|
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: 1216.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 81 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK07979 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 161 LPKDILNPANKLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASS 240
Cdd:PRK07979 161 LPKDILNPANKLPYVWPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPI 320
Cdd:PRK07979 241 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 321 VGDARQVLEQMLDLLSQETPSQPLDEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQM 400
Cdd:PRK07979 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 401 FAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGM 480
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 481 VKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHVKNNRLVFMDVIVDGTEHVYPMHIRG 560
Cdd:PRK07979 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRG 560
|
570
....*....|....
gi 502860588 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: 1096.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 81 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK08979 81 NTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 161 LPKDILNPANKLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASS 240
Cdd:PRK08979 161 LPKDCLNPAILHPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPI 320
Cdd:PRK08979 241 LMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 321 VGDARQVLEQMLDLLSQETPSQPLDEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQM 400
Cdd:PRK08979 321 VGSADKVLDSMLALLDESGETNDEAAIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 401 FAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGM 480
Cdd:PRK08979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 481 VKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEhvKNNRLVFMDVIVDGTEHVYPMHIRG 560
Cdd:PRK08979 481 VKQWQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALA--MKDRLVFVDINVDETEHVYPMQIRG 558
|
570
....*....|....
gi 502860588 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: 1011.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 84 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 164 DILNPANKLPYvwPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLMG 243
Cdd:TIGR00118 161 DVTTAEIEYPY--PEKVNLPGYRPTVKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 244 LGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPIVGD 323
Cdd:TIGR00118 239 LGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 324 ARQVLEQMLDLLSQETPsqpLDEIrDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMFAA 403
Cdd:TIGR00118 319 ARNVLEELLKKLFELKE---RKES-AWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 404 LYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMVKQ 483
Cdd:TIGR00118 395 QFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 484 WQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVDGTEHVYPMHIRGGGM 563
Cdd:TIGR00118 475 WQELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSS---NEPVLLDVVVDKPENVLPMVAPGGGL 551
|
....*..
gi 502860588 564 DEMWLSK 570
Cdd:TIGR00118 552 DEMIGEK 558
|
|
| 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: 998.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 81 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK06466 81 NAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 161 LPKDILNPANKLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASS 240
Cdd:PRK06466 161 IPKDMTNPAEKFEYEYPKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPI 320
Cdd:PRK06466 241 LMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 321 VGDARQVLEQMLDLLSQ--ETPSQPldEIRDWWQQIEQWRARQCL-KYDTQSEN-IKPQAVIETLWRLTKGEAYVTSDVG 396
Cdd:PRK06466 321 VGPVESVLTEMLAILKEigEKPDKE--ALAAWWKQIDEWRGRHGLfPYDKGDGGiIKPQQVVETLYEVTNGDAYVTSDVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 397 QHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNG 476
Cdd:PRK06466 399 QHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 477 YLGMVKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEhvKNNRLVFMDVIVDGTEHVYPM 556
Cdd:PRK06466 479 ALGMVRQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFA--MKDRLVFIDIYVDRSEHVYPM 556
|
570
....*....|....*...
gi 502860588 557 HIRGGGMDEMWLSKTERT 574
Cdd:PRK06466 557 QIADGSMRDMWLSKTERT 574
|
|
| 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: 990.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 81 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK06882 81 NAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 161 LPKDILNPANKLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASS 240
Cdd:PRK06882 161 IPKDMVNPANKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPI 320
Cdd:PRK06882 241 LMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 321 VGDARQVLEQMLDLLSQETPSQPLDEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQM 400
Cdd:PRK06882 321 VGSAKNVLEEFLSLLEEENLAKSQTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 401 FAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGM 480
Cdd:PRK06882 401 FAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 481 VKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEhVKnNRLVFMDVIVDGTEHVYPMHIRG 560
Cdd:PRK06882 481 VKQWQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFS-IK-DKLVFVDVNVDETEHVYPMQIRG 558
|
570
....*....|....
gi 502860588 561 GGMDEMWLSKTERT 574
Cdd:PRK06882 559 GAMNEMILSKPEET 572
|
|
| 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: 828.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
Cdd:PRK06965 21 SIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 84 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 164 DIlnPANKLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLMG 243
Cdd:PRK06965 181 DV--SKTPCEYEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 244 LGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNA-TVLHIDIDPTSISKTVPADVPIVG 322
Cdd:PRK06965 259 LGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRVKVDIPIVG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 323 DARQVLEQMLDLLSQETPSQPLDEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMFA 402
Cdd:PRK06965 339 DVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMWA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 403 ALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMVK 482
Cdd:PRK06965 419 AQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMVR 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 483 QWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEhvKNNRLVFMDVIVDGTEHVYPMHIRGGG 562
Cdd:PRK06965 499 QWQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALR--LKDRTVFLDFQTDPTENVWPMVQAGKG 576
|
....*.
gi 502860588 563 MDEMWL 568
Cdd:PRK06965 577 ITEMLL 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: 787.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 82 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDL 161
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 162 PKDILnpANKLPYVwPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSL 241
Cdd:COG0028 161 PKDVQ--AAEAEEE-PAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 242 MGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPIV 321
Cdd:COG0028 238 MGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 322 GDARQVLEQMLDLLSQETpsqplDEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMF 401
Cdd:COG0028 318 GDAKAVLAALLEALEPRA-----DDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 402 AALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMV 481
Cdd:COG0028 393 AARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 482 KQWQDMIYSGRHSHSYMkSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVDGTEhvypmHIRGG 561
Cdd:COG0028 473 RQWQELFYGGRYSGTDL-PNPDFAKLAEAFGAKGERVETPEELEAALEEALAS---DGPALIDVRVDPEE-----NPPGA 543
|
....*
gi 502860588 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: 780.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
Cdd:PRK09107 11 MTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 84 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 164 DILNPANKlpYVWPETV-SMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQ--LRELIEKLNLPVASS 240
Cdd:PRK09107 171 DVQFATGT--YTPPQKApVHVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVINSGPEASrlLRELVELTGFPITST 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPI 320
Cdd:PRK09107 249 LMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 321 VGDARQVLEQMLDLLSQETPSQPLDEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKG-EAYVTSDVGQHQ 399
Cdd:PRK09107 329 IGDVGHVLEDMLRLWKARGKKPDKEALADWWGQIARWRARNSLAYTPSDDVIMPQYAIQRLYELTKGrDTYITTEVGQHQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 400 MFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLG 479
Cdd:PRK09107 409 MWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMG 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 480 MVKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVDGTEHVYPMHIR 559
Cdd:PRK09107 489 MVRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDV---DKPVIFDCRVANLENCFPMIPS 565
|
....*....
gi 502860588 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: 753.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
Cdd:PRK08527 3 LSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 84 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 164 DIlnPANKLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLMG 243
Cdd:PRK08527 163 DV--TATLGEFEYPKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 244 LGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPIVGD 323
Cdd:PRK08527 241 RGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 324 ARQVLEQMLDLLSQETPSQpldeIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMFAA 403
Cdd:PRK08527 321 LKNVLKEMLEELKEENPTT----YKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 404 LYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMVKQ 483
Cdd:PRK08527 397 QFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 484 WQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEhvkNNRLVFMDVIVDGTEHVYPMHIRGGGM 563
Cdd:PRK08527 477 WQTFFYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALE---SDKVALIDVKIDRFENVLPMVPAGGAL 553
|
570
....*....|
gi 502860588 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: 692.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 81 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK06048 84 NLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLID 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 161 LPKDILNpaNKLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASS 240
Cdd:PRK06048 164 LPKDVTT--AEIDFDYPDKVELRGYKPTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPI 320
Cdd:PRK06048 242 LMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 321 VGDARQVLEQMLDLLSQETPsqpldeiRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKgEAYVTSDVGQHQM 400
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDR-------KEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 401 FAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGM 480
Cdd:PRK06048 394 WAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 481 VKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEhvkNNRLVFMDVIVDGTEHVYPMHIRG 560
Cdd:PRK06048 474 VRQWQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVA---SDRPVVIDFIVECEENVSPMVPAG 550
|
....*.
gi 502860588 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: 679.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTV---GGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK07418 20 TGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAeaeGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 82 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDL 161
Cdd:PRK07418 100 LVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 162 PKDI-LNPANKLPyVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASS 240
Cdd:PRK07418 180 PKDVgQEEFDYVP-VEPGSVKPPGYRPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPI 320
Cdd:PRK07418 259 LMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVPI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 321 VGDARQVLEQMLDLLSQETPSqplDEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKgEAYVTSDVGQHQM 400
Cdd:PRK07418 339 VGDVRKVLVKLLERSLEPTTP---PRTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAP-DAYYTTDVGQHQM 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 401 FAALYYPfDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGM 480
Cdd:PRK07418 415 WAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGM 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502860588 481 VKQWQDMIYSGRHSHSYMK-SLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVDGTEHVYPM 556
Cdd:PRK07418 494 VRQWQESFYGERYSASNMEpGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAH---DGPVLIDVHVRRDENCYPM 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: 665.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK07789 28 PERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 81 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK07789 108 NLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 161 LPKDILNpaNKLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASS 240
Cdd:PRK07789 188 IPKDALQ--AQTTFSWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPI 320
Cdd:PRK07789 266 LMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHADVPI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 321 VGDARQVLEQMLDLLSQETPSQPLDEIRDWWQQIEQWRARQCLKYDTQSE-NIKPQAVIETLWRLTKGEAYVTSDVGQHQ 399
Cdd:PRK07789 346 VGDVKEVIAELIAALRAEHAAGGKPDLTAWWAYLDGWRETYPLGYDEPSDgSLAPQYVIERLGEIAGPDAIYVAGVGQHQ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 400 MFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLG 479
Cdd:PRK07789 426 MWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLG 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 480 MVKQWQDMIYSGRHSHSYMKS----LPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEhvKNNRLVFMDVIVDGTEHVYP 555
Cdd:PRK07789 506 MVRQWQTLFYEERYSNTDLHThshrIPDFVKLAEAYGCVGLRCEREEDVDAVIEKARA--INDRPVVIDFVVGKDAMVWP 583
|
570
....*....|
gi 502860588 556 MHIRGGGMDE 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: 648.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 84 TGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:PRK06276 80 TGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 164 DILNPANKLP-YVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLM 242
Cdd:PRK06276 160 DVQEGELDLEkYPIPAKIDLPGYKPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 243 GLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPIVG 322
Cdd:PRK06276 240 GKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 323 DARQVLEQMLDLLSQETPsqplDEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKG-----EAYVTSDVGQ 397
Cdd:PRK06276 320 DAKNVLRDLLAELMKKEI----KNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDVGQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 398 HQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGY 477
Cdd:PRK06276 396 NQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 478 LGMVKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALehvKNNRLVFMDVIVDGTEhVYPMH 557
Cdd:PRK06276 476 LGMVYQWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAI---KSGEPYLLDIIIDPAE-ALPMV 551
|
....*....
