIETLWRLT-KGDAYV---TSDVGQHQMFAA 412
Cdd:PRK07092 329 RDLLALLPPSARPAPP--------------ARPMPPpAPAPGEPLSVAFVLQTLAALRpADAIVVeeaPSTRPAMQEHLP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 413 L-----YYPFDkprrwinSGGLgtmGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNN-RY 486
Cdd:PRK07092 395 MrrqgsFYTMA-------SGGL---GYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNgRY 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1334564377 487 LGMvkQWQDMIYSGRHSQSYmqSLP--DFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVD 557
Cdd:PRK07092 465 GAL--RWFAPVFGVRDVPGL--DLPglDFVALARGYGCEAVRVSDAAELADALARALAA---DGPVLVEVEVA 530
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
16-567 |
1.00e-56 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 200.21 E-value: 1.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 16 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITGI 95
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 96 ATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVVVDLPKDI- 174
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAM-RKAILNRGVAVVVLPGDVa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 175 LNPA-KKMPYAWPETVSmrsynPTTSGHKGQIKRALQTLASAKKPVVYVGGGAisAACYAPLRHIIEIFNLPVVSSLMGL 253
Cdd:PRK09124 165 LKPApERATPHWYHAPQ-----PVVTPAEEELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALRGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 254 GAFPATHRQSLGMLGMHG---TYEAnmtMHNADVIFAVGVRFDDRttnnlAKYCPNATVLHIDIDPTSISKTVNADIPVV 330
Cdd:PRK09124 238 EHVEYDNPYDVGMTGLIGfssGYHA---MMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDLGLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 331 GDARLVLEQMLELLaqdapsQPQDDIRDWWQQIEIWR-ARQCL----KYDAESESIKPQAVIETLWRLTKGDAYVTSDVG 405
Cdd:PRK09124 310 GDVKATLAALLPLL------EEKTDRKFLDKALEHYRkARKGLddlaVPSDGGKPIHPQYLARQISEFAADDAIFTCDVG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 406 QHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNR 485
Cdd:PRK09124 384 TPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 486 YLGMVKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVDGSEHVYPM 565
Cdd:PRK09124 464 VLGFVA--MEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAH---DGPALVDVVTAKQELAMPP 538
|
..
gi 1334564377 566 QI 567
Cdd:PRK09124 539 QI 540
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
205-340 |
1.51e-56 |
|
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: 186.62 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 205 IKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLPVVSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADV 284
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1334564377 285 IFAVGVRFDD-RTTNNLAKYCPNATVLHIDIDPTSISKTVNADIPVVGDARLVLEQM 340
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
7-560 |
3.42e-53 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 190.58 E-value: 3.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 7 RQAVEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIyDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGP 86
Cdd:PRK09259 4 SDQLQLTDGFHLVIDALKLNGIDTIYGVVGIPITDL-ARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 87 GATNAITGIATAYMDSIPLVILSGQVATSLIGYDA--FQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPG 164
Cdd:PRK09259 83 GFLNGLTALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 165 PVVVDLPKDILnpAKKMPYAWPETVSMRSYNPTTSGHKGQ--IKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIF 242
Cdd:PRK09259 163 GVYLDLPAKVL--AQTMDADEALTSLVKVVDPAPAQLPAPeaVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 243 NLPVVSSLMGLGAFPATHRQSLGMlgmhgtyEANMTMHNADVIFAVGVRFDDRTTNNLAK-YCPNATVLHIDIDPTSISK 321
Cdd:PRK09259 241 GIPFLPMSMAKGLLPDTHPQSAAA-------ARSLALANADVVLLVGARLNWLLSHGKGKtWGADKKFIQIDIEPQEIDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 322 TVNADIPVVGDARLVLEQMLELLAQDAPSQPQddirDWWQQIEIWRARQCLKYDAESESIKPQ-------AVIETLWRlT 394
Cdd:PRK09259 314 NRPIAAPVVGDIGSVMQALLAGLKQNTFKAPA----EWLDALAERKEKNAAKMAEKLSTDTQPmnfynalGAIRDVLK-E 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 395 KGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEmVVCVTGDGSIQMNIQELSTALQYE 474
Cdd:PRK09259 389 NPDIYLVNEGANTLDLARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAAAVETGKP-VVAIEGDSAFGFSGMEVETICRYN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 475 LPVLVLNLNNrylGMVKQWQDMIYSGRHSQSYMQSLPD--FVRLAEAYGHVGLQINRPDELESKLSEALEhvrNNRLVFV 552
Cdd:PRK09259 468 LPVTVVIFNN---GGIYRGDDVNLSGAGDPSPTVLVHHarYDKMMEAFGGVGYNVTTPDELRHALTEAIA---SGKPTLI 541
|
570
....*....|.
