|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
29-602 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 1217.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 29 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 108
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 109 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 188
Cdd:PRK07979 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 189 LPKDILNPANKLPYVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSS 268
Cdd:PRK07979 161 LPKDILNPANKLPYVWPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 269 LMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 348
Cdd:PRK07979 241 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 349 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQM 428
Cdd:PRK07979 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 429 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 508
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 509 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRG 588
Cdd:PRK07979 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRG 560
|
570
....*....|....
gi 344915208 589 GGMDEMWLSKTERT 602
Cdd:PRK07979 561 GGMDEMWLSKTERT 574
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
29-602 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 1117.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 29 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 108
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 109 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 188
Cdd:PRK08979 81 NTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 189 LPKDILNPANKLPYVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSS 268
Cdd:PRK08979 161 LPKDCLNPAILHPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 269 LMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 348
Cdd:PRK08979 241 LMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 349 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQM 428
Cdd:PRK08979 321 VGSADKVLDSMLALLDESGETNDEAAIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 429 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 508
Cdd:PRK08979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 509 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrNNRLVFVDVTVDGSEHVYPMQIRG 588
Cdd:PRK08979 481 VKQWQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAM--KDRLVFVDINVDETEHVYPMQIRG 558
|
570
....*....|....
gi 344915208 589 GGMDEMWLSKTERT 602
Cdd:PRK08979 559 GAMNEMWLSKTERT 572
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
32-598 |
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: 1046.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 32 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 111
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 112 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 191
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 192 DILNPANKLPYvcPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLMG 271
Cdd:TIGR00118 161 DVTTAEIEYPY--PEKVNLPGYRPTVKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 272 MGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGD 351
Cdd:TIGR00118 239 LGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 352 ARQVLEQMLELLSQESahqPLDEIrDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQMFAA 431
Cdd:TIGR00118 319 ARNVLEELLKKLFELK---ERKES-AWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 432 LYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQ 511
Cdd:TIGR00118 395 QFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 512 WQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSEHVYPMQIRGGGM 591
Cdd:TIGR00118 475 WQELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSS---NEPVLLDVVVDKPENVLPMVAPGGGL 551
|
....*..
gi 344915208 592 DEMWLSK 598
Cdd:TIGR00118 552 DEMIGEK 558
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
29-602 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 1003.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 29 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 108
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 109 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 188
Cdd:PRK06882 81 NAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 189 LPKDILNPANKLPYVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSS 268
Cdd:PRK06882 161 IPKDMVNPANKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 269 LMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 348
Cdd:PRK06882 241 LMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 349 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQM 428
Cdd:PRK06882 321 VGSAKNVLEEFLSLLEEENLAKSQTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 429 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 508
Cdd:PRK06882 401 FAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 509 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrNNRLVFVDVTVDGSEHVYPMQIRG 588
Cdd:PRK06882 481 VKQWQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSI--KDKLVFVDVNVDETEHVYPMQIRG 558
|
570
....*....|....
gi 344915208 589 GGMDEMWLSKTERT 602
Cdd:PRK06882 559 GAMNEMILSKPEET 572
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
29-602 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 996.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 29 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 108
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 109 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 188
Cdd:PRK06466 81 NAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 189 LPKDILNPANKLPYVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSS 268
Cdd:PRK06466 161 IPKDMTNPAEKFEYEYPKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 269 LMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 348
Cdd:PRK06466 241 LMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 349 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRALQCL-KYDTHS-EKIKPQAVIETLWRLTNGDAYVTSDVGQH 426
Cdd:PRK06466 321 VGPVESVLTEMLAILKEIGEKPDKEALAAWWKQIDEWRGRHGLfPYDKGDgGIIKPQQVVETLYEVTNGDAYVTSDVGQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 427 QMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYL 506
Cdd:PRK06466 401 QMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 507 GMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrNNRLVFVDVTVDGSEHVYPMQI 586
Cdd:PRK06466 481 GMVRQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAM--KDRLVFIDIYVDRSEHVYPMQI 558
|
570
....*....|....*.
gi 344915208 587 RGGGMDEMWLSKTERT 602
Cdd:PRK06466 559 ADGSMRDMWLSKTERT 574
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
32-596 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 829.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 32 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 111
Cdd:PRK06965 21 SIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 112 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 191
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 192 DIlnPANKLPYVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLMG 271
Cdd:PRK06965 181 DV--SKTPCEYEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 272 MGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNA-TVLHIDIDPTSISKTVTADIPIVG 350
Cdd:PRK06965 259 LGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRVKVDIPIVG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 351 DARQVLEQMLELLsQESAHQP-LDEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQMF 429
Cdd:PRK06965 339 DVKEVLKELIEQL-QTAEHGPdADALAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMW 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 430 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 509
Cdd:PRK06965 418 AAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMV 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 510 KQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrNNRLVFVDVTVDGSEHVYPMQIRGG 589
Cdd:PRK06965 498 RQWQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRL--KDRTVFLDFQTDPTENVWPMVQAGK 575
|
....*..
gi 344915208 590 GMDEMWL 596
Cdd:PRK06965 576 GITEMLL 582
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
30-594 |
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: 782.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 30 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 109
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 110 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 189
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 190 PKDILnpANKLPYVcPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSL 269
Cdd:COG0028 161 PKDVQ--AAEAEEE-PAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 270 MGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIV 349
Cdd:COG0028 238 MGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 350 GDARQVLEQMLELLSQESahqplDEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQMF 429
Cdd:COG0028 318 GDAKAVLAALLEALEPRA-----DDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 430 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 509
Cdd:COG0028 393 AARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 510 KQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHvypmqIRGG 589
Cdd:COG0028 473 RQWQELFYGGRYSGTDLPN-PDFAKLAEAFGAKGERVETPEELEAALEEALA---SDGPALIDVRVDPEEN-----PPGA 543
|
....*
gi 344915208 590 GMDEM 594
Cdd:COG0028 544 TLDEM 548
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
22-596 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 768.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 22 RQTVRQAMEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLV 101
Cdd:PRK09107 1 SAQKSHMPRQMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 102 TSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGR 181
Cdd:PRK09107 81 TSGPGATNAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 182 PGPVVVDLPKDILNPANKlpYVCP-ESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCH--QQLKETV 258
Cdd:PRK09107 161 PGPVVVDIPKDVQFATGT--YTPPqKAPVHVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVINSGPEasRLLRELV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 259 EALNLPVVSSLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSI 338
Cdd:PRK09107 239 ELTGFPITSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 339 SKTVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNG-DA 417
Cdd:PRK09107 319 NKNVRVDVPIIGDVGHVLEDMLRLWKARGKKPDKEALADWWGQIARWRARNSLAYTPSDDVIMPQYAIQRLYELTKGrDT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 418 YVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVL 497
Cdd:PRK09107 399 YITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 498 VVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLseaLEQVRNNRLVFVDVTVDG 577
Cdd:PRK09107 479 IFILNNQYMGMVRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAI---QEMIDVDKPVIFDCRVAN 555
|
570
....*....|....*....
gi 344915208 578 SEHVYPMQIRGGGMDEMWL 596
Cdd:PRK09107 556 LENCFPMIPSGKAHNEMLL 574
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
32-601 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 751.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 32 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 111
Cdd:PRK08527 3 LSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 112 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 191
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 192 DILNPANKLPYvcPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLMG 271
Cdd:PRK08527 163 DVTATLGEFEY--PKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 272 MGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGD 351
Cdd:PRK08527 241 RGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 352 ARQVLEQMLELLSQESAhqplDEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQMFAA 431
Cdd:PRK08527 321 LKNVLKEMLEELKEENP----TTYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 432 LYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQ 511
Cdd:PRK08527 397 QFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 512 WQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSEHVYPMQIRGGGM 591
Cdd:PRK08527 477 WQTFFYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALES---DKVALIDVKIDRFENVLPMVPAGGAL 553
|
570
....*....|
gi 344915208 592 DEMWLSKTER 601
Cdd:PRK08527 554 YNMILPKKKD 563
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
29-594 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 683.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 29 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 108
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 109 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 188
Cdd:PRK06048 84 NLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLID 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 189 LPKDILNPANKLPYvcPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSS 268
Cdd:PRK06048 164 LPKDVTTAEIDFDY--PDKVELRGYKPTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 269 LMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 348
Cdd:PRK06048 242 LMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 349 VGDARQVLEQMLELLSQESAhqpldeiRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNgDAYVTSDVGQHQM 428
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDR-------KEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 429 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 508
Cdd:PRK06048 394 WAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 509 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHVYPMQIRG 588
Cdd:PRK06048 474 VRQWQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVA---SDRPVVIDFIVECEENVSPMVPAG 550
|
....*.
gi 344915208 589 GGMDEM 594
Cdd:PRK06048 551 AAINEI 556
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
27-584 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 681.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 27 QAMEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTV---GGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTS 103
Cdd:PRK07418 14 VTPQRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAeaeGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 104 GPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPG 183
Cdd:PRK07418 94 GPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 184 PVVVDLPKDI-LNPANKLPyVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALN 262
Cdd:PRK07418 174 PVLIDIPKDVgQEEFDYVP-VEPGSVKPPGYRPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 263 LPVVSSLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTV 342
Cdd:PRK07418 253 IPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 343 TADIPIVGDARQVLEQMLElLSQESAHQPldEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNgDAYVTSD 422
Cdd:PRK07418 333 RPDVPIVGDVRKVLVKLLE-RSLEPTTPP--RTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAP-DAYYTTD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 423 VGQHQMFAALYYPfDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLN 502
Cdd:PRK07418 409 VGQHQMWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIIN 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 503 NRYLGMVKQWQDMIYSGRHSQSYMQ-SLPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHV 581
Cdd:PRK07418 488 NGWQGMVRQWQESFYGERYSASNMEpGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALA---HDGPVLIDVHVRRDENC 564
|
...
