|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-572 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 1070.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGAT 80
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 81 NCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVD 160
Cdd:PRK08979 81 NTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 161 LPKDVQNPKEKFPYQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTT 240
Cdd:PRK08979 161 LPKDCLNPAILHPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 241 LMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPI 320
Cdd:PRK08979 241 LMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 321 VGSVETVLEQMLEVIRECGFDNDKEALADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQM 400
Cdd:PRK08979 321 VGSADKVLDSMLALLDESGETNDEAAIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 401 FAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGM 480
Cdd:PRK08979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 481 VKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKDRLVFMDISVDPDEHVYPMQIKFGA 560
Cdd:PRK08979 481 VKQWQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRLVFVDINVDETEHVYPMQIRGGA 560
|
570
....*....|..
gi 760141809 561 MDEMWLSKTERT 572
Cdd:PRK08979 561 MNEMWLSKTERT 572
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-572 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 1048.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGAT 80
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 81 NCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVD 160
Cdd:PRK06466 81 NAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 161 LPKDVQNPKEKFPYQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTT 240
Cdd:PRK06466 161 IPKDMTNPAEKFEYEYPKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 241 LMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPI 320
Cdd:PRK06466 241 LMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 321 VGSVETVLEQMLEVIRECGFDNDKEALADWWSQINQWRSRHCLA-YEK-SATQIKPQQVIETLYKVTQGQAFVASDVGQH 398
Cdd:PRK06466 321 VGPVESVLTEMLAILKEIGEKPDKEALAAWWKQIDEWRGRHGLFpYDKgDGGIIKPQQVVETLYEVTNGDAYVTSDVGQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 399 QMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRAL 478
Cdd:PRK06466 401 QMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 479 GMVKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKDRLVFMDISVDPDEHVYPMQIKF 558
Cdd:PRK06466 481 GMVRQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAMKDRLVFIDIYVDRSEHVYPMQIAD 560
|
570
....*....|....
gi 760141809 559 GAMDEMWLSKTERT 572
Cdd:PRK06466 561 GSMRDMWLSKTERT 574
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-572 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 981.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGAT 80
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 81 NCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVD 160
Cdd:PRK07979 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 161 LPKDVQNPKEKFPYQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTT 240
Cdd:PRK07979 161 LPKDILNPANKLPYVWPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 241 LMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPI 320
Cdd:PRK07979 241 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 321 VGSVETVLEQMLEVIRECGFDNDKEALADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQM 400
Cdd:PRK07979 321 VGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 401 FAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGM 480
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 481 VKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFA--MKDRLVFMDISVDPDEHVYPMQIKF 558
Cdd:PRK07979 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEqvRNNRLVFVDVTVDGSEHVYPMQIRG 560
|
570
....*....|....
gi 760141809 559 GAMDEMWLSKTERT 572
Cdd:PRK07979 561 GGMDEMWLSKTERT 574
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-572 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 949.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGAT 80
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 81 NCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVD 160
Cdd:PRK06882 81 NAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 161 LPKDVQNPKEKFPYQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTT 240
Cdd:PRK06882 161 IPKDMVNPANKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 241 LMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPI 320
Cdd:PRK06882 241 LMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 321 VGSVETVLEQMLEVIRECGFDNDKEALADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQM 400
Cdd:PRK06882 321 VGSAKNVLEEFLSLLEEENLAKSQTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 401 FAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGM 480
Cdd:PRK06882 401 FAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 481 VKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKDRLVFMDISVDPDEHVYPMQIKFGA 560
Cdd:PRK06882 481 VKQWQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKLVFVDVNVDETEHVYPMQIRGGA 560
|
570
....*....|..
gi 760141809 561 MDEMWLSKTERT 572
Cdd:PRK06882 561 MNEMILSKPEET 572
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
4-568 |
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: 927.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 4 LSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCI 83
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 84 TGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPK 163
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 164 DVQNPKEKFPyqYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLMG 243
Cdd:TIGR00118 161 DVTTAEIEYP--YPEKVNLPGYRPTVKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 244 LGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIVGS 323
Cdd:TIGR00118 239 LGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 324 VETVLEQMLEVIRECGFDNDKealaDWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQMFAA 403
Cdd:TIGR00118 319 ARNVLEELLKKLFELKERKES----AWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 404 LYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMVKQ 483
Cdd:TIGR00118 395 QFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 484 WQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKdRLVFMDISVDPDEHVYPMQIKFGAMDE 563
Cdd:TIGR00118 475 WQELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSN-EPVLLDVVVDKPENVLPMVAPGGGLDE 553
|
....*
gi 760141809 564 MWLSK 568
Cdd:TIGR00118 554 MIGEK 558
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
4-566 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 833.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 4 LSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCI 83
Cdd:PRK06965 21 SIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 84 TGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPK 163
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 164 DVQnpKEKFPYQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLMG 243
Cdd:PRK06965 181 DVS--KTPCEYEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 244 LGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNA-TVVHIDIDPTSISKTVQAHVPIVG 322
Cdd:PRK06965 259 LGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRVKVDIPIVG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 323 SVETVLEQMLEVIRECGFDNDKEALADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQMFA 402
Cdd:PRK06965 339 DVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMWA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 403 ALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMVK 482
Cdd:PRK06965 419 AQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMVR 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 483 QWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKDRLVFMDISVDPDEHVYPMQIKFGAMD 562
Cdd:PRK06965 499 QWQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRLKDRTVFLDFQTDPTENVWPMVQAGKGIT 578
|
....
gi 760141809 563 EMWL 566
Cdd:PRK06965 579 EMLL 582
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
2-564 |
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: 797.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 2 EMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATN 81
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 82 CITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDL 161
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 162 PKDVQNpkEKFPYQyPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTL 241
Cdd:COG0028 161 PKDVQA--AEAEEE-PAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 242 MGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIV 321
Cdd:COG0028 238 MGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 322 GSVETVLEQMLEVIRECGFDndkeaLADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQMF 401
Cdd:COG0028 318 GDAKAVLAALLEALEPRADD-----RAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 402 AALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMV 481
Cdd:COG0028 393 AARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 482 KQWQKMFYGGRHSHSYMeSLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAmKDRLVFMDISVDPDEHvyPMQIkfgAM 561
Cdd:COG0028 473 RQWQELFYGGRYSGTDL-PNPDFAKLAEAFGAKGERVETPEELEAALEEALA-SDGPALIDVRVDPEEN--PPGA---TL 545
|
...
gi 760141809 562 DEM 564
Cdd:COG0028 546 DEM 548
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
4-566 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 784.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 4 LSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCI 83
Cdd:PRK09107 11 MTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 84 TGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPK 163
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 164 DVQNPKEKfpYQYPETV-SLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINA--NADHLVTKLAELLNLPVTTT 240
Cdd:PRK09107 171 DVQFATGT--YTPPQKApVHVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVINSgpEASRLLRELVELTGFPITST 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 241 LMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPI 320
Cdd:PRK09107 249 LMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 321 VGSVETVLEQMLEVIRECGFDNDKEALADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQ-AFVASDVGQHQ 399
Cdd:PRK09107 329 IGDVGHVLEDMLRLWKARGKKPDKEALADWWGQIARWRARNSLAYTPSDDVIMPQYAIQRLYELTKGRdTYITTEVGQHQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 400 MFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALG 479
Cdd:PRK09107 409 MWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMG 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 480 MVKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMkDRLVFMDISVDPDEHVYPMqIKFG 559
Cdd:PRK09107 489 MVRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDV-DKPVIFDCRVANLENCFPM-IPSG 566
|
....*...
gi 760141809 560 -AMDEMWL 566
Cdd:PRK09107 567 kAHNEMLL 574
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
4-571 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 741.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 4 LSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCI 83
Cdd:PRK08527 3 LSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 84 TGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPK 163
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 164 DVQNPKEKFpyQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLMG 243
Cdd:PRK08527 163 DVTATLGEF--EYPKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 244 LGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIVGS 323
Cdd:PRK08527 241 RGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 324 VETVLEQMLEVIREcgfdNDKEALADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQMFAA 403
Cdd:PRK08527 321 LKNVLKEMLEELKE----ENPTTYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 404 LYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMVKQ 483
Cdd:PRK08527 397 QFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 484 WQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAmKDRLVFMDISVDPDEHVYPMQIKFGAMDE 563
Cdd:PRK08527 477 WQTFFYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALE-SDKVALIDVKIDRFENVLPMVPAGGALYN 555
|
....*...
gi 760141809 564 MWLSKTER 571
Cdd:PRK08527 556 MILPKKKD 563
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-554 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 725.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGAT 80
Cdd:PRK07789 28 PERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 81 NCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVD 160
Cdd:PRK07789 108 NLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 161 LPKDVQNpkEKFPYQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTT 240
Cdd:PRK07789 188 IPKDALQ--AQTTFSWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 241 LMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPI 320
Cdd:PRK07789 266 LMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHADVPI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 321 VGSVETVLEQMLEVIRECGFDNDKEALADWWSQINQWRSRHCLAYEKSAT-QIKPQQVIETLYKVTQGQAFVASDVGQHQ 399
Cdd:PRK07789 346 VGDVKEVIAELIAALRAEHAAGGKPDLTAWWAYLDGWRETYPLGYDEPSDgSLAPQYVIERLGEIAGPDAIYVAGVGQHQ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 400 MFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALG 479
Cdd:PRK07789 426 MWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLG 505
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 760141809 480 MVKQWQKMFYGGRHS----HSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKDRLVFMDISVDPDEHVYPM 554
Cdd:PRK07789 506 MVRQWQTLFYEERYSntdlHTHSHRIPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAINDRPVVIDFVVGKDAMVWPM 584
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-554 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 708.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGkMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGAT 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD-LRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 81 NCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVD 160
Cdd:PRK06048 84 NLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLID 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 161 LPKDVQNpkEKFPYQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTT 240
Cdd:PRK06048 164 LPKDVTT--AEIDFDYPDKVELRGYKPTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 241 LMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPI 320
Cdd:PRK06048 242 LMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 321 VGSVETVLEQMLEVIRECGFdndkealADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQgQAFVASDVGQHQM 400
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDR-------KEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 401 FAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGM 480
Cdd:PRK06048 394 WAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGM 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 760141809 481 VKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMkDRLVFMDISVDPDEHVYPM 554
Cdd:PRK06048 474 VRQWQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVAS-DRPVVIDFIVECEENVSPM 546
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
5-554 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 701.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 5 SGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALF---ENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATN 81
Cdd:PRK07418 20 TGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYkaeAEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 82 CITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDL 161
Cdd:PRK07418 100 LVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 162 PKDVQnpKEKFPYQ--YPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTT 239
Cdd:PRK07418 180 PKDVG--QEEFDYVpvEPGSVKPPGYRPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 240 TLMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVP 319
Cdd:PRK07418 258 TLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 320 IVGSVETVLEQMLEVIRECGFDNDKEAladWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQgQAFVASDVGQHQ 399
Cdd:PRK07418 338 IVGDVRKVLVKLLERSLEPTTPPRTQA---WLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAP-DAYYTTDVGQHQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 400 MFAALYYPFAkPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALG 479
Cdd:PRK07418 414 MWAAQFLRNG-PRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQG 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 760141809 480 MVKQWQKMFYGGRHSHSYME-SLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAmKDRLVFMDISVDPDEHVYPM 554
Cdd:PRK07418 493 MVRQWQESFYGERYSASNMEpGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALA-HDGPVLIDVHVRRDENCYPM 567
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
4-564 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 657.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 4 LSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENgKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCI 83
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDS-DLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 84 TGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPK 163
Cdd:PRK06276 80 TGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 164 DVQNPK-EKFPYQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLM 242
Cdd:PRK06276 160 DVQEGElDLEKYPIPAKIDLPGYKPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 243 GLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIVG 322
Cdd:PRK06276 240 GKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 323 SVETVLEQMLEVIRECGFDNDKEaladWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKV-----TQGQAFVASDVGQ 397
Cdd:PRK06276 320 DAKNVLRDLLAELMKKEIKNKSE----WLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVlreidPSKNTIITTDVGQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 398 HQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRA 477
Cdd:PRK06276 396 NQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 478 LGMVKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFaMKDRLVFMDISVDPDEhVYPMQIK 557
Cdd:PRK06276 476 LGMVYQWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAI-KSGEPYLLDIIIDPAE-ALPMVPP 553
|
....*..
