|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-574 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 1226.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK07979 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 161 LPKDILNPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCS 240
Cdd:PRK07979 161 LPKDILNPANKLPYVWPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
Cdd:PRK07979 241 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
Cdd:PRK07979 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 480
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRG 560
Cdd:PRK07979 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRG 560
|
570
....*....|....
gi 90111084 561 GGMDEMWLSKTERT 574
Cdd:PRK07979 561 GGMDEMWLSKTERT 574
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-574 |
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 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK08979 81 NTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 161 LPKDILNPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCS 240
Cdd:PRK08979 161 LPKDCLNPAILHPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
Cdd:PRK08979 241 LMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
Cdd:PRK08979 321 VGSADKVLDSMLALLDESGETNDEAAIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 480
Cdd:PRK08979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrNNRLVFVDVTVDGSEHVYPMQIRG 560
Cdd:PRK08979 481 VKQWQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAM--KDRLVFVDINVDETEHVYPMQIRG 558
|
570
....*....|....
gi 90111084 561 GGMDEMWLSKTERT 574
Cdd:PRK08979 559 GAMNEMWLSKTERT 572
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
4-570 |
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: 1047.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 164 DILNPANKLPYvwPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMG 243
Cdd:TIGR00118 161 DVTTAEIEYPY--PEKVNLPGYRPTVKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 244 LGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGD 323
Cdd:TIGR00118 239 LGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 324 ARQVLEQMLELLSQESahqPLDEIrDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAA 403
Cdd:TIGR00118 319 ARNVLEELLKKLFELK---ERKES-AWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 404 LYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQ 483
Cdd:TIGR00118 395 QFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 484 WQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSEHVYPMQIRGGGM 563
Cdd:TIGR00118 475 WQELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSS---NEPVLLDVVVDKPENVLPMVAPGGGL 551
|
....*..
gi 90111084 564 DEMWLSK 570
Cdd:TIGR00118 552 DEMIGEK 558
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-574 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 1005.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK06882 81 NAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 161 LPKDILNPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCS 240
Cdd:PRK06882 161 IPKDMVNPANKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
Cdd:PRK06882 241 LMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
Cdd:PRK06882 321 VGSAKNVLEEFLSLLEEENLAKSQTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 480
Cdd:PRK06882 401 FAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrNNRLVFVDVTVDGSEHVYPMQIRG 560
Cdd:PRK06882 481 VKQWQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSI--KDKLVFVDVNVDETEHVYPMQIRG 558
|
570
....*....|....
gi 90111084 561 GGMDEMWLSKTERT 574
Cdd:PRK06882 559 GAMNEMILSKPEET 572
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-574 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 997.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK06466 81 NAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 161 LPKDILNPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCS 240
Cdd:PRK06466 161 IPKDMTNPAEKFEYEYPKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
Cdd:PRK06466 241 LMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCL-KYDTHS-EKIKPQAVIETLWRLTKGDAYVTSDVGQH 398
Cdd:PRK06466 321 VGPVESVLTEMLAILKEIGEKPDKEALAAWWKQIDEWRGRHGLfPYDKGDgGIIKPQQVVETLYEVTNGDAYVTSDVGQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 399 QMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYL 478
Cdd:PRK06466 401 QMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 479 GMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrNNRLVFVDVTVDGSEHVYPMQI 558
Cdd:PRK06466 481 GMVRQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAM--KDRLVFIDIYVDRSEHVYPMQI 558
|
570
....*....|....*.
gi 90111084 559 RGGGMDEMWLSKTERT 574
Cdd:PRK06466 559 ADGSMRDMWLSKTERT 574
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
4-568 |
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 90111084 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
Cdd:PRK06965 21 SIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 164 DIlnPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMG 243
Cdd:PRK06965 181 DV--SKTPCEYEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 244 LGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNA-TVLHIDIDPTSISKTVTADIPIVG 322
Cdd:PRK06965 259 LGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRVKVDIPIVG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 323 DARQVLEQMLELLsQESAHQP-LDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 401
Cdd:PRK06965 339 DVKEVLKELIEQL-QTAEHGPdADALAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMW 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 402 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 481
Cdd:PRK06965 418 AAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMV 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 482 KQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrNNRLVFVDVTVDGSEHVYPMQIRGG 561
Cdd:PRK06965 498 RQWQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRL--KDRTVFLDFQTDPTENVWPMVQAGK 575
|
....*..
gi 90111084 562 GMDEMWL 568
Cdd:PRK06965 576 GITEMLL 582
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
2-566 |
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: 784.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 82 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 161
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 162 PKDILnpANKLPYVwPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSL 241
Cdd:COG0028 161 PKDVQ--AAEAEEE-PAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 242 MGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIV 321
Cdd:COG0028 238 MGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 322 GDARQVLEQMLELLSQESahqplDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 401
Cdd:COG0028 318 GDAKAVLAALLEALEPRA-----DDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 402 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 481
Cdd:COG0028 393 AARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 482 KQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHvypmqIRGG 561
Cdd:COG0028 473 RQWQELFYGGRYSGTDLPN-PDFAKLAEAFGAKGERVETPEELEAALEEALA---SDGPALIDVRVDPEEN-----PPGA 543
|
....*
gi 90111084 562 GMDEM 566
Cdd:COG0028 544 TLDEM 548
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
4-568 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 772.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
Cdd:PRK09107 11 MTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 164 DILNPANKlpYVWP-ESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCH--QQLKETVEALNLPVVCS 240
Cdd:PRK09107 171 DVQFATGT--YTPPqKAPVHVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVINSGPEasRLLRELVELTGFPITST 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
Cdd:PRK09107 249 LMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKG-DAYVTSDVGQHQ 399
Cdd:PRK09107 329 IGDVGHVLEDMLRLWKARGKKPDKEALADWWGQIARWRARNSLAYTPSDDVIMPQYAIQRLYELTKGrDTYITTEVGQHQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 400 MFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLG 479
Cdd:PRK09107 409 MWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMG 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 480 MVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLseaLEQVRNNRLVFVDVTVDGSEHVYPMQIR 559
Cdd:PRK09107 489 MVRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAI---QEMIDVDKPVIFDCRVANLENCFPMIPS 565
|
....*....
gi 90111084 560 GGGMDEMWL 568
Cdd:PRK09107 566 GKAHNEMLL 574
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
4-573 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 751.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
Cdd:PRK08527 3 LSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 164 DIlnPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMG 243
Cdd:PRK08527 163 DV--TATLGEFEYPKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 244 LGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGD 323
Cdd:PRK08527 241 RGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 324 ARQVLEQMLELLSQESAhqplDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAA 403
Cdd:PRK08527 321 LKNVLKEMLEELKEENP----TTYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 404 LYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQ 483
Cdd:PRK08527 397 QFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 484 WQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSEHVYPMQIRGGGM 563
Cdd:PRK08527 477 WQTFFYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALES---DKVALIDVKIDRFENVLPMVPAGGAL 553
|
570
....*....|
gi 90111084 564 DEMWLSKTER 573
Cdd:PRK08527 554 YNMILPKKKD 563
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-566 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 684.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK06048 84 NLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLID 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 161 LPKDILNpaNKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCS 240
Cdd:PRK06048 164 LPKDVTT--AEIDFDYPDKVELRGYKPTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
Cdd:PRK06048 242 LMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 321 VGDARQVLEQMLELLSQESAhqpldeiRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKgDAYVTSDVGQHQM 400
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDR-------KEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 480
Cdd:PRK06048 394 WAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHVYPMQIRG 560
Cdd:PRK06048 474 VRQWQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVA---SDRPVVIDFIVECEENVSPMVPAG 550
|
....*.