gi 344915208 582 YPM 584
Cdd:PRK07418 565 YPM 567
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
22-593 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 667.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 22 RQTVRQAMEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLV 101
Cdd:PRK07789 21 ARPRIVAPERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 102 TSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGR 181
Cdd:PRK07789 101 TSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 182 PGPVVVDLPKDILNpaNKLPYVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEAL 261
Cdd:PRK07789 181 PGPVLVDIPKDALQ--AQTTFSWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 262 NLPVVSSLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKT 341
Cdd:PRK07789 259 GIPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 342 VTADIPIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRALQCLKYDTHSE-KIKPQAVIETLWRLTNGDAYVT 420
Cdd:PRK07789 339 RHADVPIVGDVKEVIAELIAALRAEHAAGGKPDLTAWWAYLDGWRETYPLGYDEPSDgSLAPQYVIERLGEIAGPDAIYV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 421 SDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVN 500
Cdd:PRK07789 419 AGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVAL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 501 LNNRYLGMVKQWQDMIYSGRHSQSYMQS----LPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrNNRLVFVDVTVD 576
Cdd:PRK07789 499 INNGNLGMVRQWQTLFYEERYSNTDLHThshrIPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAI--NDRPVVIDFVVG 576
|
570
....*....|....*..
gi 344915208 577 GSEHVYPMQIRGGGMDE 593
Cdd:PRK07789 577 KDAMVWPMVAAGTSNDE 593
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
32-594 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 663.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 32 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 111
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 112 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 191
Cdd:PRK06276 80 TGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 192 DILNPANKLP-YVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLM 270
Cdd:PRK06276 160 DVQEGELDLEkYPIPAKIDLPGYKPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 271 GMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVG 350
Cdd:PRK06276 240 GKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 351 DARQVLEQMLELLSQESahqpLDEIRDWWQQIEQWRAlQCLKYDTHSEK-IKPQAVIETLW-----RLTNGDAYVTSDVG 424
Cdd:PRK06276 320 DAKNVLRDLLAELMKKE----IKNKSEWLERVKKLKK-ESIPRMDFDDKpIKPQRVIKELMevlreIDPSKNTIITTDVG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 425 QHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNR 504
Cdd:PRK06276 395 QNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 505 YLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALeqvRNNRLVFVDVTVDGSEhVYPM 584
Cdd:PRK06276 475 TLGMVYQWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAI---KSGEPYLLDIIIDPAE-ALPM 550
|
570
....*....|
gi 344915208 585 QIRGGGMDEM 594
Cdd:PRK06276 551 VPPGGNLTNI 560
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
30-594 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 643.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 30 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 109
Cdd:PRK07710 14 KLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 110 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 189
Cdd:PRK07710 93 VVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 190 PKDILNPANKLPYvcPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSL 269
Cdd:PRK07710 173 PKDMVVEEGEFCY--DVQMDLPGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 270 MGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIV 349
Cdd:PRK07710 251 LGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 350 GDARQVLEQMLELLSQESAHQpldeirDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQMF 429
Cdd:PRK07710 331 ADAKQALQVLLQQEGKKENHH------EWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 430 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 509
Cdd:PRK07710 405 AAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 510 KQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHVYPMQIRGG 589
Cdd:PRK07710 485 RQWQEEFYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIE---LQEPVVIDCRVLQSEKVMPMVAPGK 561
|
....*
gi 344915208 590 GMDEM 594
Cdd:PRK07710 562 GLHEM 566
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
30-600 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 631.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 30 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 109
Cdd:PRK06725 13 EEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 110 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 189
Cdd:PRK06725 92 LVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 190 PKDILNpaNKLPYVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSL 269
Cdd:PRK06725 172 PKDVQN--EKVTSFYNEVVEIPGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 270 MGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIV 349
Cdd:PRK06725 250 MGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 350 GDARQVLEQMLellsQESAHQPLDEirdWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQMF 429
Cdd:PRK06725 330 GDVKKALHMLL----HMSIHTQTDE---WLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMW 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 430 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 509
Cdd:PRK06725 403 AAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 510 KQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHVYPMQIRGG 589
Cdd:PRK06725 483 RQWQEMFYENRLSESKIGS-PDFVKVAEAYGVKGLRATNSTEAKQVMLEAFA---HEGPVVVDFCVEEGENVFPMVPPNK 558
|
570
....*....|.
gi 344915208 590 GMDEMWLSKTE 600
Cdd:PRK06725 559 GNNEMIMKRWE 569
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
33-584 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 621.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 33 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHT---VGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 109
Cdd:CHL00099 11 TGAFALIDSLVRHGVKHIFGYPGGAILPIYDELYAwekKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 110 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 189
Cdd:CHL00099 91 LVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 190 PKDIlnPANKLPYVCPES----VSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPV 265
Cdd:CHL00099 171 PKDV--GLEKFDYYPPEPgntiIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 266 VSSLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTAD 345
Cdd:CHL00099 249 TTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 346 IPIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNgDAYVTSDVGQ 425
Cdd:CHL00099 329 VAIVGDVKKVLQELLELLKNSPNLLESEQTQAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQLAP-DAYFTTDVGQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 426 HQMFAALYYPFdKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRY 505
Cdd:CHL00099 408 HQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKW 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 506 LGMVKQWQDMIYSGRHSQSYMQS-LPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSEHVYPM 584
Cdd:CHL00099 487 QGMVRQWQQAFYGERYSHSNMEEgAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDY---DGPVLIDCQVIEDENCYPM 563
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
33-594 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 612.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 33 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 112
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 113 GIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKD 192
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 193 IlnPANKLPYVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLMGM 272
Cdd:PRK07282 171 V--SALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 273 GAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDA 352
Cdd:PRK07282 249 GTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 353 RQVLEQMLELLSQESAHqpldeiRDWWQQIEQWRAlQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQMFAAL 432
Cdd:PRK07282 329 KKALQMLLAEPTVHNNT------EKWIEKVTKDKN-RVRSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 433 YYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQW 512
Cdd:PRK07282 402 YYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 513 QDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELEsklsEALEQVRNNRLVFVDVTVDGSEHVYPMQIRGGGMD 592
Cdd:PRK07282 482 QESFYEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLA----QDLEVITEDVPMLIEVDISRKEHVLPMVPAGKSNH 557
|
..
gi 344915208 593 EM 594
Cdd:PRK07282 558 EM 559
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
34-594 |
0e+00 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 604.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 34 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 113
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 114 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 193
Cdd:PRK08978 82 LADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 194 -LNPANKLPYVCPESvsmrsynPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLMGM 272
Cdd:PRK08978 162 qLAEGELEPHLTTVE-------NEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 273 GAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDA 352
Cdd:PRK08978 235 GAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 353 RQVLEQMlellsqesaHQPLDeIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQMFAAL 432
Cdd:PRK08978 315 NALLPAL---------QQPLN-IDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 433 YYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQW 512
Cdd:PRK08978 385 HMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 513 QDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSEHVYPMQIRGGGMD 592
Cdd:PRK08978 465 QQLFFDERYSETDLSDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNS---EGPYLLHVSIDELENVWPLVPPGASNS 541
|
..
gi 344915208 593 EM 594
Cdd:PRK08978 542 EM 543
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
27-594 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 545.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 27 QAMEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPG 106
Cdd:PRK08155 8 STRKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 107 ATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVV 186
Cdd:PRK08155 88 ATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 187 VDLPKDILN--------PANKLPYVCPEsVSMRSynptttghkgqIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETV 258
Cdd:PRK08155 168 IDIPKDVQTavielealPAPAEKDAAPA-FDEES-----------IRDAAAMINAAKRPVLYLGGGVINSGAPARARELA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 259 EALNLPVVSSLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSI 338
Cdd:PRK08155 236 EKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAEL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 339 SKTVTADIPIVGDARQVLEQMLELLsqesAHQPLDEirdWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAY 418
Cdd:PRK08155 316 GKIKQPHVAIQADVDDVLAQLLPLV----EAQPRAE---WHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 419 VTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLV 498
Cdd:PRK08155 389 ITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 499 VNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALeqvrnNRL--VFVDVTVD 576
Cdd:PRK08155 469 ILMNNEALGLVHQQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAI-----NRPgpALIHVRID 543
|
570
....*....|....*...
gi 344915208 577 GSEHVYPMQIRGGGMDEM 594
Cdd:PRK08155 544 AEEKVYPMVPPGAANTEM 561
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
34-590 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 537.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 34 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 113
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 114 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 193
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 194 --------LNPANKLP-YVcpesvsMRSYNPTTTGHKGQIKRALQTlvaAKKPVVYVGGGAIMAGchQQLKETVEALNLP 264
Cdd:PLN02470 175 qqqlavpnWNQPMKLPgYL------SRLPKPPEKSQLEQIVRLISE---SKRPVVYVGGGCLNSS--EELREFVELTGIP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 265 VVSSLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTA 344
Cdd:PLN02470 244 VASTLMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 345 DIPIVGDARQVLEQMLELLSQESAHQPldEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVG 424
Cdd:PLN02470 324 HVSVCADVKLALQGLNKLLEERKAKRP--DFSAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 425 QHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNR 504
Cdd:PLN02470 402 QHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 505 YLGMVKQWQDMIYSGRHSQSYMQS-------LPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRLvfvDVTVDG 577
Cdd:PLN02470 482 HLGMVVQWEDRFYKANRAHTYLGDpdaeaeiFPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLL---DVIVPH 558
|
570
....*....|...