gi 760141809 558 FGAMDEM 564
Cdd:PRK06276 554 GGNLTNI 560
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
5-554 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 657.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 5 SGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALF---ENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATN 81
Cdd:CHL00099 11 TGAFALIDSLVRHGVKHIFGYPGGAILPIYDELYaweKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 82 CITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDL 161
Cdd:CHL00099 91 LVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 162 PKDVQnpKEKFPYQYPE----TVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPV 237
Cdd:CHL00099 171 PKDVG--LEKFDYYPPEpgntIIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 238 TTTLMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAH 317
Cdd:CHL00099 249 TTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 318 VPIVGSVETVLEQMLEVIRECGFDNDKEALADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQgQAFVASDVGQ 397
Cdd:CHL00099 329 VAIVGDVKKVLQELLELLKNSPNLLESEQTQAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQLAP-DAYFTTDVGQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 398 HQMFAALYYPfAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRA 477
Cdd:CHL00099 408 HQMWAAQFLK-CKPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKW 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 760141809 478 LGMVKQWQKMFYGGRHSHSYM-ESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKDRlVFMDISVDPDEHVYPM 554
Cdd:CHL00099 487 QGMVRQWQQAFYGERYSHSNMeEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGP-VLIDCQVIEDENCYPM 563
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
2-554 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 649.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 2 EMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGkMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATN 81
Cdd:PRK07710 14 KLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCG-IPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 82 CITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDL 161
Cdd:PRK07710 93 VVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 162 PKDVQNPKEKFPYQYPetVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTL 241
Cdd:PRK07710 173 PKDMVVEEGEFCYDVQ--MDLPGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 242 MGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIV 321
Cdd:PRK07710 251 LGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 322 GSVETVLEQMLEvirecgFDNDKEALADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQMF 401
Cdd:PRK07710 331 ADAKQALQVLLQ------QEGKKENHHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 402 AALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMV 481
Cdd:PRK07710 405 AAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMV 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 760141809 482 KQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMkDRLVFMDISVDPDEHVYPM 554
Cdd:PRK07710 485 RQWQEEFYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIEL-QEPVVIDCRVLQSEKVMPM 556
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
2-570 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 632.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 2 EMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGkMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATN 81
Cdd:PRK06725 13 EEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 82 CITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDL 161
Cdd:PRK06725 92 LVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 162 PKDVQNpkEKFPYQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTL 241
Cdd:PRK06725 172 PKDVQN--EKVTSFYNEVVEIPGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 242 MGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIV 321
Cdd:PRK06725 250 MGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 322 GSVETVLEQMLEVIRECGFDndkealaDWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQMF 401
Cdd:PRK06725 330 GDVKKALHMLLHMSIHTQTD-------EWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMW 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 402 AALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMV 481
Cdd:PRK06725 403 AAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 482 KQWQKMFYGGRHSHSYMESlPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKDRLVfMDISVDPDEHVYPMQIKFGAM 561
Cdd:PRK06725 483 RQWQEMFYENRLSESKIGS-PDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVV-VDFCVEEGENVFPMVPPNKGN 560
|
....*....
gi 760141809 562 DEMWLSKTE 570
Cdd:PRK06725 561 NEMIMKRWE 569
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
6-554 |
0e+00 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 597.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 6 GAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGkMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITG 85
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 86 IATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPKDV 165
Cdd:PRK08978 82 LADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 166 Q-NPKEKFPYQYPETvslrsyNPTKSGHKgQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLMGL 244
Cdd:PRK08978 162 QlAEGELEPHLTTVE------NEPAFPAA-ELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 245 GAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIVGSV 324
Cdd:PRK08978 235 GAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 325 ETVLEQMLEVIrecgfdndkeALADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQMFAAL 404
Cdd:PRK08978 315 NALLPALQQPL----------NIDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 405 YYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMVKQW 484
Cdd:PRK08978 385 HMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQW 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 485 QKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKDRLvFMDISVDPDEHVYPM 554
Cdd:PRK08978 465 QQLFFDERYSETDLSDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPY-LLHVSIDELENVWPL 533
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
5-564 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 592.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 5 SGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCIT 84
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 85 GIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPKD 164
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 165 VQNPKEKFPYQypETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLMGL 244
Cdd:PRK07282 171 VSALETDFIYD--PEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 245 GAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIVGSV 324
Cdd:PRK07282 249 GTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 325 ETVLEQMLEvirecgFDNDKEALADWWSQINQWRSRhCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQMFAAL 404
Cdd:PRK07282 329 KKALQMLLA------EPTVHNNTEKWIEKVTKDKNR-VRSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 405 YYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMVKQW 484
Cdd:PRK07282 402 YYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 485 QKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEkaFAMKDRLVFMDISVDPDEHVYPMQIKFGAMDEM 564
Cdd:PRK07282 482 QESFYEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLE--VITEDVPMLIEVDISRKEHVLPMVPAGKSNHEM 559
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-564 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 583.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGAT 80
Cdd:PRK08155 10 RKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 81 NCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVD 160
Cdd:PRK08155 90 NLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWID 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 161 LPKDVQNPK---EKFPyqypeTVSLRSYNPTKSGHkgQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPV 237
Cdd:PRK08155 170 IPKDVQTAVielEALP-----APAEKDAAPAFDEE--SIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 238 TTTLMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAH 317
Cdd:PRK08155 243 TMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPH 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 318 VPIVGSVETVLEQMLEVIRECgfdndkeALADWWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQ 397
Cdd:PRK08155 323 VAIQADVDDVLAQLLPLVEAQ-------PRAEWHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 398 HQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRA 477
Cdd:PRK08155 396 HQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 478 LGMVKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGI---AVSDP-AELESAMEKAFAmkdrlVFMDISVDPDEHVYP 553
Cdd:PRK08155 476 LGLVHQQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCdlnNEADPqAALQEAINRPGP-----ALIHVRIDAEEKVYP 550
|
570
....*....|.
gi 760141809 554 MQIKFGAMDEM 564
Cdd:PRK08155 551 MVPPGAANTEM 561
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
6-554 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 550.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 6 GAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITG 85
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 86 IATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPKDV 165
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 166 QN----PKEKFPYQYPETVSLRSYNPTKSghkgQIKRAAKLLVDAQRPVMYVGGGAINANADhlVTKLAELLNLPVTTTL 241
Cdd:PLN02470 175 QQqlavPNWNQPMKLPGYLSRLPKPPEKS----QLEQIVRLISESKRPVVYVGGGCLNSSEE--LREFVELTGIPVASTL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 242 MGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIV 321
Cdd:PLN02470 249 MGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVC 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 322 GSVETVLEQMLEVIREcgfdnDKEALAD---WWSQINQWRSRHCLAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQH 398
Cdd:PLN02470 329 ADVKLALQGLNKLLEE-----RKAKRPDfsaWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVGQH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 399 QMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRAL 478
Cdd:PLN02470 404 QMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 479 GMVKQWQKMFYGGRHSHSYM-------ESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAmKDRLVFMDISVDPDEHV 551
Cdd:PLN02470 484 GMVVQWEDRFYKANRAHTYLgdpdaeaEIFPDFLKFAEGCKIPAARVTRKSDLREAIQKMLD-TPGPYLLDVIVPHQEHV 562
|
...
gi 760141809 552 YPM 554
Cdd:PLN02470 563 LPM 565
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
3-567 |
3.74e-154 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 453.91 E-value: 3.74e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 3 MLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFE---NGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGA 79
Cdd:PRK06456 1 MPTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFVEdlaNGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 80 TNCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVV 159
Cdd:PRK06456 81 TNLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 160 DLPKDVQNPKEKfPYQYPETVSLRSYNPTKSG-HKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVT 238
Cdd:PRK06456 161 DIPRDIFYEKME-EIKWPEKPLVKGYRDFPTRiDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 239 TTLMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPN-ATVVHIDIDPTSISKTVQAH 317
Cdd:PRK06456 240 STFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVNIDPTDGEKAIKVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 318 VPIVGSVETVLEQMLEVIRECGFDNDKEAladWWSQINQWRSRHC-LAYEKSATQIKPQQVIETLYKVTQGQAFVASDVG 396
Cdd:PRK06456 320 VGIYGNAKIILRELIKAITELGQKRDRSA---WLKRVKEYKEYYSqFYYTEENGKLKPWKIMKTIRQALPRDAIVTTGVG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 397 QHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNR 476
Cdd:PRK06456 397 QHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 477 ALGMVKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKafAMKDRL-VFMDISVDPDEHVYPMQ 555
Cdd:PRK06456 477 TLGLVRQVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKS--AIKEDIpAVIRVPVDKEELALPTL 554
|
570
....*....|..