gi 90111084 561 GGMDEM 566
Cdd:PRK06048 551 AAINEI 556
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
5-556 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 682.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTV---GGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK07418 20 TGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAeaeGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 82 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 161
Cdd:PRK07418 100 LVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 162 PKDI-LNPANKLPyVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCS 240
Cdd:PRK07418 180 PKDVgQEEFDYVP-VEPGSVKPPGYRPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
Cdd:PRK07418 259 LMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVPI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 321 VGDARQVLEQMLElLSQESAHQPldEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKgDAYVTSDVGQHQM 400
Cdd:PRK07418 339 VGDVRKVLVKLLE-RSLEPTTPP--RTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAP-DAYYTTDVGQHQM 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 401 FAALYYPfDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 480
Cdd:PRK07418 415 WAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGM 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111084 481 VKQWQDMIYSGRHSQSYMQ-SLPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHVYPM 556
Cdd:PRK07418 494 VRQWQESFYGERYSASNMEpGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALA---HDGPVLIDVHVRRDENCYPM 567
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-565 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 670.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK07789 28 PERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK07789 108 NLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 161 LPKDILNpaNKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCS 240
Cdd:PRK07789 188 IPKDALQ--AQTTFSWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
Cdd:PRK07789 266 LMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHADVPI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSE-KIKPQAVIETLWRLTKGDAYVTSDVGQHQ 399
Cdd:PRK07789 346 VGDVKEVIAELIAALRAEHAAGGKPDLTAWWAYLDGWRETYPLGYDEPSDgSLAPQYVIERLGEIAGPDAIYVAGVGQHQ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 400 MFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLG 479
Cdd:PRK07789 426 MWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLG 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 480 MVKQWQDMIYSGRHSQSYMQS----LPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrNNRLVFVDVTVDGSEHVYP 555
Cdd:PRK07789 506 MVRQWQTLFYEERYSNTDLHThshrIPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAI--NDRPVVIDFVVGKDAMVWP 583
|
570
....*....|
gi 90111084 556 MQIRGGGMDE 565
Cdd:PRK07789 584 MVAAGTSNDE 593
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
4-566 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 657.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:PRK06276 80 TGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 164 DILNPANKLP-YVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLM 242
Cdd:PRK06276 160 DVQEGELDLEkYPIPAKIDLPGYKPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 243 GLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVG 322
Cdd:PRK06276 240 GKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 323 DARQVLEQMLELLSQESahqpLDEIRDWWQQIEQWRArQCLKYDTHSEK-IKPQAVIETLWRLTKG-----DAYVTSDVG 396
Cdd:PRK06276 320 DAKNVLRDLLAELMKKE----IKNKSEWLERVKKLKK-ESIPRMDFDDKpIKPQRVIKELMEVLREidpskNTIITTDVG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 397 QHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNR 476
Cdd:PRK06276 395 QNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 477 YLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALeqvRNNRLVFVDVTVDGSEhVYPM 556
Cdd:PRK06276 475 TLGMVYQWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAI---KSGEPYLLDIIIDPAE-ALPM 550
|
570
....*....|
gi 90111084 557 QIRGGGMDEM 566
Cdd:PRK06276 551 VPPGGNLTNI 560
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
2-566 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 642.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK07710 14 KLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 82 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 161
Cdd:PRK07710 93 VVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 162 PKDILNPANKLPYvwPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSL 241
Cdd:PRK07710 173 PKDMVVEEGEFCY--DVQMDLPGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 242 MGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIV 321
Cdd:PRK07710 251 LGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 322 GDARQVLEQMLELLSQESAHQpldeirDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 401
Cdd:PRK07710 331 ADAKQALQVLLQQEGKKENHH------EWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 402 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 481
Cdd:PRK07710 405 AAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 482 KQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHVYPMQIRGG 561
Cdd:PRK07710 485 RQWQEEFYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIE---LQEPVVIDCRVLQSEKVMPMVAPGK 561
|
....*
gi 90111084 562 GMDEM 566
Cdd:PRK07710 562 GLHEM 566
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
2-572 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 631.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK06725 13 EEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 82 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 161
Cdd:PRK06725 92 LVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 162 PKDILNpaNKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSL 241
Cdd:PRK06725 172 PKDVQN--EKVTSFYNEVVEIPGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 242 MGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIV 321
Cdd:PRK06725 250 MGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 322 GDARQVLEQMLellsQESAHQPLDEirdWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 401
Cdd:PRK06725 330 GDVKKALHMLL----HMSIHTQTDE---WLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMW 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 402 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 481
Cdd:PRK06725 403 AAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 482 KQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHVYPMQIRGG 561
Cdd:PRK06725 483 RQWQEMFYENRLSESKIGS-PDFVKVAEAYGVKGLRATNSTEAKQVMLEAFA---HEGPVVVDFCVEEGENVFPMVPPNK 558
|
570
....*....|.
gi 90111084 562 GMDEMWLSKTE 572
Cdd:PRK06725 559 GNNEMIMKRWE 569
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
5-556 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 618.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHT---VGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:CHL00099 11 TGAFALIDSLVRHGVKHIFGYPGGAILPIYDELYAwekKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 82 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 161
Cdd:CHL00099 91 LVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 162 PKDI-LNPANKLPYVWPES-VSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVC 239
Cdd:CHL00099 171 PKDVgLEKFDYYPPEPGNTiIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 240 SLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIP 319
Cdd:CHL00099 251 TLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 320 IVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLtKGDAYVTSDVGQHQ 399
Cdd:CHL00099 331 IVGDVKKVLQELLELLKNSPNLLESEQTQAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQL-APDAYFTTDVGQHQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 400 MFAALYYPFdKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLG 479
Cdd:CHL00099 410 MWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQG 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111084 480 MVKQWQDMIYSGRHSQSYMQS-LPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSEHVYPM 556
Cdd:CHL00099 489 MVRQWQQAFYGERYSHSNMEEgAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDY---DGPVLIDCQVIEDENCYPM 563
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
5-566 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 611.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 84
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 85 GIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKD 164
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 165 IlnPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMGL 244
Cdd:PRK07282 171 V--SALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 245 GAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDA 324
Cdd:PRK07282 249 GTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 325 RQVLEQMLELLSQESAHqpldeiRDWWQQIEQWRARqCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAAL 404
Cdd:PRK07282 329 KKALQMLLAEPTVHNNT------EKWIEKVTKDKNR-VRSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 405 YYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQW 484
Cdd:PRK07282 402 YYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 485 QDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELEsklsEALEQVRNNRLVFVDVTVDGSEHVYPMQIRGGGMD 564
Cdd:PRK07282 482 QESFYEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLA----QDLEVITEDVPMLIEVDISRKEHVLPMVPAGKSNH 557
|
..
gi 90111084 565 EM 566
Cdd:PRK07282 558 EM 559
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
6-566 |
0e+00 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 603.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:PRK08978 82 LADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 166 -LNPANKLPYVWPESvsmrsynPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMGL 244
Cdd:PRK08978 162 qLAEGELEPHLTTVE-------NEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 245 GAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDA 324
Cdd:PRK08978 235 GAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 325 RQVLEQMlellsqesaHQPLDeIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAAL 404
Cdd:PRK08978 315 NALLPAL---------QQPLN-IDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 405 YYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQW 484
Cdd:PRK08978 385 HMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 485 QDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSEHVYPMQIRGGGMD 564
Cdd:PRK08978 465 QQLFFDERYSETDLSDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNS---EGPYLLHVSIDELENVWPLVPPGASNS 541
|
..
gi 90111084 565 EM 566
Cdd:PRK08978 542 EM 543
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-566 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 552.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK08155 10 RKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK08155 90 NLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWID 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 161 LPKDILNPANKLPyVWPEsVSMRSYNPTTTGHkgQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCS 240
Cdd:PRK08155 170 IPKDVQTAVIELE-ALPA-PAEKDAAPAFDEE--SIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
Cdd:PRK08155 246 LMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 321 VGDARQVLEQMLELLsqesAHQPLDEirdWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
Cdd:PRK08155 326 QADVDDVLAQLLPLV----EAQPRAE---WHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQHQM 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 480
Cdd:PRK08155 399 WTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALeqvrnNRL--VFVDVTVDGSEHVYPMQI 558
Cdd:PRK08155 479 VHQQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAI-----NRPgpALIHVRIDAEEKVYPMVP 553
|
....*...
gi 90111084 559 RGGGMDEM 566
Cdd:PRK08155 554 PGAANTEM 561
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
6-562 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 541.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 166 LNPAnKLPYvWPESVSMRSY-----NPTTTGHKGQIKRALQTlvaAKKPVVYVGGGAITAGchQQLKETVEALNLPVVCS 240
Cdd:PLN02470 175 QQQL-AVPN-WNQPMKLPGYlsrlpKPPEKSQLEQIVRLISE---SKRPVVYVGGGCLNSS--EELREFVELTGIPVAST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
Cdd:PLN02470 248 LMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 321 VGDARQVLEQMLELLSQESAHQPldEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
Cdd:PLN02470 328 CADVKLALQGLNKLLEERKAKRP--DFSAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVGQHQM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 480
Cdd:PLN02470 406 WAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGM 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 481 VKQWQDMIYSGRHSQSYMQS-------LPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRLvfvDVTVDGSEHV 553
Cdd:PLN02470 486 VVQWEDRFYKANRAHTYLGDpdaeaeiFPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLL---DVIVPHQEHV 562
|
....*....
gi 90111084 554 YPMqIRGGG 562
Cdd:PLN02470 563 LPM-IPGGG 570
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
3-569 |
1.08e-144 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 429.64 E-value: 1.08e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 3 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDAL---HTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGA 79
Cdd:PRK06456 1 MPTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 80 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 159
Cdd:PRK06456 81 TNLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 160 DLPKDILNpaNKLPYV-WPESVSMRSYNP-TTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPV 237
Cdd:PRK06456 161 DIPRDIFY--EKMEEIkWPEKPLVKGYRDfPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 238 VCSLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPN-ATVLHIDIDPTSISKTVTA 316
Cdd:PRK06456 239 VSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVNIDPTDGEKAIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 317 DIPIVGDARQVLEQMLELL-------SQESAHQPLDEIRDWWQQieqwrarqcLKYDTHSEKIKPQAVIETLWRLTKGDA 389
Cdd:PRK06456 319 DVGIYGNAKIILRELIKAItelgqkrDRSAWLKRVKEYKEYYSQ---------FYYTEENGKLKPWKIMKTIRQALPRDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 390 YVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVL 469
Cdd:PRK06456 390 IVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 470 VVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDG 549
Cdd:PRK06456 470 SVIFDNRTLGLVRQVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKE---DIPAVIRVPVDK 546
|
570 580
....*....|....*....|
gi 90111084 550 SEHVYPMQIRGGGMDEMWLS 569
Cdd:PRK06456 547 EELALPTLPPGGRLKQVILR 566
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-545 |
6.60e-131 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 395.12 E-value: 6.60e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARAT-GEVGVVLVTSGPGA 79
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 80 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 159
Cdd:PRK11269 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 160 DLPKDI------LNPANKLPyvwpesvsMRSYNPTTTghKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEAL 233
Cdd:PRK11269 161 DLPFDVqvaeieFDPDTYEP--------LPVYKPAAT--RAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 234 NLPVVCSLMGLGAFPATHRQALGMLGMHGTYE-ANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISK 312
Cdd:PRK11269 231 GVPVIPTLMGWGAIPDDHPLMAGMVGLQTSHRyGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 313 TVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVT 392
Cdd:PRK11269 311 VFGPDLGIVSDAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 393 SDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVN 472
Cdd:PRK11269 391 STIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 473 LNNRYLGMVKQWQ---DMIY------SGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRL-VF 542
Cdd:PRK11269 471 VNNAYLGLIRQAQrafDMDYcvqlafENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALEQAKALMAEFRVpVV 550
|
...