gi 502860588 558 IRGGGMDEM 566
Cdd:PRK06276 552 PPGGNLTNI 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: 637.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK07710 14 KLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 82 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDL 161
Cdd:PRK07710 93 VVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 162 PKDILNPANKLPYvwPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSL 241
Cdd:PRK07710 173 PKDMVVEEGEFCY--DVQMDLPGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 242 MGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPIV 321
Cdd:PRK07710 251 LGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 322 GDARQVLEQmldLLSQETPSQPLDEirdWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMF 401
Cdd:PRK07710 331 ADAKQALQV---LLQQEGKKENHHE---WLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 402 AALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMV 481
Cdd:PRK07710 405 AAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 482 KQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEhvkNNRLVFMDVIVDGTEHVYPMHIRGG 561
Cdd:PRK07710 485 RQWQEEFYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIE---LQEPVVIDCRVLQSEKVMPMVAPGK 561
|
....*
gi 502860588 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: 630.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK06725 13 EEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 82 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDL 161
Cdd:PRK06725 92 LVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 162 PKDILNpaNKLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSL 241
Cdd:PRK06725 172 PKDVQN--EKVTSFYNEVVEIPGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 242 MGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPIV 321
Cdd:PRK06725 250 MGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 322 GDARQVLEQMLDLlsqETPSQpldeIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMF 401
Cdd:PRK06725 330 GDVKKALHMLLHM---SIHTQ----TDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMW 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 402 AALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMV 481
Cdd:PRK06725 403 AAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 482 KQWQDMIYSGRHSHSYMKSlPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVDGTEHVYPMHIRGG 561
Cdd:PRK06725 483 RQWQEMFYENRLSESKIGS-PDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAH---EGPVVVDFCVEEGENVFPMVPPNK 558
|
570
....*....|.
gi 502860588 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: 619.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHT---VGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:CHL00099 11 TGAFALIDSLVRHGVKHIFGYPGGAILPIYDELYAwekKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 82 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDL 161
Cdd:CHL00099 91 LVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 162 PKDI-LNPANKLPYVWPET-VSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVAS 239
Cdd:CHL00099 171 PKDVgLEKFDYYPPEPGNTiIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 240 SLMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVP 319
Cdd:CHL00099 251 TLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 320 IVGDARQVLEQMLDLLSQETPSQPLDEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLtKGEAYVTSDVGQHQ 399
Cdd:CHL00099 331 IVGDVKKVLQELLELLKNSPNLLESEQTQAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQL-APDAYFTTDVGQHQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 400 MFAALYYPFdKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLG 479
Cdd:CHL00099 410 MWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQG 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502860588 480 MVKQWQDMIYSGRHSHSYM-KSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVDGTEHVYPM 556
Cdd:CHL00099 489 MVRQWQQAFYGERYSHSNMeEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDY---DGPVLIDCQVIEDENCYPM 563
|
|
| 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: 604.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 86 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:PRK08978 82 LADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 166 -LNPANKLPYVWPETvsmrsynPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLMGL 244
Cdd:PRK08978 162 qLAEGELEPHLTTVE-------NEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 245 GAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPIVGDA 324
Cdd:PRK08978 235 GAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 325 RQVLEQMldllsqetpSQPLDeIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMFAAL 404
Cdd:PRK08978 315 NALLPAL---------QQPLN-IDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 405 YYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMVKQW 484
Cdd:PRK08978 385 HMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 485 QDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVDGTEHVYPMHIRGGGMD 564
Cdd:PRK08978 465 QQLFFDERYSETDLSDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNS---EGPYLLHVSIDELENVWPLVPPGASNS 541
|
..
gi 502860588 565 EM 566
Cdd:PRK08978 542 EM 543
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
5-566 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 601.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 84
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 85 GIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPKD 164
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 165 IlnPANKLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLMGL 244
Cdd:PRK07282 171 V--SALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 245 GAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPIVGDA 324
Cdd:PRK07282 249 GTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 325 RQVLEQMLDLLSQETpsqpldEIRDWWQQIEQWRARqCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMFAAL 404
Cdd:PRK07282 329 KKALQMLLAEPTVHN------NTEKWIEKVTKDKNR-VRSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 405 YYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMVKQW 484
Cdd:PRK07282 402 YYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 485 QDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPaeleAKLAEALEHVKNNRLVFMDVIVDGTEHVYPMHIRGGGMD 564
Cdd:PRK07282 482 QESFYEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNP----ETLAQDLEVITEDVPMLIEVDISRKEHVLPMVPAGKSNH 557
|
..
gi 502860588 565 EM 566
Cdd:PRK07282 558 EM 559
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
6-562 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 562.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 86 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 166 LNPAnKLPYvWPETVSMRSY-----NPTTQGHKGQIKRALHTllaAKKPVVYVGGGAVNSACEaqLRELIEKLNLPVASS 240
Cdd:PLN02470 175 QQQL-AVPN-WNQPMKLPGYlsrlpKPPEKSQLEQIVRLISE---SKRPVVYVGGGCLNSSEE--LREFVELTGIPVAST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPI 320
Cdd:PLN02470 248 LMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 321 VGDARQVLEQMLDLLSQETPSQPldEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQM 400
Cdd:PLN02470 328 CADVKLALQGLNKLLEERKAKRP--DFSAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVGQHQM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 401 FAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGM 480
Cdd:PLN02470 406 WAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGM 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 481 VKQWQDMIYSGRHSHSYMKS-------LPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHVKNnrlVFMDVIVDGTEHV 553
Cdd:PLN02470 486 VVQWEDRFYKANRAHTYLGDpdaeaeiFPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGP---YLLDVIVPHQEHV 562
|
....*....
gi 502860588 554 YPMhIRGGG 562
Cdd:PLN02470 563 LPM-IPGGG 570
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-566 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 548.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK08155 10 RKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 81 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK08155 90 NLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWID 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 161 LPKDILNPANKLPyVWPEtVSMRSYNPTTQGHkgQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASS 240
Cdd:PRK08155 170 IPKDVQTAVIELE-ALPA-PAEKDAAPAFDEE--SIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPI 320
Cdd:PRK08155 246 LMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 321 VGDARQVLEQMLDLLSqetpSQPLDEirdWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQM 400
Cdd:PRK08155 326 QADVDDVLAQLLPLVE----AQPRAE---WHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQHQM 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 401 FAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGM 480
Cdd:PRK08155 399 WTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 481 VKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALehvknNRL--VFMDVIVDGTEHVYPMHI 558
Cdd:PRK08155 479 VHQQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAI-----NRPgpALIHVRIDAEEKVYPMVP 553
|
....*...
gi 502860588 559 RGGGMDEM 566
Cdd:PRK08155 554 PGAANTEM 561
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
3-569 |
8.35e-141 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 419.63 E-value: 8.35e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 3 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDAL---HTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGA 79
Cdd:PRK06456 1 MPTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 80 TNAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVV 159
Cdd:PRK06456 81 TNLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 160 DLPKDILNpaNKLPYV-WPETVSMRSYNP-TTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPV 237
Cdd:PRK06456 161 DIPRDIFY--EKMEEIkWPEKPLVKGYRDfPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 238 ASSLMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPN-ATVLHIDIDPTSISKTVPA 316
Cdd:PRK06456 239 VSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVNIDPTDGEKAIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 317 DVPIVGDARQVLEQMLDLL-------SQETPSQPLDEIRDWWQQieqwrarqcLKYDTQSENIKPQAVIETLWRLTKGEA 389
Cdd:PRK06456 319 DVGIYGNAKIILRELIKAItelgqkrDRSAWLKRVKEYKEYYSQ---------FYYTEENGKLKPWKIMKTIRQALPRDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 390 YVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVL 469
Cdd:PRK06456 390 IVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 470 VLNLNNGYLGMVKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEAlehVKNNRLVFMDVIVDG 549
Cdd:PRK06456 470 SVIFDNRTLGLVRQVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSA---IKEDIPAVIRVPVDK 546
|
570 580
....*....|....*....|
gi 502860588 550 TEHVYPMHIRGGGMDEMWLS 569
Cdd:PRK06456 547 EELALPTLPPGGRLKQVILR 566
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-548 |
1.67e-134 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 404.36 E-value: 1.67e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARAT-GEVGVVLVTSGPGA 79
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 80 TNAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVV 159
Cdd:PRK11269 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 160 DLPKDI------LNPANKLPyvwpetvsMRSYNPTTqgHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKL 233
Cdd:PRK11269 161 DLPFDVqvaeieFDPDTYEP--------LPVYKPAA--TRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 234 NLPVASSLMGLGAFPATHRQALGMLGMHGTYE-ANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISK 312
Cdd:PRK11269 231 GVPVIPTLMGWGAIPDDHPLMAGMVGLQTSHRyGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 313 TVPADVPIVGDARQVLEQMLDLLSQETPSQPLDEIRDWWQQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVT 392
Cdd:PRK11269 311 VFGPDLGIVSDAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 393 SDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELP-VLVL 471
Cdd:PRK11269 391 STIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPyIHVL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 472 nLNNGYLGMVKQWQ---DMIYSGRHSHSYMKSLP------DFVRLAEAYGHVGMRVTEPAELEAKLAEALEHVKNNRL-V 541
Cdd:PRK11269 471 -VNNAYLGLIRQAQrafDMDYCVQLAFENINSPElngygvDHVKVAEGLGCKAIRVFKPEDIAPALEQAKALMAEFRVpV 549
|
....*..