gi 760141809 556 IKFGAMDEMWLS 567
Cdd:PRK06456 555 PPGGRLKQVILR 566
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-534 |
1.92e-126 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 383.56 E-value: 1.92e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARST-GKVGTVLVTSGPGA 79
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 80 TNCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVV 159
Cdd:PRK11269 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 160 DLPKDVQNPKEKFPyqyPETVS-LRSYNPTksGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVT 238
Cdd:PRK11269 161 DLPFDVQVAEIEFD---PDTYEpLPVYKPA--ATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 239 TTLMGLGAFSGVHPQFIGMLGMHGTFE-ANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAH 317
Cdd:PRK11269 236 PTLMGWGAIPDDHPLMAGMVGLQTSHRyGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 318 VPIVGSVETVLEQMLEVIRECGfdnDKEALADW--WSQINQWRSRHCLayEKS---ATQIKPQQVIETLYKVTQGQAFVA 392
Cdd:PRK11269 316 LGIVSDAKAALELLVEVAREWK---AAGRLPDRsaWVADCQERKRTLL--RKThfdNVPIKPQRVYEEMNKAFGRDTCYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 393 SDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIIS 472
Cdd:PRK11269 391 STIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVL 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 760141809 473 INNRALGMVKQWQKMF---------YGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAM 534
Cdd:PRK11269 471 VNNAYLGLIRQAQRAFdmdycvqlaFENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALEQAKAL 541
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
6-533 |
1.90e-117 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 358.76 E-value: 1.90e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 6 GAQMVVRALEDQGVEHVFGYPGGSVLDIYDALfENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITG 85
Cdd:PRK08322 3 AADLFVKCLENEGVEYIFGIPGEENLDLLEAL-RDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 86 IATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPKDV 165
Cdd:PRK08322 82 VAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 166 QnpKEkfpyQYPETVSLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLMGLG 245
Cdd:PRK08322 162 A--AE----ETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 246 AFSGVHPQFIGMLG-MHGTFEaNKTMHNADLIFAVGArfdDRVTNNVAKFCPNA--TVVHIDIDPTSISKTVQAHVPIVG 322
Cdd:PRK08322 236 VIPETHPLSLGTAGlSQGDYV-HCAIEHADLIINVGH---DVIEKPPFFMNPNGdkKVIHINFLPAEVDPVYFPQVEVVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 323 SVETVLEQMLEVIRECGFDNDKEALadwwsQINQWRSRHclaYEKSATQ----IKPQQVIETLYKVTQGQAFVASDVGQH 398
Cdd:PRK08322 312 DIANSLWQLKERLADQPHWDFPRFL-----KIREAIEAH---LEEGADDdrfpMKPQRIVADLRKVMPDDDIVILDNGAY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 399 QMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRAL 478
Cdd:PRK08322 384 KIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAY 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 760141809 479 GMVKqWQKMFYGGRhsHSYME-SLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFA 533
Cdd:PRK08322 464 GMIR-WKQENMGFE--DFGLDfGNPDFVKYAESYGAKGYRVESADDLLPTLEEALA 516
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
372-554 |
1.09e-108 |
|
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: 322.91 E-value: 1.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 372 IKPQQVIETLYKVTQGQAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSV 451
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 452 QMNIQELSTCMQYGVPIKIISINNRALGMVKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKA 531
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|...
gi 760141809 532 FAmKDRLVFMDISVDPDEHVYPM 554
Cdd:cd02015 161 LA-SDGPVLLDVLVDPEENVLPM 182
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-548 |
1.82e-103 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 322.98 E-value: 1.82e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGAT 80
Cdd:PRK08199 5 PRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 81 NCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVD 160
Cdd:PRK08199 85 NASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 161 LPKDVQnpkekfpYQYPETVSLRSYNPTKsGHKG--QIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVT 238
Cdd:PRK08199 165 LPEDVL-------SETAEVPDAPPYRRVA-AAPGaaDLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 239 TTLMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKF---CPNATVVHIDIDPTSISKTVQ 315
Cdd:PRK08199 237 CAFRRQDLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGYTLLdipVPRQTLVHVHPDAEELGRVYR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 316 AHVPIVGSVETVLEQMLEVirecgfdnDKEALADWwsqiNQWRSRHCLAYEK-SATQIKPQ-----QVIETLYKVTQGQA 389
Cdd:PRK08199 317 PDLAIVADPAAFAAALAAL--------EPPASPAW----AEWTAAAHADYLAwSAPLPGPGavqlgEVMAWLRERLPADA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 390 FVASDVGQHQMFAALYYPFAKPRQWI--NSgglGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVP 467
Cdd:PRK08199 385 IITNGAGNYATWLHRFFRFRRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLP 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 468 IKIISINNRALGMVKQWQKMFYGGRHSHSYMESlPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKdRLVFMDISVDP 547
Cdd:PRK08199 462 IIVIVVNNGMYGTIRMHQEREYPGRVSGTDLTN-PDFAALARAYGGHGETVERTEDFAPAFERALASG-KPALIEIRIDP 539
|
.
gi 760141809 548 D 548
Cdd:PRK08199 540 E 540
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-559 |
4.72e-103 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 322.34 E-value: 4.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDAL-FENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGA 79
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 80 TNCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIP----EAIKKAYyiaasGRPG 155
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPeivnQAIRTAY-----EKKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 156 PVVVDLPKDVQNPKEKFPYQYP-ETVSLRSYNPTKSghkgQIKRAAKLLVDAQRPVMYVGGGAINANADhlVTKLAELLN 234
Cdd:PRK08611 156 VAVLTIPDDLPAQKIKDTTNKTvDTFRPTVPSPKPK----DIKKAAKLINKAKKPVILAGLGAKHAKEE--LLAFAEKAK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 235 LPVTTTLMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRvtnnvaKFCPN-ATVVHIDIDPTSISKT 313
Cdd:PRK08611 230 IPIIHTLPAKGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPKkAKAIQIDTDPANIGKR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 314 VQAHVPIVGSVETVLEQMLEVIR---ECGF-DNDKEALADWWSQINQWRsrhclayEKSATQIKPQQVIETLYKVTQGQA 389
Cdd:PRK08611 304 YPVNVGLVGDAKKALHQLTENIKhveDRRFlEACQENMAKWWKWMEEDE-------NNASTPIKPERVMAAIQKIADDDA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 390 FVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIK 469
Cdd:PRK08611 377 VLSVDVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 470 IISINNRALGMVKQWQKMfyGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAmKDRLVFMDISVDPDE 549
Cdd:PRK08611 457 VVVLNNQQLAFIKYEQQA--AGELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALA-QDKPVIIDVYVDPNA 533
|
570
....*....|
gi 760141809 550 HVYPMQIKFG 559
Cdd:PRK08611 534 APLPGKIVND 543
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-553 |
5.05e-102 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 318.88 E-value: 5.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLV-RHEQAAVHMADGYARSTGKVGTVLVTSGPGA 79
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHtRHEQAAGYMAFGYARSTGRPGVCSVVPGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 80 TNCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQ--ET-DMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGP 156
Cdd:PRK08266 81 LNAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 157 VVVDLPKDVqnpkekFPYQYPETVSLRSYNPTK-SGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADhlVTKLAELLNL 235
Cdd:PRK08266 161 VALEMPWDV------FGQRAPVAAAPPLRPAPPpAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEE--IRELAEMLQA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 236 PVTTTLMGLGAFSGVHPQFIGMLGmhgtfeANKTMHNADLIFAVGARFDDRVTNnvAKFCP-NATVVHIDIDPTSISKTv 314
Cdd:PRK08266 233 PVVAFRSGRGIVSDRHPLGLNFAA------AYELWPQTDVVIGIGSRLELPTFR--WPWRPdGLKVIRIDIDPTEMRRL- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 315 QAHVPIVGSVETVLEQMLEVIRECGFDND------KEALADWWSQInqwrsrhclayeksaTQIKPQ-QVIETLYKVTQG 387
Cdd:PRK08266 304 KPDVAIVADAKAGTAALLDALSKAGSKRPsrraelRELKAAARQRI---------------QAVQPQaSYLRAIREALPD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 388 QAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVP 467
Cdd:PRK08266 369 DGIFVDELSQVGFASWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 468 IKIISINNRALGMVKQWQKMFYGGRHSHSYMESlPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAmKDRLVFMDISVDP 547
Cdd:PRK08266 449 VVTVVFNNNAYGNVRRDQKRRFGGRVVASDLVN-PDFVKLAESFGVAAFRVDSPEELRAALEAALA-HGGPVLIEVPVPR 526
|
....*.
gi 760141809 548 DEHVYP 553
Cdd:PRK08266 527 GSEASP 532
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
11-546 |
9.82e-95 |
|
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: 301.01 E-value: 9.82e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 11 VRALEDQGVEHVFGYPGGSVLDIYDaLFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITGIATAY 90
Cdd:TIGR03457 9 VEVLVANGVTHAFGIMGSAFMDAMD-LFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAIAAAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 91 MDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRpGPVVVDLPKDvqnpke 170
Cdd:TIGR03457 88 WAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRD------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 171 kFPYQYPETVSLRsynPTK----SGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLMGLGA 246
Cdd:TIGR03457 161 -YFYGEIDVEIPR---PVRldrgAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 247 FSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGAR---FDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIVGS 323
Cdd:TIGR03457 237 FPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRlgpFGTLPQYGIDYWPKNAKIIQVDANAKMIGLVKKVTVGICGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 324 VETVLEQMLEVIRECGFDNDKEAL--------ADWWSQINQW-RSRHCLAYEKSATQ-------IKPQQVIETLYKVTQG 387
Cdd:TIGR03457 317 AKAAAAEILQRLAGKAGDANRAERkakiqaerSAWEQELSEMtHERDPFSLDMIVEQrqeegnwLHPRQVLRELEKAMPE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 388 QAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVP 467
Cdd:TIGR03457 397 DAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 468 IKIISINNRALGMVKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFA--MKDRLVFMDISV 545
Cdd:TIGR03457 477 VTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAaqAEGKTTVIEIVC 556
|
.