gi 90111084 543 VDV 545
Cdd:PRK11269 551 VEV 553
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
6-551 |
1.33e-110 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 341.04 E-value: 1.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:PRK08322 3 AADLFVKCLENEGVEYIFGIPGEENLDLLEALRD-SSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:PRK08322 82 VAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 166 ---LNPANKLPyvwpesvsmRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLM 242
Cdd:PRK08322 162 aaeETDGKPLP---------RSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 243 GLGAFPATHRQALGMLG-MHGTYEaNMTMHNADVIFAVG---VRFDDRTTNnlakycPNA--TVLHIDIDPTSISKTVTA 316
Cdd:PRK08322 233 GKGVIPETHPLSLGTAGlSQGDYV-HCAIEHADLIINVGhdvIEKPPFFMN------PNGdkKVIHINFLPAEVDPVYFP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 317 DIPIVGDARQVLEQMLELLSqESAHQPLDEIRDWWQQIEQwrarqclKYDTHSEK----IKPQAVIETLWRLTKGDAYVT 392
Cdd:PRK08322 306 QVEVVGDIANSLWQLKERLA-DQPHWDFPRFLKIREAIEA-------HLEEGADDdrfpMKPQRIVADLRKVMPDDDIVI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 393 SDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVN 472
Cdd:PRK08322 378 LDNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 473 LNNRYLGMVKqWQDMIYSGRHsqSYMQ-SLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSE 551
Cdd:PRK08322 458 LNDNAYGMIR-WKQENMGFED--FGLDfGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQ---PGVHVIDCPVDYSE 531
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-533 |
3.15e-109 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 338.00 E-value: 3.15e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK08199 5 PRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK08199 85 NASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 161 LPKDIL----NPANKLPYVWPEsvsmrsynptTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLP 236
Cdd:PRK08199 165 LPEDVLsetaEVPDAPPYRRVA----------AAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 237 VVCSLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNN---LAKYCPNATVLHIDIDPTSISKT 313
Cdd:PRK08199 235 VACAFRRQDLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELGRV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 314 VTADIPIVGDARQVLEQMLELlsqESAHQP--LDEIRDWWQQIEQWRARQCLKYDTHSEkikpqAVIETLWRLTKGDAYV 391
Cdd:PRK08199 315 YRPDLAIVADPAAFAAALAAL---EPPASPawAEWTAAAHADYLAWSAPLPGPGAVQLG-----EVMAWLRERLPADAII 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 392 TSDVGQHQMFAALYYPFDKPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVV 471
Cdd:PRK08199 387 TNGAGNYATWLHRFFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVI 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111084 472 NLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALE 533
Cdd:PRK08199 466 VVNNGMYGTIRMHQEREYPGRVSGTDLTN-PDFAALARAYGGHGETVERTEDFAPAFERALA 526
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
372-556 |
1.48e-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: 320.21 E-value: 1.48e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 372 IKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSI 451
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 452 QMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEA 531
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|....*
gi 90111084 532 LEqvrNNRLVFVDVTVDGSEHVYPM 556
Cdd:cd02015 161 LA---SDGPVLLDVLVDPEENVLPM 182
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-551 |
2.22e-106 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 330.05 E-value: 2.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLV-RHEQAAVHMADGLARATGEVGVVLVTSGPGA 79
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHtRHEQAAGYMAFGYARSTGRPGVCSVVPGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 80 TNAITGIATAYMDSIPLVVLSGQVATSLI--GYDAFQEC-DMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGP 156
Cdd:PRK08266 81 LNAGAALLTAYGCNSPVLCLTGQIPSALIgkGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 157 VVVDLPKDILN------PANKLPYVWPESVsmrsyNPTttghkgQIKRALQTLVAAKKPVVYVGGGAITAGchQQLKETV 230
Cdd:PRK08266 161 VALEMPWDVFGqrapvaAAPPLRPAPPPAP-----DPD------AIAAAAALIAAAKNPMIFVGGGAAGAG--EEIRELA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 231 EALNLPVVCSLMGLGAFPATHRQALGMLGmhgtyeANMTMHNADVIFAVGVRFDDRTTNnlAKYCP-NATVLHIDIDPTS 309
Cdd:PRK08266 228 EMLQAPVVAFRSGRGIVSDRHPLGLNFAA------AYELWPQTDVVIGIGSRLELPTFR--WPWRPdGLKVIRIDIDPTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 310 ISKTvTADIPIVGDARQVLEQMLELLSQESAHQP-----LDEIRDWWQQieqwrarqclkydtHSEKIKPQ-----AVIE 379
Cdd:PRK08266 300 MRRL-KPDVAIVADAKAGTAALLDALSKAGSKRPsrraeLRELKAAARQ--------------RIQAVQPQasylrAIRE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 380 TLWRltkgDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELS 459
Cdd:PRK08266 365 ALPD----DGIFVDELSQVGFASWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 460 TALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALeqvRNNR 539
Cdd:PRK08266 441 TAVQHNIGVVTVVFNNNAYGNVRRDQKRRFGGRVVASDLVN-PDFVKLAESFGVAAFRVDSPEELRAALEAAL---AHGG 516
|
570
....*....|...
gi 90111084 540 LVFVDVTV-DGSE 551
Cdd:PRK08266 517 PVLIEVPVpRGSE 529
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
7-549 |
3.88e-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: 315.26 E-value: 3.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDaLHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
Cdd:TIGR03457 5 SEAFVEVLVANGVTHAFGIMGSAFMDAMD-LFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKDIL 166
Cdd:TIGR03457 84 AAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRDYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 167 NPANKLPYVWPESVSMRSYNPTTtghkgqIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMGLGA 246
Cdd:TIGR03457 163 YGEIDVEIPRPVRLDRGAGGATS------LAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 247 FPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTT--NNLAKYCP-NATVLHIDIDPTSISKTVTADIPIVGD 323
Cdd:TIGR03457 237 FPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLGPFGTlpQYGIDYWPkNAKIIQVDANAKMIGLVKKVTVGICGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 324 ARQVLEQMLELL-------SQESAHQPLDEIR-DWWQQIEQW---RARQCLKYDTHSEK-----IKPQAVIETLWRLTKG 387
Cdd:TIGR03457 317 AKAAAAEILQRLagkagdaNRAERKAKIQAERsAWEQELSEMtheRDPFSLDMIVEQRQeegnwLHPRQVLRELEKAMPE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 388 DAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELP 467
Cdd:TIGR03457 397 DAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 468 VLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRLVFVDVTV 547
Cdd:TIGR03457 477 VTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQAEGKTTVIEIVC 556
|
..
gi 90111084 548 DG 549
Cdd:TIGR03457 557 TR 558
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-561 |
1.48e-98 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 310.78 E-value: 1.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTV-GGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGA 79
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 80 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVV 159
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 160 DLPKDILNPANKLPYVWPeSVSMRSYNPTTtgHKGQIKRALQTLVAAKKPVVYVGGGAITAGchQQLKETVEALNLPVVC 239
Cdd:PRK08611 160 TIPDDLPAQKIKDTTNKT-VDTFRPTVPSP--KPKDIKKAAKLINKAKKPVILAGLGAKHAK--EELLAFAEKAKIPIIH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 240 SLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRttnnlaKYCPN-ATVLHIDIDPTSISKTVTADI 318
Cdd:PRK08611 235 TLPAKGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPKkAKAIQIDTDPANIGKRYPVNV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 319 PIVGDARQVLEQMLELLSQESAHQPLDEIRD----WWQQIEQWRARQclkydthSEKIKPQAVIETLWRLTKGDAYVTSD 394
Cdd:PRK08611 309 GLVGDAKKALHQLTENIKHVEDRRFLEACQEnmakWWKWMEEDENNA-------STPIKPERVMAAIQKIADDDAVLSVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 395 VGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLN 474
Cdd:PRK08611 382 VGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 475 NRYLGMVKQWQdmiysgrhsQS-----YMQSL--PDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTV 547
Cdd:PRK08611 462 NQQLAFIKYEQ---------QAageleYAIDLsdMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQ---DKPVIIDVYV 529
|
570
....*....|....
gi 90111084 548 DGSEHVYPMQIRGG 561
Cdd:PRK08611 530 DPNAAPLPGKIVND 543
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-545 |
6.80e-96 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 304.23 E-value: 6.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMlSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDaLHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK07525 4 MKM-TPSEAFVETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVD 160
Cdd:PRK07525 82 NFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 161 LPKDIlnpanklpyvWPESVSMRSYNPTT----TGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLP 236
Cdd:PRK07525 161 IPRDY----------FYGVIDVEIPQPVRlergAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 237 VVCSLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTnnLAK----YCP-NATVLHIDIDPTSIS 311
Cdd:PRK07525 231 VACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPFGT--LPQygidYWPkDAKIIQVDINPDRIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 312 KTVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIR---------DWWQQIEQW-------------RARqclkyDTHS 369
Cdd:PRK07525 309 LTKKVSVGICGDAKAVARELLARLAERLAGDAGREERkaliaaeksAWEQELSSWdhedddpgtdwneEAR-----ARKP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 370 EKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDG 449
Cdd:PRK07525 384 DYMHPRQALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 450 SIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLS 529
Cdd:PRK07525 464 AWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALK 543
|
570
....*....|....*.
