|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-562 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 1188.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 1 MASSGTTSNTMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVC 80
Cdd:PRK08155 1 MASSGTTSTRKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 81 MACSGPGATNLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQS 160
Cdd:PRK08155 81 MACSGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 161 GRPGPVWIDIPKDVQAATIELETLPEPGERAPAPAFAPESVREAAAMINAAKRPVLYLGGGVIN--APQPIRDLAEKANL 238
Cdd:PRK08155 161 GRPGPVWIDIPKDVQTAVIELEALPAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINsgAPARARELAEKAQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 239 PTTMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQ 318
Cdd:PRK08155 241 PTTMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 319 PHVAIQGDVAEVLAQLTPQIEAQPRDEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWT 398
Cdd:PRK08155 321 PHVAIQADVDDVLAQLLPLVEAQPRAEWHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQHQMWT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 399 AQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVH 478
Cdd:PRK08155 401 AQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 479 QQQSLFYQQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKVYPMVPPGAANTE 558
Cdd:PRK08155 481 QQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYPMVPPGAANTE 560
|
....
gi 895912174 559 MVGE 562
Cdd:PRK08155 561 MIGE 564
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
11-559 |
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: 706.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 11 MRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATN 90
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 91 LITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDI 170
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 171 PKDVQAATIELE-TLPEPGERAPAPAFAPESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLMAL 247
Cdd:COG0028 161 PKDVQAAEAEEEpAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARraGAAEELRALAERLGAPVVTTLMGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 248 GMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDV 327
Cdd:COG0028 241 GAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIVGDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 328 AEVLAQLTPQIEAQPRD--EWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLN 405
Cdd:COG0028 321 KAVLAALLEALEPRADDraAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 406 RPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFY 485
Cdd:COG0028 401 RPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFY 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 895912174 486 QQGVFaATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQkvypmVPPGAANTEM 559
Cdd:COG0028 481 GGRYS-GTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEE-----NPPGATLDEM 548
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
14-560 |
0e+00 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 702.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQStQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK08978 2 NGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDG-GVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK08978 81 GLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 VQAATIELETLPEPgeRAPAPAFAPESVREAAAMINAAKRPVLYLGGGV--INAPQPIRDLAEKANLPTTMTLMALGMLP 251
Cdd:PRK08978 161 IQLAEGELEPHLTT--VENEPAFPAAELEQARALLAQAKKPVLYVGGGVgmAGAVPALREFLAATGMPAVATLKGLGAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 252 KAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDVAEVL 331
Cdd:PRK08978 239 ADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLNALL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 332 AQLTPQIEAQPrdeWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRPRQWL 411
Cdd:PRK08978 319 PALQQPLNIDA---WRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 412 TSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFyqqgvFA 491
Cdd:PRK08978 396 TSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQLF-----FD 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 895912174 492 ATYPGMI-----NFMQIAAGFGL--QTCDLNNEADpqAALQAIIDRPGPALIHVRIDAQQKVYPMVPPGAANTEMV 560
Cdd:PRK08978 471 ERYSETDlsdnpDFVMLASAFGIpgQTITRKDQVE--AALDTLLNSEGPYLLHVSIDELENVWPLVPPGASNSEML 544
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
14-562 |
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: 651.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:TIGR00118 2 SGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:TIGR00118 82 GIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 VQAATIELEtLPE----PGERaPAPAFAPESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLMAL 247
Cdd:TIGR00118 162 VTTAEIEYP-YPEkvnlPGYR-PTVKGHPLQIKKAAELINLAKKPVILVGGGVIiaGASEELKELAERIQIPVTTTLMGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 248 GMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDV 327
Cdd:TIGR00118 240 GSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 328 AEVLAQLTPQI--EAQPRD-EWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPL 404
Cdd:TIGR00118 320 RNVLEELLKKLfeLKERKEsAWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQFYPF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 405 NRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLF 484
Cdd:TIGR00118 400 RKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQWQELF 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 895912174 485 YQQGvFAATYPGMI-NFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKVYPMVPPGAANTEMVGE 562
Cdd:TIGR00118 480 YEER-YSHTHMGSLpDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVAPGGGLDEMIGE 557
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
11-560 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 615.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 11 MRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATN 90
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 91 LITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDI 170
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 171 PKDVQAA--------TIELETLpepgerAPAPAFAPESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPT 240
Cdd:PRK08527 161 PKDVTATlgefeypkEISLKTY------KPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAIlsNASEEIRELVKKTGIPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 241 TMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPH 320
Cdd:PRK08527 235 VETLMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNAD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 321 VAIQGDVAEVLAQLTPQIEA---QPRDEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMW 397
Cdd:PRK08527 315 YPIVGDLKNVLKEMLEELKEenpTTYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 398 TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLV 477
Cdd:PRK08527 395 VAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 478 HQQQSLFYQQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKVYPMVPPGAANT 557
Cdd:PRK08527 475 RQWQTFFYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLPMVPAGGALY 554
|
...