gi 344915208 578 SEHVYPMqIRGGG 590
Cdd:PLN02470 559 QEHVLPM-IPGGG 570
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
31-597 |
2.83e-144 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 429.64 E-value: 2.83e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 31 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDAL---HTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGA 107
Cdd:PRK06456 1 MPTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 108 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 187
Cdd:PRK06456 81 TNLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 188 DLPKDILNpaNKLPYV-CPESVSMRSYNP-TTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPV 265
Cdd:PRK06456 161 DIPRDIFY--EKMEEIkWPEKPLVKGYRDfPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 266 VSSLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPN-ATVLHIDIDPTSISKTVTA 344
Cdd:PRK06456 239 VSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVNIDPTDGEKAIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 345 DIPIVGDARQVLEQMLELL-------SQESAHQPLDEIRDWWQQieqwralqcLKYDTHSEKIKPQAVIETLWRLTNGDA 417
Cdd:PRK06456 319 DVGIYGNAKIILRELIKAItelgqkrDRSAWLKRVKEYKEYYSQ---------FYYTEENGKLKPWKIMKTIRQALPRDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 418 YVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVL 497
Cdd:PRK06456 390 IVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 498 VVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDG 577
Cdd:PRK06456 470 SVIFDNRTLGLVRQVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKE---DIPAVIRVPVDK 546
|
570 580
....*....|....*....|
gi 344915208 578 SEHVYPMQIRGGGMDEMWLS 597
Cdd:PRK06456 547 EELALPTLPPGGRLKQVILR 566
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
29-573 |
3.37e-131 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 396.66 E-value: 3.37e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 29 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARAT-GEVGVVLVTSGPGA 107
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 108 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 187
Cdd:PRK11269 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 188 DLPKDI------LNPANKLPyvcpesvsMRSYNPTTTghKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEAL 261
Cdd:PRK11269 161 DLPFDVqvaeieFDPDTYEP--------LPVYKPAAT--RAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 262 NLPVVSSLMGMGAFPATHRQALGMLGMHGTYE-ANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISK 340
Cdd:PRK11269 231 GVPVIPTLMGWGAIPDDHPLMAGMVGLQTSHRyGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 341 TVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVT 420
Cdd:PRK11269 311 VFGPDLGIVSDAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 421 SDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVN 500
Cdd:PRK11269 391 STIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 501 LNNRYLGMVKQWQ---DMIY------SGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRL-VF 570
Cdd:PRK11269 471 VNNAYLGLIRQAQrafDMDYcvqlafENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALEQAKALMAEFRVpVV 550
|
...
gi 344915208 571 VDV 573
Cdd:PRK11269 551 VEV 553
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
34-579 |
1.45e-110 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 341.81 E-value: 1.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 34 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 113
Cdd:PRK08322 3 AADLFVKCLENEGVEYIFGIPGEENLDLLEALRD-SSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 114 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 193
Cdd:PRK08322 82 VAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 194 ---LNPANKLPyvcpesvsmRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLM 270
Cdd:PRK08322 162 aaeETDGKPLP---------RSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 271 GMGAFPATHRQALGMLG-MHGTYEaNMTMHNADVIFAVG---VRFDDRttnnlaKYCPNA--TVLHIDIDPTSISKTVTA 344
Cdd:PRK08322 233 GKGVIPETHPLSLGTAGlSQGDYV-HCAIEHADLIINVGhdvIEKPPF------FMNPNGdkKVIHINFLPAEVDPVYFP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 345 DIPIVGDARQVLEQMLELLSqESAHQPLDEIRDWWQQIEQwralqclKYDTHSEK----IKPQAVIETLWRLTNGDAYVT 420
Cdd:PRK08322 306 QVEVVGDIANSLWQLKERLA-DQPHWDFPRFLKIREAIEA-------HLEEGADDdrfpMKPQRIVADLRKVMPDDDIVI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 421 SDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVN 500
Cdd:PRK08322 378 LDNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 501 LNNRYLGMVKqWQDMIYSGRHsqSYMQ-SLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSE 579
Cdd:PRK08322 458 LNDNAYGMIR-WKQENMGFED--FGLDfGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQ---PGVHVIDCPVDYSE 531
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
29-579 |
6.46e-108 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 335.06 E-value: 6.46e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 29 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLV-RHEQAAVHMADGLARATGEVGVVLVTSGPGA 107
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHtRHEQAAGYMAFGYARSTGRPGVCSVVPGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 108 TNAITGIATAYMDSIPLVVLSGQVATSLI--GYDAFQEC-DMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGP 184
Cdd:PRK08266 81 LNAGAALLTAYGCNSPVLCLTGQIPSALIgkGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 185 VVVDLPKDILN------PANKLPYVCPESVsmrsyNPTttghkgQIKRALQTLVAAKKPVVYVGGGAIMAGchQQLKETV 258
Cdd:PRK08266 161 VALEMPWDVFGqrapvaAAPPLRPAPPPAP-----DPD------AIAAAAALIAAAKNPMIFVGGGAAGAG--EEIRELA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 259 EALNLPVVSSLMGMGAFPATHRQALGMLGmhgtyeANMTMHNADVIFAVGVRFDDRTTNnlAKYCP-NATVLHIDIDPTS 337
Cdd:PRK08266 228 EMLQAPVVAFRSGRGIVSDRHPLGLNFAA------AYELWPQTDVVIGIGSRLELPTFR--WPWRPdGLKVIRIDIDPTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 338 ISKTvTADIPIVGDARQVLEQMLELLSQESAHQP-----LDEIRDWWQQieqwralqclkydtHSEKIKPQ-----AVIE 407
Cdd:PRK08266 300 MRRL-KPDVAIVADAKAGTAALLDALSKAGSKRPsrraeLRELKAAARQ--------------RIQAVQPQasylrAIRE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 408 TLWRltngDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELS 487
Cdd:PRK08266 365 ALPD----DGIFVDELSQVGFASWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 488 TALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALeqvRNNR 567
Cdd:PRK08266 441 TAVQHNIGVVTVVFNNNAYGNVRRDQKRRFGGRVVASDLVN-PDFVKLAESFGVAAFRVDSPEELRAALEAAL---AHGG 516
|
570
....*....|...
gi 344915208 568 LVFVDVTV-DGSE 579
Cdd:PRK08266 517 PVLIEVPVpRGSE 529
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
400-584 |
6.08e-107 |
|
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: 319.44 E-value: 6.08e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 400 IKPQAVIETLWRLTNGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSI 479
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 480 QMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEA 559
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|....*
gi 344915208 560 LEqvrNNRLVFVDVTVDGSEHVYPM 584
Cdd:cd02015 161 LA---SDGPVLLDVLVDPEENVLPM 182
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
27-561 |
2.11e-106 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 331.45 E-value: 2.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 27 QAMEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPG 106
Cdd:PRK08199 3 STPRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 107 ATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVV 186
Cdd:PRK08199 83 ATNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 187 VDLPKDIL----NPANKLPYVCPEsvsmrsynptTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALN 262
Cdd:PRK08199 163 LALPEDVLsetaEVPDAPPYRRVA----------AAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 263 LPVVSSLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNN---LAKYCPNATVLHIDIDPTSIS 339
Cdd:PRK08199 233 LPVACAFRRQDLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 340 KTVTADIPIVGDARQVLEQMLELlsqESAHQP--LDEIRDWWQQIEQWRALQCLKYDTHSEkikpqAVIETLWRLTNGDA 417
Cdd:PRK08199 313 RVYRPDLAIVADPAAFAAALAAL---EPPASPawAEWTAAAHADYLAWSAPLPGPGAVQLG-----EVMAWLRERLPADA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 418 YVTSDVGQHQMFAALYYPFDKPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVL 497
Cdd:PRK08199 385 IITNGAGNYATWLHRFFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPII 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 344915208 498 VVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALE 561
Cdd:PRK08199 464 VIVVNNGMYGTIRMHQEREYPGRVSGTDLTN-PDFAALARAYGGHGETVERTEDFAPAFERALA 526
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
35-577 |
4.70e-100 |
|
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: 315.65 E-value: 4.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 35 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDaLHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 114
Cdd:TIGR03457 5 SEAFVEVLVANGVTHAFGIMGSAFMDAMD-LFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 115 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKDIL 194
Cdd:TIGR03457 84 AAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRDYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 195 npANKLPYVCPESVSMRSynptTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLMGMGA 274
Cdd:TIGR03457 163 --YGEIDVEIPRPVRLDR----GAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 275 FPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTT--NNLAKYCP-NATVLHIDIDPTSISKTVTADIPIVGD 351
Cdd:TIGR03457 237 FPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLGPFGTlpQYGIDYWPkNAKIIQVDANAKMIGLVKKVTVGICGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 352 ARQVLEQMLELL-------SQESAHQPLDEIR-DWWQQIEQW---RALQCLKYDTHSEK-----IKPQAVIETLWRLTNG 415
Cdd:TIGR03457 317 AKAAAAEILQRLagkagdaNRAERKAKIQAERsAWEQELSEMtheRDPFSLDMIVEQRQeegnwLHPRQVLRELEKAMPE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 416 DAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELP 495
Cdd:TIGR03457 397 DAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 496 VLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRLVFVDVTV 575
Cdd:TIGR03457 477 VTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQAEGKTTVIEIVC 556
|
..
gi 344915208 576 DG 577
Cdd:TIGR03457 557 TR 558
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
29-589 |
1.82e-98 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 311.55 E-value: 1.82e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 29 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTV-GGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGA 107
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 108 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVV 187
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 188 DLPKDILNPANKLPYVCPeSVSMRSYNPTTtgHKGQIKRALQTLVAAKKPVVYVGGGAIMAGchQQLKETVEALNLPVVS 267
Cdd:PRK08611 160 TIPDDLPAQKIKDTTNKT-VDTFRPTVPSP--KPKDIKKAAKLINKAKKPVILAGLGAKHAK--EELLAFAEKAKIPIIH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 268 SLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRttnnlaKYCPN-ATVLHIDIDPTSISKTVTADI 346
Cdd:PRK08611 235 TLPAKGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPKkAKAIQIDTDPANIGKRYPVNV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 347 PIVGDARQVLEQMLELLSQESAHQPLDEIRD----WWQQIEQWRALQclkydthSEKIKPQAVIETLWRLTNGDAYVTSD 422
Cdd:PRK08611 309 GLVGDAKKALHQLTENIKHVEDRRFLEACQEnmakWWKWMEEDENNA-------STPIKPERVMAAIQKIADDDAVLSVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 423 VGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLN 502
Cdd:PRK08611 382 VGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 503 NRYLGMVKQWQdmiysgrhsQS-----YMQSL--PDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTV 575
Cdd:PRK08611 462 NQQLAFIKYEQ---------QAageleYAIDLsdMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQ---DKPVIIDVYV 529
|
570
....*....|....