gi 90111084 530 EALEQVRNNRLVFVDV 545
Cdd:PRK07525 544 RAIDAQNEGKTTVIEI 559
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
3-553 |
2.08e-92 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 293.42 E-value: 2.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 3 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNA 82
Cdd:PRK07524 1 MTTCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAG-SGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 83 ITGIATAYMDSIPLVVLSG-QVATSL-IGYDAFQEC-DMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 159
Cdd:PRK07524 80 ATAMGQAYADSIPMLVISSvNRRASLgKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 160 DLPKDILnpANKLPYVWPESVSmRSYNPTTtgHKGQIKRALQTLVAAKKPVVYVGGGAITAGchQQLKETVEALNLPVVC 239
Cdd:PRK07524 160 EIPLDVL--AAPADHLLPAPPT-RPARPGP--APAALAQAAERLAAARRPLILAGGGALAAA--AALRALAERLDAPVAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 240 SLMGLGAFPATHRQALGmlgmhgtyeANMT-------MHNADVIFAVG---------VRFDDRttnnlakYCPNATVLHI 303
Cdd:PRK07524 233 TINAKGLLPAGHPLLLG---------ASQSlpavralIAEADVVLAVGtelgetdydVYFDGG-------FPLPGELIRI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 304 DIDPTSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPldeirdwWQQIEQWRARQCLKyDTHSEKIKPQAVIETLWR 383
Cdd:PRK07524 297 DIDPDQLARNYPPALALVGDARAALEALLARLPGQAAAAD-------WGAARVAALRQALR-AEWDPLTAAQVALLDTIL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 384 LTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSG-GLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTAL 462
Cdd:PRK07524 369 AALPDAIFVGDSTQPVYAGNLYFDADAPRRWFNAStGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 463 QYELPVLVVNLNNRYLGMVKqwqdmiysgrhsqSYMQSL-----------PDFVRLAEAYGHVGIQISHPHELESKLSEA 531
Cdd:PRK07524 449 EADLPLIVLLWNNDGYGEIR-------------RYMVARdiepvgvdpytPDFIALARAFGCAAERVADLEQLQAALRAA 515
|
570 580
....*....|....*....|..
gi 90111084 532 LEQvrnNRLVFVDVTVDGSEHV 553
Cdd:PRK07524 516 FAR---PGPTLIEVDQACWFAA 534
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
5-557 |
2.07e-88 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 283.67 E-value: 2.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 84
Cdd:PRK08617 6 YGADLVVDSLINQGVKYVFGIPGAKIDRVFDALED-SGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 85 GIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKD 164
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 165 ILN-PANKLPYVWPESVSMRSYNPtttghkGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMG 243
Cdd:PRK08617 165 VVDaPVTSKAIAPLSKPKLGPASP------EDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 244 LGAFPATH-RQALGMLGMHGTYEANMTMHNADVIFAVG---VRFDDRTTNNLakycPNATVLHIDIDPTSISKTVTADIP 319
Cdd:PRK08617 239 AGVISRELeDHFFGRVGLFRNQPGDELLKKADLVITIGydpIEYEPRNWNSE----GDATIIHIDVLPAEIDNYYQPERE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 320 IVGDARQVLEQMLELLSQ----ESAHQPLDEIRdwwqqiEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDV 395
Cdd:PRK08617 315 LIGDIAATLDLLAEKLDGlslsPQSLEILEELR------AQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 396 GQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNN 475
Cdd:PRK08617 389 GSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWND 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 476 RYLGMVKQWQDMIY---SGRHSQSYmqslpDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDGSEH 552
Cdd:PRK08617 469 GHYNMVEFQEEMKYgrsSGVDFGPV-----DFVKYAESFGAKGLRVTSPDELEPVLREALAT---DGPVVIDIPVDYSDN 540
|
....*
gi 90111084 553 VYPMQ 557
Cdd:PRK08617 541 IKLME 545
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-557 |
5.57e-87 |
|
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: 279.71 E-value: 5.57e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALED-KGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 166 LNpanklpyvwpESVSMRSYNPTTTGHKG-----QIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCS 240
Cdd:TIGR02418 160 VD----------SPVSVKAIPASYAPKLGaapddAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 241 LMGLGAFPAT-HRQALGMLGMHGTYEANMTMHNADVIFAVG---VRFDDRTTNNLAkycpNATVLHIDIDPTSISKTVTA 316
Cdd:TIGR02418 230 FQGAGAVSRElEDHFFGRVGLFRNQPGDRLLKQADLVITIGydpIEYEPRNWNSEN----DATIVHIDVEPAQIDNNYQP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 317 DIPIVGDarqvLEQMLELLSQESAH-----QPLDEIRDWWQQIEQWRARqclKYDTHSEKIKPQAVIETLWRLTKGDAYV 391
Cdd:TIGR02418 306 DLELVGD----IASTLDLLAERIPGyelppDALAILEDLKQQREALDRV---PATLKQAHLHPLEIIKAMQAIVTDDVTV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 392 TSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVL-V 470
Cdd:TIGR02418 379 TVDMGSHYIWMARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVhI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 471 VNLNNRYlGMVKQWQDMIYsgrHSQSYMQSLP-DFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVDG 549
Cdd:TIGR02418 459 IWNDNGY-NMVEFQEEMKY---QRSSGVDFGPiDFVKYAESFGAKGLRVESPDQLEPTLRQAMEV---EGPVVVDIPVDY 531
|
....*...
gi 90111084 550 SEHVYPMQ 557
Cdd:TIGR02418 532 SDNPKLMS 539
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
2-545 |
1.59e-86 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 279.00 E-value: 1.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALhtvgGIDHVLVRHEQAAVHMADGLARATG--EVGVVLVTSGPGA 79
Cdd:PRK06154 18 KTMKVAEAVAEILKEEGVELLFGFPVNELFDAAAAA----GIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 80 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDA-FQECDMVgisRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVV 158
Cdd:PRK06154 94 ENAFGGVAQAYGDSVPVLFLPTGYPRGSTDVAPnFESLRNY---RHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 159 VDLPKDILN-PANKLPYVWPESVSMRSY-NPTTtghkgqIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLP 236
Cdd:PRK06154 171 LELPVDVLAeELDELPLDHRPSRRSRPGaDPVE------VVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 237 VVCSLMGLGAFPATHRQALGMLGMhgTYEANMT--MHNADVIFAVGVRFddrTTNNLAKYCP-NATVLHIDIDPTSISKT 313
Cdd:PRK06154 245 VMTTLNGKSAFPEDHPLALGSGGR--ARPATVAhfLREADVLFGIGCSL---TRSYYGLPMPeGKTIIHSTLDDADLNKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 314 VTADIPIVGDARQVLEQMLELLSQESAHQP---------LDEIRDWWqqIEQWRArqclKYDTHSEKIKPQAVI-ETLWR 383
Cdd:PRK06154 320 YPIDHGLVGDAALVLKQMIEELRRRVGPDRgraqqvaaeIEAVRAAW--LAKWMP----KLTSDSTPINPYRVVwELQHA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 384 LTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQ 463
Cdd:PRK06154 394 VDIKTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 464 YELPVLVVNLNNRYLGmvkqwqdmiysgrhsqSYMQSLP-------------DFVRLAEAYGHVGIQISHPHELESKLSE 530
Cdd:PRK06154 474 ERIPILTILLNNFSMG----------------GYDKVMPvsttkyratdisgDYAAIARALGGYGERVEDPEMLVPALLR 537
|
570
....*....|....*
gi 90111084 531 ALEQVRNNRLVFVDV 545
Cdd:PRK06154 538 ALRKVKEGTPALLEV 552
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
3-556 |
5.37e-82 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 266.70 E-value: 5.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 3 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNA 82
Cdd:PRK06457 1 MPSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRK-SKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 83 ITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLP 162
Cdd:PRK06457 80 LNGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 163 KDILNPANKLPYVWPESVSMRSYNPTTTGHKGQIKRalqtlvaAKKPVVYVGGGAITAGchQQLKETVEALNLPVVCSLM 242
Cdd:PRK06457 159 VDILRKSSEYKGSKNTEVGKVKYSIDFSRAKELIKE-------SEKPVLLIGGGTRGLG--KEINRFAEKIGAPIIYTLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 243 GLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNlakycPNATVLHIDIDPTSISKTVTADIPIVG 322
Cdd:PRK06457 230 GKGILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLN-----KSAKVIQVDIDNSNIGKRLDVDLSYPI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 323 DARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQwrarqcLKYDThSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFA 402
Cdd:PRK06457 305 PVAEFLNIDIEEKSDKFYEELKGKKEDWLDSISK------QENSL-DKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 403 ALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMAL-PEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 481
Cdd:PRK06457 378 ARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAVeNKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111084 482 KQWQD-MIYSGRHSQSYMqslPDFVRLAEAYGHVGIQISHPHELESKLSEALeqvRNNRLVFVDVTVDGSEHvyPM 556
Cdd:PRK06457 458 KFEQEvMGYPEWGVDLYN---PDFTKIAESIGFKGFRLEEPKEAEEIIEEFL---NTKGPAVLDAIVDPNER--PM 525
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
5-552 |
7.75e-77 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 253.92 E-value: 7.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 5 SGAEMVVRSLIDQGVKQVFGYpggavlDIYDALHTVG---GIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFGQ------SLPSALFLAAeaiGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 82 AITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDL 161
Cdd:PRK06112 89 LVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 162 PKDILNPANKLPYVwPESVSMRSYnP--TTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVC 239
Cdd:PRK06112 169 PADLLTAAAAAPAA-PRSNSLGHF-PldRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVAT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 240 SLMGLGAFPATHRQALGMLGM------HGTYEANMtMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKT 313
Cdd:PRK06112 247 TNMGKGAVDETHPLSLGVVGSlmgprsPGRHLRDL-VREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGRN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 314 VTAdIPIVGDARQVLEQMLELLSQESAHQPLDE-------IRDWWQQIEQWRARQclkYDTHSEKIKPQAVIETLWRLTK 386
Cdd:PRK06112 326 YEA-LRLVGDARLTLAALTDALRGRDLAARAGRraalepaIAAGREAHREDSAPV---ALSDASPIRPERIMAELQAVLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 387 GDAYVTSDVGQHQMFAALYYPFDKPR-RWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYE 465
Cdd:PRK06112 402 GDTIVVADASYSSIWVANFLTARRAGmRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 466 LPVLVVNLNNRYLGMVKQWQDMIYsGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHEleskLSEALEQVRNNRLVFV-D 544
Cdd:PRK06112 482 VPVTIVVLNNGILGFQKHAETVKF-GTHTDACHFAAVDHAAIARACGCDGVRVEDPAE----LAQALAAAMAAPGPTLiE 556
|
....*...