gi 1334564377 553 DVTVD---GSE 560
Cdd:PRK09259 542 NVVIDpaaGTE 552
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
16-557 |
3.06e-52 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 188.27 E-value: 3.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 16 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITGI 95
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 96 ATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWlAASGRPGPVVVDLPKDIl 175
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQ-HAVAGGGVSVVTLPGDI- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 176 npAKKMPYAWPETVSMRSYNPTTSGHKGQIKRALQTLASAKKPVVYVGGGAISAacYAPLRHIIEIFNLPVVSSLMGLGA 255
Cdd:PRK06546 164 --ADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGA--HAEVLALAEKIKAPVGHSLRGKEW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 256 FPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRF--DDrttnnlakYCPNATVLHIDIDPTSISKTVNADIPVVGDA 333
Cdd:PRK06546 240 IQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFpyDQ--------FLPDVRTAQVDIDPEHLGRRTRVDLAVHGDV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 334 RLVLEQMLELLAQ-------DAPSQPQDDIRDwwqqieiwRARQCLKYDAESES-IKPQAVIETLWRLTKGDAYVTSDVG 405
Cdd:PRK06546 312 AETIRALLPLVKEktdrrflDRMLKKHARKLE--------KVVGAYTRKVEKHTpIHPEYVASILDELAADDAVFTVDTG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 406 QHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNR 485
Cdd:PRK06546 384 MCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNS 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334564377 486 YLGMVKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVD 557
Cdd:PRK06546 464 TLGMVK--LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAH---PGPALVDVVTD 530
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
23-557 |
5.12e-52 |
|
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: 186.90 E-value: 5.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 23 LIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGdVGVVLVTSGPGATNAITGIATAYMDS 102
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 103 IPLVILSG------QVATSLI-------GYDAFQEcdmvgISRPV-VKHSFLVKQT--EDIPQVLKKAFwlaASGRpgPV 166
Cdd:COG3961 94 VPVVHIVGapgtraQRRGPLLhhtlgdgDFDHFLR-----MFEEVtVAQAVLTPENaaAEIDRVLAAAL---REKR--PV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 167 VVDLPKDILNpakkMPYAWPETVSMRSYNPTTSGHKGQ-IKRALQTLASAKKPVVYVGGGAISAACYAPLRHIIEIFNLP 245
Cdd:COG3961 164 YIELPRDVAD----APIEPPEAPLPLPPPASDPAALAAaVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 246 VVSSLMGLGAFPATHRQSLgmlgmhGTYEANM-------TMHNADVIFAVGVRFDDRTTNNL-AKYCPNATvlhIDIDP- 316
Cdd:COG3961 240 VATTLLGKSVLDESHPQFI------GTYAGAAsspevreYVENADCVLCLGVVFTDTNTGGFtAQLDPERT---IDIQPd 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 317 -TSISKTVNADIPvvgdarlvLEQMLELLAQDAPSQPqddirdwwqqiEIWRARQCLkydAESESIKPQAVI--ETLWR- 392
Cdd:COG3961 311 sVRVGGHIYPGVS--------LADFLEALAELLKKRS-----------APLPAPAPP---PPPPPAAPDAPLtqDRLWQr 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 393 ----LTKGDAyVTSDVGQhQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELS 468
Cdd:COG3961 369 lqafLDPGDI-VVADTGT-SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 469 TALQYELPVLVLNLNNR-Y------LGM------VKQWqdmiysgrhsqsymqslpDFVRLAEAYG---HVGLQINRPDE 532
Cdd:COG3961 447 TMLRYGLKPIIFVLNNDgYtieraiHGPdgpyndIANW------------------DYAKLPEAFGggnALGFRVTTEGE 508
|
570 580
....*....|....*....|....*..