gi 344915208 576 DGSEHVYPMQIRGG 589
Cdd:PRK08611 530 DPNAAPLPGKIVND 543
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
29-573 |
1.44e-94 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 301.53 E-value: 1.44e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 29 MEMlSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDaLHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 108
Cdd:PRK07525 4 MKM-TPSEAFVETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 109 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVD 188
Cdd:PRK07525 82 NFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 189 LPKDILnpanklpY-VCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVS 267
Cdd:PRK07525 161 IPRDYF-------YgVIDVEIPQPVRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVAC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 268 SLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTnnLAK----YCP-NATVLHIDIDPTSISKTV 342
Cdd:PRK07525 234 GYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPFGT--LPQygidYWPkDAKIIQVDINPDRIGLTK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 343 TADIPIVGDARQVLEQMLELLSQESAHQPLDEIR---------DWWQQIEQWralqclkydTHSE--------------- 398
Cdd:PRK07525 312 KVSVGICGDAKAVARELLARLAERLAGDAGREERkaliaaeksAWEQELSSW---------DHEDddpgtdwneearark 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 399 --KIKPQAVIETLWRLTNGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGD 476
Cdd:PRK07525 383 pdYMHPRQALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 477 GSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKL 556
Cdd:PRK07525 463 GAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPAL 542
|
570
....*....|....*..
gi 344915208 557 SEALEQVRNNRLVFVDV 573
Cdd:PRK07525 543 KRAIDAQNEGKTTVIEI 559
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
31-581 |
1.13e-90 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 289.95 E-value: 1.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 31 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNA 110
Cdd:PRK07524 1 MTTCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAG-SGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 111 ITGIATAYMDSIPLVVLSG-QVATSL-IGYDAFQEC-DMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 187
Cdd:PRK07524 80 ATAMGQAYADSIPMLVISSvNRRASLgKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 188 DLPKDILN-PANKLPYVCPESVSMRSYNPTTtghkgqIKRALQTLVAAKKPVVYVGGGAIMAGchQQLKETVEALNLPVV 266
Cdd:PRK07524 160 EIPLDVLAaPADHLLPAPPTRPARPGPAPAA------LAQAAERLAAARRPLILAGGGALAAA--AALRALAERLDAPVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 267 SSLMGMGAFPATHRQALGmlgmhgtyeANMT-------MHNADVIFAVG---------VRFDDRttnnlakYCPNATVLH 330
Cdd:PRK07524 232 LTINAKGLLPAGHPLLLG---------ASQSlpavralIAEADVVLAVGtelgetdydVYFDGG-------FPLPGELIR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 331 IDIDPTSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIR--DWWQQI-EQWRALQclkydtHSEkikpQAVIE 407
Cdd:PRK07524 296 IDIDPDQLARNYPPALALVGDARAALEALLARLPGQAAAADWGAARvaALRQALrAEWDPLT------AAQ----VALLD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 408 TLwRLTNGDAYVTSDVGQHQMFAALYYPFDKPRRWINSG-GLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQEL 486
Cdd:PRK07524 366 TI-LAALPDAIFVGDSTQPVYAGNLYFDADAPRRWFNAStGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPEL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 487 STALQYELPVLVVNLNNRYLGMVKqwqdmiysgrhsqSYMQSL-----------PDFVRLAEAYGHVGIQISHPHELESK 555
Cdd:PRK07524 445 ASAVEADLPLIVLLWNNDGYGEIR-------------RYMVARdiepvgvdpytPDFIALARAFGCAAERVADLEQLQAA 511
|
570 580
....*....|....*....|....*.
gi 344915208 556 LSEALEQvrnNRLVFVDVTVDGSEHV 581
Cdd:PRK07524 512 LRAAFAR---PGPTLIEVDQACWFAA 534
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
33-585 |
1.93e-88 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 284.44 E-value: 1.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 33 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 112
Cdd:PRK08617 6 YGADLVVDSLINQGVKYVFGIPGAKIDRVFDALED-SGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 113 GIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKD 192
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 193 ILN-PANKLPYVCPESVSMRSYNPtttghkGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLMG 271
Cdd:PRK08617 165 VVDaPVTSKAIAPLSKPKLGPASP------EDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 272 MGAFPATH-RQALGMLGMHGTYEANMTMHNADVIFAVG---VRFDDRTTNNLakycPNATVLHIDIDPTSISKTVTADIP 347
Cdd:PRK08617 239 AGVISRELeDHFFGRVGLFRNQPGDELLKKADLVITIGydpIEYEPRNWNSE----GDATIIHIDVLPAEIDNYYQPERE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 348 IVGDARQVLEQMLELLSQ----ESAHQPLDEIRdwwqqiEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDV 423
Cdd:PRK08617 315 LIGDIAATLDLLAEKLDGlslsPQSLEILEELR------AQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 424 GQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNN 503
Cdd:PRK08617 389 GSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWND 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 504 RYLGMVKQWQDMIY---SGRHSQSYmqslpDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSEH 580
Cdd:PRK08617 469 GHYNMVEFQEEMKYgrsSGVDFGPV-----DFVKYAESFGAKGLRVTSPDELEPVLREALAT---DGPVVIDIPVDYSDN 540
|
....*
gi 344915208 581 VYPMQ 585
Cdd:PRK08617 541 IKLME 545
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
34-585 |
4.88e-88 |
|
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: 283.18 E-value: 4.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 34 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 113
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALED-KGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 114 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 193
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 194 LNpanklpyvcpESVSMRSYNPTTTGHKG-----QIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSS 268
Cdd:TIGR02418 160 VD----------SPVSVKAIPASYAPKLGaapddAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 269 LMGMGAFPAT-HRQALGMLGMHGTYEANMTMHNADVIFAVG---VRFDDRTTNNLAkycpNATVLHIDIDPTSISKTVTA 344
Cdd:TIGR02418 230 FQGAGAVSRElEDHFFGRVGLFRNQPGDRLLKQADLVITIGydpIEYEPRNWNSEN----DATIVHIDVEPAQIDNNYQP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 345 DIPIVGDarqvLEQMLELLSQESAH-----QPLDEIRDWWQQIEqwrALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYV 419
Cdd:TIGR02418 306 DLELVGD----IASTLDLLAERIPGyelppDALAILEDLKQQRE---ALDRVPATLKQAHLHPLEIIKAMQAIVTDDVTV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 420 TSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVL-V 498
Cdd:TIGR02418 379 TVDMGSHYIWMARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVhI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 499 VNLNNRYlGMVKQWQDMIYsgrHSQSYMQSLP-DFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDG 577
Cdd:TIGR02418 459 IWNDNGY-NMVEFQEEMKY---QRSSGVDFGPiDFVKYAESFGAKGLRVESPDQLEPTLRQAMEV---EGPVVVDIPVDY 531
|
....*...
gi 344915208 578 SEHVYPMQ 585
Cdd:TIGR02418 532 SDNPKLMS 539
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
30-573 |
2.94e-86 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 279.39 E-value: 2.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 30 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALhtvgGIDHVLVRHEQAAVHMADGLARATG--EVGVVLVTSGPGA 107
Cdd:PRK06154 18 KTMKVAEAVAEILKEEGVELLFGFPVNELFDAAAAA----GIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 108 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDA-FQECDMVgisRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVV 186
Cdd:PRK06154 94 ENAFGGVAQAYGDSVPVLFLPTGYPRGSTDVAPnFESLRNY---RHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 187 VDLPKDILN---PANKLPYVcPESVSMRSYNPTTtghkgqIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNL 263
Cdd:PRK06154 171 LELPVDVLAeelDELPLDHR-PSRRSRPGADPVE------VVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 264 PVVSSLMGMGAFPATHRQALGMLGMhgTYEANMT--MHNADVIFAVGVRFddrTTNNLAKYCP-NATVLHIDIDPTSISK 340
Cdd:PRK06154 244 PVMTTLNGKSAFPEDHPLALGSGGR--ARPATVAhfLREADVLFGIGCSL---TRSYYGLPMPeGKTIIHSTLDDADLNK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 341 TVTADIPIVGDARQVLEQMLELLSQESAHQP---------LDEIRDWWqqIEQWRAlqclKYDTHSEKIKPQAVI-ETLW 410
Cdd:PRK06154 319 DYPIDHGLVGDAALVLKQMIEELRRRVGPDRgraqqvaaeIEAVRAAW--LAKWMP----KLTSDSTPINPYRVVwELQH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 411 RLTNGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTAL 490
Cdd:PRK06154 393 AVDIKTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 491 QYELPVLVVNLNNRYLGmvkqwqdmiysgrhsqSYMQSLP-------------DFVRLAEAYGHVGIQISHPHELESKLS 557
Cdd:PRK06154 473 RERIPILTILLNNFSMG----------------GYDKVMPvsttkyratdisgDYAAIARALGGYGERVEDPEMLVPALL 536
|
570
....*....|....*.
gi 344915208 558 EALEQVRNNRLVFVDV 573
Cdd:PRK06154 537 RALRKVKEGTPALLEV 552
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
31-584 |
1.10e-80 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 264.38 E-value: 1.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 31 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNA 110
Cdd:PRK06457 1 MPSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRK-SKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 111 ITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLP 190
Cdd:PRK06457 80 LNGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 191 KDILNPANKLPYVCPESVSMRSYNPTTTGHKGQIKRalqtlvaAKKPVVYVGGGAIMAGchQQLKETVEALNLPVVSSLM 270
Cdd:PRK06457 159 VDILRKSSEYKGSKNTEVGKVKYSIDFSRAKELIKE-------SEKPVLLIGGGTRGLG--KEINRFAEKIGAPIIYTLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 271 GMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNlakycPNATVLHIDIDPTSISKTVTADIPIVG 350
Cdd:PRK06457 230 GKGILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLN-----KSAKVIQVDIDNSNIGKRLDVDLSYPI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 351 DARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQwralqcLKYDThSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQMFA 430
Cdd:PRK06457 305 PVAEFLNIDIEEKSDKFYEELKGKKEDWLDSISK------QENSL-DKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 431 ALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMAL-PEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 509
Cdd:PRK06457 378 ARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAVeNKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 344915208 510 KQWQD-MIYSGRHSQSYMqslPDFVRLAEAYGHVGIQISHPHELESKLSEALeqvRNNRLVFVDVTVDGSEHvyPM 584
Cdd:PRK06457 458 KFEQEvMGYPEWGVDLYN---PDFTKIAESIGFKGFRLEEPKEAEEIIEEFL---NTKGPAVLDAIVDPNER--PM 525
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
22-580 |
7.75e-77 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 254.69 E-value: 7.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 22 RQTVRQAMEMLSGAEMVVRSLIDQGVKQVFGYpggavlDIYDALHTVG---GIDHVLVRHEQAAVHMADGLARATGEVGV 98
Cdd:PRK06112 4 PLSAPGFTLNGTVAHAIARALKRHGVEQIFGQ------SLPSALFLAAeaiGIRQIAYRTENAGGAMADGYARVSGKVAV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 99 VLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAA 178
Cdd:PRK06112 78 VTAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 179 SGRPGPVVVDLPKDILNPANKLPYVcPESVSMRSYnP--TTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKE 256
Cdd:PRK06112 158 SGRPGPVVLLLPADLLTAAAAAPAA-PRSNSLGHF-PldRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 257 TVEALNLPVVSSLMGMGAFPATHRQALGMLGM------HGTYEANMtMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLH 330
Cdd:PRK06112 236 LQSLAGLPVATTNMGKGAVDETHPLSLGVVGSlmgprsPGRHLRDL-VREADVVLLVGTRTNQNGTDSWSLYPEQAQYIH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 331 IDIDPTSISKTVTAdIPIVGDARQVLEQMLELLSQESAHQPLDE-------IRDWWQQIEQWRALQclkYDTHSEKIKPQ 403
Cdd:PRK06112 315 IDVDGEEVGRNYEA-LRLVGDARLTLAALTDALRGRDLAARAGRraalepaIAAGREAHREDSAPV---ALSDASPIRPE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 404 AVIETLWRLTNGDAYVTSDVGQHQMFAALYYPFDKPR-RWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMN 482
Cdd:PRK06112 391 RIMAELQAVLTGDTIVVADASYSSIWVANFLTARRAGmRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 483 IQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYsGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHEleskLSEALEQ 562
Cdd:PRK06112 471 WAELETARRMGVPVTIVVLNNGILGFQKHAETVKF-GTHTDACHFAAVDHAAIARACGCDGVRVEDPAE----LAQALAA 545
|
570
....*....|....*....