gi 895912174 558 EMV 560
Cdd:PRK08527 555 NMI 557
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
3-561 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 615.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 3 SSGTTSNTMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQ---IRHILARHEQGAGFIAQGMARTEGKPAV 79
Cdd:PRK07418 9 GDSTTVTPQRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAegwLKHILVRHEQGAAHAADGYARATGKVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 80 CMACSGPGATNLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQ 159
Cdd:PRK07418 89 CFGTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIAS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 160 SGRPGPVWIDIPKDVqaATIELETLP-EPGERAPaPAF------APESVREAAAMINAAKRPVLYLGGGVI--NAPQPIR 230
Cdd:PRK07418 169 SGRPGPVLIDIPKDV--GQEEFDYVPvEPGSVKP-PGYrptvkgNPRQINAALKLIEEAERPLLYVGGGAIsaGAHAELK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 231 DLAEKANLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDR 310
Cdd:PRK07418 246 ELAERFQIPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 311 SELGKIKQPHVAIQGDVAEVLAQLTPQIE---AQPR-DEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDeAI 386
Cdd:PRK07418 326 AEVGKNRRPDVPIVGDVRKVLVKLLERSLeptTPPRtQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAPD-AY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 387 ITTDVGQHQMWTAQaYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKI 466
Cdd:PRK07418 405 YTTDVGQHQMWAAQ-FLRNGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKT 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 467 ILLNNEALGLVHQQQSLFYQQGVFAATY-PGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQK 545
Cdd:PRK07418 484 VIINNGWQGMVRQWQESFYGERYSASNMePGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRRDEN 563
|
570
....*....|....*.
gi 895912174 546 VYPMVPPGAANTEMVG 561
Cdd:PRK07418 564 CYPMVPPGKSNAQMVG 579
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
2-558 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 611.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 2 ASSGTTSNTMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCM 81
Cdd:PRK07789 20 AARPRIVAPERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 82 ACSGPGATNLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSG 161
Cdd:PRK07789 100 ATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 162 RPGPVWIDIPKDVQAATIELETLPE---PGERaPAPAFAPESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKA 236
Cdd:PRK07789 180 RPGPVLVDIPKDALQAQTTFSWPPRmdlPGYR-PVTKPHGKQIREAAKLIAAARRPVLYVGGGVIraEASAELRELAELT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 237 NLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKI 316
Cdd:PRK07789 259 GIPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 317 KQPHVAIQGDVAEVLAQLTPQIEAQPR-------DEWRQLVADLQREFPCAIQQESD-PLSHYGLINAVAACVDDEAIIT 388
Cdd:PRK07789 339 RHADVPIVGDVKEVIAELIAALRAEHAaggkpdlTAWWAYLDGWRETYPLGYDEPSDgSLAPQYVIERLGEIAGPDAIYV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 389 TDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIIL 468
Cdd:PRK07789 419 AGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVAL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 469 LNNEALGLVHQQQSLFYQQ---GVFAATYPGMI-NFMQIAAGFGLQTCDLNNEADPQAALQ---AIIDRPGPALIHVRID 541
Cdd:PRK07789 499 INNGNLGMVRQWQTLFYEErysNTDLHTHSHRIpDFVKLAEAYGCVGLRCEREEDVDAVIEkarAINDRPVVIDFVVGKD 578
|
570
....*....|....*..