gi 502860588 542 FMDVIVD 548
Cdd:PRK11269 550 VVEVILE 556
|
|
| Gcl |
COG3960 |
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism]; |
7-546 |
9.57e-121 |
|
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443160 [Multi-domain] Cd Length: 588 Bit Score: 368.61 E-value: 9.57e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARAT-GEVGVVLVTSGPGATNAITG 85
Cdd:COG3960 6 VDAAVAVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHVLARHVEGASHMAEGYTRAKaGNIGVCIGTSGPAGTDMITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 86 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:COG3960 86 LYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVLEPAQVPRVFQQAFHLMRSGRPGPVLIDLPIDV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 166 ------LNPANKLPyvwpetvsMRSYNPttQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVAS 239
Cdd:COG3960 166 qmaeieFDIDTYEP--------LPVYKP--AATRAQIEKALDMLNAAERPLIVAGGGIINADASDLLVEFAELTGVPVIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 240 SLMGLGAFPATHRQALGMLGMHGTYE-ANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVPADV 318
Cdd:COG3960 236 TLMGWGSIPDDHPLMAGMVGLQTSHRyGNATLLASDFVLGIGNRWANRHTGSLDVYTKGRKFVHVDIEPTQIGRVFAPDL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 319 PIVGDARQVLEQMLDLLSQETPSQPLdeiRDWWQQIEQWRAR-QCLKYDTQSEN--IKPQAVIETLWRLTKGEAYVTSDV 395
Cdd:COG3960 316 GIVSDAKAALELFVEVARERKAAGKL---PDRSAWAAECQERkRTMLRKTHFDNvpIKPQRVYEEMNKAFGRDTRYVSTI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 396 GQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNN 475
Cdd:COG3960 393 GLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVVAADPDRPVVALSGDYDFQFMIEELAVGAQFKLPYIHVVVNN 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 476 GYLGMVKQWQ---DMIYSGRHSHSYMKSLP------DFVRLAEAYGHVGMRVTEPAELEAKLAEALEHVKNNRL-VFMDV 545
Cdd:COG3960 473 SYLGLIRQAQrgfDMDYCVQLAFENINAPElggygvDHVKVAEGLGCKAIRVTDPEEIAPAFEEAKALMAEHRVpVVVEV 552
|
.
gi 502860588 546 I 546
Cdd:COG3960 553 I 553
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
6-533 |
6.04e-113 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 347.20 E-value: 6.04e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:PRK08322 3 AADLFVKCLENEGVEYIFGIPGEENLDLLEALRD-SSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 86 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:PRK08322 82 VAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 166 ---LNPANKLPyvwpetvsmRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLM 242
Cdd:PRK08322 162 aaeETDGKPLP---------RSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 243 GLGAFPATHRQALGMLGMH-GTYEaNMTMHHSDVIFAVG---VRFDDRTTNnlakycPNA--TVLHIDIDPTSISKTVPA 316
Cdd:PRK08322 233 GKGVIPETHPLSLGTAGLSqGDYV-HCAIEHADLIINVGhdvIEKPPFFMN------PNGdkKVIHINFLPAEVDPVYFP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 317 DVPIVGDARQVLEQMLDLLS--QETPSQPLDEIRDwwQQIEQWRARQclkyDTQSENIKPQAVIETLWRLTKGEAYVTSD 394
Cdd:PRK08322 306 QVEVVGDIANSLWQLKERLAdqPHWDFPRFLKIRE--AIEAHLEEGA----DDDRFPMKPQRIVADLRKVMPDDDIVILD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 395 VGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLN 474
Cdd:PRK08322 380 NGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILN 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502860588 475 -NGYlGMVKqWQDMIYSGRhsHSYMK-SLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALE 533
Cdd:PRK08322 460 dNAY-GMIR-WKQENMGFE--DFGLDfGNPDFVKYAESYGAKGYRVESADDLLPTLEEALA 516
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-536 |
1.51e-112 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 346.48 E-value: 1.51e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK08199 5 PRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 81 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVD 160
Cdd:PRK08199 85 NASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 161 LPKDIL----NPANKLPYVWPEtvsmrsynptTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLP 236
Cdd:PRK08199 165 LPEDVLsetaEVPDAPPYRRVA----------AAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 237 VASSLMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNN---LAKYCPNATVLHIDIDPTSISKT 313
Cdd:PRK08199 235 VACAFRRQDLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELGRV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 314 VPADVPIVGDARQVLEQMLDLlsqETPSQP--LDEIRDWWQQIEQWRARQCLKYDTQSEnikpqAVIETLWRLTKGEAYV 391
Cdd:PRK08199 315 YRPDLAIVADPAAFAAALAAL---EPPASPawAEWTAAAHADYLAWSAPLPGPGAVQLG-----EVMAWLRERLPADAII 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 392 TSDVGQHQMFAALYYPFDKPRHWI--NSgglGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVL 469
Cdd:PRK08199 387 TNGAGNYATWLHRFFRFRRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPII 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502860588 470 VLNLNNGYLGMVKQWQDMIYSGRHSHSYMKSlPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHVK 536
Cdd:PRK08199 464 VIVVNNGMYGTIRMHQEREYPGRVSGTDLTN-PDFAALARAYGGHGETVERTEDFAPAFERALASGK 529
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-534 |
3.07e-110 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 340.07 E-value: 3.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLV-RHEQAAVHMADGLARATGEVGVVLVTSGPGA 79
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHtRHEQAAGYMAFGYARSTGRPGVCSVVPGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 80 TNAITGIATAYMDSIPLVILSGQVATSLI--GYDAFQEC-DMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGP 156
Cdd:PRK08266 81 LNAGAALLTAYGCNSPVLCLTGQIPSALIgkGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 157 VVVDLPKDILN------PANKLPYVWPETVsmrsyNPTtqghkgQIKRALHTLLAAKKPVVYVGGGAVNSACEaqLRELI 230
Cdd:PRK08266 161 VALEMPWDVFGqrapvaAAPPLRPAPPPAP-----DPD------AIAAAAALIAAAKNPMIFVGGGAAGAGEE--IRELA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 231 EKLNLPVASSLMGLGAFPATHRQALGMLGmhgtyeANMTMHHSDVIFAVGVRFDDRTTNnlAKYCP-NATVLHIDIDPTS 309
Cdd:PRK08266 228 EMLQAPVVAFRSGRGIVSDRHPLGLNFAA------AYELWPQTDVVIGIGSRLELPTFR--WPWRPdGLKVIRIDIDPTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 310 ISKTVPaDVPIVGDARQVLEQMLDLLSQETPSQP-----LDEIRDWWQQieqwrarqclkydtQSENIKPQ-----AVIE 379
Cdd:PRK08266 300 MRRLKP-DVAIVADAKAGTAALLDALSKAGSKRPsrraeLRELKAAARQ--------------RIQAVQPQasylrAIRE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 380 TLWRltkgEAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELS 459
Cdd:PRK08266 365 ALPD----DGIFVDELSQVGFASWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELA 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502860588 460 TALQYELPVLVLNLNNGYLGMVKQWQDMIYSGRHSHSYMKSlPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEH 534
Cdd:PRK08266 441 TAVQHNIGVVTVVFNNNAYGNVRRDQKRRFGGRVVASDLVN-PDFVKLAESFGVAAFRVDSPEELRAALEAALAH 514
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
372-556 |
5.29e-109 |
|
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: 324.07 E-value: 5.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 372 IKPQAVIETLWRLTKGEAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSI 451
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 452 QMNIQELSTALQYELPVLVLNLNNGYLGMVKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEA 531
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|....*
gi 502860588 532 LEHvknNRLVFMDVIVDGTEHVYPM 556
Cdd:cd02015 161 LAS---DGPVLLDVLVDPEENVLPM 182
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
7-550 |
7.28e-96 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 304.09 E-value: 7.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDaLHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
Cdd:TIGR03457 5 SEAFVEVLVANGVTHAFGIMGSAFMDAMD-LFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 87 ATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRpGPVVVDLPKDIL 166
Cdd:TIGR03457 84 AAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRDYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 167 NPANKLPYVWPETVSMRSYNPTTqghkgqIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLMGLGA 246
Cdd:TIGR03457 163 YGEIDVEIPRPVRLDRGAGGATS------LAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 247 FPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTT--NNLAKYCP-NATVLHIDIDPTSISKTVPADVPIVGD 323
Cdd:TIGR03457 237 FPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLGPFGTlpQYGIDYWPkNAKIIQVDANAKMIGLVKKVTVGICGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 324 ARQVLEQMLDLL-------SQETPSQPLDEIR-DWWQQIEQW-RARQCLKYDTQSEN-------IKPQAVIETLWRLTKG 387
Cdd:TIGR03457 317 AKAAAAEILQRLagkagdaNRAERKAKIQAERsAWEQELSEMtHERDPFSLDMIVEQrqeegnwLHPRQVLRELEKAMPE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 388 EAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELP 467
Cdd:TIGR03457 397 DAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 468 VLVLNLNNGYLGMVKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHVKNNRLVFMDVIV 547
Cdd:TIGR03457 477 VTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQAEGKTTVIEIVC 556
|
...
gi 502860588 548 DGT 550
Cdd:TIGR03457 557 TRE 559
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-561 |
1.74e-94 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 300.38 E-value: 1.74e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTV-GGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGA 79
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 80 TNAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRpGPVVV 159
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 160 DLPKDILNPANKLPYVWPeTVSMRSYNPTTqgHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEaqLRELIEKLNLPVAS 239
Cdd:PRK08611 160 TIPDDLPAQKIKDTTNKT-VDTFRPTVPSP--KPKDIKKAAKLINKAKKPVILAGLGAKHAKEE--LLAFAEKAKIPIIH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 240 SLMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRttnnlaKYCPN-ATVLHIDIDPTSISKTVPADV 318
Cdd:PRK08611 235 TLPAKGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPKkAKAIQIDTDPANIGKRYPVNV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 319 PIVGDARQVLEQMLDLLSQETPSQPLDEIRD----WWQQIEQwrarqclKYDTQSENIKPQAVIETLWRLTKGEAYVTSD 394
Cdd:PRK08611 309 GLVGDAKKALHQLTENIKHVEDRRFLEACQEnmakWWKWMEE-------DENNASTPIKPERVMAAIQKIADDDAVLSVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 395 VGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLN 474
Cdd:PRK08611 382 VGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 475 NGYLGMVKQWQDMiySGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALehvKNNRLVFMDVIVDGTEHVY 554
Cdd:PRK08611 462 NQQLAFIKYEQQA--AGELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEAL---AQDKPVIIDVYVDPNAAPL 536
|
....*..
gi 502860588 555 PMHIRGG 561
Cdd:PRK08611 537 PGKIVND 543
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-547 |
1.91e-94 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 300.38 E-value: 1.91e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMlSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDaLHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK07525 4 MKM-TPSEAFVETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 81 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRpGPVVVD 160
Cdd:PRK07525 82 NFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 161 LPKDIlnpanklpyvWPETVSMRSYNPTT----QGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLP 236
Cdd:PRK07525 161 IPRDY----------FYGVIDVEIPQPVRlergAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 237 VASSLMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTnnLAK----YCP-NATVLHIDIDPTSIS 311
Cdd:PRK07525 231 VACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPFGT--LPQygidYWPkDAKIIQVDINPDRIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 312 KTVPADVPIVGDARQVLEQMLDLLSQETPSQPLDEIR---------DWWQQIEQW---RARQCLKYDTQSENIKPQAVI- 378
Cdd:PRK07525 309 LTKKVSVGICGDAKAVARELLARLAERLAGDAGREERkaliaaeksAWEQELSSWdheDDDPGTDWNEEARARKPDYMHp 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 379 -ETLWRLTKG---EAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMN 454
Cdd:PRK07525 389 rQALREIQKAlpeDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGIS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 455 IQELSTALQYELPVLVLNLNNGYLGMVKQWQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEH 534
Cdd:PRK07525 469 MNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDA 548
|
570
....*....|...