gi 1334564377 533 LEsklsEALEHVRNN--RLVFVDVTVD 557
Cdd:COG3961 509 LE----EALAAAEANtdRLTLIEVVLD 531
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
385-556 |
2.10e-50 |
|
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: 171.28 E-value: 2.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 385 AVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNI 464
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 465 QELSTALQYELPVLVLNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGLQINRPDELESKLSEALEHv 544
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSN-PDFAALAEAYGAKGVRVEDPEDLEAALAEALAA- 158
|
170
....*....|..
gi 1334564377 545 rnNRLVFVDVTV 556
Cdd:cd00568 159 --GGPALIEVKT 168
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
381-560 |
3.68e-41 |
|
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: 146.91 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 381 IKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSI 460
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 461 QMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQDMIYSGRHSQSymQSLPDFVRLAEAYGHVGLQINRPDELESKLSEA 540
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVD--LPNPDFAKIAEAMGIKGIRVEDPDELEAALDEA 159
|
170 180
....*....|....*....|
gi 1334564377 541 LEHvrnNRLVFVDVTVDGSE 560
Cdd:cd02014 160 LAA---DGPVVIDVVTDPNE 176
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
16-174 |
3.92e-41 |
|
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: 146.16 E-value: 3.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 16 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAITGI 95
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1334564377 96 ATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKDI 174
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGDV 160
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
383-560 |
3.26e-39 |
|
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: 141.66 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 383 PQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQM 462
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 463 NIQELSTALQYELPVLVLNLNNRYLGMVKqWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGLQINRPDELESKLSEALE 542
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIK-WKQEKEYGRDSGVDFGN-PDFVKYAESFGAKGYRIESADDLLPVLERALA 158
|
170
....*....|....*...
gi 1334564377 543 hvrNNRLVFVDVTVDGSE 560
Cdd:cd02010 159 ---ADGVHVIDCPVDYSE 173
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
26-172 |
3.16e-32 |
|
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: 121.30 E-value: 3.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 26 QGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGdVGVVLVTSGPGATNAITGIATAYMDSIPL 105
Cdd:cd06586 10 WGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADAAAEHLPV 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1334564377 106 VILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVVVDLPK 172
Cdd:cd06586 89 VFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAI-RTAYASQGPVVVRLPR 154
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
381-558 |
2.11e-28 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 112.22 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 381 IKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSI 460
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 461 QMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGLQINRPDELESKLSEA 540
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELES-ESFAKIAEACGAKGITVDKPEDVGPALQKA 162
|
170
....*....|....*...
gi 1334564377 541 LEHVRNNRLVFVDVTVDG 558
Cdd:cd02013 163 IAMMAEGKTTVIEIVCDQ 180
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
383-543 |
7.48e-26 |
|
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: 104.21 E-value: 7.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 383 PQAVIETLWRLTKGDA-----YVTSDVGQHQMFaalyyPFDKPRRWINSGGlGTMGFGLPAALGVKMALPKEMVVCVTGD 457
Cdd:cd02002 3 PEYLAAALAAALPEDAiivdeAVTNGLPLRDQL-----PLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 458 GSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQDMIYSGRHSQS--YMQSL----PDFVRLAEAYGHVGLQINRPD 531
Cdd:cd02002 77 GSFMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENapDGLDLldpgIDFAAIAKAFGVEAERVETPE 156
|
170
....*....|..
gi 1334564377 532 ELESKLSEALEH 543
Cdd:cd02002 157 ELDEALREALAE 168
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
383-557 |
1.13e-25 |
|
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: 103.77 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 383 PQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQM 462
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 463 NIQELSTALQYELPVLVLNLNNrylgmvkqwqDMIYSGRHSQSYMQSLPDFV----------RLAEAYGHVGLQINRPDE 532
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNN----------GGWYQGLDGQQLSYGLGLPVttllpdtrydLVAEAFGGKGELVTTPEE 150
|
170 180
....*....|....*....|....*
gi 1334564377 533 LESKLSEALEHvrnNRLVFVDVTVD 557
Cdd:cd02004 151 LKPALKRALAS---GKPALINVIID 172
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
381-552 |
4.71e-25 |
|
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: 102.74 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 381 IKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSI 460
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 461 QMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQ---DMIYSGRHSQSYMQSLP------DFVRLAEAYGHVGLQINRPD 531
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQrafDMDYQVNLAFENINSSElggygvDHVKVAEGLGCKAIRVTKPE 167
|
170 180
....*....|....*....|.