gi 895912174 542 AQqkVYPMVPPGAANTE 558
Cdd:PRK07789 579 AM--VWPMVAAGTSNDE 593
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
6-562 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 602.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 6 TTSNTMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQStQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSG 85
Cdd:PRK06048 1 MTGSTEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDS-DLRHILVRHEQAAAHAADGYARATGKVGVCVATSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 86 PGATNLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGP 165
Cdd:PRK06048 80 PGATNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 166 VWIDIPKDVQAATIELEtLPEPGE-RAPAPAFA--PESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPT 240
Cdd:PRK06048 160 VLIDLPKDVTTAEIDFD-YPDKVElRGYKPTYKgnPQQIKRAAELIMKAERPIIYAGGGVIssNASEELVELAETIPAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 241 TMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPH 320
Cdd:PRK06048 239 TTTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 321 VAIQGDVAEVLAQLTPQIEAQPRDEWRQLVADLQREFPCAIQQESDPLSHYGLINAVA-ACVDdeAIITTDVGQHQMWTA 399
Cdd:PRK06048 319 VPIVGDAKQVLKSLIKYVQYCDRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYeLCPD--AIIVTEVGQHQMWAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 400 QAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQ 479
Cdd:PRK06048 397 QYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 480 QQSLFYQQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKVYPMVPPGAANTEM 559
Cdd:PRK06048 477 WQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSPMVPAGAAINEI 556
|
...
gi 895912174 560 VGE 562
Cdd:PRK06048 557 LDL 559
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
7-561 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 588.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 7 TSNTMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDAL---SQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMAC 83
Cdd:CHL00099 4 QLTLREKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 84 SGPGATNLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRP 163
Cdd:CHL00099 84 SGPGATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 164 GPVWIDIPKDVQAATIELETlPEPGERA-PAPAFAPES------VREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAE 234
Cdd:CHL00099 164 GPVLIDIPKDVGLEKFDYYP-PEPGNTIiKILGCRPIYkptikrIEQAAKLILQSSQPLLYVGGGAIisDAHQEITELAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 235 KANLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELG 314
Cdd:CHL00099 243 LYKIPVTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 315 KIKQPHVAIQGDVAEVLAQL-------TPQIEAQPRDEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDeAII 387
Cdd:CHL00099 323 KNRIPQVAIVGDVKKVLQELlellknsPNLLESEQTQAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQLAPD-AYF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 388 TTDVGQHQMWTAQaYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKII 467
Cdd:CHL00099 402 TTDVGQHQMWAAQ-FLKCKPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 468 LLNNEALGLVHQQQSLFYQQGvFAATY--PGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQK 545
Cdd:CHL00099 481 IINNKWQGMVRQWQQAFYGER-YSHSNmeEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDEN 559
|
570
....*....|....*.
gi 895912174 546 VYPMVPPGAANTEMVG 561
Cdd:CHL00099 560 CYPMVAPGKSNSQMIG 575
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
1-560 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 573.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 1 MASSGTTSNTMrfTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVC 80
Cdd:PRK09107 1 SAQKSHMPRQM--TGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 81 MACSGPGATNLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQS 160
Cdd:PRK09107 79 LVTSGPGATNAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 161 GRPGPVWIDIPKDVQAATielETLPEPGERAPAPAFAP------ESVREAAAMINAAKRPVLYLGGGVIN----APQPIR 230
Cdd:PRK09107 159 GRPGPVVVDIPKDVQFAT---GTYTPPQKAPVHVSYQPkvkgdaEAITEAVELLANAKRPVIYSGGGVINsgpeASRLLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 231 DLAEKANLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDR 310
Cdd:PRK09107 236 ELVELTGFPITSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 311 SELGKIKQPHVAIQGDVAEVLAQLTPQIEAQPR-------DEWRQLVADLQREFPCAIQQESDP-LSHYGLINAVAACVD 382
Cdd:PRK09107 316 SSINKNVRVDVPIIGDVGHVLEDMLRLWKARGKkpdkealADWWGQIARWRARNSLAYTPSDDViMPQYAIQRLYELTKG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 383 DEAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQL 462
Cdd:PRK09107 396 RDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 463 DVKIILLNNEALGLVHQQQSLFYQQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDA 542
Cdd:PRK09107 476 PVKIFILNNQYMGMVRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVAN 555
|
570
....*....|....*...