gi 502860588 535 VKNNRLVFMDVIV 547
Cdd:PRK07525 549 QNEGKTTVIEIMC 561
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
5-533 |
7.02e-93 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 295.23 E-value: 7.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 84
Cdd:PRK08617 6 YGADLVVDSLINQGVKYVFGIPGAKIDRVFDALED-SGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 85 GIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPKD 164
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 165 ILN-PANKLPYVWPETVSMRSYNPttqghkGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLMG 243
Cdd:PRK08617 165 VVDaPVTSKAIAPLSKPKLGPASP------EDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 244 LGAFPATH-RQALGMLGMHGTYEANMTMHHSDVIFAVG---VRFDDRTTNNLakycPNATVLHIDIDPTSISKTVPADVP 319
Cdd:PRK08617 239 AGVISRELeDHFFGRVGLFRNQPGDELLKKADLVITIGydpIEYEPRNWNSE----GDATIIHIDVLPAEIDNYYQPERE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 320 IVGDARQVLEQMLDLLSQ-ETPSQPLDEIRDWWQQIEQwraRQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQH 398
Cdd:PRK08617 315 LIGDIAATLDLLAEKLDGlSLSPQSLEILEELRAQLEE---LAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 399 QMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYL 478
Cdd:PRK08617 392 YIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHY 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502860588 479 GMVKQWQDMIY---SGRHSHSYmkslpDFVRLAEAYGHVGMRVTEPAELEAKLAEALE 533
Cdd:PRK08617 472 NMVEFQEEMKYgrsSGVDFGPV-----DFVKYAESFGAKGLRVTSPDELEPVLREALA 524
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-548 |
2.46e-92 |
|
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: 293.58 E-value: 2.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALED-KGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 86 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 166 LNpanklpyvwpETVSMRSYNPTTQGHKG-----QIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASS 240
Cdd:TIGR02418 160 VD----------SPVSVKAIPASYAPKLGaapddAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGLGAFPAT-HRQALGMLGMHGTYEANMTMHHSDVIFAVG---VRFDDRTTNNLAkycpNATVLHIDIDPTSISKTVPA 316
Cdd:TIGR02418 230 FQGAGAVSRElEDHFFGRVGLFRNQPGDRLLKQADLVITIGydpIEYEPRNWNSEN----DATIVHIDVEPAQIDNNYQP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 317 DVPIVGDarqvLEQMLDLLSQ-----ETPSQPLDEIRDWWQQIEQWRARqclKYDTQSENIKPQAVIETLWRLTKGEAYV 391
Cdd:TIGR02418 306 DLELVGD----IASTLDLLAEripgyELPPDALAILEDLKQQREALDRV---PATLKQAHLHPLEIIKAMQAIVTDDVTV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 392 TSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVL 471
Cdd:TIGR02418 379 TVDMGSHYIWMARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHI 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502860588 472 NLNNGYLGMVKQWQDMIYsgrHSHSYMKSLP-DFVRLAEAYGHVGMRVTEPAELEAKLAEALEhvkNNRLVFMDVIVD 548
Cdd:TIGR02418 459 IWNDNGYNMVEFQEEMKY---QRSSGVDFGPiDFVKYAESFGAKGLRVESPDQLEPTLRQAME---VEGPVVVDIPVD 530
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
3-553 |
5.08e-92 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 292.65 E-value: 5.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 3 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNA 82
Cdd:PRK07524 1 MTTCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAG-SGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 83 ITGIATAYMDSIP-LVILSGQVATSL-IGYDAFQEC-DMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVV 159
Cdd:PRK07524 80 ATAMGQAYADSIPmLVISSVNRRASLgKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 160 DLPKDILnpANKLPYVWPETVSmRSYNPTTqgHKGQIKRALHTLLAAKKPVVYVGGGAVnsACEAQLRELIEKLNLPVAS 239
Cdd:PRK07524 160 EIPLDVL--AAPADHLLPAPPT-RPARPGP--APAALAQAAERLAAARRPLILAGGGAL--AAAAALRALAERLDAPVAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 240 SLMGLGAFPATHRQALGmlgmhgtyeANMT-------MHHSDVIFAVG---------VRFDDRttnnlakYCPNATVLHI 303
Cdd:PRK07524 233 TINAKGLLPAGHPLLLG---------ASQSlpavralIAEADVVLAVGtelgetdydVYFDGG-------FPLPGELIRI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 304 DIDPTSISKTVPADVPIVGDARQVLEQMLDLLSQETPSQPLDEIR--DWWQQI-EQWRArqclkyDTQSEnikpQAVIET 380
Cdd:PRK07524 297 DIDPDQLARNYPPALALVGDARAALEALLARLPGQAAAADWGAARvaALRQALrAEWDP------LTAAQ----VALLDT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 381 LWRLTKGEAYVtSDVGQHQMFAALYYPFDKPRHWINSG-GLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELS 459
Cdd:PRK07524 367 ILAALPDAIFV-GDSTQPVYAGNLYFDADAPRRWFNAStGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 460 TALQYELPVLVLNLNNGYLGMVKqwQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNR 539
Cdd:PRK07524 446 SAVEADLPLIVLLWNNDGYGEIR--RYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFAR---PG 520
|
570
....*....|....
gi 502860588 540 LVFMDVIVDGTEHV 553
Cdd:PRK07524 521 PTLIEVDQACWFAA 534
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
2-546 |
4.76e-91 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 290.95 E-value: 4.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALhtvgGIDHVLVRHEQAAVHMADGLARATG--EVGVVLVTSGPGA 79
Cdd:PRK06154 18 KTMKVAEAVAEILKEEGVELLFGFPVNELFDAAAAA----GIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 80 TNAITGIATAYMDSIPLVILSGQVATSLIGYDA-FQECDMVgisRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVV 158
Cdd:PRK06154 94 ENAFGGVAQAYGDSVPVLFLPTGYPRGSTDVAPnFESLRNY---RHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 159 VDLPKDILN---PANKLPYvwpeTVSMRSynpTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNL 235
Cdd:PRK06154 171 LELPVDVLAeelDELPLDH----RPSRRS---RPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 236 PVASSLMGLGAFPATHRQALGMLGM-------HGTYEAnmtmhhsDVIFAVGVRFddrTTNNLAKYCP-NATVLHIDIDP 307
Cdd:PRK06154 244 PVMTTLNGKSAFPEDHPLALGSGGRarpatvaHFLREA-------DVLFGIGCSL---TRSYYGLPMPeGKTIIHSTLDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 308 TSISKTVPADVPIVGDARQVLEQMLDLLSQETPSQP---------LDEIRDWWqqIEQWRArqclKYDTQSENIKPQAVI 378
Cdd:PRK06154 314 ADLNKDYPIDHGLVGDAALVLKQMIEELRRRVGPDRgraqqvaaeIEAVRAAW--LAKWMP----KLTSDSTPINPYRVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 379 -ETLWRLTKGEAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQE 457
Cdd:PRK06154 388 wELQHAVDIKTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 458 LSTALQYELPVLVLNLNNGYLGmvkqwqdmiysgrhshSYMKSLP-------------DFVRLAEAYGHVGMRVTEPAEL 524
Cdd:PRK06154 468 FETAVRERIPILTILLNNFSMG----------------GYDKVMPvsttkyratdisgDYAAIARALGGYGERVEDPEML 531
|
570 580
....*....|....*....|..