gi 760141809 546 D 546
Cdd:TIGR03457 557 T 557
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
3-533 |
5.05e-94 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 297.66 E-value: 5.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 3 MLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALfENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNC 82
Cdd:PRK07524 1 MTTCGEALVRLLEAYGVETVFGIPGVHTVELYRGL-AGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 83 ITGIATAYMDSIPLVILSG--QVPTSMIGEDAFQET-DMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVV 159
Cdd:PRK07524 80 ATAMGQAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 160 DLPKDVqnpkekFPYQYPETVSLRSYNPTKSG-HKGQIKRAAKLLVDAQRPVMYVGGGAINANADhlVTKLAELLNLPVT 238
Cdd:PRK07524 160 EIPLDV------LAAPADHLLPAPPTRPARPGpAPAALAQAAERLAAARRPLILAGGGALAAAAA--LRALAERLDAPVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 239 TTLMGLGAFSGVHPQFIGmlgmhgtfeANKT-------MHNADLIFAVGARFDDRVTNNVAK--FCPNATVVHIDIDPTS 309
Cdd:PRK07524 232 LTINAKGLLPAGHPLLLG---------ASQSlpavralIAEADVVLAVGTELGETDYDVYFDggFPLPGELIRIDIDPDQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 310 ISKTVQAHVPIVGSVETVLEQMLEVIrecgfdNDKEALADWWSQINQwRSRHCLAYEKSATQIKPQQVIETLYKVTQGQA 389
Cdd:PRK07524 303 LARNYPPALALVGDARAALEALLARL------PGQAAAADWGAARVA-ALRQALRAEWDPLTAAQVALLDTILAALPDAI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 390 FVaSDVGQHQMFAALYYPFAKPRQWINSG-GLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPI 468
Cdd:PRK07524 376 FV-GDSTQPVYAGNLYFDADAPRRWFNAStGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPL 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 760141809 469 KIISINNRALGMVKqwqkmfyggrhshSYMESL-----------PDFVKLAEAYGHVGIAVSDPAELESAMEKAFA 533
Cdd:PRK07524 455 IVLLWNNDGYGEIR-------------RYMVARdiepvgvdpytPDFIALARAFGCAAERVADLEQLQAALRAAFA 517
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
11-537 |
1.04e-91 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 293.44 E-value: 1.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 11 VRALEDQGVEHVFGYPGGSVLDIYDaLFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITGIATAY 90
Cdd:PRK07525 13 VETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 91 MDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRpGPVVVDLPKDvqnpke 170
Cdd:PRK07525 92 WAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 171 kFPYQ-----YPETVSLrsynPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLMGLG 245
Cdd:PRK07525 165 -YFYGvidveIPQPVRL----ERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLHND 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 246 AFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGAR---FDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIVG 322
Cdd:PRK07525 240 AFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRlnpFGTLPQYGIDYWPKDAKIIQVDINPDRIGLTKKVSVGICG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 323 SVETVLEQMLEVIRE--CGFDNDKEALAD-------WWSQINQW--------RSRHCLAYEKSATQIKPQQVIETLYKVT 385
Cdd:PRK07525 320 DAKAVARELLARLAErlAGDAGREERKALiaaeksaWEQELSSWdhedddpgTDWNEEARARKPDYMHPRQALREIQKAL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 386 QGQAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYG 465
Cdd:PRK07525 400 PEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHN 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 760141809 466 VPIKIISINNRALGMVKQWQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKDR 537
Cdd:PRK07525 480 WPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDAQNE 551
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
5-563 |
4.15e-88 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 283.58 E-value: 4.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 5 SGAQMVVRALEDQGVEHVFGYpggsvlDIYDALF---ENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATN 81
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFGQ------SLPSALFlaaEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 82 CITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDL 161
Cdd:PRK06112 89 LVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 162 PKDVQNPKEKFPyQYPETVSLRSYNPTKS-GHKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTT 240
Cdd:PRK06112 169 PADLLTAAAAAP-AAPRSNSLGHFPLDRTvPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 241 LMGLGAFSGVHPQFIGMLG--MHGTFEANKTMH---NADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTSISKTVQ 315
Cdd:PRK06112 248 NMGKGAVDETHPLSLGVVGslMGPRSPGRHLRDlvrEADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGRNYE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 316 AhVPIVGSVETVLEQMLEVIRECGFDNDKEALADWWSQINQWRSRHCL----AYEKSATQIKPQQVIETLYKVTQGQAFV 391
Cdd:PRK06112 328 A-LRLVGDARLTLAALTDALRGRDLAARAGRRAALEPAIAAGREAHREdsapVALSDASPIRPERIMAELQAVLTGDTIV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 392 ASDVGQHQMFAALYYPFAKPRQ-WINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKI 470
Cdd:PRK06112 407 VADASYSSIWVANFLTARRAGMrFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTI 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 471 ISINNRALGMVKQWQKMFYGGRHSHSYMESLpDFVKLAEAYGHVGIAVSDPAELESAMEKafAMKDRLVFMdISVDPDEH 550
Cdd:PRK06112 487 VVLNNGILGFQKHAETVKFGTHTDACHFAAV-DHAAIARACGCDGVRVEDPAELAQALAA--AMAAPGPTL-IEVITDPS 562
|
570
....*....|...
gi 760141809 551 VYPMQIKFGAMDE 563
Cdd:PRK06112 563 AFPPISFFEPMDR 575
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
3-567 |
8.46e-88 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 282.10 E-value: 8.46e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 3 MLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENgKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNC 82
Cdd:PRK06457 1 MPSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKS-KVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 83 ITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRpGPVVVDLP 162
Cdd:PRK06457 80 LNGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 163 KDVQNPKEKFPYQYPETVSlrsynptKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADhlVTKLAELLNLPVTTTLM 242
Cdd:PRK06457 159 VDILRKSSEYKGSKNTEVG-------KVKYSIDFSRAKELIKESEKPVLLIGGGTRGLGKE--INRFAEKIGAPIIYTLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 243 GLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDdrvtnNVAKFCPNATVVHIDIDPTSISKTVQAHVPIVG 322
Cdd:PRK06457 230 GKGILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFP-----YVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 323 SVETVLEQMLEVIRECGFDNDKEALADWWSQINQWRSrhclayeKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQMFA 402
Cdd:PRK06457 305 PVAEFLNIDIEEKSDKFYEELKGKKEDWLDSISKQEN-------SLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 403 ALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFA-NPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMV 481
Cdd:PRK06457 378 ARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 482 KQWQK-MFYGGRHSHSYMeslPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMKDRLVfMDISVDPDEHVYPMQIKFGA 560
Cdd:PRK06457 458 KFEQEvMGYPEWGVDLYN---PDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAV-LDAIVDPNERPMPPKLTFKQ 533
|
....*..
gi 760141809 561 MDEMWLS 567
Cdd:PRK06457 534 AGEYVLS 540
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-546 |
2.68e-87 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 280.48 E-value: 2.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 6 GAQMVVRALEDQGVEHVFGYPGGSVLDIYDALfENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITG 85
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDAL-EDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 86 IATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPKDV 165
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 166 QNpkekfpyqypETVSLRSYNPTKSGHKG-----QIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTT 240
Cdd:TIGR02418 160 VD----------SPVSVKAIPASYAPKLGaapddAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 241 LMGLGAFS-GVHPQFIGMLGMHGTFEANKTMHNADLIFAVG---ARFDDRVTNNVAkfcpNATVVHIDIDPTSISKTVQA 316
Cdd:TIGR02418 230 FQGAGAVSrELEDHFFGRVGLFRNQPGDRLLKQADLVITIGydpIEYEPRNWNSEN----DATIVHIDVEPAQIDNNYQP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 317 HVPIVGSVETVLEQMLEVIRECGFDND-KEALADWWSQINQWRSRhclAYEKSATQIKPQQVIETLYKVTQGQAFVASDV 395
Cdd:TIGR02418 306 DLELVGDIASTLDLLAERIPGYELPPDaLAILEDLKQQREALDRV---PATLKQAHLHPLEIIKAMQAIVTDDVTVTVDM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 396 GQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINN 475
Cdd:TIGR02418 383 GSHYIWMARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWND 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 760141809 476 RALGMVKQWQKMFYggrHSHSYMESLP-DFVKLAEAYGHVGIAVSDPAELESAMEKAFAMkDRLVFMDISVD 546
Cdd:TIGR02418 463 NGYNMVEFQEEMKY---QRSSGVDFGPiDFVKYAESFGAKGLRVESPDQLEPTLRQAMEV-EGPVVVDIPVD 530
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
5-546 |
3.81e-87 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 280.20 E-value: 3.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 5 SGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALfENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCIT 84
Cdd:PRK08617 6 YGADLVVDSLINQGVKYVFGIPGAKIDRVFDAL-EDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 85 GIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPKD 164
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 165 VQNPkekfpyqyPETV-SLRSYNPTKSG--HKGQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTL 241
Cdd:PRK08617 165 VVDA--------PVTSkAIAPLSKPKLGpaSPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 242 MGLGAFSGVH-PQFIGMLGMHGTFEANKTMHNADLIFAVG---ARFDDRVTNNVakfcPNATVVHIDIDPTSISKTVQAH 317
Cdd:PRK08617 237 QAAGVISRELeDHFFGRVGLFRNQPGDELLKKADLVITIGydpIEYEPRNWNSE----GDATIIHIDVLPAEIDNYYQPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 318 VPIVGSVETVLEQMLEVIRECGFDND-KEALADWWSQINQWRSRhclAYEKSATQIKPQQVIETLYKVTQGQAFVASDVG 396
Cdd:PRK08617 313 RELIGDIAATLDLLAEKLDGLSLSPQsLEILEELRAQLEELAER---PARLEEGAVHPLRIIRALQDIVTDDTTVTVDVG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 397 QHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNR 476
Cdd:PRK08617 390 SHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDG 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 760141809 477 ALGMVKQWQKMFYG---GRHSHSYmeslpDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMkDRLVFMDISVD 546
Cdd:PRK08617 470 HYNMVEFQEEMKYGrssGVDFGPV-----DFVKYAESFGAKGLRVTSPDELEPVLREALAT-DGPVVIDIPVD 536
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
2-531 |
1.16e-76 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 253.20 E-value: 1.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 2 EMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALfengKMEHVLVRHEQAAVHMADGYARSTG--KVGTVLVTSGPGA 79
Cdd:PRK06154 18 KTMKVAEAVAEILKEEGVELLFGFPVNELFDAAAAA----GIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 80 TNCITGIATAYMDSIPLVILSGQVPTSMigEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVV 159
Cdd:PRK06154 94 ENAFGGVAQAYGDSVPVLFLPTGYPRGS--TDVAPNFESLRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 160 DLPKDV-QNPKEKFPYQYpeTVSLRSYNPTKSGHkgqIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVT 238
Cdd:PRK06154 172 ELPVDVlAEELDELPLDH--RPSRRSRPGADPVE---VVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 239 TTLMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDrvTNNVAKFCPNATVVHIDIDPTSISKTVQAHV 318
Cdd:PRK06154 247 TTLNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTR--SYYGLPMPEGKTIIHSTLDDADLNKDYPIDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 319 PIVGSVETVLEQMLEVIREcGFDNDKEALADWWSQIN--------QWRSRhclaYEKSATQIKPQQVI-ETLYKVTQGQA 389
Cdd:PRK06154 325 GLVGDAALVLKQMIEELRR-RVGPDRGRAQQVAAEIEavraawlaKWMPK----LTSDSTPINPYRVVwELQHAVDIKTV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 390 FVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIK 469
Cdd:PRK06154 400 IITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPIL 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 760141809 470 IISINNRALGmvkqwqkmfyggrhshSYMESLP-------------DFVKLAEAYGHVGIAVSDPAELESAMEKA 531
Cdd:PRK06154 480 TILLNNFSMG----------------GYDKVMPvsttkyratdisgDYAAIARALGGYGERVEDPEMLVPALLRA 538
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-163 |
2.53e-74 |
|
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: 233.58 E-value: 2.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 8 QMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGkMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITGIA 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSG-IRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 760141809 88 TAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPK 163
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
6-552 |
1.18e-70 |
|
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: 237.43 E-value: 1.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 6 GAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGK-MEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCIT 84
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAERDrIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 85 GIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIP----EAIKKAYyiaasGRPGPVVVD 160
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPhvidEAIRRAY-----AHNGVAVVT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 161 LPKDvqnpkekFPYQ-------YPETVSLRSYN-PTKSGHkgQIKRAAKLLVDAQRPVMYVGGGAINANADhlVTKLAEL 232
Cdd:TIGR02720 156 IPVD-------FGWQeipdndyYASSVSYQTPLlPAPDVE--AVTRAVQTLKAAERPVIYYGIGARKAGEE--LEALSEK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 233 LNLPVTTTLMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFD----DRVTNNVAKFcpnatvVHIDIDPT 308
Cdd:TIGR02720 225 LKIPLISTGLAKGIIEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPfaevSKAFKNTKYF------IQIDIDPA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 309 SISKTVQAHVPIVGSVETVLEQMLEVIrecgfdNDKEALAdWW----SQINQWRSRHCLAYEKSATQIKPQQVIETLYKV 384
Cdd:TIGR02720 299 KLGKRHHTDIAVLADAKKALAAILAQV------EPRESTP-WWqanvANVKNWRAYLASLEDKTEGPLQAYQVYRAINKI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 385 TQGQAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQY 464
Cdd:TIGR02720 372 AEDDAIYSIDVGDININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 465 GVPIKIISINNRALGMVKQWQKmfygGRHSHSYMESLP--DFVKLAEAYGHVGIAVSDPAELESAMEKAFAMK-DRLVFM 541
Cdd:TIGR02720 452 HLPVINIVFSNCTYGFIKDEQE----DTNQPLIGVDFNdaDFAKIAEGVGAVGFRVNKIEQLPAVFEQAKAIKqGKPVLI 527
|
570
....*....|....*.