gi 344915208 563 VRNNRLVFV-DVTVDGSEH 580
Cdd:PRK06112 546 AMAAPGPTLiEVITDPSAF 564
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
46-577 |
1.25e-73 |
|
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: 246.29 E-value: 1.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 46 GVKQVFGYPGGAVLDIYDALHT-VGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPL 124
Cdd:TIGR02720 13 GVDHIYGIPGGSFNSTMDALSAeRDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYDAKEDHVPV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 125 VVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVVVDLPKDilnpankLPYV- 203
Cdd:TIGR02720 93 LALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAI-RRAYAHNGVAVVTIPVD-------FGWQe 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 204 CPE------SVSMRSYN-PTTTGHkgQIKRALQTLVAAKKPVVYVGGGAIMAGchQQLKETVEALNLPVVSSLMGMGAFP 276
Cdd:TIGR02720 165 IPDndyyasSVSYQTPLlPAPDVE--AVTRAVQTLKAAERPVIYYGIGARKAG--EELEALSEKLKIPLISTGLAKGIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 277 ATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFD----DRTTNNlAKYcpnatVLHIDIDPTSISKTVTADIPIVGDA 352
Cdd:TIGR02720 241 DRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPfaevSKAFKN-TKY-----FIQIDIDPAKLGKRHHTDIAVLADA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 353 RQVLEQMLELLSQESAHQpldeirdWWQ----QIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQM 428
Cdd:TIGR02720 315 KKALAAILAQVEPRESTP-------WWQanvaNVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDINI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 429 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 508
Cdd:TIGR02720 388 NSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGF 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344915208 509 VKQWQDmiysGRHSQSYMQSLP--DFVRLAEAYGHVGIQISHPHELESKLSEALeQVRNNRLVFVDVTVDG 577
Cdd:TIGR02720 468 IKDEQE----DTNQPLIGVDFNdaDFAKIAEGVGAVGFRVNKIEQLPAVFEQAK-AIKQGKPVLIDAKITG 533
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
36-191 |
3.40e-72 |
|
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: 228.57 E-value: 3.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 36 EMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIA 115
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 344915208 116 TAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 191
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
35-576 |
3.91e-69 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 234.80 E-value: 3.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 35 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGG-IDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 113
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 114 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVkHSFLVKQT--EDIPQVLKKAFWLAASGRpGPVVVDLPK 191
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVA-GAFVQMVTvpEQLRHLVDRAVRTALAER-TVTAVILPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 192 DIlnpaNKLPYVCPE--------SVSMRSynPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAimAGCHQQLKETVEALNL 263
Cdd:PRK08273 164 DV----QELEYEPPPhahgtvhsGVGYTR--PRVVPYDEDLRRAAEVLNAGRKVAILVGAGA--LGATDEVIAVAERLGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 264 PVVSSLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDdrttnnLAKYCP---NATVLHIDIDPTSISK 340
Cdd:PRK08273 236 GVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFP------YSEFLPkegQARGVQIDIDGRMLGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 341 TVTADIPIVGDARQVLEQMLELLSQESAHQPLDEI----RDWWQQIEQwRALqclkydTHSEKIKPQAVIETLWRLTNGD 416
Cdd:PRK08273 310 RYPMEVNLVGDAAETLRALLPLLERKKDRSWRERIekwvARWWETLEA-RAM------VPADPVNPQRVFWELSPRLPDN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 417 AYVTSDVGQhqmfAALYYPFD-KPRRWIN---SGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMN-IQELSTALQ 491
Cdd:PRK08273 383 AILTADSGS----CANWYARDlRMRRGMMaslSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 492 Y----ELPVLVVN-LNNRYLGMVkQWQDMIYSGRHSQSYMQSLPDF--VRLAEAYGHVGIQISHPHELESKLSEALEQvr 564
Cdd:PRK08273 459 YwrqwSDPRLIVLvLNNRDLNQV-TWEQRVMEGDPKFEASQDLPDVpyARFAELLGLKGIRVDDPEQLGAAWDEALAA-- 535
|
570
....*....|..
gi 344915208 565 nNRLVFVDVTVD 576
Cdd:PRK08273 536 -DRPVVLEVKTD 546
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
34-517 |
2.19e-66 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 226.14 E-value: 2.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 34 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 113
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGARE-EGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 114 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 193
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 194 L---NPANKLPYVCPESVSMRSYNPTttghkgQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLM 270
Cdd:PRK05858 166 AfsmADDDGRPGALTELPAGPTPDPD------ALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 271 GMGAFPATHRQALgmlgmhgTYEANMTMHNADVIFAVGVRFDDRTtnNLAKYCPNATVLHIDIDPTSISKTVTADIPIVG 350
Cdd:PRK05858 240 GRGVVPADHPLAF-------SRARGKALGEADVVLVVGVPMDFRL--GFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 351 DARQVLEQMLELLSQESAHQP-LDEIRDwwqQIEQWRALQCLKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGQHQMF 429
Cdd:PRK05858 311 DLSAILSALAGAGGDRTDHQGwIEELRT---AETAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 430 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 509
Cdd:PRK05858 388 AGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLE 467
|
....*...
gi 344915208 510 KQWQDMIY 517
Cdd:PRK05858 468 KHPMEALY 475
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
30-560 |
4.06e-64 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 219.86 E-value: 4.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 30 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 109
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 110 AITGIATAYMDSIPLVVLSGQVATSLIGYDA--FQEC-DMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVV 186
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 187 VDLPKDILNPANKLPY-VCPESVSMRSYNPtttghkGQIKRALQTLVAAKKPVVYVGGGAimAGCHQQLKETVEaLNLPV 265
Cdd:PRK07064 161 VEIPIDIQAAEIELPDdLAPVHVAVPEPDA------AAVAELAERLAAARRPLLWLGGGA--RHAGAEVKRLVD-LGFGV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 266 VSSLMGMGAFPATHRQALGMLGMHGTYEAnmTMHNADVIFAVGVRFDDRTTNNLAKYCPnATVLHIDIDPTSISKTVTAD 345
Cdd:PRK07064 232 VTSTQGRGVVPEDHPASLGAFNNSAAVEA--LYKTCDLLLVVGSRLRGNETLKYSLALP-RPLIRVDADAAADGRGYPND 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 346 IPIVGDARQVLEQMLELLSQESAHQP--LDEIRDWWQQIEqwralqclkyDTHSEKIKPQAVI-ETLWRLTNGDAYVTSD 422
Cdd:PRK07064 309 LFVHGDAARVLARLADRLEGRLSVDPafAADLRAAREAAV----------ADLRKGLGPYAKLvDALRAALPRDGNWVRD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 423 VG-QHQMFAALYYPFDKPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNL 501
Cdd:PRK07064 379 VTiSNSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLM 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 344915208 502 NNRYLGMVKQWQDMIYSGRHsqsYMQSL--PDFVRLAEAYGHVGIQISHPHELESKLSEAL 560
Cdd:PRK07064 458 NDGGYGVIRNIQDAQYGGRR---YYVELhtPDFALLAASLGLPHWRVTSADDFEAVLREAL 515
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
34-194 |
6.79e-64 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 207.47 E-value: 6.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 34 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 113
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 114 IATAYMDSIPLVVLSGQVATSLIGYDAFQ-ECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKD 192
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 344915208 193 IL 194
Cdd:pfam02776 161 VL 162
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
422-573 |
1.32e-63 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 205.90 E-value: 1.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 422 DVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNL 501
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 344915208 502 NNRYLGMVKQWQDMIYSGRHSQSYMQSL--PDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDV 573
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGKILppVDFAKLAEAYGAKGARVESPEELEEALKEALEH---DGPALIDV 151
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
28-578 |
2.16e-63 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 218.72 E-value: 2.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 28 AMEMLSGAEMVVRSLIDQGVKQVFGYPG---GAVLDIYDALHTVGGI--DHVLVRHEQAAVHMADGLARATGEVGVVLVT 102
Cdd:PRK08327 3 ALTMYTAAELFLELLKELGVDYIFINSGtdyPPIIEAKARARAAGRPlpEFVICPHEIVAISMAHGYALVTGKPQAVMVH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 103 SGPGATNAITGIATAYMDSIPLVVLSGQVATS----------LIGY--DAFqecDMVGISRPVVKHSFLVKQTEDIPQVL 170
Cdd:PRK08327 83 VDVGTANALGGVHNAARSRIPVLVFAGRSPYTeegelgsrntRIHWtqEMR---DQGGLVREYVKWDYEIRRGDQIGEVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 171 KKAFWLAASGRPGPVVVDLPKDILnpANKLPYVcpeSVSMRSYNPTTTGH--KGQIKRALQTLVAAKKPVVYVGGGAIMA 248
Cdd:PRK08327 160 ARAIQIAMSEPKGPVYLTLPREVL--AEEVPEV---KADAGRQMAPAPPApdPEDIARAAEMLAAAERPVIITWRAGRTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 249 GCHQQLKETVEALNLPVVSSLMGMGAFPATHrqalgmlGMHGTYEANMTMHNADVIFAVGvrfddrttnNLAKYCP---- 324
Cdd:PRK08327 235 EGFASLRRLAEELAIPVVEYAGEVVNYPSDH-------PLHLGPDPRADLAEADLVLVVD---------SDVPWIPkkir 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 325 ---NATVLHIDIDPtsiSKTVT------ADIPIVGDARQVLEQMLELL--SQESAHQPLDEIRDWWQQI---EQWRALQC 390
Cdd:PRK08327 299 pdaDARVIQIDVDP---LKSRIplwgfpCDLCIQADTSTALDQLEERLksLASAERRRARRRRAAVRELrirQEAAKRAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 391 LKYDTHSEKIKPQAVIETLWRLTNGDAYVTSDVGqhqmFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETV 470
Cdd:PRK08327 376 IERLKDRGPITPAYLSYCLGEVADEYDAIVTEYP----FVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 471 VCVTGDGSIQMNIQE--LSTALQYELPVLVVNLNNRYLGMVKQWQDMIYS---GRHSQSYMQS----LPDFVRLAEAYGH 541
Cdd:PRK08327 452 IATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPegyAARKGTFPGTdfdpRPDFAKIAEAFGG 531
|
570 580 590
....*....|....*....|....*....|....*...