gi 502860588 525 EAKLAEALEHVKNNRLVFMDVI 546
Cdd:PRK06154 532 VPALLRALRKVKEGTPALLEVI 553
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
3-556 |
4.87e-81 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 264.38 E-value: 4.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 3 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNA 82
Cdd:PRK06457 1 MPSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRK-SKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 83 ITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRpGPVVVDLP 162
Cdd:PRK06457 80 LNGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 163 KDILNPANKLPYVWPETVSMRSYNPTTQGHKGQIKRalhtllaAKKPVVYVGGGAVNSAceAQLRELIEKLNLPVASSLM 242
Cdd:PRK06457 159 VDILRKSSEYKGSKNTEVGKVKYSIDFSRAKELIKE-------SEKPVLLIGGGTRGLG--KEINRFAEKIGAPIIYTLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 243 GLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNlakycPNATVLHIDIDPTSISKTVPADVPIVG 322
Cdd:PRK06457 230 GKGILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLN-----KSAKVIQVDIDNSNIGKRLDVDLSYPI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 323 DARQVLEQMLDLLSQETPSQPLDEIRDWWQQIEQwrarqcLKYDTqSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMFA 402
Cdd:PRK06457 305 PVAEFLNIDIEEKSDKFYEELKGKKEDWLDSISK------QENSL-DKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 403 ALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNET-VVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMV 481
Cdd:PRK06457 378 ARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAVENKRqVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502860588 482 KQWQD-MIYSGRHSHSYMkslPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVDGTEHvyPM 556
Cdd:PRK06457 458 KFEQEvMGYPEWGVDLYN---PDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNT---KGPAVLDAIVDPNER--PM 525
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
5-555 |
6.29e-77 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 254.30 E-value: 6.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 5 SGAEMVVRSLIDQGVKQVFGYpggavlDIYDALHTVG---GIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFGQ------SLPSALFLAAeaiGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 82 AITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDL 161
Cdd:PRK06112 89 LVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 162 PKDILNPANKLPYVwPETVSMRSYnP--TTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVAS 239
Cdd:PRK06112 169 PADLLTAAAAAPAA-PRSNSLGHF-PldRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVAT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 240 SLMGLGAFPATHRQALGMLGM------HGTYEANMtMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKT 313
Cdd:PRK06112 247 TNMGKGAVDETHPLSLGVVGSlmgprsPGRHLRDL-VREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGRN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 314 VPAdVPIVGDARQVLEQMLDLLSQETPSQPLDE-------IRDWWQQIEQWRARQclkYDTQSENIKPQAVIETLWRLTK 386
Cdd:PRK06112 326 YEA-LRLVGDARLTLAALTDALRGRDLAARAGRraalepaIAAGREAHREDSAPV---ALSDASPIRPERIMAELQAVLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 387 GEAYVTSDVGQHQMFAALYYPFDKPR-HWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYE 465
Cdd:PRK06112 402 GDTIVVADASYSSIWVANFLTARRAGmRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 466 LPVLVLNLNNGYLGMVKQWQDMIYsGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALehvKNNRLVFMDV 545
Cdd:PRK06112 482 VPVTIVVLNNGILGFQKHAETVKF-GTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAM---AAPGPTLIEV 557
|
570
....*....|
gi 502860588 546 IVDgtEHVYP 555
Cdd:PRK06112 558 ITD--PSAFP 565
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
18-554 |
1.84e-73 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 245.13 E-value: 1.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 18 GVKQVFGYPGGAVLDIYDALHT-VGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPL 96
Cdd:TIGR02720 13 GVDHIYGIPGGSFNSTMDALSAeRDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYDAKEDHVPV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 97 VILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFwLAASGRPGPVVVDLPKDIlnPANKLP--Y 174
Cdd:TIGR02720 93 LALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAI-RRAYAHNGVAVVTIPVDF--GWQEIPdnD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 175 VWPETVSMRSYN---PTTQghkgQIKRALHTLLAAKKPVVYVGGGAVNSACEaqLRELIEKLNLPVASSLMGLGAFPATH 251
Cdd:TIGR02720 170 YYASSVSYQTPLlpaPDVE----AVTRAVQTLKAAERPVIYYGIGARKAGEE--LEALSEKLKIPLISTGLAKGIIEDRY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 252 RQALGMLGMHGTYEANMTMHHSDVIFAVGVRFD----DRTTNNlAKYcpnatVLHIDIDPTSISKTVPADVPIVGDARQV 327
Cdd:TIGR02720 244 PAYLGSAYRVAQKPANEALFQADLVLFVGNNYPfaevSKAFKN-TKY-----FIQIDIDPAKLGKRHHTDIAVLADAKKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 328 LEQMLDLLSQETPSQpldeirdWWQ----QIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMFAA 403
Cdd:TIGR02720 318 LAAILAQVEPRESTP-------WWQanvaNVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 404 LYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMVKQ 483
Cdd:TIGR02720 391 RHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKD 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502860588 484 WQDmiysGRHSHSYMKSLP--DFVRLAEAYGHVGMRVTEPAELEAKLAEALEhVKNNRLVFMDVIVDG-----TEHVY 554
Cdd:TIGR02720 471 EQE----DTNQPLIGVDFNdaDFAKIAEGVGAVGFRVNKIEQLPAVFEQAKA-IKQGKPVLIDAKITGdrplpVEKLR 543
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-163 |
2.50e-71 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 225.49 E-value: 2.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 8 EMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIA 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502860588 88 TAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPK 163
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
7-560 |
6.97e-70 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 235.96 E-value: 6.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGG-IDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 86 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVkHSFLVKQT--EDIPGVLKKAFWLAASGRpGPVVVDLPK 163
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVA-GAFVQMVTvpEQLRHLVDRAVRTALAER-TVTAVILPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 164 DIlnpaNKLPYVWPE----TVsmrsynPTTQGHKG--------QIKRALHTLLAAKKPVVYVGGGAVNSAceAQLRELIE 231
Cdd:PRK08273 164 DV----QELEYEPPPhahgTV------HSGVGYTRprvvpydeDLRRAAEVLNAGRKVAILVGAGALGAT--DEVIAVAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 232 KLNLPVASSLMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRFDdrttnnLAKYCP---NATVLHIDIDPT 308
Cdd:PRK08273 232 RLGAGVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFP------YSEFLPkegQARGVQIDIDGR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 309 SISKTVPADVPIVGDARQVLEQMLDLLSQETPsqpldeiRDWWQQIEQWRARQCLKYDTQSEN----IKPQAVIETLWRL 384
Cdd:PRK08273 306 MLGLRYPMEVNLVGDAAETLRALLPLLERKKD-------RSWRERIEKWVARWWETLEARAMVpadpVNPQRVFWELSPR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 385 TKGEAYVTSDVGQhqmfAALYYPFD-KPRHWIN---SGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMN-IQELS 459
Cdd:PRK08273 379 LPDNAILTADSGS----CANWYARDlRMRRGMMaslSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 460 TALQY-----ELPVLVLNLNNGYLGMVkQWQDMIYSGRHSHSYMKSLPDF--VRLAEAYGHVGMRVTEPAELEAKLAEAL 532
Cdd:PRK08273 455 TVAKYwrqwsDPRLIVLVLNNRDLNQV-TWEQRVMEGDPKFEASQDLPDVpyARFAELLGLKGIRVDDPEQLGAAWDEAL 533
|
570 580
....*....|....*....|....*...
gi 502860588 533 EhvkNNRLVFMDVIVDGTEHVYPMHIRG 560
Cdd:PRK08273 534 A---ADRPVVLEVKTDPNVPPLPPHITL 558
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
2-534 |
1.02e-69 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 234.11 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 82 AITGIATAYMDSIPLVILSGQVATSLIGYDA--FQEC-DMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVV 158
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 159 VDLPKDIlnpaNKLPYVWPETVSMrSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSAceAQLRELIEkLNLPVA 238
Cdd:PRK07064 161 VEIPIDI----QAAEIELPDDLAP-VHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAG--AEVKRLVD-LGFGVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 239 SSLMGLGAFPATHRQALGMLGMHGTYEAnmTMHHSDVIFAVGVRFDDRTTNNLAKYCPnATVLHIDIDPTSISKTVPADV 318
Cdd:PRK07064 233 TSTQGRGVVPEDHPASLGAFNNSAAVEA--LYKTCDLLLVVGSRLRGNETLKYSLALP-RPLIRVDADAAADGRGYPNDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 319 PIVGDARQVLEQMLDLLSQETPSQPldeirDWWQQIEqwRARQcLKYDTQSENIKPQAVI-ETLWRLTKGEAYVTSDVG- 396
Cdd:PRK07064 310 FVHGDAARVLARLADRLEGRLSVDP-----AFAADLR--AARE-AAVADLRKGLGPYAKLvDALRAALPRDGNWVRDVTi 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 397 QHQMFAALYYPFDKPRHWINSGGlGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNG 476
Cdd:PRK07064 382 SNSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDG 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502860588 477 YLGMVKQWQDMIYSGRHSHSYMKSlPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEH 534
Cdd:PRK07064 461 GYGVIRNIQDAQYGGRRYYVELHT-PDFALLAASLGLPHWRVTSADDFEAVLREALAK 517
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
394-545 |
1.36e-66 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 213.22 E-value: 1.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 394 DVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNL 473
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502860588 474 NNGYLGMVKQWQDMIYSGRHSHSYMKSL--PDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDV 545
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGKILppVDFAKLAEAYGAKGARVESPEELEEALKEALEH---DGPALIDV 151
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
6-533 |
6.95e-65 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 221.52 E-value: 6.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGARE-EGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 86 IATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPKDI 165
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 166 L---NPANKLPYVWPETVSMRSYNPTtqghkgQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLM 242
Cdd:PRK05858 166 AfsmADDDGRPGALTELPAGPTPDPD------ALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 243 GLGAFPATHRQALgmlgmhgTYEANMTMHHSDVIFAVGVRFDDRTtnNLAKYCPNATVLHIDIDPTSISKTVPADVPIVG 322
Cdd:PRK05858 240 GRGVVPADHPLAF-------SRARGKALGEADVVLVVGVPMDFRL--GFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 323 DARQVLEQMLDLLSQETPSQP-LDEIRDwwqQIEQWRARQCLKYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGQHQMF 401
Cdd:PRK05858 311 DLSAILSALAGAGGDRTDHQGwIEELRT---AETAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 402 AALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMV 481
Cdd:PRK05858 388 AGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLE 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502860588 482 KQWQDMIYsgrhSHSYMKSLPDFVR---LAEAYGHVGMRVTEPAELEAKLAEALE 533
Cdd:PRK05858 468 KHPMEALY----GYDVAADLRPGTRydeVVRALGGHGELVTVPAELGPALERAFA 518
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-550 |
2.85e-64 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 220.26 E-value: 2.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPG---GAVLDIYDALHTVGGI--DHVLVRHEQAAVHMADGLARATGEVGVVLVTS 75
Cdd:PRK08327 4 LTMYTAAELFLELLKELGVDYIFINSGtdyPPIIEAKARARAAGRPlpEFVICPHEIVAISMAHGYALVTGKPQAVMVHV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 76 GPGATNAITGIATAYMDSIPLVILSGQVATS----------LIGY--DAFqecDMVGISRPVVKHSFLVKQTEDIPGVLK 143
Cdd:PRK08327 84 DVGTANALGGVHNAARSRIPVLVFAGRSPYTeegelgsrntRIHWtqEMR---DQGGLVREYVKWDYEIRRGDQIGEVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 144 KAFWLAASGRPGPVVVDLPKDILnpANKLPYVwpeTVSMRSYNPTTQGH--KGQIKRALHTLLAAKKPVVYVGGGAVNSA 221
Cdd:PRK08327 161 RAIQIAMSEPKGPVYLTLPREVL--AEEVPEV---KADAGRQMAPAPPApdPEDIARAAEMLAAAERPVIITWRAGRTAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 222 CEAQLRELIEKLNLPVASSLMGLGAFPATHrqalgmlGMHGTYEANMTMHHSDVIFAVGvrfddrttnNLAKYCP----- 296
Cdd:PRK08327 236 GFASLRRLAEELAIPVVEYAGEVVNYPSDH-------PLHLGPDPRADLAEADLVLVVD---------SDVPWIPkkirp 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 297 --NATVLHIDIDPtsiSKT------VPADVPIVGDARQVLEQMLDLL--SQETPSQPLDEIRDWWQQI---EQWRARQCL 363
Cdd:PRK08327 300 daDARVIQIDVDP---LKSriplwgFPCDLCIQADTSTALDQLEERLksLASAERRRARRRRAAVRELrirQEAAKRAEI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 364 KYDTQSENIKPQAVIETLWRLTKGEAYVTSDVGqhqmFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVV 443
Cdd:PRK08327 377 ERLKDRGPITPAYLSYCLGEVADEYDAIVTEYP----FVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 444 CVTGDGSIQMNIQE--LSTALQYELPVLVLNLNNGYLGMVKQWQDMIYS---GRHSHSYM----KSLPDFVRLAEAYGHV 514
Cdd:PRK08327 453 ATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPegyAARKGTFPgtdfDPRPDFAKIAEAFGGY 532
|
570 580 590
....*....|....*....|....*....|....*..