gi 760141809 542 DISVD-----PDEHVY 552
Cdd:TIGR02720 528 DAKITgdrplPVEKLR 543
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
6-533 |
2.03e-70 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 236.16 E-value: 2.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 6 GAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGkMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITG 85
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 86 IATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPKD- 164
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDh 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 165 VQNPKEKFPYQYPETVSLRSYNPTKSghkgQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLMGL 244
Cdd:PRK05858 166 AFSMADDDGRPGALTELPAGPTPDPD----ALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 245 GAFSGVHPQFIgmlgmhgTFEANKTMHNADLIFAVGARFDDRVtnNVAKFCPNATVVHIDIDPTSISktvqAHVPIVGSV 324
Cdd:PRK05858 242 GVVPADHPLAF-------SRARGKALGEADVVLVVGVPMDFRL--GFGVFGGTAQLVHVDDAPPQRA----HHRPVAAGL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 325 ETVLEQMLEVIRECGfdNDKEALADWwsqINQWRSRHCLAYEKSATQ-------IKPQQVIETLYKVTQGQAFVASDVGQ 397
Cdd:PRK05858 309 YGDLSAILSALAGAG--GDRTDHQGW---IEELRTAETAARARDAAEladdrdpIHPMRVYGELAPLLDRDAIVIGDGGD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 398 HQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRA 477
Cdd:PRK05858 384 FVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGI 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 760141809 478 LGMVKQWQKMFYGgrhsHSYMESL-PD--FVKLAEAYGHVGIAVSDPAELESAMEKAFA 533
Cdd:PRK05858 464 WGLEKHPMEALYG----YDVAADLrPGtrYDEVVRALGGHGELVTVPAELGPALERAFA 518
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
7-548 |
1.71e-68 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 232.11 E-value: 1.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 7 AQMVVRALEDQGVEHVFGYPGGSVLDIYDALFE-NGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITG 85
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGRaDDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 86 IATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVkHSFL--CKKASDIPEAIKKAYYIAASGRpGPVVVDLPK 163
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVA-GAFVqmVTVPEQLRHLVDRAVRTALAER-TVTAVILPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 164 DVQN-PKEKFPYQYPETVSLRSYN-PTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADhlVTKLAELLNLPVTTTL 241
Cdd:PRK08273 164 DVQElEYEPPPHAHGTVHSGVGYTrPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDE--VIAVAERLGAGVAKAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 242 MGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDdrvtnnVAKFCP---NATVVHIDIDPTSISKTVQAHV 318
Cdd:PRK08273 242 LGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFP------YSEFLPkegQARGVQIDIDGRMLGLRYPMEV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 319 PIVGSVETVLEQMLEVIREcgfDNDK-------EALADWWsQINQWRSRHclayekSATQIKPQQVIETLYKVTQGQAFV 391
Cdd:PRK08273 316 NLVGDAAETLRALLPLLER---KKDRswrerieKWVARWW-ETLEARAMV------PADPVNPQRVFWELSPRLPDNAIL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 392 ASDVG------------QHQMFAALyypfakprqwinSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMN-IQEL 458
Cdd:PRK08273 386 TADSGscanwyardlrmRRGMMASL------------SGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAEL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 459 STCMQY-----GVPIKIISINNRALGMVkQWQKMFYGGRHSHSYMESLPDF--VKLAEAYGHVGIAVSDPAELESAMEKA 531
Cdd:PRK08273 454 ITVAKYwrqwsDPRLIVLVLNNRDLNQV-TWEQRVMEGDPKFEASQDLPDVpyARFAELLGLKGIRVDDPEQLGAAWDEA 532
|
570
....*....|....*..
gi 760141809 532 FAmKDRLVFMDISVDPD 548
Cdd:PRK08273 533 LA-ADRPVVLEVKTDPN 548
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
6-166 |
2.04e-66 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 213.25 E-value: 2.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 6 GAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITG 85
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 86 IATAYMDSIPLVILSGQVPTSMIGEDAFQ-ETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLPKD 164
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 760141809 165 VQ 166
Cdd:pfam02776 161 VL 162
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
394-543 |
1.10e-65 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 210.90 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 394 DVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISI 473
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 760141809 474 NNRALGMVKQWQKMFYGGRHSHSYMESL--PDFVKLAEAYGHVGIAVSDPAELESAMEKAFAmKDRLVFMDI 543
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGKILppVDFAKLAEAYGAKGARVESPEELEEALKEALE-HDGPALIDV 151
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
2-535 |
9.32e-64 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 218.32 E-value: 9.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 2 EMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATN 81
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 82 CITGIATAYMDSIPLVILSGQVPTSMIGEDA--FQET-DMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVV 158
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 159 VDLPKDVQNPKEKFPYQY-PETVSLRSYNPtksghkGQIKRAAKLLVDAQRPVMYVGGGAINANADhlVTKLAElLNLPV 237
Cdd:PRK07064 161 VEIPIDIQAAEIELPDDLaPVHVAVPEPDA------AAVAELAERLAAARRPLLWLGGGARHAGAE--VKRLVD-LGFGV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 238 TTTLMGLGAFSGVHPQFIGMLGMHGTFEAnkTMHNADLIFAVGARFDDRVTNNVAKFCPnATVVHIDIDPTSISKTVQAH 317
Cdd:PRK07064 232 VTSTQGRGVVPEDHPASLGAFNNSAAVEA--LYKTCDLLLVVGSRLRGNETLKYSLALP-RPLIRVDADAAADGRGYPND 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 318 VPIVGSVETVLEQMLEVIREcGFDNDkealADWWSQInqwRSRHCLAYEKSATQIKPQQVI-ETLYKVTQGQAFVASDVG 396
Cdd:PRK07064 309 LFVHGDAARVLARLADRLEG-RLSVD----PAFAADL---RAAREAAVADLRKGLGPYAKLvDALRAALPRDGNWVRDVT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 397 -QHQMFAALYYPFAKPRQWINSGGlGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINN 475
Cdd:PRK07064 381 iSNSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMND 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 476 RALGMVKQWQKMFYGGRHSHSYMESlPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAMK 535
Cdd:PRK07064 460 GGYGVIRNIQDAQYGGRRYYVELHT-PDFALLAASLGLPHWRVTSADDFEAVLREALAKE 518
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
7-561 |
4.03e-62 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 214.85 E-value: 4.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 7 AQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITGI 86
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 87 ATAYMDSIPLVILSGQVPTSMIGEDAFQET-------------DMIGISR--PVVKHSflckkasdipeAIKKAYyiaas 151
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQIGSGFFQEThpdrlfvecsgycEMVSSAEqaPRVLHS-----------AIQHAV----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 152 GRPGPVVVDLPKDVQNpkEKFPYQYPETVsLRSYNPTKSGHKGQIKRAAKLLVDAQRPVMYVGGGAINANADhlVTKLAE 231
Cdd:PRK06546 150 AGGGVSVVTLPGDIAD--EPAPEGFAPSV-ISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAE--VLALAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 232 LLNLPVTTTLMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARF--DDrvtnnvakFCPNATVVHIDIDPTS 309
Cdd:PRK06546 225 KIKAPVGHSLRGKEWIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFpyDQ--------FLPDVRTAQVDIDPEH 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 310 ISKTVQAHVPIVGSVETVLEQMLEVIREcgfDNDKEALADWWSQINQWRSRHCLAYEKSA---TQIKPQQVIETLYKVTQ 386
Cdd:PRK06546 297 LGRRTRVDLAVHGDVAETIRALLPLVKE---KTDRRFLDRMLKKHARKLEKVVGAYTRKVekhTPIHPEYVASILDELAA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 387 GQAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGV 466
Cdd:PRK06546 374 DDAVFTVDTGMCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 467 PIKIISINNRALGMVKqwQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAmKDRLVFMDISVD 546
Cdd:PRK06546 454 PVKVVVFNNSTLGMVK--LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFA-HPGPALVDVVTD 530
|
570
....*....|....*
gi 760141809 547 PDEHVYPMQIKFGAM 561
Cdd:PRK06546 531 PNALSIPPTITGEQV 545
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-548 |
1.14e-60 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 210.63 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDAL--FENGKMEH---VLVRHEQAAVHMADGYARSTGKVGTVLVTS 75
Cdd:PRK08327 4 LTMYTAAELFLELLKELGVDYIFINSGTDYPPIIEAKarARAAGRPLpefVICPHEIVAISMAHGYALVTGKPQAVMVHV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 76 GPGATNCITGIATAYMDSIPLVILSGQVPTSMIGE----DAF----QET-DMIGISRPVVKHSFLCKKASDIPEAIKKAY 146
Cdd:PRK08327 84 DVGTANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrNTRihwtQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 147 YIAASGRPGPVVVDLPKDVQnpKEKFPYqypETVSLRSYNPTKSGH--KGQIKRAAKLLVDAQRPVMYVGGGAINANADH 224
Cdd:PRK08327 164 QIAMSEPKGPVYLTLPREVL--AEEVPE---VKADAGRQMAPAPPApdPEDIARAAEMLAAAERPVIITWRAGRTAEGFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 225 LVTKLAELLNLPVTTTLMGLGAFSGVHPqfigmlgMHGTFEANKTMHNADLIFAVgarfDDRV----TNNVAKfcPNATV 300
Cdd:PRK08327 239 SLRRLAEELAIPVVEYAGEVVNYPSDHP-------LHLGPDPRADLAEADLVLVV----DSDVpwipKKIRPD--ADARV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 301 VHIDIDPtsiSKT------VQAHVPIVGSVETVLEQMLEVIRECGFDND--KEALADWWSQIN---QWRSRHCLAYEKSA 369
Cdd:PRK08327 306 IQIDVDP---LKSriplwgFPCDLCIQADTSTALDQLEERLKSLASAERrrARRRRAAVRELRirqEAAKRAEIERLKDR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 370 TQIKPQQVIETLYKVTQGQAFVASDVGqhqmFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDG 449
Cdd:PRK08327 383 GPITPAYLSYCLGEVADEYDAIVTEYP----FVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 450 SVQMNIQELSTCM--QYGVPIKIISINNRALGMVKQ-WQKMFYGG--RHSHSYMES----LPDFVKLAEAYGHVGIAVSD 520
Cdd:PRK08327 459 SFIFGVPEAAHWVaeRYGLPVLVVVFNNGGWLAVKEaVLEVYPEGyaARKGTFPGTdfdpRPDFAKIAEAFGGYGERVED 538
|
570 580 590
....*....|....*....|....*....|.