gi 344915208 542 VGIQISHPHELESKLSEALEQVRN-NRLVFVDVTVDGS 578
Cdd:PRK08327 532 YGERVEDPEELKGALRRALAAVRKgRRSAVLDVIVDRV 569
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
24-576 |
1.00e-61 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 213.28 E-value: 1.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 24 TVRQA-MEMLsgaemvvRSLidqGVKQVFGYPGGAVLDIYDALHtvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVT 102
Cdd:PRK07092 13 TVRDAtIDLL-------RRF---GITTVFGNPGSTELPFLRDFP--DDFRYVLGLQEAVVVGMADGYAQATGNAAFVNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 103 SGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAF-QECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGR 181
Cdd:PRK07092 81 SAAGVGNAMGNLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 182 PGPVVVDLPKDILN-PAnklPYVCPESVSmRSYNPTttghKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEA 260
Cdd:PRK07092 161 RGPVFVSIPYDDWDqPA---EPLPARTVS-SAVRPD----PAALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 261 LNLPV-VSSLMGMGAFPATHRQALGML-GMHGTYEANMTMHnaDVIFAVGV---RFDDRTTnnlAKYCP-NATVLHIDID 334
Cdd:PRK07092 233 HRAPVwVAPMSGRCSFPEDHPLFAGFLpASREKISALLDGH--DLVLVIGApvfTYHVEGP---GPHLPeGAELVQLTDD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 335 PTSISKTVTADiPIVGDARQVLEQMLELL--SQESAHQPLdeirdwwQQIEQWRALqclkydthSEKIKPQAVIETLWRL 412
Cdd:PRK07092 308 PGEAAWAPMGD-AIVGDIRLALRDLLALLppSARPAPPAR-------PMPPPAPAP--------GEPLSVAFVLQTLAAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 413 TNGDA-YV---TSDVGQHQMFAAL-----YYPFDkprrwinSGGLgtmGFGLPAALGVKMALPEETVVCVTGDGSIQMNI 483
Cdd:PRK07092 372 RPADAiVVeeaPSTRPAMQEHLPMrrqgsFYTMA-------SGGL---GYGLPAAVGVALAQPGRRVIGLIGDGSAMYSI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 484 QELSTALQYELPVLVVNLNN-RYLGMvkQWQDMIYSGRHSQSYmqSLP--DFVRLAEAYGHVGIQISHPHELESKLSEAL 560
Cdd:PRK07092 442 QALWSAAQLKLPVTFVILNNgRYGAL--RWFAPVFGVRDVPGL--DLPglDFVALARGYGCEAVRVSDAAELADALARAL 517
|
570
....*....|....*.
gi 344915208 561 eqvRNNRLVFVDVTVD 576
Cdd:PRK07092 518 ---AADGPVLVEVEVA 530
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
35-586 |
1.86e-61 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 213.70 E-value: 1.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 35 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 114
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 115 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVVVDLPKDI- 193
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAM-RKAILNRGVAVVVLPGDVa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 194 LNPAnklpyvcPESVSMRSYN---PTTTGHKGQIKRALQTLVAAKKPVVYVGGGAimAGCHQQLKETVEALNLPVVSSLM 270
Cdd:PRK09124 165 LKPA-------PERATPHWYHapqPVVTPAEEELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 271 GMGAFPATHRQALGMLGMHG---TYEAnmtMHNADVIFAVGVRFDDRttnnlAKYCPNATVLHIDIDPTSISKTVTADIP 347
Cdd:PRK09124 236 GKEHVEYDNPYDVGMTGLIGfssGYHA---MMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDLG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 348 IVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQwrALQCLKYDTHSEK-IKPQAVIETLWRLTNGDAYVTSDVGQH 426
Cdd:PRK09124 308 LVGDVKATLAALLPLLEEKTDRKFLDKALEHYRKARK--GLDDLAVPSDGGKpIHPQYLARQISEFAADDAIFTCDVGTP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 427 QMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYL 506
Cdd:PRK09124 386 TVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 507 GMVKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHVYPMQI 586
Cdd:PRK09124 466 GFVA--MEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFA---HDGPALVDVVTAKQELAMPPQI 540
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
35-576 |
9.72e-61 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 211.77 E-value: 9.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 35 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 114
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 115 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWlAASGRPGPVVVDLPKDIl 194
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQ-HAVAGGGVSVVTLPGDI- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 195 npANKLPYVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAimAGCHQQLKETVEALNLPVVSSLMGMGA 274
Cdd:PRK06546 164 --ADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGV--RGAHAEVLALAEKIKAPVGHSLRGKEW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 275 FPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRF--DDrttnnlakYCPNATVLHIDIDPTSISKTVTADIPIVGDA 352
Cdd:PRK06546 240 IQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFpyDQ--------FLPDVRTAQVDIDPEHLGRRTRVDLAVHGDV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 353 RQVLEQMLELLSQESAHQPLDEIRDwwqqiEQWRALQCL--KYDTHSEK---IKPQAVIETLWRLTNGDAYVTSDVGQHQ 427
Cdd:PRK06546 312 AETIRALLPLVKEKTDRRFLDRMLK-----KHARKLEKVvgAYTRKVEKhtpIHPEYVASILDELAADDAVFTVDTGMCN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 428 MFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLG 507
Cdd:PRK06546 387 VWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLG 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344915208 508 MVKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALeqvRNNRLVFVDVTVD 576
Cdd:PRK06546 467 MVK--LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAF---AHPGPALVDVVTD 530
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
224-359 |
1.63e-59 |
|
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: 194.70 E-value: 1.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 224 IKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALNLPVVSSLMGMGAFPATHRQALGMLGMHGTYEANMTMHNADV 303
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 344915208 304 IFAVGVRFDD-RTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDARQVLEQM 359
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
23-579 |
7.70e-54 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 192.89 E-value: 7.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 23 QTVRQAMEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIyDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVT 102
Cdd:PRK09259 1 TAMSDQLQLTDGFHLVIDALKLNGIDTIYGVVGIPITDL-ARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 103 SGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDA--FQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASG 180
Cdd:PRK09259 80 SAPGFLNGLTALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 181 RPGPVVVDLPKDIL-----------------NPANK-LPyvCPESVsmrsynptttghkgqiKRALQTLVAAKKPVVYVG 242
Cdd:PRK09259 160 RPGGVYLDLPAKVLaqtmdadealtslvkvvDPAPAqLP--APEAV----------------DRALDLLKKAKRPLIILG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 243 GGAIMAGCHQQLKETVEALNLPVVSSLMGMGAFPATHRQALGMlgmhgtyEANMTMHNADVIFAVGVRFDDRTTNNLAK- 321
Cdd:PRK09259 222 KGAAYAQADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAA-------ARSLALANADVVLLVGARLNWLLSHGKGKt 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 322 YCPNATVLHIDIDPTSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPLdeirDWWQQIEQWRALQCLKYDTHSEKIK 401
Cdd:PRK09259 295 WGADKKFIQIDIEPQEIDSNRPIAAPVVGDIGSVMQALLAGLKQNTFKAPA----EWLDALAERKEKNAAKMAEKLSTDT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 402 PQ-------AVIETLWRlTNGDAYVTSD-----------VGQHQmfaalyypfdkPRRWINSGGLGTMGFGLPAALG--V 461
Cdd:PRK09259 371 QPmnfynalGAIRDVLK-ENPDIYLVNEgantldlarniIDMYK-----------PRHRLDCGTWGVMGIGMGYAIAaaV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 462 KMALPeetVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNrylGMVKQWQDMIYSGRHSQSYMQSLPD--FVRLAEAY 539
Cdd:PRK09259 439 ETGKP---VVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNN---GGIYRGDDVNLSGAGDPSPTVLVHHarYDKMMEAF 512
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 344915208 540 GHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVD---GSE 579
Cdd:PRK09259 513 GGVGYNVTTPDELRHALTEAIA---SGKPTLINVVIDpaaGTE 552
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
42-576 |
7.62e-53 |
|
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: 189.60 E-value: 7.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 42 LIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDS 121
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 122 IPLVVLSG------QVATSLI-------GYDAFQEcdmvgISRPV-VKHSFLVKQT--EDIPQVLKKAFwlaASGRpgPV 185
Cdd:COG3961 94 VPVVHIVGapgtraQRRGPLLhhtlgdgDFDHFLR-----MFEEVtVAQAVLTPENaaAEIDRVLAAAL---REKR--PV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 186 VVDLPKDILN---PANKLPYVCPESVSmrsyNPTTtgHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVEALN 262
Cdd:COG3961 164 YIELPRDVADapiEPPEAPLPLPPPAS----DPAA--LAAAVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 263 LPVVSSLMGMGAFPATHRQALgmlgmhGTYEANM-------TMHNADVIFAVGVRFDDRTTNNL-AKYCPNATvlhIDID 334
Cdd:COG3961 238 IPVATTLLGKSVLDESHPQFI------GTYAGAAsspevreYVENADCVLCLGVVFTDTNTGGFtAQLDPERT---IDIQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 335 P--TSISKTVTADIPIvgdaRQVLEQMLELLSQESAHQPLDEIRDwwqqieqwralqclkydtHSEKIKPQAVI--ETLW 410
Cdd:COG3961 309 PdsVRVGGHIYPGVSL----ADFLEALAELLKKRSAPLPAPAPPP------------------PPPPAAPDAPLtqDRLW 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 411 R-----LTNGDAyVTSDVGQhQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQE 485
Cdd:COG3961 367 QrlqafLDPGDI-VVADTGT-SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 486 LSTALQYELPVLVVNLNNR-Y------LGM------VKQWqdmiysgrhsqsymqslpDFVRLAEAYG---HVGIQISHP 549
Cdd:COG3961 445 LSTMLRYGLKPIIFVLNNDgYtieraiHGPdgpyndIANW------------------DYAKLPEAFGggnALGFRVTTE 506
|
570 580
....*....|....*....|....*....