gi 502860588 515 GMRVTEPAELEAKLAEALEHVKN-NRLVFMDVIVDGT 550
Cdd:PRK08327 533 GERVEDPEELKGALRRALAAVRKgRRSAVLDVIVDRV 569
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
6-166 |
1.48e-62 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 203.24 E-value: 1.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 86 IATAYMDSIPLVILSGQVATSLIGYDAFQ-ECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPKD 164
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 502860588 165 IL 166
Cdd:pfam02776 161 VL 162
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
17-548 |
3.03e-61 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 211.35 E-value: 3.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 17 QGVKQVFGYPGGAVLDIYDALHtvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPL 96
Cdd:PRK07092 25 FGITTVFGNPGSTELPFLRDFP--DDFRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFTAFKNHTPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 97 VILSGQVATSLIGYDAF-QECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVVDLPKDILN-PAnklPY 174
Cdd:PRK07092 103 VITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYDDWDqPA---EP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 175 VWPETVSmRSYNPTTQghkgQIKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLM-GLGAFPATHRQ 253
Cdd:PRK07092 180 LPARTVS-SAVRPDPA----ALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPVWVAPMsGRCSFPEDHPL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 254 ALGML-GMHGTYEANMTMHhsDVIFAVGV---RFDDRTTnnlAKYCP-NATVLHIDIDPTSISKTvPADVPIVGDARQVL 328
Cdd:PRK07092 255 FAGFLpASREKISALLDGH--DLVLVIGApvfTYHVEGP---GPHLPeGAELVQLTDDPGEAAWA-PMGDAIVGDIRLAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 329 EQMLDLLSQETPSQPldeirdwwqqieqwRARQCLK-YDTQSENIKPQAVIETLWRLT-KGEAYV---TSDVGQHQMFAA 403
Cdd:PRK07092 329 RDLLALLPPSARPAP--------------PARPMPPpAPAPGEPLSVAFVLQTLAALRpADAIVVeeaPSTRPAMQEHLP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 404 L-----YYPFDkprhwinSGGLgtmGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYL 478
Cdd:PRK07092 395 MrrqgsFYTMA-------SGGL---GYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRY 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502860588 479 GMVkQWQDMIYSGRHSHSYmkSLP--DFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVD 548
Cdd:PRK07092 465 GAL-RWFAPVFGVRDVPGL--DLPglDFVALARGYGCEAVRVSDAAELADALARALAA---DGPVLVEVEVA 530
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
196-331 |
1.45e-59 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 194.32 E-value: 1.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 196 IKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPVASSLMGLGAFPATHRQALGMLGMHGTYEANMTMHHSDV 275
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 502860588 276 IFAVGVRFDD-RTTNNLAKYCPNATVLHIDIDPTSISKTVPADVPIVGDARQVLEQM 331
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
7-548 |
1.35e-57 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 202.53 E-value: 1.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 87 ATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWlAASGRPGPVVVDLPKDIL 166
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQ-HAVAGGGVSVVTLPGDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 167 NPANKLPYVwpeTVSMRSYNPTTQGHKGQIKRALHTLLAAKKPVVYVGGGAVNSacEAQLRELIEKLNLPVASSLMGLGA 246
Cdd:PRK06546 165 DEPAPEGFA---PSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGA--HAEVLALAEKIKAPVGHSLRGKEW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 247 FPATHRQALGMLGMHGTYEANMTMHHSDVIFAVGVRF--DDrttnnlakYCPNATVLHIDIDPTSISKTVPADVPIVGDA 324
Cdd:PRK06546 240 IQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFpyDQ--------FLPDVRTAQVDIDPEHLGRRTRVDLAVHGDV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 325 RQVLEQMLDLLSQETPSQPLDEIRDwwqqiEQWRARQCL--KYDTQSEN---IKPQAVIETLWRLTKGEAYVTSDVGQHQ 399
Cdd:PRK06546 312 AETIRALLPLVKEKTDRRFLDRMLK-----KHARKLEKVvgAYTRKVEKhtpIHPEYVASILDELAADDAVFTVDTGMCN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 400 MFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLG 479
Cdd:PRK06546 387 VWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLG 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502860588 480 MVKqwQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVD 548
Cdd:PRK06546 467 MVK--LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAH---PGPALVDVVTD 530
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
7-558 |
7.48e-57 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 200.60 E-value: 7.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 87 ATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFwLAASGRPGPVVVDLPKDI- 165
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAM-RKAILNRGVAVVVLPGDVa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 166 LNPANK-LPYVWPETVSmrsynPTTQGHKGQIKRALHTLLAAKKPVVYVGGGavnsaCE---AQLRELIEKLNLPVASSL 241
Cdd:PRK09124 165 LKPAPErATPHWYHAPQ-----PVVTPAEEELRKLAALLNGSSNITLLCGSG-----CAgahDELVALAETLKAPIVHAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 242 MGLGAFPATHRQALGMLGMHG---TYEAnmtMHHSDVIFAVGVRFDDRttnnlAKYCPNATVLHIDIDPTSISKTVPADV 318
Cdd:PRK09124 235 RGKEHVEYDNPYDVGMTGLIGfssGYHA---MMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 319 PIVGDARQVLEQMLDLLSQETPSQPLDEIRDWWQqieqwRARQCL----KYDTQSENIKPQAVIETLWRLTKGEAYVTSD 394
Cdd:PRK09124 307 GLVGDVKATLAALLPLLEEKTDRKFLDKALEHYR-----KARKGLddlaVPSDGGKPIHPQYLARQISEFAADDAIFTCD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 395 VGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLN 474
Cdd:PRK09124 382 VGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 475 NGYLGMVKqwQDMIYSGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEHvknNRLVFMDVIVDGTEHVY 554
Cdd:PRK09124 462 NSVLGFVA--MEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAH---DGPALVDVVTAKQELAM 536
|
....
gi 502860588 555 PMHI 558
Cdd:PRK09124 537 PPQI 540
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
2-551 |
5.25e-56 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 197.90 E-value: 5.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 2 EMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIyDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATN 81
Cdd:PRK09259 8 QLTDGFHLVIDALKLNGIDTIYGVVGIPITDL-ARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 82 AITGIATAYMDSIPLVILSGQVATSLIGYDA--FQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRPGPVVV 159
Cdd:PRK09259 87 GLTALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 160 DLPKDILnpANKLPYVWPETVSMRSYNPTTQGHKGQ--IKRALHTLLAAKKPVVYVGGGAVNSACEAQLRELIEKLNLPV 237
Cdd:PRK09259 167 DLPAKVL--AQTMDADEALTSLVKVVDPAPAQLPAPeaVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 238 ASSLMGLGAFPATHRQALGMlgmhgtyEANMTMHHSDVIFAVGVRFDDRTTNNLAK-YCPNATVLHIDIDPTSISKTVPA 316
Cdd:PRK09259 245 LPMSMAKGLLPDTHPQSAAA-------ARSLALANADVVLLVGARLNWLLSHGKGKtWGADKKFIQIDIEPQEIDSNRPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 317 DVPIVGDARQVLEQMLDLLSQETPSQPLdeirDWWQQIEQWRARQCLKY-DTQSENIKPQ------AVIETLWRlTKGEA 389
Cdd:PRK09259 318 AAPVVGDIGSVMQALLAGLKQNTFKAPA----EWLDALAERKEKNAAKMaEKLSTDTQPMnfynalGAIRDVLK-ENPDI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 390 YVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALG--VKLALPnetVVCVTGDGSIQMNIQELSTALQYELP 467
Cdd:PRK09259 393 YLVNEGANTLDLARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAaaVETGKP---VVAIEGDSAFGFSGMEVETICRYNLP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 468 VLVLNLNNG--YLGmvkqwQDMIYSGRHSHSYMKSLPD--FVRLAEAYGHVGMRVTEPAELEAKLAEAlehVKNNRLVFM 543
Cdd:PRK09259 470 VTVVIFNNGgiYRG-----DDVNLSGAGDPSPTVLVHHarYDKMMEAFGGVGYNVTTPDELRHALTEA---IASGKPTLI 541
|
570
....*....|.
gi 502860588 544 DVIVD---GTE 551
Cdd:PRK09259 542 NVVIDpaaGTE 552
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
14-548 |
1.04e-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: 188.44 E-value: 1.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 14 LIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDS 93
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 94 IPLVILSG------QVATSLI-------GYDAFQEcdmvgISRPV-VKHSFLVKQT--EDIPGVLKKAFwlaASGRPgpV 157
Cdd:COG3961 94 VPVVHIVGapgtraQRRGPLLhhtlgdgDFDHFLR-----MFEEVtVAQAVLTPENaaAEIDRVLAAAL---REKRP--V 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 158 VVDLPKDILNpankLPYVWPETVSMRSYNPTTQGHKGQIKRALHTLLA-AKKPVVYVGGGAVNSACEAQLRELIEKLNLP 236
Cdd:COG3961 164 YIELPRDVAD----APIEPPEAPLPLPPPASDPAALAAAVAAAAERLAkAKRPVILAGVEVHRFGLQEELLALAEKTGIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 237 VASSLMGLGAFPATHRQALGmlgmhgTYEANM-------TMHHSDVIFAVGVRFDDRTTNNL-AKYCPNATvlhIDIDP- 307
Cdd:COG3961 240 VATTLLGKSVLDESHPQFIG------TYAGAAsspevreYVENADCVLCLGVVFTDTNTGGFtAQLDPERT---IDIQPd 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 308 -TSISKTVPADVPIvgdaRQVLEQMLDLLSQETPSQPLDEIRDWWQQIEqwrarqclkydtqsenikPQAVI--ETLWR- 383
Cdd:COG3961 311 sVRVGGHIYPGVSL----ADFLEALAELLKKRSAPLPAPAPPPPPPPAA------------------PDAPLtqDRLWQr 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 384 ----LTKGEAyVTSDVGQhQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELS 459
Cdd:COG3961 369 lqafLDPGDI-VVADTGT-SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 460 TALQYELP--VLVLNlNNGY------LGM------VKQWqdmiysgrhshsymkslpDFVRLAEAYG---HVGMRVTEPA 522
Cdd:COG3961 447 TMLRYGLKpiIFVLN-NDGYtieraiHGPdgpyndIANW------------------DYAKLPEAFGggnALGFRVTTEG 507
|
570 580
....*....|....*....|....*.
gi 502860588 523 ELEAKLAEALEHvkNNRLVFMDVIVD 548
Cdd:COG3961 508 ELEEALAAAEAN--TDRLTLIEVVLD 531
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
376-534 |
8.66e-52 |
|
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: 174.75 E-value: 8.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 376 AVIETLWRLTKGEAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNI 455
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502860588 456 QELSTALQYELPVLVLNLNNGYLGMVKQWQDMIYSGRHSHSYMKSlPDFVRLAEAYGHVGMRVTEPAELEAKLAEALEH 534
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSN-PDFAALAEAYGAKGVRVEDPEDLEAALAEALAA 158
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
372-548 |
1.26e-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: 150.76 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 372 IKPQAVIETLWRLTKGEAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSI 451
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 452 QMNIQELSTALQYELPVLVLNLNNGYLGMVKQWQDMiySGRHSHSYMKSLPDFVRLAEAYGHVGMRVTEPAELEAKLAEA 531
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEV--MGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEA 159
|
170
....*....|....*..