gi 1334564377 532 ELESKLSEALEHVRNNRLVFV 552
Cdd:cd02006 168 ELAAAFEQAKKLMAEHRVPVV 188
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
410-557 |
2.36e-20 |
|
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: 88.75 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 410 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 489
Cdd:cd02005 30 FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTI 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1334564377 490 VKQWQDMiysgrhSQSYMQSLP-DFVRLAEAYG----HVGLQINRPDELESKLSEALEHvrNNRLVFVDVTVD 557
Cdd:cd02005 110 ERAIHGP------EASYNDIANwNYTKLPEVFGggggGLSFRVKTEGELDEALKDALFN--RDKLSLIEVILP 174
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
14-543 |
2.92e-20 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 94.14 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 14 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAIT 93
Cdd:PRK07586 2 NGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 94 GIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVvkhSFLVKQTEDIPQV--LKKAFWLAASGRPGPVVVD-L 170
Cdd:PRK07586 82 NLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPV---SGWVRRSESAADVaaDAAAAVAAARGAPGQVATLiL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 171 PKDIlnpakkmpyAW-----PETVSMRSYNPTTSGHkgQIKRALQTLASAKKPVVYVGGGA-----------ISAACYAp 234
Cdd:PRK07586 159 PADV---------AWseggpPAPPPPAPAPAAVDPA--AVEAAAAALRSGEPTVLLLGGRAlrerglaaaarIAAATGA- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 235 lRHIIEIFN--------LPVVSSLmglgAFPAthRQSLGMLGmhgtyeanmtmhNADVIFAVGVRfddrttnnlakycpn 306
Cdd:PRK07586 227 -RLLAETFParmergagRPAVERL----PYFA--EQALAQLA------------GVRHLVLVGAK--------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 307 atvlhidiDPTSI-------SKTVNADIPVV------GDARLVLEQMLELL-AQDAPSQPQDDIRDwwqqieiwrarqcl 372
Cdd:PRK07586 273 --------APVAFfaypgkpSRLVPEGCEVHtlagpgEDAAAALEALADALgAKPAAPPLAAPARP-------------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 373 kyDAESESIKPQAVIETLWRLTKGDAYVTSDVGqhqMFAALYYPFD---KPRRWINSGGlGTMGFGLPAALGVKMALPKE 449
Cdd:PRK07586 331 --PLPTGALTPEAIAQVIAALLPENAIVVDESI---TSGRGFFPATagaAPHDWLTLTG-GAIGQGLPLATGAAVACPDR 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 450 MVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNR-Y--LGMVKQWQDMIYSGRHSQSyMQSL----PDFVRLAEAYGH 522
Cdd:PRK07586 405 KVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRaYaiLRGELARVGAGNPGPRALD-MLDLddpdLDWVALAEGMGV 483
|
570 580
....*....|....*....|.
gi 1334564377 523 VGLQINRPDELESKLSEALEH 543
Cdd:PRK07586 484 PARRVTTAEEFADALAAALAE 504
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
9-550 |
2.62e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 91.47 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 9 AVEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGA 88
Cdd:PRK12474 1 MGQTMNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 89 TNAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVvkhSFLVKQTEDIPQV---LKKAFWLAASGRPGP 165
Cdd:PRK12474 81 ANGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPV---SRWVHRSASAGAVdsdVARAVQAAQSAPGGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 166 VVVDLPKDIlnpakkmpyAWPETV----SMRSYNPTTSgHKGQIKRALQTLASAKKPVVYVGGGA-----------ISAA 230
Cdd:PRK12474 158 ATLIMPADV---------AWNEAAyaaqPLRGIGPAPV-AAETVERIAALLRNGKKSALLLRGSAlrgapleaagrIQAK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 231 CYAPLrhIIEIFNlPVVSSLMG---LGAFPATHRQSLGMLgmhgtyeanmtmHNADVIFAVGVRfddrttnnlakycPNA 307
Cdd:PRK12474 228 TGVRL--YCDTFA-PRIERGAGrvpIERIPYFHEQITAFL------------KDVEQLVLVGAK-------------PPV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 308 TVLHIDIDPTSISKTvNADIPVVGDARLVLEQMLELLAQ--DAPSQPqddirdwwqqieIWRARQCLKyDAESESIKPQA 385
Cdd:PRK12474 280 SFFAYPGKPSWGAPP-GCEIVYLAQPDEDLAQALQDLADavDAPAEP------------AARTPLALP-ALPKGALNSLG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 386 VIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGlGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQ 465
Cdd:PRK12474 346 VAQLIAHRTPDQAIYADEALTSGLFFDMSYDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQ 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 466 ELSTALQYELPVLVLNLNNRYLGMVkqWQDMIY-----SGRHSQSYMQ-SLP--DFVRLAEAYGHVGLQINRPDELESKL 537
Cdd:PRK12474 425 ALWTMARENLDVTVVIFANRSYAIL--NGELQRvgaqgAGRNALSMLDlHNPelNWMKIAEGLGVEASRATTAEEFSAQY 502
|
570
....*....|...