gi 90111084 545 VTVDGSEH 552
Cdd:PRK06112 557 VITDPSAF 564
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
18-549 |
1.39e-72 |
|
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: 242.82 E-value: 1.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 18 GVKQVFGYPGGAVLDIYDALHT-VGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPL 96
Cdd:TIGR02720 13 GVDHIYGIPGGSFNSTMDALSAeRDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYDAKEDHVPV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 97 VVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVVVDLPKDIlnPANKLP--Y 174
Cdd:TIGR02720 93 LALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAI-RRAYAHNGVAVVTIPVDF--GWQEIPdnD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 175 VWPESVSMRSYN-PTTTGHkgQIKRALQTLVAAKKPVVYVGGGAITAGchQQLKETVEALNLPVVCSLMGLGAFPATHRQ 253
Cdd:TIGR02720 170 YYASSVSYQTPLlPAPDVE--AVTRAVQTLKAAERPVIYYGIGARKAG--EELEALSEKLKIPLISTGLAKGIIEDRYPA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 254 ALGMLGMHGTYEANMTMHNADVIFAVGVRFD----DRTTNNlAKYcpnatVLHIDIDPTSISKTVTADIPIVGDARQVLE 329
Cdd:TIGR02720 246 YLGSAYRVAQKPANEALFQADLVLFVGNNYPfaevSKAFKN-TKY-----FIQIDIDPAKLGKRHHTDIAVLADAKKALA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 330 QMLELLSQESAHQpldeirdWWQ----QIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALY 405
Cdd:TIGR02720 320 AILAQVEPRESTP-------WWQanvaNVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 406 YPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQ 485
Cdd:TIGR02720 393 LKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQ 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111084 486 DmiysGRHSQSYMQSLP--DFVRLAEAYGHVGIQISHPHELESKLSEALeQVRNNRLVFVDVTVDG 549
Cdd:TIGR02720 473 E----DTNQPLIGVDFNdaDFAKIAEGVGAVGFRVNKIEQLPAVFEQAK-AIKQGKPVLIDAKITG 533
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-163 |
1.65e-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: 1.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 8 EMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIA 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111084 88 TAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
7-548 |
1.37e-68 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 232.49 E-value: 1.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGG-IDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVkHSFLVKQT--EDIPQVLKKAFWLAASGRpGPVVVDLPK 163
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVA-GAFVQMVTvpEQLRHLVDRAVRTALAER-TVTAVILPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 164 DIlnpaNKLPYVWPE--------SVSMRSynPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAitAGCHQQLKETVEALNL 235
Cdd:PRK08273 164 DV----QELEYEPPPhahgtvhsGVGYTR--PRVVPYDEDLRRAAEVLNAGRKVAILVGAGA--LGATDEVIAVAERLGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 236 PVVCSLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDdrttnnLAKYCP---NATVLHIDIDPTSISK 312
Cdd:PRK08273 236 GVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFP------YSEFLPkegQARGVQIDIDGRMLGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 313 TVTADIPIVGDARQVLEQMLELLSQesahqplDEIRDWWQQIEQWRAR--QCLKYDTH--SEKIKPQAVIETLWRLTKGD 388
Cdd:PRK08273 310 RYPMEVNLVGDAAETLRALLPLLER-------KKDRSWRERIEKWVARwwETLEARAMvpADPVNPQRVFWELSPRLPDN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 389 AYVTSDVGQhqmfAALYYPFD-KPRRWIN---SGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMN-IQELSTALQ 463
Cdd:PRK08273 383 AILTADSGS----CANWYARDlRMRRGMMaslSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 464 Y----ELPVLVVN-LNNRYLGMVkQWQDMIYSGRHSQSYMQSLPDF--VRLAEAYGHVGIQISHPHELESKLSEALEQvr 536
Cdd:PRK08273 459 YwrqwSDPRLIVLvLNNRDLNQV-TWEQRVMEGDPKFEASQDLPDVpyARFAELLGLKGIRVDDPEQLGAAWDEALAA-- 535
|
570
....*....|..
gi 90111084 537 nNRLVFVDVTVD 548
Cdd:PRK08273 536 -DRPVVLEVKTD 546
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
6-489 |
2.15e-65 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 222.67 E-value: 2.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGARE-EGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 166 L---NPANKLPYVWPESVSMRSYNPTttghkgQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLM 242
Cdd:PRK05858 166 AfsmADDDGRPGALTELPAGPTPDPD------ALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 243 GLGAFPATHRQALgmlgmhgTYEANMTMHNADVIFAVGVRFDDRTtnNLAKYCPNATVLHIDIDPTSISKTVTADIPIVG 322
Cdd:PRK05858 240 GRGVVPADHPLAF-------SRARGKALGEADVVLVVGVPMDFRL--GFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 323 DARQVLEQMLELLSQESAHQP-LDEIRDwwqQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 401
Cdd:PRK05858 311 DLSAILSALAGAGGDRTDHQGwIEELRT---AETAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 402 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMV 481
Cdd:PRK05858 388 AGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLE 467
|
....*...
gi 90111084 482 KQWQDMIY 489
Cdd:PRK05858 468 KHPMEALY 475
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
6-166 |
4.06e-64 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 207.47 E-value: 4.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQ-ECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKD 164
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 90111084 165 IL 166
Cdd:pfam02776 161 VL 162
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
394-545 |
6.24e-64 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 206.28 E-value: 6.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 394 DVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNL 473
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111084 474 NNRYLGMVKQWQDMIYSGRHSQSYMQSL--PDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDV 545
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGKILppVDFAKLAEAYGAKGARVESPEELEEALKEALEH---DGPALIDV 151
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
2-532 |
9.64e-64 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 218.32 E-value: 9.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 82 AITGIATAYMDSIPLVVLSGQVATSLIGYDA--FQEC-DMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVV 158
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 159 VDLPKDIlnpaNKLPYVWPESVSMrSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGchQQLKETVEaLNLPVV 238
Cdd:PRK07064 161 VEIPIDI----QAAEIELPDDLAP-VHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAG--AEVKRLVD-LGFGVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 239 CSLMGLGAFPATHRQALGMLGMHGTYEAnmTMHNADVIFAVGVRFDDRTTNNLAKYCPnATVLHIDIDPTSISKTVTADI 318
Cdd:PRK07064 233 TSTQGRGVVPEDHPASLGAFNNSAAVEA--LYKTCDLLLVVGSRLRGNETLKYSLALP-RPLIRVDADAAADGRGYPNDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 319 PIVGDARQVLEQMLELLSQESAHQPldeirDWWQQIEqwRARQcLKYDTHSEKIKPQAVI-ETLWRLTKGDAYVTSDVG- 396
Cdd:PRK07064 310 FVHGDAARVLARLADRLEGRLSVDP-----AFAADLR--AARE-AAVADLRKGLGPYAKLvDALRAALPRDGNWVRDVTi 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 397 QHQMFAALYYPFDKPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNR 476
Cdd:PRK07064 382 SNSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDG 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 90111084 477 YLGMVKQWQDMIYSGRHsqsYMQSL--PDFVRLAEAYGHVGIQISHPHELESKLSEAL 532
Cdd:PRK07064 461 GYGVIRNIQDAQYGGRR---YYVELhtPDFALLAASLGLPHWRVTSADDFEAVLREAL 515
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-550 |
3.92e-63 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 217.17 E-value: 3.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPG---GAVLDIYDALHTVGGI--DHVLVRHEQAAVHMADGLARATGEVGVVLVTS 75
Cdd:PRK08327 4 LTMYTAAELFLELLKELGVDYIFINSGtdyPPIIEAKARARAAGRPlpEFVICPHEIVAISMAHGYALVTGKPQAVMVHV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 76 GPGATNAITGIATAYMDSIPLVVLSGQVATS----------LIGY--DAFqecDMVGISRPVVKHSFLVKQTEDIPQVLK 143
Cdd:PRK08327 84 DVGTANALGGVHNAARSRIPVLVFAGRSPYTeegelgsrntRIHWtqEMR---DQGGLVREYVKWDYEIRRGDQIGEVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 144 KAFWLAASGRPGPVVVDLPKDILnpANKLPYVwpeSVSMRSYNPTTTGH--KGQIKRALQTLVAAKKPVVYVGGGAITAG 221
Cdd:PRK08327 161 RAIQIAMSEPKGPVYLTLPREVL--AEEVPEV---KADAGRQMAPAPPApdPEDIARAAEMLAAAERPVIITWRAGRTAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 222 CHQQLKETVEALNLPVVCSLMGLGAFPATHrqalgmlGMHGTYEANMTMHNADVIFAVGvrfddrttnNLAKYCP----- 296
Cdd:PRK08327 236 GFASLRRLAEELAIPVVEYAGEVVNYPSDH-------PLHLGPDPRADLAEADLVLVVD---------SDVPWIPkkirp 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 297 --NATVLHIDIDPtsiSKTVT------ADIPIVGDARQVLEQMLELL--SQESAHQPLDEIRDWWQQI---EQWRARQCL 363
Cdd:PRK08327 300 daDARVIQIDVDP---LKSRIplwgfpCDLCIQADTSTALDQLEERLksLASAERRRARRRRAAVRELrirQEAAKRAEI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 364 KYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGqhqmFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVV 443
Cdd:PRK08327 377 ERLKDRGPITPAYLSYCLGEVADEYDAIVTEYP----FVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 444 CVTGDGSIQMNIQE--LSTALQYELPVLVVNLNNRYLGMVKQWQDMIYS---GRHSQSYMQS----LPDFVRLAEAYGHV 514
Cdd:PRK08327 453 ATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPegyAARKGTFPGTdfdpRPDFAKIAEAFGGY 532
|
570 580 590
....*....|....*....|....*....|....*..