gi 344915208 550 HELEsklsEALEQVRNN--RLVFVDVTVD 576
Cdd:COG3961 507 GELE----EALAAAEANtdRLTLIEVVLD 531
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
404-575 |
4.75e-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: 170.90 E-value: 4.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 404 AVIETLWRLTNGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNI 483
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 484 QELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALEQv 563
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSN-PDFAALAEAYGAKGVRVEDPEDLEAALAEALAA- 158
|
170
....*....|..
gi 344915208 564 rnNRLVFVDVTV 575
Cdd:cd00568 159 --GGPALIEVKT 168
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
35-193 |
5.75e-42 |
|
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: 148.85 E-value: 5.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 35 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 114
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344915208 115 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKDI 193
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGDV 160
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
400-579 |
6.99e-42 |
|
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: 149.22 E-value: 6.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 400 IKPQAVIETLWRLTNGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSI 479
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 480 QMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSymQSLPDFVRLAEAYGHVGIQISHPHELESKLSEA 559
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVD--LPNPDFAKIAEAMGIKGIRVEDPDELEAALDEA 159
|
170 180
....*....|....*....|
gi 344915208 560 LEQvrnNRLVFVDVTVDGSE 579
Cdd:cd02014 160 LAA---DGPVVIDVVTDPNE 176
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
402-579 |
4.42e-40 |
|
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: 143.97 E-value: 4.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 402 PQAVIETLWRLTNGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQM 481
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 482 NIQELSTALQYELPVLVVNLNNRYLGMVKqWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALE 561
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIK-WKQEKEYGRDSGVDFGN-PDFVKYAESFGAKGYRIESADDLLPVLERALA 158
|
170
....*....|....*...
gi 344915208 562 QvrnNRLVFVDVTVDGSE 579
Cdd:cd02010 159 A---DGVHVIDCPVDYSE 173
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
45-191 |
1.88e-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: 122.07 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 45 QGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDSIPL 124
Cdd:cd06586 10 WGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADAAAEHLPV 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 344915208 125 VVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVVVDLPK 191
Cdd:cd06586 89 VFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAI-RTAYASQGPVVVRLPR 154
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
398-577 |
8.15e-31 |
|
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: 119.15 E-value: 8.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 398 EKIKPQAVIETLWRLTNGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDG 477
Cdd:cd02013 2 NPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 478 SIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLS 557
Cdd:cd02013 82 AWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELES-ESFAKIAEACGAKGITVDKPEDVGPALQ 160
|
170 180
....*....|....*....|
gi 344915208 558 EALEQVRNNRLVFVDVTVDG 577
Cdd:cd02013 161 KAIAMMAEGKTTVIEIVCDQ 180
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
395-571 |
1.10e-26 |
|
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: 107.75 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 395 THSEKI--KPQAVIETLWRLTNGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVC 472
Cdd:cd02006 1 THFDDVpiKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 473 VTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQ---DMIYSGRHSQSYMQSLP------DFVRLAEAYGHVG 543
Cdd:cd02006 81 LSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQrafDMDYQVNLAFENINSSElggygvDHVKVAEGLGCKA 160
|
170 180
....*....|....*....|....*...
gi 344915208 544 IQISHPHELESKLSEALEQVRNNRLVFV 571
Cdd:cd02006 161 IRVTKPEELAAAFEQAKKLMAEHRVPVV 188
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
402-562 |
1.56e-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: 106.53 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 402 PQAVIETLWRLTNGDA-----YVTSDVGQHQMFaalyyPFDKPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVTGD 476
Cdd:cd02002 3 PEYLAAALAAALPEDAiivdeAVTNGLPLRDQL-----PLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 477 GSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQS--YMQSL----PDFVRLAEAYGHVGIQISHPH 550
Cdd:cd02002 77 GSFMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENapDGLDLldpgIDFAAIAKAFGVEAERVETPE 156
|
170
....*....|..
gi 344915208 551 ELESKLSEALEQ 562
Cdd:cd02002 157 ELDEALREALAE 168
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
402-576 |
1.55e-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: 103.38 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 402 PQAVIETLWRLTNGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQM 481
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 482 NIQELSTALQYELPVLVVNLNNrylgmvkqwqDMIYSGRHSQSYMQSLPDFV----------RLAEAYGHVGIQISHPHE 551
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNN----------GGWYQGLDGQQLSYGLGLPVttllpdtrydLVAEAFGGKGELVTTPEE 150
|
170 180
....*....|....*....|....*
gi 344915208 552 LESKLSEALEqvrNNRLVFVDVTVD 576
Cdd:cd02004 151 LKPALKRALA---SGKPALINVIID 172
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
407-576 |
3.39e-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: 88.36 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 407 ETLWR-----LTNGDAYVTsDVGQHQmFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQM 481
Cdd:cd02005 5 ARLWQqvqnfLKPNDILVA-ETGTSW-FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 482 NIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMiysgrhSQSYMQSLP-DFVRLAEAYG----HVGIQISHPHELESKL 556
Cdd:cd02005 83 TVQELSTMIRYGLNPIIFLINNDGYTIERAIHGP------EASYNDIANwNYTKLPEVFGggggGLSFRVKTEGELDEAL 156
|
170 180
....*....|....*....|
gi 344915208 557 SEALEqvRNNRLVFVDVTVD 576
Cdd:cd02005 157 KDALF--NRDKLSLIEVILP 174
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
33-562 |
2.94e-19 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 91.06 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 33 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 112
Cdd:PRK07586 2 NGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 113 GIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVvkhSFLVKQTEDIPQV--LKKAFWLAASGRPGPVVVD-L 189
Cdd:PRK07586 82 NLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPV---SGWVRRSESAADVaaDAAAAVAAARGAPGQVATLiL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 190 PKDI-LNPANKLPYVcPESVSMRSYNPTTtghkgqIKRALQTLVAAKKPVVYVGGGA-----------IMA--GChQQLK 255
Cdd:PRK07586 159 PADVaWSEGGPPAPP-PPAPAPAAVDPAA------VEAAAAALRSGEPTVLLLGGRAlrerglaaaarIAAatGA-RLLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 256 ETVEAL-----NLPVVSSLmgmgAFPAthRQALGMLGmhgtyeanmtmhNADVIFAVGVRfddrttnnlakycpnatvlh 330
Cdd:PRK07586 231 ETFPARmergaGRPAVERL----PYFA--EQALAQLA------------GVRHLVLVGAK-------------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 331 idiDPTSI-------SKTVTADIPIV------GDARQVLEQMLELLSQESAHQPLDEIRDWwqqieqwralqclkyDTHS 397
Cdd:PRK07586 273 ---APVAFfaypgkpSRLVPEGCEVHtlagpgEDAAAALEALADALGAKPAAPPLAAPARP---------------PLPT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 398 EKIKPQAVIETLWRLTNGDAYVTSDVGqhqMFAALYYPFD---KPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVT 474
Cdd:PRK07586 335 GALTPEAIAQVIAALLPENAIVVDESI---TSGRGFFPATagaAPHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQ 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 475 GDGSIQMNIQELSTALQYELPVLVVNLNNR-Y------LGMVKQWQDmiysGRHSQSyMQSL----PDFVRLAEAYGHVG 543
Cdd:PRK07586 411 GDGSAMYTIQALWTQARENLDVTTVIFANRaYailrgeLARVGAGNP----GPRALD-MLDLddpdLDWVALAEGMGVPA 485
|
570
....*....|....*....