gi 1334564377 538 SEALEHvRNNRLV 550
Cdd:PRK12474 503 AAAMAQ-RGPRLI 514
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
23-155 |
5.49e-17 |
|
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: 78.31 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 23 LIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGdVGVVLVTSGPGATNAITGIATAYMDS 102
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 103 IPLVILSGQVATSLIG-------------YDAFQECdmvgiSRPVVKHS-FLVKQ---TEDIPQVLKKAF 155
Cdd:cd07038 86 VPVVHIVGAPSTKAQAsglllhhtlgdgdFDVFLKM-----FEEITCAAaRLTDPenaAEEIDRVLRTAL 150
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
19-171 |
1.46e-14 |
|
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: 71.38 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 19 VVRSLIDQGVKQVFGYPGG-----AVldiydALHTVGGIDHVLVRHEQAAVHMADGLARATGDVGVVLVTSGPGATNAIT 93
Cdd:cd07037 3 LVEELKRLGVRDVVISPGSrsaplAL-----AAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 94 GIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSF---LVKQTEDIP---QVLKKAFWLAASGRPGPVV 167
Cdd:cd07037 78 AVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVdlpPPEDDDDLWyllRLANRAVLEALSAPPGPVH 157
|
....
gi 1334564377 168 VDLP 171
Cdd:cd07037 158 LNLP 161
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
428-557 |
2.63e-12 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 66.17 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 428 GLGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQDMIYSGR------ 501
Cdd:cd02003 46 GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSfgtefr 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334564377 502 -----HSQSYMQSLP-DFVRLAEAYGHVGLQINRPDELESKLSEALEHvrnNRLVFVDVTVD 557
Cdd:cd02003 126 drdqeSGQLDGALLPvDFAANARSLGARVEKVKTIEELKAALAKAKAS---DRTTVIVIKTD 184
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
21-484 |
4.33e-10 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 62.41 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 21 RSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGdVGVVLVTSGPGATNAITGIATAYM 100
Cdd:PLN02573 24 RRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGAYS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 101 DSIPLVILSG----------QVATSLIGYDAF-QE--CdmvgiSRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVV 167
Cdd:PLN02573 103 ENLPVICIVGgpnsndygtnRILHHTIGLPDFsQElrC-----FQTVTCYQAVINNLEDAHELIDTAI-STALKESKPVY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 168 V----DLPkDILNPA---KKMPYAWPETVSmrsyNPTtsGHKGQIKRALQTLASAKKPVVyVGGGAI--SAACYAPLRhI 238
Cdd:PLN02573 177 IsvscNLA-AIPHPTfsrEPVPFFLTPRLS----NKM--SLEAAVEAAAEFLNKAVKPVL-VGGPKLrvAKACKAFVE-L 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 239 IEIFNLPVVSSLMGLGAFPATHRQSLGML-GMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPT 317
Cdd:PLN02573 248 ADASGYPVAVMPSAKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 318 SIsktvnADIPVVGdaRLVLEQMLELLAQDApsQPQDDIRDWWQQIEIwRARQCLKyDAESESIKPQAVIETLWRLTKGD 397
Cdd:PLN02573 328 TI-----GNGPAFG--CVLMKDFLEALAKRV--KKNTTAYENYKRIFV-PEGEPLK-SEPGEPLRVNVLFKHIQKMLSGD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 398 AYVTSDVGQhqmfaalyypfdkprRWINSGGL--------------GTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMN 463
Cdd:PLN02573 397 TAVIAETGD---------------SWFNCQKLklpegcgyefqmqyGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVT 461
|
490 500
....*....|....*....|.