gi 760141809 521 PAELESAMEKAFA-MKD--RLVFMDISVDPD 548
Cdd:PRK08327 539 PEELKGALRRALAaVRKgrRSAVLDVIVDRV 569
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
14-546 |
2.59e-60 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 208.66 E-value: 2.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 14 LEDQGVEHVFGYPGGSVLDIYDALFENgkMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITGIATAYMDS 93
Cdd:PRK07092 22 LRRFGITTVFGNPGSTELPFLRDFPDD--FRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFTAFKNH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 94 IPLVILSGQVPTSMIGEDAF-QETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVDLP-KDVQNPKEK 171
Cdd:PRK07092 100 TPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPyDDWDQPAEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 172 FPyqyPETVSlRSYNPTKSghkgQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLM-GLGAFSGV 250
Cdd:PRK07092 180 LP---ARTVS-SAVRPDPA----ALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPVWVAPMsGRCSFPED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 251 HPQFIGML-GMHGTFEANKTMHnaDLIFAVGAR-FDDRVTNNVAKFCPNATVVHIDIDPTSISKTvqahvP----IVGSV 324
Cdd:PRK07092 252 HPLFAGFLpASREKISALLDGH--DLVLVIGAPvFTYHVEGPGPHLPEGAELVQLTDDPGEAAWA-----PmgdaIVGDI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 325 ETVLEQMLEVIRECgfdnDKEALadwwsqinQWRSRHClAYEKSATQIKPQQVIETLYKVTQGQAFVASDVGQHQ--MFA 402
Cdd:PRK07092 325 RLALRDLLALLPPS----ARPAP--------PARPMPP-PAPAPGEPLSVAFVLQTLAALRPADAIVVEEAPSTRpaMQE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 403 AL-------YYPFAkprqwinSGGLgtmGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINN 475
Cdd:PRK07092 392 HLpmrrqgsFYTMA-------SGGL---GYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNN 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 760141809 476 RALGMVKQWQKMFyGGRHSHSyMEsLP--DFVKLAEAYGHVGIAVSDPAELESAMEKAFAMkDRLVFMDISVD 546
Cdd:PRK07092 462 GRYGALRWFAPVF-GVRDVPG-LD-LPglDFVALARGYGCEAVRVSDAAELADALARALAA-DGPVLVEVEVA 530
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
196-331 |
5.17e-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: 192.78 E-value: 5.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 196 IKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAELLNLPVTTTLMGLGAFSGVHPQFIGMLGMHGTFEANKTMHNADL 275
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 760141809 276 IFAVGARFDD-RVTNNVAKFCPNATVVHIDIDPTSISKTVQAHVPIVGSVETVLEQM 331
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
7-558 |
4.21e-55 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 195.59 E-value: 4.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 7 AQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITGI 86
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 87 ATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYiAASGRPGPVVVDLPKDV- 165
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMR-KAILNRGVAVVVLPGDVa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 166 --QNPKEKFPYQYPETVSLRSynPTKSghkgQIKRAAKLLVDAQRPVMYVGGGAINANADhlVTKLAELLNLPVTTTLMG 243
Cdd:PRK09124 165 lkPAPERATPHWYHAPQPVVT--PAEE----ELRKLAALLNGSSNITLLCGSGCAGAHDE--LVALAETLKAPIVHALRG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 244 LGAFSGVHPQFIGMLGMHGTFEANKTMHNADLIFAVGARFDDRvtnnvaKFCP-NATVVHIDIDPTSISKTVQAHVPIVG 322
Cdd:PRK09124 237 KEHVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR------QFYPtDAKIIQIDINPGSLGRRSPVDLGLVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 323 SVETVLEQ---MLEVIRECGF-DNDKEALADWWSQINQwrsrhcLAYEKSATQ-IKPQQVIETLYKVTQGQAFVASDVGQ 397
Cdd:PRK09124 311 DVKATLAAllpLLEEKTDRKFlDKALEHYRKARKGLDD------LAVPSDGGKpIHPQYLARQISEFAADDAIFTCDVGT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 398 HQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRA 477
Cdd:PRK09124 385 PTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 478 LGMVKqwQKMFYGGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFAmKDRLVFMDISVDPDEHVYPMQIK 557
Cdd:PRK09124 465 LGFVA--MEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFA-HDGPALVDVVTAKQELAMPPQIK 541
|
.
gi 760141809 558 F 558
Cdd:PRK09124 542 L 542
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
7-550 |
1.03e-54 |
|
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: 193.84 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 7 AQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGkVGTVLVTSGPGATNCITGI 86
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 87 ATAYMDSIPLVILSGQVPTS----------MIGE---DAFQEtdmigISRPVVkhsflCKKAS--------DIPEAIKKA 145
Cdd:COG3961 87 AGAYAERVPVVHIVGAPGTRaqrrgpllhhTLGDgdfDHFLR-----MFEEVT-----VAQAVltpenaaaEIDRVLAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 146 YYiaaSGRPgpVVVDLPKDV-----QNPKEKFPYQYPET--VSLRSYnptksghkgqIKRAAKLLVDAQRPVMYVGGGAI 218
Cdd:COG3961 157 LR---EKRP--VYIELPRDVadapiEPPEAPLPLPPPASdpAALAAA----------VAAAAERLAKAKRPVILAGVEVH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 219 NANADHLVTKLAELLNLPVTTTLMGLGAFSGVHPQFIGM-LGMHGTFEANKTMHNADLIFAVGARFDDRVTNN-VAKFCP 296
Cdd:COG3961 222 RFGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGVVFTDTNTGGfTAQLDP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 297 NATvvhIDIDP--TSISKTVQAHVPIVGSVETVLEQMLEV-----IRECG----FDNDKEAL--ADWWSQINQWrsrhcl 363
Cdd:COG3961 302 ERT---IDIQPdsVRVGGHIYPGVSLADFLEALAELLKKRsaplpAPAPPppppPAAPDAPLtqDRLWQRLQAF------ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 364 ayeksatqIKPQQVIetlykvtqgqafVAsDVGQhQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVC 443
Cdd:COG3961 373 --------LDPGDIV------------VA-DTGT-SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 444 CVTGDGSVQMNIQELSTCMQYGVPIKIISINN------RAL-GM------VKQWqkmfyggrhshsymeslpDFVKLAEA 510
Cdd:COG3961 431 LLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNdgytieRAIhGPdgpyndIANW------------------DYAKLPEA 492
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 760141809 511 YG---HVGIAVSDPAELESAMEKAFAMKDRLVFMDISVDPDEH 550
Cdd:COG3961 493 FGggnALGFRVTTEGELEEALAAAEANTDRLTLIEVVLDKMDA 535
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
376-533 |
1.27e-48 |
|
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: 166.28 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 376 QVIETLYKVTQGQAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNI 455
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 760141809 456 QELSTCMQYGVPIKIISINNRALGMVKQWQKMFYGGRHSHSYMeSLPDFVKLAEAYGHVGIAVSDPAELESAMEKAFA 533
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDL-SNPDFAALAEAYGAKGVRVEDPEDLEAALAEALA 157
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
2-533 |
1.98e-47 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 174.40 E-value: 1.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 2 EMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGkMEHVLVRHEQAAVHMA--DGYArsTGKVGTVLVTSGPGA 79
Cdd:PRK09259 8 QLTDGFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEG-IRYIGFRHEQSAGNAAaaAGFL--TQKPGVCLTVSAPGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 80 TNCITGIATAYMDSIPLVILSGQVPTSMI----GEdaFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPG 155
Cdd:PRK09259 85 LNGLTALANATTNCFPMIMISGSSEREIVdlqqGD--YEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 156 PVVVDLPKDV---QNPKEK-----------FPYQYPETVSlrsynptksghkgqIKRAAKLLVDAQRPVMYVGGGAINAN 221
Cdd:PRK09259 163 GVYLDLPAKVlaqTMDADEaltslvkvvdpAPAQLPAPEA--------------VDRALDLLKKAKRPLIILGKGAAYAQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 222 ADHLVTKLAELLNLPVTTTLMGLGAFSGVHPQFIGmlgmhgtfeANKTM--HNADLIFAVGARFDDRVTNNVAK-FCPNA 298
Cdd:PRK09259 229 ADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAA---------AARSLalANADVVLLVGARLNWLLSHGKGKtWGADK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 299 TVVHIDIDPTSISKTVQAHVPIVGSVETVLEQMLEVIRECGFDndkeALADWWSQINQWRSRHClayEKSATQIKPQQ-- 376
Cdd:PRK09259 300 KFIQIDIEPQEIDSNRPIAAPVVGDIGSVMQALLAGLKQNTFK----APAEWLDALAERKEKNA---AKMAEKLSTDTqp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 377 --------VIETLYKVTQGQAFV-----ASDVGqhQMFAALYypfaKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVc 443
Cdd:PRK09259 373 mnfynalgAIRDVLKENPDIYLVneganTLDLA--RNIIDMY----KPRHRLDCGTWGVMGIGMGYAIAAAVETGKPVV- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 444 CVTGDGSVQMNIQELSTCMQYGVPIKIISINNralGMVKQWQKMFYGGRHSHSYMESLPD--FVKLAEAYGHVGIAVSDP 521
Cdd:PRK09259 446 AIEGDSAFGFSGMEVETICRYNLPVTVVIFNN---GGIYRGDDVNLSGAGDPSPTVLVHHarYDKMMEAFGGVGYNVTTP 522
|
570
....*....|..