gi 90111084 515 GIQISHPHELESKLSEALEQVRN-NRLVFVDVTVDGS 550
Cdd:PRK08327 533 GERVEDPEELKGALRRALAAVRKgRRSAVLDVIVDRV 569
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
7-558 |
3.47e-62 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 214.85 E-value: 3.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVVVDLPKDI- 165
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAM-RKAILNRGVAVVVLPGDVa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 166 LNPAnklpyvwPESVSMRSYN---PTTTGHKGQIKRALQTLVAAKKPVVYVGGGaiTAGCHQQLKETVEALNLPVVCSLM 242
Cdd:PRK09124 165 LKPA-------PERATPHWYHapqPVVTPAEEELRKLAALLNGSSNITLLCGSG--CAGAHDELVALAETLKAPIVHALR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 243 GLGAFPATHRQALGMLGMHG---TYEAnmtMHNADVIFAVGVRFDDRttnnlAKYCPNATVLHIDIDPTSISKTVTADIP 319
Cdd:PRK09124 236 GKEHVEYDNPYDVGMTGLIGfssGYHA---MMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDLG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 320 IVGDARQVLEQMLELLSQESAHQPLDEIRDWWQqieqwRARQCL----KYDTHSEKIKPQAVIETLWRLTKGDAYVTSDV 395
Cdd:PRK09124 308 LVGDVKATLAALLPLLEEKTDRKFLDKALEHYR-----KARKGLddlaVPSDGGKPIHPQYLARQISEFAADDAIFTCDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 396 GQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNN 475
Cdd:PRK09124 383 GTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNN 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 476 RYLGMVKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEqvrNNRLVFVDVTVDGSEHVYP 555
Cdd:PRK09124 463 SVLGFVA--MEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFA---HDGPALVDVVTAKQELAMP 537
|
...
gi 90111084 556 MQI 558
Cdd:PRK09124 538 PQI 540
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
17-548 |
3.12e-60 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 208.66 E-value: 3.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 17 QGVKQVFGYPGGAVLDIYDALHtvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPL 96
Cdd:PRK07092 25 FGITTVFGNPGSTELPFLRDFP--DDFRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFTAFKNHTPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 97 VVLSGQVATSLIGYDAF-QECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDILN-PAnklPY 174
Cdd:PRK07092 103 VITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYDDWDqPA---EP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 175 VWPESVSmRSYNPTttghKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLM-GLGAFPATHRQ 253
Cdd:PRK07092 180 LPARTVS-SAVRPD----PAALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPVWVAPMsGRCSFPEDHPL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 254 ALGML-GMHGTYEANMTMHnaDVIFAVGV---RFDDRTTnnlAKYCP-NATVLHIDIDPTSISKTVTADiPIVGDARQVL 328
Cdd:PRK07092 255 FAGFLpASREKISALLDGH--DLVLVIGApvfTYHVEGP---GPHLPeGAELVQLTDDPGEAAWAPMGD-AIVGDIRLAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 329 EQMLELL--SQESAHQPLdeirdwwQQIEQWRARqclkydthSEKIKPQAVIETLWRLT-KGDAYV---TSDVGQHQMFA 402
Cdd:PRK07092 329 RDLLALLppSARPAPPAR-------PMPPPAPAP--------GEPLSVAFVLQTLAALRpADAIVVeeaPSTRPAMQEHL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 403 AL-----YYPFDkprrwinSGGLgtmGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNN-R 476
Cdd:PRK07092 394 PMrrqgsFYTMA-------SGGL---GYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNgR 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111084 477 YLGMvkQWQDMIYSGRHSQSYmqSLP--DFVRLAEAYGHVGIQISHPHELESKLSEALeqvRNNRLVFVDVTVD 548
Cdd:PRK07092 464 YGAL--RWFAPVFGVRDVPGL--DLPglDFVALARGYGCEAVRVSDAAELADALARAL---AADGPVLVEVEVA 530
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
196-331 |
9.83e-60 |
|
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: 9.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 196 IKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADV 275
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 90111084 276 IFAVGVRFDD-RTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDARQVLEQM 331
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
7-548 |
2.25e-59 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 207.53 E-value: 2.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWlAASGRPGPVVVDLPKDIL 166
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQ-HAVAGGGVSVVTLPGDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 167 NPANKLPYVwpeSVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGaiTAGCHQQLKETVEALNLPVVCSLMGLGA 246
Cdd:PRK06546 165 DEPAPEGFA---PSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAG--VRGAHAEVLALAEKIKAPVGHSLRGKEW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 247 FPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRF--DDrttnnlakYCPNATVLHIDIDPTSISKTVTADIPIVGDA 324
Cdd:PRK06546 240 IQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFpyDQ--------FLPDVRTAQVDIDPEHLGRRTRVDLAVHGDV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 325 RQVLEQMLELLSQESAHQPLDEIRDwwqqiEQWRARQCL--KYDTHSEK---IKPQAVIETLWRLTKGDAYVTSDVGQHQ 399
Cdd:PRK06546 312 AETIRALLPLVKEKTDRRFLDRMLK-----KHARKLEKVvgAYTRKVEKhtpIHPEYVASILDELAADDAVFTVDTGMCN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 400 MFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLG 479
Cdd:PRK06546 387 VWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLG 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111084 480 MVKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQvrnNRLVFVDVTVD 548
Cdd:PRK06546 467 MVK--LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAH---PGPALVDVVTD 530
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
14-548 |
6.20e-52 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 186.52 E-value: 6.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 14 LIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDS 93
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 94 IPLVVLSG------QVATSLI-------GYDAFQEcdmvgISRPV-VKHSFLVKQT--EDIPQVLKKAFwlaASGRpgPV 157
Cdd:COG3961 94 VPVVHIVGapgtraQRRGPLLhhtlgdgDFDHFLR-----MFEEVtVAQAVLTPENaaAEIDRVLAAAL---REKR--PV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 158 VVDLPKDILNpankLPYVWPESVSMRSYNPTTTGHKGQ-IKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLP 236
Cdd:COG3961 164 YIELPRDVAD----APIEPPEAPLPLPPPASDPAALAAaVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 237 VVCSLMGLGAFPATHRQALgmlgmhGTYEANM-------TMHNADVIFAVGVRFDDRTTNNL-AKYCPNATvlhIDIDP- 307
Cdd:COG3961 240 VATTLLGKSVLDESHPQFI------GTYAGAAsspevreYVENADCVLCLGVVFTDTNTGGFtAQLDPERT---IDIQPd 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 308 -TSISKTVTADIPIvgdaRQVLEQMLELLSQESAHQPLDEIRDwwqqieqwrarqclkydtHSEKIKPQAVI--ETLWR- 383
Cdd:COG3961 311 sVRVGGHIYPGVSL----ADFLEALAELLKKRSAPLPAPAPPP------------------PPPPAAPDAPLtqDRLWQr 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 384 ----LTKGDAyVTSDVGQhQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELS 459
Cdd:COG3961 369 lqafLDPGDI-VVADTGT-SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 460 TALQYELPVLVVNLNNR-Y------LGM------VKQWqdmiysgrhsqsymqslpDFVRLAEAYG---HVGIQISHPHE 523
Cdd:COG3961 447 TMLRYGLKPIIFVLNNDgYtieraiHGPdgpyndIANW------------------DYAKLPEAFGggnALGFRVTTEGE 508
|
570 580
....*....|....*....|....*..