gi 1334564377 464 IQELSTALQYELPVLVLNLNN 484
Cdd:PLN02573 462 AQDVSTMIRCGQKSIIFLINN 482
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
429-572 |
8.68e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 49.83 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 429 LGTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTalqyelpvlVLNLNNRYLGMVkQWQDMIYSGRHSQSYMQ 508
Cdd:PRK06163 56 LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGT---------IAALAPKNLTII-VMDNGVYQITGGQPTLT 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334564377 509 S-LPDFVRLAEAYGHVGLQ-INRPDELESKLSEALehvRNNRLVFVDVTVD-----GSEHVYPMQIRGGGM 572
Cdd:PRK06163 126 SqTVDVVAIARGAGLENSHwAADEAHFEALVDQAL---SGPGPSFIAVRIDdkpgvGTTERDPAQIRERFM 193
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
385-489 |
1.03e-05 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440637 [Multi-domain] Cd Length: 262 Bit Score: 47.45 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 385 AVIETLWRLTKGD-AYVTSDVGQHqmfAALYYPFDKPrrWINSgglgTMGFGLPAALGVKMALPKEMVVCVTGDG---SI 460
Cdd:COG1013 27 LLLKALDELLDGDkTVVVSGIGCS---SVAPGYFNVP--GFHT----LHGRAAAVATGIKLANPDLTVIVFGGDGdtyDI 97
|
90 100 110
....*....|....*....|....*....|
gi 1334564377 461 QMNiqELSTALQYELPVLVLNLNNR-YlGM 489
Cdd:COG1013 98 GGN--HLIHAARRNEDITYIVYDNEiY-GN 124
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
385-543 |
1.28e-05 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 46.12 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 385 AVIETLWRLTKGDAYVTSDVGQHQMFAAlyypfdKPRRWINsgGLGTMGFGLPAALGVKMALPKEMVVCVTGDGS-IQMN 463
Cdd:cd02008 14 PSFYALRKAFKKDSIVSGDIGCYTLGAL------PPLNAID--TCTCMGASIGVAIGMAKASEDKKVVAVIGDSTfFHSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 464 IQELSTALQYELPVLVLNLNNRYLGMVKQwQDMIYSGrHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELES---KLSEA 540
Cdd:cd02008 86 ILGLINAVYNKANITVVILDNRTTAMTGG-QPHPGTG-KTLTEPTTVIDIEALVRAIGVKRVVVVDPYDLKAireELKEA 163
|
...
gi 1334564377 541 LEH 543
Cdd:cd02008 164 LAV 166
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
413-541 |
5.68e-05 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 43.63 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 413 LYYPFDKPRRWINsggLGTMGFGLPAALGVKMALPKEMVVcVTGDGSIQMNIQELSTALQYE-LPVLVLNLNNRylgmvk 491
Cdd:cd02001 28 LYDVQDRDGHFYM---LGSMGLAGSIGLGLALGLSRKVIV-VDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNR------ 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1334564377 492 qwqdmIYSGRHSQSYMQSLPDFVRLAEAYGHVGLQINRPDELESKLSEAL 541
Cdd:cd02001 98 -----AYGSTGGQPTPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLL 142
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
413-542 |
6.25e-05 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 43.82 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 413 LYYPFDKPRrwiNSGGLGTMGFGLPAALGVKMALPKEmVVCVTGDGSIQMNIQELSTALQyELP---VLVLnLNNRylgm 489
Cdd:cd03372 28 LYAAGDRPL---NFYMLGSMGLASSIGLGLALAQPRK-VIVIDGDGSLLMNLGALATIAA-EKPknlIIVV-LDNG---- 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1334564377 490 vkqwqdmIYSGRHSQ-SYMQSLPDFVRLAEAYG-HVGLQINRPDELESKLSEALE 542
Cdd:cd03372 98 -------AYGSTGNQpTHAGKKTDLEAVAKACGlDNVATVASEEAFEKAVEQALD 145
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
424-491 |
2.54e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 43.29 E-value: 2.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1334564377 424 INSGGL-GTMGFGLPAALGVKMALPKEMVVCVTGDG---SIQMN--IQelstALQYELPVLVLNLNNRYLGMVK 491
Cdd:PRK11867 62 INTYGFhTIHGRALAIATGLKLANPDLTVIVVTGDGdalAIGGNhfIH----ALRRNIDITYILFNNQIYGLTK 131