gi 760141809 522 AELESAMEKAFA 533
Cdd:PRK09259 523 DELRHALTEAIA 534
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
372-549 |
1.91e-44 |
|
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: 155.38 E-value: 1.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 372 IKPQQVIETLYKVTQGQAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSV 451
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 452 QMNIQELSTCMQYGVPIKIISINNRALGMVKQWQKMFygGRHSHSYMESLPDFVKLAEAYGHVGIAVSDPAELESAMEKA 531
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVM--GQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEA 159
|
170
....*....|....*...
gi 760141809 532 FAMkDRLVFMDISVDPDE 549
Cdd:cd02014 160 LAA-DGPVVIDVVTDPNE 176
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
7-166 |
1.92e-43 |
|
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: 152.32 E-value: 1.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 7 AQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCITGI 86
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 87 ATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRpGPVVVDLPKDVQ 166
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGDVQ 161
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
374-546 |
1.07e-39 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 142.81 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 374 PQQVIETLYKVTQGQAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQM 453
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 454 NIQELSTCMQYGVPIKIISINNRALGMVKqWQKMFYGGRhsHSYME-SLPDFVKLAEAYGHVGIAVSDPAELESAMEKAF 532
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIK-WKQEKEYGR--DSGVDfGNPDFVKYAESFGAKGYRIESADDLLPVLERAL 157
|
170
....*....|....
gi 760141809 533 AmKDRLVFMDISVD 546
Cdd:cd02010 158 A-ADGVHVIDCPVD 170
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
10-163 |
7.36e-35 |
|
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: 128.62 E-value: 7.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 10 VVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKvGTVLVTSGPGATNCITGIATA 89
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGP-PVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 760141809 90 YMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGrPGPVVVDLPK 163
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
372-547 |
1.17e-32 |
|
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: 124.16 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 372 IKPQQVIETLYKVTQGQAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSV 451
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 452 QMNIQELSTCMQYGVPIKIISINNRALGMVKQWQKMFYGGRHSHSYMESlPDFVKLAEAYGHVGIAVSDPAELESAMEKA 531
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELES-ESFAKIAEACGAKGITVDKPEDVGPALQKA 162
|
170
....*....|....*...
gi 760141809 532 FAM--KDRLVFMDISVDP 547
Cdd:cd02013 163 IAMmaEGKTTVIEIVCDQ 180
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
374-533 |
3.60e-27 |
|
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: 108.00 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 374 PQQVIETLYKVTQGQAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQM 453
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 454 NIQELSTCMQYGVPIKIISINNRALGMVKQWQK-MFYGGRHSHSYMESLpDFVKLAEAYGHVGIAVSDPAELESAMEKAF 532
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQlSYGLGLPVTTLLPDT-RYDLVAEAFGGKGELVTTPEELKPALKRAL 159
|
.
gi 760141809 533 A 533
Cdd:cd02004 160 A 160
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
405-533 |
8.06e-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: 106.91 E-value: 8.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 405 YYPFAKPRQWINSGGlGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMVKQW 484
Cdd:cd02002 34 QLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALWTAARYGLPVTVVILNNRGYGALRSF 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 760141809 485 QKMFYGGRHSHSYMESL------PDFVKLAEAYGHVGIAVSDPAELESAMEKAFA 533
Cdd:cd02002 113 LKRVGPEGPGENAPDGLdlldpgIDFAAIAKAFGVEAERVETPEELDEALREALA 167
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
372-534 |
3.15e-25 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 103.51 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 372 IKPQQVIETLYKVTQGQAFVASDVGQHQMFAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSV 451
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 452 QMNIQELSTCMQYGVPIKIISINNRALGMVKQWQKMFyggrhSHSYMESLP--------------DFVKLAEAYGHVGIA 517
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAF-----DMDYQVNLAfeninsselggygvDHVKVAEGLGCKAIR 162
|
170
....*....|....*..
gi 760141809 518 VSDPAELESAMEKAFAM 534
Cdd:cd02006 163 VTKPEELAAAFEQAKKL 179
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
401-549 |
6.88e-25 |
|
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: 101.84 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 401 FAALYYPFAKPRQWINSGGLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGM 480
Cdd:cd02005 30 FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTI 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 760141809 481 vkqwQKMFYGGRHSHSYMESLpDFVKLAEAYG----HVGIAVSDPAELESAMEKAFAMKDRLVFMDISVDPDE 549
Cdd:cd02005 110 ----ERAIHGPEASYNDIANW-NYTKLPEVFGggggGLSFRVKTEGELDEALKDALFNRDKLSLIEVILPKDD 177
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
5-533 |
4.43e-21 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 96.84 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 5 SGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCIT 84
Cdd:PRK07586 2 NGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 85 GIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPV---VKHSflcKKASDIP----EAIKkayyiAASGRPGPV 157
Cdd:PRK07586 82 NLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVsgwVRRS---ESAADVAadaaAAVA-----AARGAPGQV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 158 VVD-LPKDVQ-NPKEKfPYQYPETVSLRSYNPTksghkgQIKRAAKLLVDAQRPVMYVGGGAINANADHLVTKLAEL--- 232
Cdd:PRK07586 154 ATLiLPADVAwSEGGP-PAPPPPAPAPAAVDPA------AVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAAtga 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 233 -LNLPVTTTLM----GLGAFSGVhPQFIGMlgmhgtfeANKTMHNADLIFAVGAR-------FDDRVTNNVAKFCPNATV 300
Cdd:PRK07586 227 rLLAETFPARMergaGRPAVERL-PYFAEQ--------ALAQLAGVRHLVLVGAKapvaffaYPGKPSRLVPEGCEVHTL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 301 VHIDIDPTSIsktVQAHVPIVGS--VETVLEQMLEVIRECGfDNDKEALAdwwsqinqwrsrhclayeKSATQIKPQQVI 378
Cdd:PRK07586 298 AGPGEDAAAA---LEALADALGAkpAAPPLAAPARPPLPTG-ALTPEAIA------------------QVIAALLPENAI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 379 ETLYKVTQGQAFVASDVGqhqmfaalyypfAKPRQWINSGGlGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQEL 458
Cdd:PRK07586 356 VVDESITSGRGFFPATAG------------AAPHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQAL 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 459 STCMQYGVPIKIISINNRA---LGMVKQWQKMFYGGRHSHSyMESL----PDFVKLAEAYGHVGIAVSDPAELESAMEKA 531
Cdd:PRK07586 423 WTQARENLDVTTVIFANRAyaiLRGELARVGAGNPGPRALD-MLDLddpdLDWVALAEGMGVPARRVTTAEEFADALAAA 501
|
..
gi 760141809 532 FA 533
Cdd:PRK07586 502 LA 503
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
11-112 |
8.53e-20 |
|
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: 86.39 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 11 VRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGkVGTVLVTSGPGATNCITGIATAY 90
Cdd:cd07038 4 LERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAY 82
|
90 100
....*....|....*....|..
gi 760141809 91 MDSIPLVILSGQVPTSMIGEDA 112
Cdd:cd07038 83 AEHVPVVHIVGAPSTKAQASGL 104
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
1-477 |
2.80e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 88.01 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 1 MEMLSGAQMVVRALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGAT 80
Cdd:PRK12474 2 GQTMNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 81 NCITGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSFLCKKASDIPEAIKKAYYIAASGRPGPVVVD 160
Cdd:PRK12474 82 NGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 161 LPKDVQNPKEKFPYQypetvSLRSYNPTKSgHKGQIKRAAKLLVDAQRPVMYVGGGAINAN----ADHLVTKLAELLNLP 236
Cdd:PRK12474 162 MPADVAWNEAAYAAQ-----PLRGIGPAPV-AAETVERIAALLRNGKKSALLLRGSALRGApleaAGRIQAKTGVRLYCD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 237 VTTTLMGLGA-------FSGVHPQFIGMLgmhgtfeanktmHNADLIFAVGARfddrvtNNVAKFC-PNAtvvhididpt 308
Cdd:PRK12474 236 TFAPRIERGAgrvpierIPYFHEQITAFL------------KDVEQLVLVGAK------PPVSFFAyPGK---------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 309 sisktvqahvPIVGSVETVleqmlEVIRECGFDNDK----EALADWWSQINQWRSRHCLAY-EKSATQIKPQQVIETLYK 383
Cdd:PRK12474 288 ----------PSWGAPPGC-----EIVYLAQPDEDLaqalQDLADAVDAPAEPAARTPLALpALPKGALNSLGVAQLIAH 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 384 VTQGQAFVASDVGQHQMFAALYYPFAKPRQWINSGGlGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQ 463
Cdd:PRK12474 353 RTPDQAIYADEALTSGLFFDMSYDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMAR 431
|
490
....*....|....