gi 895912174 543 QQKVYPMVPPGAANTEMV 560
Cdd:PRK09107 556 LENCFPMIPSGKAHNEML 573
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
14-560 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 562.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTqIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK06725 16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 VQAATIELETLPEPGERAPAPAFAPES--VREAAAMINAAKRPVLYLGGGVIN--APQPIRDLAEKANLPTTMTLMALGM 249
Cdd:PRK06725 175 VQNEKVTSFYNEVVEIPGYKPEPRPDSmkLREVAKAISKAKRPLLYIGGGVIHsgGSEELIEFARENRIPVVSTLMGLGA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 250 LPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDVAE 329
Cdd:PRK06725 255 YPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVGDVKK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 330 VLAQLTPQIEAQPRDEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRPRQ 409
Cdd:PRK06725 335 ALHMLLHMSIHTQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 410 WLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFYQQGv 489
Cdd:PRK06725 415 FLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEMFYENR- 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 895912174 490 FAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKVYPMVPPGAANTEMV 560
Cdd:PRK06725 494 LSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFPMVPPNKGNNEMI 564
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
15-562 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 559.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 15 GAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLITA 94
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 175 QA--ATIELET---LPEPGERAPAPAfAPESVREAAAMINAAKRPVLYLGGGVINAPQPIRDLAEKANLPTTMTLMALGM 249
Cdd:PLN02470 175 QQqlAVPNWNQpmkLPGYLSRLPKPP-EKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGLGA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 250 LPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDVAE 329
Cdd:PLN02470 254 FPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADVKL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 330 VLAQLTPQIEAQPRD-----EWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPL 404
Cdd:PLN02470 334 ALQGLNKLLEERKAKrpdfsAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 405 NRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLF 484
Cdd:PLN02470 414 KEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQWEDRF 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 485 YqQGVFAATYPG--------MINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKVYPMVPPGAAN 556
Cdd:PLN02470 494 Y-KANRAHTYLGdpdaeaeiFPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLPMIPGGGTF 572
|
....*.
gi 895912174 557 TEMVGE 562
Cdd:PLN02470 573 KDIITE 578
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
1-561 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 547.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 1 MASSGTTSNTMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQStQIRHILARHEQGAGFIAQGMARTEGKPAVC 80
Cdd:PRK07710 4 MRTMSSKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDC-GIPHILTRHEQGAIHAAEGYARISGKPGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 81 MACSGPGATNLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQS 160
Cdd:PRK07710 83 IATSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 161 GRPGPVWIDIPKDVQAATIELETLPE---PGERapaPAFAPE--SVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLA 233
Cdd:PRK07710 163 GRPGPVLIDIPKDMVVEEGEFCYDVQmdlPGYQ---PNYEPNllQIRKLVQAVSVAKKPVILAGAGVLhaKASKELTSYA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 234 EKANLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSEL 313
Cdd:PRK07710 240 EQQEIPVVHTLLGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 314 GKIKQPHVAIQGDVAEVLAQLTPQIEAQPR-DEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVG 392
Cdd:PRK07710 320 GKNVPTEIPIVADAKQALQVLLQQEGKKENhHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 393 QHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNE 472
Cdd:PRK07710 400 QHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 473 ALGLVHQQQSLFYQQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKVYPMVPP 552
Cdd:PRK07710 480 ALGMVRQWQEEFYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMPMVAP 559
|
....*....
gi 895912174 553 GAANTEMVG 561
Cdd:PRK07710 560 GKGLHEMVG 568
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
14-562 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 547.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQStQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK06276 2 KGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDS-DLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK06276 81 GIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 VQAATIELETLPEPGErAPAPAFAPES------VREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLM 245
Cdd:PRK06276 161 VQEGELDLEKYPIPAK-IDLPGYKPTTfghplqIKKAAELIAEAERPVILAGGGVIisGASEELIELSELVKIPVCTTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 246 ALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQG 325
Cdd:PRK06276 240 GKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 326 DVAEVLAQLTPQIEA---QPRDEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDD-----EAIITTDVGQHQMW 397
Cdd:PRK06276 320 DAKNVLRDLLAELMKkeiKNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQMW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 398 TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLV 477