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
430-556 |
3.09e-04 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 41.91 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 430 GTMGFGLPAALGVKMALPKEMVVCVTGDGSIQMNIQELSTALQYELPVLV-LNLNNRYLGMVkqwqdmiySGRHSQSYMQ 508
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPANLIhIVLNNGAHDSV--------GGQPTVSFDV 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1334564377 509 SLPDFVRlAEAYGHVgLQINRPDELESKLSEALehvRNNRLVFVDVTV 556
Cdd:cd03371 120 SLPAIAK-ACGYRAV-YEVPSLEELVAALAKAL---AADGPAFIEVKV 162
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
424-491 |
5.74e-04 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 41.36 E-value: 5.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334564377 424 INSGGL-GTMGFGLPAALGVKMALPKEMVVCVTGDG---SIQMNiqELSTALQYELPVLVLNLNNRYLGMVK 491
Cdd:cd03375 44 FNTYGFhTLHGRALAVATGVKLANPDLTVIVVSGDGdlaAIGGN--HFIHAARRNIDITVIVHNNQIYGLTK 113
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| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
15-120 |
8.12e-04 |
|
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, 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. 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 of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate.
Pssm-ID: 132917 [Multi-domain] Cd Length: 160 Bit Score: 40.18 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 15 GAEMVVRSLIDQGVKQVFGYPG---GAVLDIYDAlHTVGGIDHVLVR--HEQAAVHMADGlARATGDVGVVlVTSGPGAT 89
Cdd:cd07034 1 GNEAVARGALAAGVDVVAAYPItpsTEIAETLAK-AVLGELGGVVVQaeSEHAAAEAAIG-ASAAGARAMT-ATSGPGLN 77
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90 100 110
....*....|....*....|....*....|....
gi 1334564377 90 NAITGIATAYMDSIPLVILSGQ---VATSLIGYD 120
Cdd:cd07034 78 LMAEALYLAAGAELPLVIVVAQrpgPSTGLPKPD 111
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| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
438-548 |
1.66e-03 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 40.89 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 438 AALGVKMALPKEMVVCVTGDGSiqMNIQELSTALQ----YELPVLVLNLNNRYlgmvkqwqdMIYSGRHSQSymqSLPDF 513
Cdd:COG1071 139 AALAAKLRGEDEVAVAFFGDGA--TSEGDFHEALNfaavWKLPVVFVCENNGY---------AISTPVERQT---AVETI 204
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90 100 110
....*....|....*....|....*....|....*..
gi 1334564377 514 VRLAEAYGHVGLQI--NRPDELESKLSEALEHVRNNR 548
Cdd:COG1071 205 ADRAAGYGIPGVRVdgNDVLAVYAAVKEAVERARAGE 241
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| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
438-548 |
5.47e-03 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 39.02 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334564377 438 AALGVKMALPKEMVVCVTGDGSIQ-------MNIqelstALQYELPVLVLNLNNRY-LGMvkqwqdmiysgrhSQSYMQS 509
Cdd:cd02000 116 AALALKYRGEDRVAVCFFGDGATNegdfheaLNF-----AALWKLPVIFVCENNGYaIST-------------PTSRQTA 177
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90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1334564377 510 LPDFVRLAEAYGHVGLQI--NRPDELESKLSEALEHVRNNR 548
Cdd:cd02000 178 GTSIADRAAAYGIPGIRVdgNDVLAVYEAAKEAVERARAGG 218
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|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
424-491 |
6.13e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 39.09 E-value: 6.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334564377 424 INSGGL-GTMGFGLPAALGVKMALPKEMVVCVTGDG---SIQMNiqELSTALQYELPVLVLNLNNRYLGMVK 491
Cdd:PRK05778 63 FLSHGLhTLHGRAIAFATGAKLANPDLEVIVVGGDGdlaSIGGG--HFIHAGRRNIDITVIVENNGIYGLTK 132
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