gi 760141809 464 YGVPIKIISINNRA 477
Cdd:PRK12474 432 ENLDVTVVIFANRS 445
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
419-547 |
1.24e-17 |
|
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: 81.58 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 419 GLGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVPIKIISINNRALGMVKQWQKMFYGGRHSHSY- 497
Cdd:cd02003 46 GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGTEFr 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 760141809 498 ---------MESLP--DFVKLAEAYGHVGIAVSDPAELESAMEKAFAmKDRLVFMDISVDP 547
Cdd:cd02003 126 drdqesgqlDGALLpvDFAANARSLGARVEKVKTIEELKAALAKAKA-SDRTTVIVIKTDP 185
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
8-162 |
3.22e-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: 73.30 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 8 QMVVRALEDQGVEHVFGYPGGS----VLdiydALFENGKMEHVLVRHEQAAVHMADGYARSTGKVGTVLVTSGPGATNCI 83
Cdd:cd07037 1 QALVEELKRLGVRDVVISPGSRsaplAL----AAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 84 TGIATAYMDSIPLVILSGQVPTSMIGEDAFQETDMIGISRPVVKHSF---LCKKASDIPE---AIKKAYYIAASGRPGPV 157
Cdd:cd07037 77 PAVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVdlpPPEDDDDLWYllrLANRAVLEALSAPPGPV 156
|
....*
gi 760141809 158 VVDLP 162
Cdd:cd07037 157 HLNLP 161
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
12-475 |
4.91e-12 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 68.57 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 12 RALEDQGVEHVFGYPGGSVLDIYDALFENGKMEHVLVRHEQAAVHMADGYARSTGkVGTVLVTSGPGATNCITGIATAYM 91
Cdd:PLN02573 24 RRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGAYS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 92 DSIPLVILSGQvPTS-----------MIGEDAF-QETDMIgisRPVVKHSFLCKKASDIPEAIKKAyyIA-ASGRPGPVV 158
Cdd:PLN02573 103 ENLPVICIVGG-PNSndygtnrilhhTIGLPDFsQELRCF---QTVTCYQAVINNLEDAHELIDTA--IStALKESKPVY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 159 V----DLPkDVQNP---KEKFPYQYPETVSlrsynpTKSGHKGQIKRAAKLLVDAQRPVMyVGGGAIN-ANADHLVTKLA 230
Cdd:PLN02573 177 IsvscNLA-AIPHPtfsREPVPFFLTPRLS------NKMSLEAAVEAAAEFLNKAVKPVL-VGGPKLRvAKACKAFVELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 231 ELLNLPVTTTLMGLGAFSGVHPQFIGML-GMHGTFEANKTMHNADLIFAVGARFDDRVTNNVAKFCPNATVVHIDIDPTS 309
Cdd:PLN02573 249 DASGYPVAVMPSAKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 310 IsktvqAHVPIVGSVetVLEQMLEVI------RECGFDNDKealadwwsqinqwrsRHCLAYEKSATQiKPQQVIET--L 381
Cdd:PLN02573 329 I-----GNGPAFGCV--LMKDFLEALakrvkkNTTAYENYK---------------RIFVPEGEPLKS-EPGEPLRVnvL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 382 YKVTQ----GQAFVASDVGQhqmfaalyypfakprQWINSGGL--------------GTMGFGIPAAMGAQFANPDA-VV 442
Cdd:PLN02573 386 FKHIQkmlsGDTAVIAETGD---------------SWFNCQKLklpegcgyefqmqyGSIGWSVGATLGYAQAAPDKrVI 450
|
490 500 510
....*....|....*....|....*....|...
gi 760141809 443 CCVtGDGSVQMNIQELSTCMQYGVPIKIISINN 475
Cdd:PLN02573 451 ACI-GDGSFQVTAQDVSTMIRCGQKSIIFLINN 482
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
421-550 |
4.08e-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: 50.39 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 421 GTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTCMQYGVP-IKIISINNRALGMVkqwqkmfyGGRHSHSYME 499
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPAnLIHIVLNNGAHDSV--------GGQPTVSFDV 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 760141809 500 SLPDFVKlAEAYGHVgIAVSDPAELESAMEKAFAMkDRLVFMDISVDPDEH 550
Cdd:cd03371 120 SLPAIAK-ACGYRAV-YEVPSLEELVAALAKALAA-DGPAFIEVKVRPGSR 167
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
375-535 |
5.45e-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: 48.22 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 375 QQVIETLYKvtQGQAFVASDVGQHqmfAALYYPFAKPrqWINSgglgTMGFGIPAAMGAQFANPDAVVCCVTGDG-SVQM 453
Cdd:COG1013 29 LKALDELLD--GDKTVVVSGIGCS---SVAPGYFNVP--GFHT----LHGRAAAVATGIKLANPDLTVIVFGGDGdTYDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 454 NIQELSTCMQYGVPIKIISINNRALGMVkqwqkmfyGGRHS-----HSYMESLP--------DFVKLAEAYGHVGIA--- 517
Cdd:COG1013 98 GGNHLIHAARRNEDITYIVYDNEIYGNT--------GGQRSpttplGAKTTTTPygkpeppkDPAEIAAAHGATYVAras 169
|
170
....*....|....*...
gi 760141809 518 VSDPAELESAMEKAFAMK 535
Cdd:COG1013 170 VGDPKDLKKKIKKAIEHK 187
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
413-532 |
1.03e-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: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 413 QWINSGGL-GTMGFGIPAAMGAQFANPDAVVCCVTGDG---SVQMNiqELSTCMQYGVPIKIISINNRALGMVK------ 482
Cdd:cd03375 42 YYFNTYGFhTLHGRALAVATGVKLANPDLTVIVVSGDGdlaAIGGN--HFIHAARRNIDITVIVHNNQIYGLTKgqaspt 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 760141809 483 ----QWQKMFYGGRHSHSYmeslpDFVKLAEAYGHVGIA---VSDPAELESAMEKAF 532
Cdd:cd03375 120 tpegFKTKTTPYGNIEEPF-----NPLALALAAGATFVArgfSGDIKQLKEIIKKAI 171
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
420-548 |
4.92e-05 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 44.20 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 420 LGTMGFGIPAAMGAQFANPDAVVCcVTGDGSVQMNIQELSTcMQYGVP--IKIISINNRALGMVkqwqkmfyGGRHSHSy 497
Cdd:cd03372 41 LGSMGLASSIGLGLALAQPRKVIV-IDGDGSLLMNLGALAT-IAAEKPknLIIVVLDNGAYGST--------GNQPTHA- 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 760141809 498 mESLPDFVKLAEAYG-HVGIAVSDPAELESAMEKAfamKDRLVFMDISVDPD 548
Cdd:cd03372 110 -GKKTDLEAVAKACGlDNVATVASEEAFEKAVEQA---LDGPSFIHVKIKPG 157
|
|
| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
6-102 |
2.68e-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: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 6 GAQMVVRALEDQGVEHVFGYPG---GSVLDIYDAlFENGKMEHVLVR--HEQAAVHMADGyARSTGKVGTVlVTSGPGAT 80
Cdd:cd07034 1 GNEAVARGALAAGVDVVAAYPItpsTEIAETLAK-AVLGELGGVVVQaeSEHAAAEAAIG-ASAAGARAMT-ATSGPGLN 77
|
90 100
....*....|....*....|..
gi 760141809 81 NCITGIATAYMDSIPLVILSGQ 102
Cdd:cd07034 78 LMAEALYLAAGAELPLVIVVAQ 99
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
420-533 |
5.98e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 41.36 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 420 LGTMGFGIPAAMGAQFANPDAVVCCVTGDGSVQMNIQELSTcmqygvpikIISINNRALGMVkQWQKMFY---GGRHSHS 496
Cdd:PRK06163 56 LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGT---------IAALAPKNLTII-VMDNGVYqitGGQPTLT 125
|
90 100 110
....*....|....*....|....*....|....*...
gi 760141809 497 ymESLPDFVKLAEAYGHVGIA-VSDPAELESAMEKAFA 533
Cdd:PRK06163 126 --SQTVDVVAIARGAGLENSHwAADEAHFEALVDQALS 161
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
420-548 |
7.46e-04 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 40.55 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 420 LGTMGFGIPAAMGAQFANPDAVVCcVTGDGSVQMNIQELSTCMQY-GVPIKIISINNRALGMVkqwqkmfyGGRHSHSYM 498
Cdd:cd02001 41 LGSMGLAGSIGLGLALGLSRKVIV-VDGDGSLLMNPGVLLTAGEFtPLNLILVVLDNRAYGST--------GGQPTPSSN 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 760141809 499 ESLPdfvKLAEAYGHVGIAVSDPAELESAMEKAFAMkDRLVFMDISVDPD 548
Cdd:cd02001 112 VNLE---AWAAACGYLVLSAPLLGGLGSEFAGLLAT-TGPTLLHAPIAPG 157
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
380-449 |
9.37e-04 |
|
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: 40.34 E-value: 9.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 380 TLYKVTQGQAFVASDVGQHQMFAAlyypfaKPRQWINsgGLGTMGFGIPAAMGAQFANPDAVVCCVTGDG 449
Cdd:cd02008 18 ALRKAFKKDSIVSGDIGCYTLGAL------PPLNAID--TCTCMGASIGVAIGMAKASEDKKVVAVIGDS 79
|
|
| TPP_PK |
cd02011 |
Thiamine pyrophosphate (TPP) family, Phosphoketolase (PK) subfamily, TPP-binding module; PK ... |
415-449 |
1.19e-03 |
|
Thiamine pyrophosphate (TPP) family, Phosphoketolase (PK) subfamily, TPP-binding module; PK catalyzes the conversion of D-xylulose 5-phosphate and phosphate to acetyl phosphate, D-glyceraldehyde-3-phosphate and H2O. This enzyme requires divalent magnesium ions and TPP for activity.
Pssm-ID: 238969 [Multi-domain] Cd Length: 227 Bit Score: 40.78 E-value: 1.19e-03
10 20 30
....*....|....*....|....*....|....*
gi 760141809 415 INSGGlgTMGFGIPAAMGAQFANPDAVVCCVTGDG 449
Cdd:cd02011 58 IHEGG--ELGYSLSHAYGAVFDNPDLIVACVVGDG 90
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
415-482 |
4.75e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 39.09 E-value: 4.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 760141809 415 INSGGL-GTMGFGIPAAMGAQFANPDAVVCCVTGDG---SVQMNiqELSTCMQYGVPIKIISINNRALGMVK 482
Cdd:PRK05778 63 FLSHGLhTLHGRAIAFATGAKLANPDLEVIVVGGDGdlaSIGGG--HFIHAGRRNIDITVIVENNGIYGLTK 132
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
408-518 |
6.77e-03 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 39.16 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 408 FAKPRQWInsGGLGTMGFGIPAAMGAQFA-----------NPDAVVCCVTGDGSVqmNIQELSTCMQ----YGVPIKIIS 472
Cdd:PLN02374 183 FSKEHNLL--GGFAFIGEGIPVATGAAFSskyrrevlkeeSCDDVTLAFFGDGTC--NNGQFFECLNmaalWKLPIVFVV 258
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 760141809 473 INNR-ALGMvkqwqkmfyggrhSHSYMESLPDFVKLAEAYGHVGIAV 518
Cdd:PLN02374 259 ENNLwAIGM-------------SHLRATSDPEIWKKGPAFGMPGVHV 292
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
408-518 |
8.92e-03 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 38.69 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 760141809 408 FAKPRQWInsGGLGTMGFGIPAAMGAQFAN-----------PDAVVCCVTGDGSVqmNIQELSTCMQYGV----PIKIIS 472
Cdd:CHL00149 117 FSAPHNFL--GGFAFIGEGIPIALGAAFQSiyrqqvlkevqPLRVTACFFGDGTT--NNGQFFECLNMAVlwklPIIFVV 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 760141809 473 INNR-ALGMvkqwqkmfyggrhSHSYMESLPDFVKLAEAYGHVGIAV 518
Cdd:CHL00149 193 ENNQwAIGM-------------AHHRSTSIPEIHKKAEAFGLPGIEV 226
|
|
| |