gi 502860588 532 LEHvknNRLVFMDVIVD 548
Cdd:cd02014 160 LAA---DGPVVIDVVTD 173
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
7-165 |
4.16e-41 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 146.16 E-value: 4.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502860588 87 ATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFWLAASGRpGPVVVDLPKDI 165
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGDV 160
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
374-551 |
2.13e-40 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 144.74 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 374 PQAVIETLWRLTKGEAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQM 453
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 454 NIQELSTALQYELPVLVLNLNNGYLGMVKqWQDMIYSGRhsHSYMK-SLPDFVRLAEAYGHVGMRVTEPAELEAKLAEAL 532
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIK-WKQEKEYGR--DSGVDfGNPDFVKYAESFGAKGYRIESADDLLPVLERAL 157
|
170
....*....|....*....
gi 502860588 533 ehvKNNRLVFMDVIVDGTE 551
Cdd:cd02010 158 ---AADGVHVIDCPVDYSE 173
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
17-163 |
5.57e-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: 120.91 E-value: 5.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 17 QGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDSIPL 96
Cdd:cd06586 10 WGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADAAAEHLPV 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502860588 97 VILSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPGVLKKAFwLAASGRPGPVVVDLPK 163
Cdd:cd06586 89 VFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAI-RTAYASQGPVVVRLPR 154
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
374-548 |
5.99e-29 |
|
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: 113.01 E-value: 5.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 374 PQAVIETLWRLTKGEAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQM 453
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 454 NIQELSTALQYELPVLVLNLNNGYLGMVKQWQ-DMIYSGRHSHSYMKSLpDFVRLAEAYGHVGMRVTEPAELEAKLAEAL 532
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQqLSYGLGLPVTTLLPDT-RYDLVAEAFGGKGELVTTPEELKPALKRAL 159
|
170
....*....|....*.
gi 502860588 533 EHvknNRLVFMDVIVD 548
Cdd:cd02004 160 AS---GKPALINVIID 172
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
372-548 |
9.64e-29 |
|
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: 113.14 E-value: 9.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 372 IKPQAVIETLWRLTKGEAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSI 451
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 452 QMNIQELSTALQYELPVLVLNLNNGYLGMVKQWQ---DMIYSGRHSHSYMKSLP------DFVRLAEAYGHVGMRVTEPA 522
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQrafDMDYQVNLAFENINSSElggygvDHVKVAEGLGCKAIRVTKPE 167
|
170 180
....*....|....*....|....*..
gi 502860588 523 ELEAKLAEALEHVKNNRL-VFMDVIVD 548
Cdd:cd02006 168 ELAAAFEQAKKLMAEHRVpVVVEAILE 194
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
372-550 |
1.57e-27 |
|
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: 109.52 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 372 IKPQAVIETLWRLTKGEAYVTSDVGQHQMFAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSI 451
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 452 QMNIQELSTALQYELPVLVLNLNNGYLGMVKQWQDMIYSGRHSHSYMKSlPDFVRLAEAYGHVGMRVTEPAELEAKLAEA 531
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELES-ESFAKIAEACGAKGITVDKPEDVGPALQKA 162
|
170
....*....|....*....
gi 502860588 532 LEHVKNNRLVFMDVIVDGT 550
Cdd:cd02013 163 IAMMAEGKTTVIEIVCDQE 181
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
374-534 |
6.12e-27 |
|
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: 107.30 E-value: 6.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 374 PQAVIETLWRLTKGEA-----YVTSDVGQHQMFaalyyPFDKPRHWINSGGlGTMGFGLPAALGVKLALPNETVVCVTGD 448
Cdd:cd02002 3 PEYLAAALAAALPEDAiivdeAVTNGLPLRDQL-----PLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 449 GSIQMNIQELSTALQYELPVLVLNLNNGYLGMVKQWQDMIYSGRHSHS--YMKSL----PDFVRLAEAYGHVGMRVTEPA 522
Cdd:cd02002 77 GSFMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENapDGLDLldpgIDFAAIAKAFGVEAERVETPE 156
|
170
....*....|..
gi 502860588 523 ELEAKLAEALEH 534
Cdd:cd02002 157 ELDEALREALAE 168
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
401-548 |
3.34e-22 |
|
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: 94.14 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 401 FAALYYPFDKPRHWINSGGLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNN-GYlg 479
Cdd:cd02005 30 FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNdGY-- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502860588 480 MVKQwqdMIYSGRHSHSYMKSLpDFVRLAEAYG----HVGMRVTEPAELEAKLAEALEHvkNNRLVFMDVIVD 548
Cdd:cd02005 108 TIER---AIHGPEASYNDIANW-NYTKLPEVFGggggGLSFRVKTEGELDEALKDALFN--RDKLSLIEVILP 174
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
5-534 |
1.51e-20 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 94.91 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 84
Cdd:PRK07586 2 NGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 85 GIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVvkhSFLVKQTEDIPGV--LKKAFWLAASGRPGPVVVD-L 161
Cdd:PRK07586 82 NLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPV---SGWVRRSESAADVaaDAAAAVAAARGAPGQVATLiL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 162 PKDI-LNPANKLPYVwPETVSMRSYNPTTqghkgqIKRALHTLLAAKKPVVYVGGGavnsACEAQLRELIEKLNLPVASS 240
Cdd:PRK07586 159 PADVaWSEGGPPAPP-PPAPAPAAVDPAA------VEAAAAALRSGEPTVLLLGGR----ALRERGLAAAARIAAATGAR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 241 LMGlGAFPATHR----------------QALGMLGmhGTyeanmtmhhsDVIFAVGVRfddrttnnlakycpnatvlhid 304
Cdd:PRK07586 228 LLA-ETFPARMErgagrpaverlpyfaeQALAQLA--GV----------RHLVLVGAK---------------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 305 iDPTSI-------SKTVPADVPIV------GDARQVLEQMLDLLSQETPSQPLDEIRDWwqqieqwrarqclkyDTQSEN 371
Cdd:PRK07586 273 -APVAFfaypgkpSRLVPEGCEVHtlagpgEDAAAALEALADALGAKPAAPPLAAPARP---------------PLPTGA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 372 IKPQAVIETLWRLTKGEAYVTSDVGqhqMFAALYYPF--DKPRH-WINSGGlGTMGFGLPAALGVKLALPNETVVCVTGD 448
Cdd:PRK07586 337 LTPEAIAQVIAALLPENAIVVDESI---TSGRGFFPAtaGAAPHdWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGD 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 449 GSIQMNIQELSTALQYELPVLVLNLNNG-Y--LGMVKQWQDMIYSGRHSHSyMKSL----PDFVRLAEAYGHVGMRVTEP 521
Cdd:PRK07586 413 GSAMYTIQALWTQARENLDVTTVIFANRaYaiLRGELARVGAGNPGPRALD-MLDLddpdLDWVALAEGMGVPARRVTTA 491
|
570
....*....|...
gi 502860588 522 AELEAKLAEALEH 534
Cdd:PRK07586 492 EEFADALAAALAE 504
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
1-532 |
1.62e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 88.78 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
Cdd:PRK12474 2 GQTMNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 81 NAITGIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVvkhSFLVKQTEDIPGV---LKKAFWLAASGRPGPV 157
Cdd:PRK12474 82 NGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPV---SRWVHRSASAGAVdsdVARAVQAAQSAPGGIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 158 VVDLPKDIL-NP----ANKLPYVWPETVSMRSynpttqghkgqIKRALHTLLAAKKPVVYVGGGAVNsacEAQLrELIEK 232
Cdd:PRK12474 159 TLIMPADVAwNEaayaAQPLRGIGPAPVAAET-----------VERIAALLRNGKKSALLLRGSALR---GAPL-EAAGR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 233 LNLPVASSLMGLGAFPATHRqalgmlGMHGTYEANMTMHHSdvifaVGVRF-DDRTTNNLAKYCPNATVLHIdidPTSIS 311
Cdd:PRK12474 224 IQAKTGVRLYCDTFAPRIER------GAGRVPIERIPYFHE-----QITAFlKDVEQLVLVGAKPPVSFFAY---PGKPS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 312 KTVPADVPIVGDAR--QVLEQMLDLLSQE--TPSQPLDeirdwwqqieqwRARQCLKyDTQSENIKPQAVIETLWRLTKG 387
Cdd:PRK12474 290 WGAPPGCEIVYLAQpdEDLAQALQDLADAvdAPAEPAA------------RTPLALP-ALPKGALNSLGVAQLIAHRTPD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 388 EAYVTSDVGQHQMFAALYYPFDKPRHWINSGGlGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELP 467
Cdd:PRK12474 357 QAIYADEALTSGLFFDMSYDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLD 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502860588 468 VLVLNLNNGYLGMVkqWQDMIY-----SGRHSHSyMKSLP----DFVRLAEAYGHVGMRVTEPAELEAKLAEAL 532
Cdd:PRK12474 436 VTVVIFANRSYAIL--NGELQRvgaqgAGRNALS-MLDLHnpelNWMKIAEGLGVEASRATTAEEFSAQYAAAM 506
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
14-146 |
6.80e-16 |
|
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: 75.22 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 14 LIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDS 93
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 94 IPLVILSGQVATSLIG-------------YDAFQECdmvgiSRPVVKHS-FLVKQ---TEDIPGVLKKAF 146
Cdd:cd07038 86 VPVVHIVGAPSTKAQAsglllhhtlgdgdFDVFLKM-----FEEITCAAaRLTDPenaAEEIDRVLRTAL 150
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
10-162 |
6.22e-15 |
|
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: 72.53 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 10 VVRSLIDQGVKQVFGYPGG-----AVldiydALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 84
Cdd:cd07037 3 LVEELKRLGVRDVVISPGSrsaplAL-----AAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 85 GIATAYMDSIPLVILSGQVATSLIGYDAFQECDMVGISRPVVKHSF---LVKQTEDIPGVLKK---AFWLAASGRPGPVV 158
Cdd:cd07037 78 AVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVdlpPPEDDDDLWYLLRLanrAVLEALSAPPGPVH 157
|
....