gi 90111084 524 LEsklsEALEQVRNN--RLVFVDVTVD 548
Cdd:COG3961 509 LE----EALAAAEANtdRLTLIEVVLD 531
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
2-551 |
2.43e-51 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 185.19 E-value: 2.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIyDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK09259 8 QLTDGFHLVIDALKLNGIDTIYGVVGIPITDL-ARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 82 AITGIATAYMDSIPLVVLSGQVATSLIGYDA--FQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVV 159
Cdd:PRK09259 87 GLTALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 160 DLPKDIL-----------------NPANK-LPYvwPESVsmrsynptttghkgqiKRALQTLVAAKKPVVYVGGGAITAG 221
Cdd:PRK09259 167 DLPAKVLaqtmdadealtslvkvvDPAPAqLPA--PEAV----------------DRALDLLKKAKRPLIILGKGAAYAQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 222 CHQQLKETVEALNLPVVCSLMGLGAFPATHRQALGMlgmhgtyEANMTMHNADVIFAVGVRFDDRTTNNLAK-YCPNATV 300
Cdd:PRK09259 229 ADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAA-------ARSLALANADVVLLVGARLNWLLSHGKGKtWGADKKF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 301 LHIDIDPTSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPLdeirDWWQQIEQWRARQCLKYDTHSEKIKPQ----- 375
Cdd:PRK09259 302 IQIDIEPQEIDSNRPIAAPVVGDIGSVMQALLAGLKQNTFKAPA----EWLDALAERKEKNAAKMAEKLSTDTQPmnfyn 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 376 --AVIETLWRlTKGDAYVTSD-----------VGQHQmfaalyypfdkPRRWINSGGLGTMGFGLPAALG--VKMALPee 440
Cdd:PRK09259 378 alGAIRDVLK-ENPDIYLVNEgantldlarniIDMYK-----------PRHRLDCGTWGVMGIGMGYAIAaaVETGKP-- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 441 tVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNrylGMVKQWQDMIYSGRHSQSYMQSLPD--FVRLAEAYGHVGIQI 518
Cdd:PRK09259 444 -VVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNN---GGIYRGDDVNLSGAGDPSPTVLVHHarYDKMMEAFGGVGYNV 519
|
570 580 590
....*....|....*....|....*....|....*.
gi 90111084 519 SHPHELESKLSEALEqvrNNRLVFVDVTVD---GSE 551
Cdd:PRK09259 520 TTPDELRHALTEAIA---SGKPTLINVVIDpaaGTE 552
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
376-547 |
3.61e-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: 170.51 E-value: 3.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 376 AVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNI 455
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 456 QELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALEQv 535
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSN-PDFAALAEAYGAKGVRVEDPEDLEAALAEALAA- 158
|
170
....*....|..
gi 90111084 536 rnNRLVFVDVTV 547
Cdd:cd00568 159 --GGPALIEVKT 168
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
372-551 |
2.49e-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: 149.99 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 372 IKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSI 451
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 452 QMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSymQSLPDFVRLAEAYGHVGIQISHPHELESKLSEA 531
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVD--LPNPDFAKIAEAMGIKGIRVEDPDELEAALDEA 159
|
170 180
....*....|....*....|
gi 90111084 532 LEQvrnNRLVFVDVTVDGSE 551
Cdd:cd02014 160 LAA---DGPVVIDVVTDPNE 176
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
7-165 |
4.70e-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: 148.47 E-value: 4.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111084 87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKDI 165
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGDV 160
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
374-551 |
1.64e-39 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 142.04 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 374 PQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQM 453
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 454 NIQELSTALQYELPVLVVNLNNRYLGMVKqWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLSEALE 533
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIK-WKQEKEYGRDSGVDFGN-PDFVKYAESFGAKGYRIESADDLLPVLERALA 158
|
170
....*....|....*...
gi 90111084 534 QvrnNRLVFVDVTVDGSE 551
Cdd:cd02010 159 A---DGVHVIDCPVDYSE 173
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
17-163 |
1.36e-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: 122.45 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 17 QGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDSIPL 96
Cdd:cd06586 10 WGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADAAAEHLPV 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111084 97 VVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVVVDLPK 163
Cdd:cd06586 89 VFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAI-RTAYASQGPVVVRLPR 154
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
370-549 |
4.83e-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: 119.54 E-value: 4.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 370 EKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDG 449
Cdd:cd02013 2 NPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 450 SIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYGHVGIQISHPHELESKLS 529
Cdd:cd02013 82 AWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELES-ESFAKIAEACGAKGITVDKPEDVGPALQ 160
|
170 180
....*....|....*....|
gi 90111084 530 EALEQVRNNRLVFVDVTVDG 549
Cdd:cd02013 161 KAIAMMAEGKTTVIEIVCDQ 180
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
367-543 |
1.44e-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: 107.37 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 367 THSEKI--KPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVC 444
Cdd:cd02006 1 THFDDVpiKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 445 VTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQ---DMIYSGRHSQSYMQSLP------DFVRLAEAYGHVG 515
Cdd:cd02006 81 LSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQrafDMDYQVNLAFENINSSElggygvDHVKVAEGLGCKA 160
|
170 180
....*....|....*....|....*...
gi 90111084 516 IQISHPHELESKLSEALEQVRNNRLVFV 543
Cdd:cd02006 161 IRVTKPEELAAAFEQAKKLMAEHRVPVV 188
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
374-534 |
1.97e-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: 106.14 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 374 PQAVIETLWRLTKGDA-----YVTSDVGQHQMFaalyyPFDKPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVTGD 448
Cdd:cd02002 3 PEYLAAALAAALPEDAiivdeAVTNGLPLRDQL-----PLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 449 GSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQS--YMQSL----PDFVRLAEAYGHVGIQISHPH 522
Cdd:cd02002 77 GSFMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENapDGLDLldpgIDFAAIAKAFGVEAERVETPE 156
|
170
....*....|..
gi 90111084 523 ELESKLSEALEQ 534
Cdd:cd02002 157 ELDEALREALAE 168
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
374-548 |
8.13e-26 |
|
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: 104.15 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 374 PQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQM 453
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 454 NIQELSTALQYELPVLVVNLNNrylgmvkqwqDMIYSGRHSQSYMQSLPDFV----------RLAEAYGHVGIQISHPHE 523
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNN----------GGWYQGLDGQQLSYGLGLPVttllpdtrydLVAEAFGGKGELVTTPEE 150
|
170 180
....*....|....*....|....*
gi 90111084 524 LESKLSEALEqvrNNRLVFVDVTVD 548
Cdd:cd02004 151 LKPALKRALA---SGKPALINVIID 172
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
401-548 |
3.88e-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: 87.97 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGM 480
Cdd:cd02005 30 FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTI 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111084 481 VKQWQDMiysgrhSQSYMQSLP-DFVRLAEAYG----HVGIQISHPHELESKLSEALEqvRNNRLVFVDVTVD 548
Cdd:cd02005 110 ERAIHGP------EASYNDIANwNYTKLPEVFGggggGLSFRVKTEGELDEALKDALF--NRDKLSLIEVILP 174
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
5-534 |
1.32e-19 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 92.21 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 84
Cdd:PRK07586 2 NGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 85 GIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVvkhSFLVKQTEDIPQV--LKKAFWLAASGRPGPVVVD-L 161
Cdd:PRK07586 82 NLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPV---SGWVRRSESAADVaaDAAAAVAAARGAPGQVATLiL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 162 PKDI-LNPANKLPYVwPESVSMRSYNPTTtghkgqIKRALQTLVAAKKPVVYVGGGAITA-------------GChQQLK 227
Cdd:PRK07586 159 PADVaWSEGGPPAPP-PPAPAPAAVDPAA------VEAAAAALRSGEPTVLLLGGRALRErglaaaariaaatGA-RLLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 228 ETVEAlnlpvvcsLMGLGA-FPATHR------QALGMLGmhgtyeanmtmhNADVIFAVGVRfddrttnnlakycpnatv 300
Cdd:PRK07586 231 ETFPA--------RMERGAgRPAVERlpyfaeQALAQLA------------GVRHLVLVGAK------------------ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 301 lhidiDPTSI-------SKTVTADIPIV------GDARQVLEQMLELLSQESAHQPLDEIRDWwqqieqwrarqclkyDT 367
Cdd:PRK07586 273 -----APVAFfaypgkpSRLVPEGCEVHtlagpgEDAAAALEALADALGAKPAAPPLAAPARP---------------PL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 368 HSEKIKPQAVIETLWRLTKGDAYVTSDVGqhqMFAALYYPFD---KPRRWINSGGlGTMGFGLPAALGVKMALPEETVVC 444
Cdd:PRK07586 333 PTGALTPEAIAQVIAALLPENAIVVDESI---TSGRGFFPATagaAPHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLA 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 445 VTGDGSIQMNIQELSTALQYELPVLVVNLNNR-Y--LGMVKQWQDMIYSGRHSQSyMQSL----PDFVRLAEAYGHVGIQ 517
Cdd:PRK07586 409 LQGDGSAMYTIQALWTQARENLDVTTVIFANRaYaiLRGELARVGAGNPGPRALD-MLDLddpdLDWVALAEGMGVPARR 487
|
570
....*....|....*..