gi 344915208 544 IQISHPHELESKLSEALEQ 562
Cdd:PRK07586 486 RRVTTAEEFADALAAALAE 504
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
28-569 |
1.49e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 89.16 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 28 AMEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGA 107
Cdd:PRK12474 1 MGQTMNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 108 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVvkhSFLVKQTEDIPQV---LKKAFWLAASGRPGP 184
Cdd:PRK12474 81 ANGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPV---SRWVHRSASAGAVdsdVARAVQAAQSAPGGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 185 VVVDLPKDIL-NP----ANKLPYVCPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAIMAGCHQQLKETVE 259
Cdd:PRK12474 158 ATLIMPADVAwNEaayaAQPLRGIGPAPVAAETVERIAALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVRLYCDTF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 260 ALNLPVVSSLMGMGAFPATHRQALGMLgmhgtyeanmtmHNADVIFAVGVRfddrttnnlakycPNATVLHIDIDPTSIS 339
Cdd:PRK12474 238 APRIERGAGRVPIERIPYFHEQITAFL------------KDVEQLVLVGAK-------------PPVSFFAYPGKPSWGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 340 KTvTADIPIVGDARQVLEQMLELLSQE--SAHQPLDEIRdwwqqieqwRALQCLKydthSEKIKPQAVIETLWRLTNGDA 417
Cdd:PRK12474 293 PP-GCEIVYLAQPDEDLAQALQDLADAvdAPAEPAARTP---------LALPALP----KGALNSLGVAQLIAHRTPDQA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 418 YVTSDVGQHQMFAALYYPFDKPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVL 497
Cdd:PRK12474 359 IYADEALTSGLFFDMSYDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVT 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 498 VVNLNNRYLGMVkqWQDMIY-----SGRHSQSYMQ-SLP--DFVRLAEAYGHVGIQISHPHELESKLSEALEQvRNNRLV 569
Cdd:PRK12474 438 VVIFANRSYAIL--NGELQRvgaqgAGRNALSMLDlHNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQ-RGPRLI 514
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
42-174 |
1.37e-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: 80.23 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 42 LIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDS 121
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 122 IPLVVLSGQVATSLIG-------------YDAFQECdmvgiSRPVVKHS-FLVKQ---TEDIPQVLKKAF 174
Cdd:cd07038 86 VPVVHIVGAPSTKAQAsglllhhtlgdgdFDVFLKM-----FEEITCAAaRLTDPenaAEEIDRVLRTAL 150
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
38-190 |
6.52e-16 |
|
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: 75.61 E-value: 6.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 38 VVRSLIDQGVKQVFGYPGG-----AVldiydALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 112
Cdd:cd07037 3 LVEELKRLGVRDVVISPGSrsaplAL-----AAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 113 GIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSF---LVKQTEDIP---QVLKKAFWLAASGRPGPVV 186
Cdd:cd07037 78 AVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVdlpPPEDDDDLWyllRLANRAVLEALSAPPGPVH 157
|
....
gi 344915208 187 VDLP 190
Cdd:cd07037 158 LNLP 161
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
447-576 |
1.83e-13 |
|
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: 69.64 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 447 GLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGR------ 520
Cdd:cd02003 46 GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSfgtefr 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 344915208 521 -----HSQSYMQSLP-DFVRLAEAYGHVGIQISHPHELEsklsEALEQVR-NNRLVFVDVTVD 576
Cdd:cd02003 126 drdqeSGQLDGALLPvDFAANARSLGARVEKVKTIEELK----AALAKAKaSDRTTVIVIKTD 184
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
40-503 |
3.44e-10 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 62.80 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 40 RSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYM 119
Cdd:PLN02573 24 RRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGAYS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 120 DSIPLVVLSG----------QVATSLIGYDAF-QE--CdmvgiSRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVV 186
Cdd:PLN02573 103 ENLPVICIVGgpnsndygtnRILHHTIGLPDFsQElrC-----FQTVTCYQAVINNLEDAHELIDTAI-STALKESKPVY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 187 V----DLPkDILNPANKLPYVcPESVSMRSYNPttTGHKGQIKRALQTLVAAKKPVVyVGGGAI-MAGCHQQLKETVEAL 261
Cdd:PLN02573 177 IsvscNLA-AIPHPTFSREPV-PFFLTPRLSNK--MSLEAAVEAAAEFLNKAVKPVL-VGGPKLrVAKACKAFVELADAS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 262 NLPVVSSLMGMGAFPATHRQALGML-GMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDptsisK 340
Cdd:PLN02573 252 GYPVAVMPSAKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPD-----R 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 341 TVTADIPIVGDArqVLEQMLELLSQ-----ESAHQPLDEIrdwwqQIEQWRALQCLKydthSEKIKPQAVIETLWRLTNG 415
Cdd:PLN02573 327 VTIGNGPAFGCV--LMKDFLEALAKrvkknTTAYENYKRI-----FVPEGEPLKSEP----GEPLRVNVLFKHIQKMLSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 416 DAYVTSDVGQhqmfaalyypfdkprRWINSGGL--------------GTMGFGLPAALGVKMALPEETVVCVTGDGSIQM 481
Cdd:PLN02573 396 DTAVIAETGD---------------SWFNCQKLklpegcgyefqmqyGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQV 460
|
490 500
....*....|....*....|..
gi 344915208 482 NIQELSTALQYELPVLVVNLNN 503
Cdd:PLN02573 461 TAQDVSTMIRCGQKSIIFLINN 482
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
448-591 |
4.10e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 53.68 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 448 LGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTalqyelpvlVVNLNNRYLGMVkQWQDMIYSGRHSQSYMQ 527
Cdd:PRK06163 56 LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGT---------IAALAPKNLTII-VMDNGVYQITGGQPTLT 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 344915208 528 S-LPDFVRLAEAyghVGIQISH----PHELESKLSEALeqvRNNRLVFVDVTVD-----GSEHVYPMQIRGGGM 591
Cdd:PRK06163 126 SqTVDVVAIARG---AGLENSHwaadEAHFEALVDQAL---SGPGPSFIAVRIDdkpgvGTTERDPAQIRERFM 193
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
404-508 |
1.32e-06 |
|
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: 50.14 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 404 AVIETLWRLTNGD-AYVTSDVGQHqmfAALYYPFDKPrrWINSgglgTMGFGLPAALGVKMALPEETVVCVTGDG---SI 479
Cdd:COG1013 27 LLLKALDELLDGDkTVVVSGIGCS---SVAPGYFNVP--GFHT----LHGRAAAVATGIKLANPDLTVIVFGGDGdtyDI 97
|
90 100 110
....*....|....*....|....*....|
gi 344915208 480 QMNiqELSTALQYELPVLVVNLNNR-YlGM 508
Cdd:COG1013 98 GGN--HLIHAARRNEDITYIVYDNEiY-GN 124
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
443-510 |
2.27e-05 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 46.37 E-value: 2.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 344915208 443 INSGGL-GTMGFGLPAALGVKMALPEETVVCVTGDG---SIQMN--IQelstALQYELPVLVVNLNNRYLGMVK 510
Cdd:PRK11867 62 INTYGFhTIHGRALAIATGLKLANPDLTVIVVTGDGdalAIGGNhfIH----ALRRNIDITYILFNNQIYGLTK 131
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
404-508 |
4.56e-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: 44.19 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 404 AVIETLWRLTNGDAYVTSDVGQHQMFAAlyypfdKPRRWINsgGLGTMGFGLPAALGVKMALPEETVVCVTGDGS-IQMN 482
Cdd:cd02008 14 PSFYALRKAFKKDSIVSGDIGCYTLGAL------PPLNAID--TCTCMGASIGVAIGMAKASEDKKVVAVIGDSTfFHSG 85
|
90 100
....*....|....*....|....*.
gi 344915208 483 IQELSTALQYELPVLVVNLNNRYLGM 508
Cdd:cd02008 86 ILGLINAVYNKANITVVILDNRTTAM 111
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
443-510 |
5.90e-05 |
|
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: 44.44 E-value: 5.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 344915208 443 INSGGL-GTMGFGLPAALGVKMALPEETVVCVTGDG---SIQMNiqELSTALQYELPVLVVNLNNRYLGMVK 510
Cdd:cd03375 44 FNTYGFhTLHGRALAVATGVKLANPDLTVIVVSGDGdlaAIGGN--HFIHAARRNIDITVIVHNNQIYGLTK 113
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
432-561 |
7.99e-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: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 432 LYYPFDKPRrwiNSGGLGTMGFGLPAALGVKMALPEEtVVCVTGDGSIQMNIQELSTALQyELP--VLVVNLNNRylgmv 509
Cdd:cd03372 28 LYAAGDRPL---NFYMLGSMGLASSIGLGLALAQPRK-VIVIDGDGSLLMNLGALATIAA-EKPknLIIVVLDNG----- 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 344915208 510 kqwqdmIYSGRHSQ-SYMQSLPDFVRLAEAYG-HVGIQISHPHELESKLSEALE 561
Cdd:cd03372 98 ------AYGSTGNQpTHAGKKTDLEAVAKACGlDNVATVASEEAFEKAVEQALD 145
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
432-560 |
1.15e-04 |
|
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: 42.86 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344915208 432 LYYPFDKPRRWINsggLGTMGFGLPAALGVKMALPEETVVcVTGDGSIQMNIQELSTALQYE-LPVLVVNLNNRylgmvk 510
Cdd:cd02001 28 LYDVQDRDGHFYM---LGSMGLAGSIGLGLALGLSRKVIV-VDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNR------ 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 344915208 511 qwqdmIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEAL 560
Cdd:cd02001 98 -----AYGSTGGQPTPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLL 142
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
449-575 |
3.01e-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: 42.30 E-value: 3.01e-04
10 20 30 40 50 60 70 80
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gi 344915208 449 GTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLV-VNLNNRYLGMVkqwqdmiySGRHSQSYMQ 527
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPANLIhIVLNNGAHDSV--------GGQPTVSFDV 119
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90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 344915208 528 SLPDFVRlAEAYGHVgIQISHPHELESKLSEALEQvrnNRLVFVDVTV 575
Cdd:cd03371 120 SLPAIAK-ACGYRAV-YEVPSLEELVAALAKALAA---DGPAFIEVKV 162
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| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
34-139 |
4.83e-04 |
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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: 40.95 E-value: 4.83e-04
10 20 30 40 50 60 70 80
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gi 344915208 34 GAEMVVRSLIDQGVKQVFGYPG---GAVLDIYDAlHTVGGIDHVLVR--HEQAAVHMADGlARATGEVGVVlVTSGPGAT 108
Cdd:cd07034 1 GNEAVARGALAAGVDVVAAYPItpsTEIAETLAK-AVLGELGGVVVQaeSEHAAAEAAIG-ASAAGARAMT-ATSGPGLN 77
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90 100 110
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gi 344915208 109 NAITGIATAYMDSIPLVVLSGQ---VATSLIGYD 139
Cdd:cd07034 78 LMAEALYLAAGAELPLVIVVAQrpgPSTGLPKPD 111
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| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
443-510 |
1.31e-03 |
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2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 41.02 E-value: 1.31e-03
10 20 30 40 50 60 70
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gi 344915208 443 INSGGL-GTMGFGLPAALGVKMALPEETVVCVTGDG---SIQMNiqELSTALQYELPVLVVNLNNRYLGMVK 510
Cdd:PRK05778 63 FLSHGLhTLHGRAIAFATGAKLANPDLEVIVVGGDGdlaSIGGG--HFIHAGRRNIDITVIVENNGIYGLTK 132
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