gi 502860588 159 VDLP 162
Cdd:cd07037 158 LNLP 161
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
419-531 |
1.19e-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: 70.03 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 419 GLGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNGYLGMVKQWQDMIYSG------R 492
Cdd:cd02003 46 GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGsfgtefR 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 502860588 493 HSHSYMKSLP------DFVRLAEAYGHVGMRVTEPAELEAKLAEA 531
Cdd:cd02003 126 DRDQESGQLDgallpvDFAANARSLGARVEKVKTIEELKAALAKA 170
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
12-547 |
3.20e-12 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 68.96 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 12 RSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYM 91
Cdd:PLN02573 24 RRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGAYS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 92 DSIPLVILSG----------QVATSLIGYDAF-QE--CdmvgiSRPVVKHSFLVKQTEDIPGVLKKAFwLAASGRPGPVV 158
Cdd:PLN02573 103 ENLPVICIVGgpnsndygtnRILHHTIGLPDFsQElrC-----FQTVTCYQAVINNLEDAHELIDTAI-STALKESKPVY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 159 V----DLPkDILNPANKLPYVwPETVSMRSYNPttQGHKGQIKRALHTLLAAKKPVVyVGGGA--VNSACEAQLrELIEK 232
Cdd:PLN02573 177 IsvscNLA-AIPHPTFSREPV-PFFLTPRLSNK--MSLEAAVEAAAEFLNKAVKPVL-VGGPKlrVAKACKAFV-ELADA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 233 LNLPVASSLMGLGAFPATHRQALGML-GMHGTYEANMTMHHSDVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSIs 311
Cdd:PLN02573 251 SGYPVAVMPSAKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTI- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 312 ktvpADVPIVGdarQVLeqMLDLLSQetpsqpldeirdwwqqieqwRARQCLKYDTQSENIKPQAVIE-TLWRLTKGEAY 390
Cdd:PLN02573 330 ----GNGPAFG---CVL--MKDFLEA--------------------LAKRVKKNTTAYENYKRIFVPEgEPLKSEPGEPL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 391 VTSDVGQH--QMF----AALYYPFDKprhWINSGGL--------------GTMGFGLPAALGVKLALPNETVVCVTGDGS 450
Cdd:PLN02573 381 RVNVLFKHiqKMLsgdtAVIAETGDS---WFNCQKLklpegcgyefqmqyGSIGWSVGATLGYAQAAPDKRVIACIGDGS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 451 IQMNIQELSTALQYELPVLVLNLNN-GYLGMVKqwqdmIYSGrhSHSYMKSLpDFVRLAEAYgHVG------MRVTEPAE 523
Cdd:PLN02573 458 FQVTAQDVSTMIRCGQKSIIFLINNgGYTIEVE-----IHDG--PYNVIKNW-NYTGLVDAI-HNGegkcwtAKVRTEEE 528
|
570 580
....*....|....*....|....
gi 502860588 524 LEAKLAEALEHvKNNRLVFMDVIV 547
Cdd:PLN02573 529 LIEAIATATGE-KKDCLCFIEVIV 551
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
421-532 |
1.37e-07 |
|
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: 51.93 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 421 GTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTALQYELPVLV-LNLNNGYLGMVkqwqdmiySGRHSHSYMK 499
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPANLIhIVLNNGAHDSV--------GGQPTVSFDV 119
|
90 100 110
....*....|....*....|....*....|...
gi 502860588 500 SLPDFVRlAEAYGHVgMRVTEPAELEAKLAEAL 532
Cdd:cd03371 120 SLPAIAK-ACGYRAV-YEVPSLEELVAALAKAL 150
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
376-534 |
1.52e-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: 49.76 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 376 AVIETLWRLTKGE-AYVTSDVGQHqmfAALYYPFDKPrhWINSgglgTMGFGLPAALGVKLALPNETVVCVTGDG---SI 451
Cdd:COG1013 27 LLLKALDELLDGDkTVVVSGIGCS---SVAPGYFNVP--GFHT----LHGRAAAVATGIKLANPDLTVIVFGGDGdtyDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 452 QMNiqELSTALQYELPVLVLNLNNG-YlGMVK-QwqdmiYSG---RHSHSymKSLP--------DFVRLAEAYGH--VGm 516
Cdd:COG1013 98 GGN--HLIHAARRNEDITYIVYDNEiY-GNTGgQ-----RSPttpLGAKT--TTTPygkpeppkDPAEIAAAHGAtyVA- 166
|
170 180
....*....|....*....|
gi 502860588 517 RVT--EPAELEAKLAEALEH 534
Cdd:COG1013 167 RASvgDPKDLKKKIKKAIEH 186
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
420-563 |
1.90e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 48.67 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 420 LGTMGFGLPAALGVKLALPNETVVCVTGDGSIQMNIQELSTalqyelpVLVLNLNNgyLGMVkQWQDMIYSGRHSH-SYM 498
Cdd:PRK06163 56 LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGT-------IAALAPKN--LTII-VMDNGVYQITGGQpTLT 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502860588 499 KSLPDFVRLAEAYGHVGMR-VTEPAELEAKLAEALEhvkNNRLVFMDVIVD-----GTEHVYPMHIRGGGM 563
Cdd:PRK06163 126 SQTVDVVAIARGAGLENSHwAADEAHFEALVDQALS---GPGPSFIAVRIDdkpgvGTTERDPAQIRERFM 193
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
404-536 |
3.82e-06 |
|
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: 47.67 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 404 LYYPFDKPRHWINsggLGTMGFGLPAALGVKLALPnETVVCVTGDGSIQMNIQELSTALQyELP---VLVLnLNNGYLGm 480
Cdd:cd03372 28 LYAAGDRPLNFYM---LGSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGALATIAA-EKPknlIIVV-LDNGAYG- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502860588 481 vkqwqdmIYSGRHSHSYMKSlpDFVRLAEAYG-HVGMRVTEPAELEAKLAEALE-----HVK 536
Cdd:cd03372 101 -------STGNQPTHAGKKT--DLEAVAKACGlDNVATVASEEAFEKAVEQALDgpsfiHVK 153
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
404-532 |
7.15e-06 |
|
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: 46.33 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 404 LYYPFDKPRHWINsggLGTMGFGLPAALGVKLALPNETVVcVTGDGSIQMNIQELSTALQYE-LPVLVLNLNNGYLGMVk 482
Cdd:cd02001 28 LYDVQDRDGHFYM---LGSMGLAGSIGLGLALGLSRKVIV-VDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNRAYGST- 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 502860588 483 qwqdmiySGRHSHSYMKSLPDfvrLAEAYGHVGMRVTEPAELEAKLAEAL 532
Cdd:cd02001 103 -------GGQPTPSSNVNLEA---WAAACGYLVLSAPLLGGLGSEFAGLL 142
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
413-482 |
1.10e-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: 46.36 E-value: 1.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502860588 413 HWINSGGL-GTMGFGLPAALGVKLALPNETVVCVTGDG---SIQMNiqELSTALQYELPVLVLNLNNGYLGMVK 482
Cdd:cd03375 42 YYFNTYGFhTLHGRALAVATGVKLANPDLTVIVVSGDGdlaAIGGN--HFIHAARRNIDITVIVHNNQIYGLTK 113
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|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
376-534 |
2.13e-05 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 45.35 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 376 AVIETLWRLTKGEAYVTSDVGQHQMFAAlyypfdKPRHWINsgGLGTMGFGLPAALGVKLALPNETVVCVTGDGS-IQMN 454
Cdd:cd02008 14 PSFYALRKAFKKDSIVSGDIGCYTLGAL------PPLNAID--TCTCMGASIGVAIGMAKASEDKKVVAVIGDSTfFHSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 455 IQELSTALQYELPVLVLNLNNGYLGMVKQwQDMIYSGRHSHSYMKsLPDFVRLAEAYGHVGMRVTEP---AELEAKLAEA 531
Cdd:cd02008 86 ILGLINAVYNKANITVVILDNRTTAMTGG-QPHPGTGKTLTEPTT-VIDIEALVRAIGVKRVVVVDPydlKAIREELKEA 163
|
...
gi 502860588 532 LEH 534
Cdd:cd02008 164 LAV 166
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
413-482 |
1.96e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 43.71 E-value: 1.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502860588 413 HWINSGGL-GTMGFGLPAALGVKLALPNETVVCVTGDG---SIQMNiqELSTALQYELPVLVLNLNNGYLGMVK 482
Cdd:PRK05778 61 GYFLSHGLhTLHGRAIAFATGAKLANPDLEVIVVGGDGdlaSIGGG--HFIHAGRRNIDITVIVENNGIYGLTK 132
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
413-454 |
2.25e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 43.29 E-value: 2.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 502860588 413 HWINSGGL-GTMGFGLPAALGVKLALPNETVVCVTGDG---SIQMN 454
Cdd:PRK11867 60 GYINTYGFhTIHGRALAIATGLKLANPDLTVIVVTGDGdalAIGGN 105
|
|
| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
6-111 |
3.07e-04 |
|
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate.
Pssm-ID: 132917 [Multi-domain] Cd Length: 160 Bit Score: 41.72 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 6 GAEMVVRSLIDQGVKQVFGYPG---GAVLDIYDAlHTVGGIDHVLVR--HEQAAVHMADGlARATGEVGVVlVTSGPGAT 80
Cdd:cd07034 1 GNEAVARGALAAGVDVVAAYPItpsTEIAETLAK-AVLGELGGVVVQaeSEHAAAEAAIG-ASAAGARAMT-ATSGPGLN 77
|
90 100 110
....*....|....*....|....*....|....
gi 502860588 81 NAITGIATAYMDSIPLVILSGQ---VATSLIGYD 111
Cdd:cd07034 78 LMAEALYLAAGAELPLVIVVAQrpgPSTGLPKPD 111
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
429-539 |
1.21e-03 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 41.28 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 429 AALGVKLALPNETVVCVTGDGSiqMNIQELSTALQ----YELPVLVLNLNNGYlGMvkqwqdmiySGRHSHSYMKslPDF 504
Cdd:COG1071 139 AALAAKLRGEDEVAVAFFGDGA--TSEGDFHEALNfaavWKLPVVFVCENNGY-AI---------STPVERQTAV--ETI 204
|
90 100 110
....*....|....*....|....*....|....*..
gi 502860588 505 VRLAEAYGHVGMRV--TEPAELEAKLAEALEHVKNNR 539
Cdd:COG1071 205 ADRAAGYGIPGVRVdgNDVLAVYAAVKEAVERARAGE 241
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
408-539 |
3.73e-03 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 39.40 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860588 408 FDKPRHwiNSGGLGTMGFGLPAALGVKLAL----PNETVVCVTGDGSIQ-------MNIqelstALQYELPVLVLNLNNG 476
Cdd:cd02000 93 GDKEKN--FFGGNGIVGGQVPLAAGAALALkyrgEDRVAVCFFGDGATNegdfheaLNF-----AALWKLPVIFVCENNG 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502860588 477 YlGMvkqwqdmiySGRHSHSYmkSLPDFVRLAEAYGHVGMRV--TEPAELEAKLAEALEHVKNNR 539
Cdd:cd02000 166 Y-AI---------STPTSRQT--AGTSIADRAAAYGIPGIRVdgNDVLAVYEAAKEAVERARAGG 218
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