gi 90111084 518 ISHPHELESKLSEALEQ 534
Cdd:PRK07586 488 VTTAEEFADALAAALAE 504
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
1-541 |
2.47e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 88.39 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK12474 2 GQTMNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVvkhSFLVKQTEDIPQV---LKKAFWLAASGRPGPV 157
Cdd:PRK12474 82 NGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPV---SRWVHRSASAGAVdsdVARAVQAAQSAPGGIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 158 VVDLPKDIL-NP----ANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEA 232
Cdd:PRK12474 159 TLIMPADVAwNEaayaAQPLRGIGPAPVAAETVERIAALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVRLYCDTFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 233 LNLPVVCSLMGLGAFPATHRQALGMLgmhgtyeanmtmHNADVIFAVGVRfddrttnnlakycPNATVLHIDIDPTSISK 312
Cdd:PRK12474 239 PRIERGAGRVPIERIPYFHEQITAFL------------KDVEQLVLVGAK-------------PPVSFFAYPGKPSWGAP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 313 TvTADIPIVGDARQVLEQMLELLSQE--SAHQPLDeirdwwqqieqwRARQCLKyDTHSEKIKPQAVIETLWRLTKGDAY 390
Cdd:PRK12474 294 P-GCEIVYLAQPDEDLAQALQDLADAvdAPAEPAA------------RTPLALP-ALPKGALNSLGVAQLIAHRTPDQAI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 391 VTSDVGQHQMFAALYYPFDKPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLV 470
Cdd:PRK12474 360 YADEALTSGLFFDMSYDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTV 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111084 471 VNLNNRYLGMVkqWQDMIY-----SGRHSQSYMQ-SLP--DFVRLAEAYGHVGIQISHPHELESKLSEALEQvRNNRLV 541
Cdd:PRK12474 439 VIFANRSYAIL--NGELQRvgaqgAGRNALSMLDlHNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQ-RGPRLI 514
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
14-146 |
1.25e-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: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 14 LIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDS 93
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 94 IPLVVLSGQVATSLIG-------------YDAFQECdmvgiSRPVVKHS-FLVKQ---TEDIPQVLKKAF 146
Cdd:cd07038 86 VPVVHIVGAPSTKAQAsglllhhtlgdgdFDVFLKM-----FEEITCAAaRLTDPenaAEEIDRVLRTAL 150
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
10-162 |
5.87e-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: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 10 VVRSLIDQGVKQVFGYPGG-----AVldiydALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 84
Cdd:cd07037 3 LVEELKRLGVRDVVISPGSrsaplAL-----AAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 85 GIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSF---LVKQTEDIP---QVLKKAFWLAASGRPGPVV 158
Cdd:cd07037 78 AVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVdlpPPEDDDDLWyllRLANRAVLEALSAPPGPVH 157
|
....
gi 90111084 159 VDLP 162
Cdd:cd07037 158 LNLP 161
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
419-548 |
2.04e-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: 69.26 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 419 GLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGR------ 492
Cdd:cd02003 46 GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSfgtefr 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111084 493 -----HSQSYMQSLP-DFVRLAEAYGHVGIQISHPHELEsklsEALEQVR-NNRLVFVDVTVD 548
Cdd:cd02003 126 drdqeSGQLDGALLPvDFAANARSLGARVEKVKTIEELK----AALAKAKaSDRTTVIVIKTD 184
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
12-475 |
8.90e-10 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 61.25 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 12 RSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYM 91
Cdd:PLN02573 24 RRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGAYS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 92 DSIPLVVLSG----------QVATSLIGYDAF-QE--CdmvgiSRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVV 158
Cdd:PLN02573 103 ENLPVICIVGgpnsndygtnRILHHTIGLPDFsQElrC-----FQTVTCYQAVINNLEDAHELIDTAI-STALKESKPVY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 159 V----DLPkDILNPANKLPYVwPESVSMRSYNPttTGHKGQIKRALQTLVAAKKPVVyVGGGAI-TAGCHQQLKETVEAL 233
Cdd:PLN02573 177 IsvscNLA-AIPHPTFSREPV-PFFLTPRLSNK--MSLEAAVEAAAEFLNKAVKPVL-VGGPKLrVAKACKAFVELADAS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 234 NLPVVCSLMGLGAFPATHRQALGML-GMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISK 312
Cdd:PLN02573 252 GYPVAVMPSAKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 313 TVTADIPIVGDARQVLEQML------------------ELLSQEsAHQPLdEIRDWWQQIEqwrarQCLKYDThsekikp 374
Cdd:PLN02573 332 GPAFGCVLMKDFLEALAKRVkknttayenykrifvpegEPLKSE-PGEPL-RVNVLFKHIQ-----KMLSGDT------- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 375 qAVI-ET--LW------RLTKGDAYvtsdvgQHQMfaaLYypfdkprrwinsgglGTMGFGLPAALGVKMALPEETVVCV 445
Cdd:PLN02573 398 -AVIaETgdSWfncqklKLPEGCGY------EFQM---QY---------------GSIGWSVGATLGYAQAAPDKRVIAC 452
|
490 500 510
....*....|....*....|....*....|
gi 90111084 446 TGDGSIQMNIQELSTALQYELPVLVVNLNN 475
Cdd:PLN02573 453 IGDGSFQVTAQDVSTMIRCGQKSIIFLINN 482
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
420-563 |
3.82e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 53.68 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 420 LGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTalqyelpvlVVNLNNRYLGMVkQWQDMIYSGRHSQSYMQ 499
Cdd:PRK06163 56 LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGT---------IAALAPKNLTII-VMDNGVYQITGGQPTLT 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111084 500 S-LPDFVRLAEAyghVGIQISH----PHELESKLSEALeqvRNNRLVFVDVTVD-----GSEHVYPMQIRGGGM 563
Cdd:PRK06163 126 SqTVDVVAIARG---AGLENSHwaadEAHFEALVDQAL---SGPGPSFIAVRIDdkpgvGTTERDPAQIRERFM 193
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
376-480 |
1.01e-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: 50.53 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 376 AVIETLWRLTKGD-AYVTSDVGQHqmfAALYYPFDKPrrWINSgglgTMGFGLPAALGVKMALPEETVVCVTGDG---SI 451
Cdd:COG1013 27 LLLKALDELLDGDkTVVVSGIGCS---SVAPGYFNVP--GFHT----LHGRAAAVATGIKLANPDLTVIVFGGDGdtyDI 97
|
90 100 110
....*....|....*....|....*....|
gi 90111084 452 QMNiqELSTALQYELPVLVVNLNNR-YlGM 480
Cdd:COG1013 98 GGN--HLIHAARRNEDITYIVYDNEiY-GN 124
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
376-480 |
9.47e-06 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 46.50 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 376 AVIETLWRLTKGDAYVTSDVGQHQMFAAlyypfdKPRRWINsgGLGTMGFGLPAALGVKMALPEETVVCVTGDGS-IQMN 454
Cdd:cd02008 14 PSFYALRKAFKKDSIVSGDIGCYTLGAL------PPLNAID--TCTCMGASIGVAIGMAKASEDKKVVAVIGDSTfFHSG 85
|
90 100
....*....|....*....|....*.
gi 90111084 455 IQELSTALQYELPVLVVNLNNRYLGM 480
Cdd:cd02008 86 ILGLINAVYNKANITVVILDNRTTAM 111
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
415-482 |
2.13e-05 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 46.37 E-value: 2.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111084 415 INSGGL-GTMGFGLPAALGVKMALPEETVVCVTGDG---SIQMN--IQelstALQYELPVLVVNLNNRYLGMVK 482
Cdd:PRK11867 62 INTYGFhTIHGRALAIATGLKLANPDLTVIVVTGDGdalAIGGNhfIH----ALRRNIDITYILFNNQIYGLTK 131
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
415-482 |
5.21e-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: 5.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111084 415 INSGGL-GTMGFGLPAALGVKMALPEETVVCVTGDG---SIQMNiqELSTALQYELPVLVVNLNNRYLGMVK 482
Cdd:cd03375 44 FNTYGFhTLHGRALAVATGVKLANPDLTVIVVSGDGdlaAIGGN--HFIHAARRNIDITVIVHNNQIYGLTK 113
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
404-533 |
6.74e-05 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 43.82 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 404 LYYPFDKPRrwiNSGGLGTMGFGLPAALGVKMALPEEtVVCVTGDGSIQMNIQELSTALQyELP--VLVVNLNNRylgmv 481
Cdd:cd03372 28 LYAAGDRPL---NFYMLGSMGLASSIGLGLALAQPRK-VIVIDGDGSLLMNLGALATIAA-EKPknLIIVVLDNG----- 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 90111084 482 kqwqdmIYSGRHSQ-SYMQSLPDFVRLAEAYG-HVGIQISHPHELESKLSEALE 533
Cdd:cd03372 98 ------AYGSTGNQpTHAGKKTDLEAVAKACGlDNVATVASEEAFEKAVEQALD 145
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
404-532 |
1.19e-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: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 404 LYYPFDKPRRWINsggLGTMGFGLPAALGVKMALPEETVVcVTGDGSIQMNIQELSTALQYE-LPVLVVNLNNRylgmvk 482
Cdd:cd02001 28 LYDVQDRDGHFYM---LGSMGLAGSIGLGLALGLSRKVIV-VDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNR------ 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 90111084 483 qwqdmIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEAL 532
Cdd:cd02001 98 -----AYGSTGGQPTPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLL 142
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
421-547 |
2.25e-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: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 421 GTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLV-VNLNNRYLGMVkqwqdmiySGRHSQSYMQ 499
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPANLIhIVLNNGAHDSV--------GGQPTVSFDV 119
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90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 90111084 500 SLPDFVRlAEAYGHVgIQISHPHELESKLSEALEQvrnNRLVFVDVTV 547
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 ... |
6-111 |
4.23e-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: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111084 6 GAEMVVRSLIDQGVKQVFGYPG---GAVLDIYDAlHTVGGIDHVLVR--HEQAAVHMADGlARATGEVGVVlVTSGPGAT 80
Cdd:cd07034 1 GNEAVARGALAAGVDVVAAYPItpsTEIAETLAK-AVLGELGGVVVQaeSEHAAAEAAIG-ASAAGARAMT-ATSGPGLN 77
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90 100 110
....*....|....*....|....*....|....
gi 90111084 81 NAITGIATAYMDSIPLVVLSGQ---VATSLIGYD 111
Cdd:cd07034 78 LMAEALYLAAGAELPLVIVVAQrpgPSTGLPKPD 111
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| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
415-482 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111084 415 INSGGL-GTMGFGLPAALGVKMALPEETVVCVTGDG---SIQMNiqELSTALQYELPVLVVNLNNRYLGMVK 482
Cdd:PRK05778 63 FLSHGLhTLHGRAIAFATGAKLANPDLEVIVVGGDGdlaSIGGG--HFIHAGRRNIDITVIVENNGIYGLTK 132
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