Cdd:PRK06276 400 MAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 478 HQQQSLFYQQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKVyPMVPPGAANT 557
Cdd:PRK06276 480 YQWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAL-PMVPPGGNLT 558
|
....*
gi 895912174 558 EMVGE 562
Cdd:PRK06276 559 NILGP 563
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
14-559 |
6.29e-178 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 514.29 E-value: 6.29e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK06466 5 SGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK06466 85 GIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPKD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 VQAATIELE-TLPEPGE-RAPAPAFAPES--VREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLMAL 247
Cdd:PRK06466 165 MTNPAEKFEyEYPKKVKlRSYSPAVRGHSgqIRKAVEMLLAAKRPVIYSGGGVVlgNASALLTELAHLLNLPVTNTLMGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 248 GMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDV 327
Cdd:PRK06466 245 GGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPIVGPV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 328 AEVLAQL---------TPQIEAQPR-----DEWRQLVADLQREFPcaiqqESDPLSHYGLINAVAACVDDEAIITTDVGQ 393
Cdd:PRK06466 325 ESVLTEMlailkeigeKPDKEALAAwwkqiDEWRGRHGLFPYDKG-----DGGIIKPQQVVETLYEVTNGDAYVTSDVGQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 394 HQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEA 473
Cdd:PRK06466 400 HQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 474 LGLVHQQQSLFYqQGVFAATY-PGMINFMQIAAGFGLQTCDLNNEADPQAALQ---AIIDRpgPALIHVRIDAQQKVYPM 549
Cdd:PRK06466 480 LGMVRQWQDMQY-EGRHSHSYmESLPDFVKLAEAYGHVGIRITDLKDLKPKLEeafAMKDR--LVFIDIYVDRSEHVYPM 556
|
570
....*....|
gi 895912174 550 VPPGAANTEM 559
Cdd:PRK06466 557 QIADGSMRDM 566
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
14-561 |
2.20e-175 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 507.44 E-value: 2.20e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 VQaaTIELETLPEPGERAPA--PAFAP--ESVREAAAMINAAKRPVLYLGGGV--INAPQPIRDLAEKANLPTTMTLMAL 247
Cdd:PRK07282 171 VS--ALETDFIYDPEVNLPSyqPTLEPndMQIKKILKQLSKAKKPVILAGGGInyAEAATELNAFAERYQIPVVTTLLGQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 248 GMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDV 327
Cdd:PRK07282 249 GTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 328 AEVLAQL--TPQIEAQPRDeWRQLVADLQREFPCAIQQESDpLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLN 405
Cdd:PRK07282 329 KKALQMLlaEPTVHNNTEK-WIEKVTKDKNRVRSYDKKERV-VQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 406 RPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFY 485
Cdd:PRK07282 407 NERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESFY 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 895912174 486 QQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQaIIDRPGPALIHVRIDAQQKVYPMVPPGAANTEMVG 561
Cdd:PRK07282 487 EGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLE-VITEDVPMLIEVDISRKEHVLPMVPAGKSNHEMLG 561
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
14-559 |
2.39e-171 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 497.42 E-value: 2.39e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK08979 5 SGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK08979 85 GIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 VQAATIELE-TLPEP-GERAPAPAFAPE--SVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLMAL 247
Cdd:PRK08979 165 CLNPAILHPyEYPESiKMRSYNPTTSGHkgQIKRGLQALLAAKKPVLYVGGGAIisGADKQILQLAEKLNLPVVSTLMGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 248 GMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDV 327
Cdd:PRK08979 245 GAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPIVGSA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 328 AEVLAQLTPQIEAQPR-------DEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQ 400
Cdd:PRK08979 325 DKVLDSMLALLDESGEtndeaaiASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQMFAAL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 401 AYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQ 480
Cdd:PRK08979 405 YYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMVKQW 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 481 QSLFYqQGVFAATYPGMI-NFMQIAAGFGLQTCDLNNEADPQAALQ---AIIDRpgPALIHVRIDAQQKVYPMVPPGAAN 556
Cdd:PRK08979 485 QDMIY-QGRHSHSYMDSVpDFAKIAEAYGHVGIRISDPDELESGLEkalAMKDR--LVFVDINVDETEHVYPMQIRGGAM 561
|
...
gi 895912174 557 TEM 559
Cdd:PRK08979 562 NEM 564
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
3-560 |
5.83e-161 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 471.59 E-value: 5.83e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 3 SSGTTSNTMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMA 82
Cdd:PRK06965 11 AESLSPPAADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 83 CSGPGATNLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGR 162
Cdd:PRK06965 91 TSGPGVTNAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 163 PGPVWIDIPKDVQAATIELEtLPEPGE-RAPAPAFAPES--VREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKAN 237
Cdd:PRK06965 171 PGPVVVDIPKDVSKTPCEYE-YPKSVEmRSYNPVTKGHSgqIRKAVSLLLSAKRPYIYTGGGVIlaNASRELRQLADLLG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 238 LPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNA-KIIHVDIDRSELGKI 316
Cdd:PRK06965 250 YPVTNTLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 317 KQPHVAIQGDVAEVLAQLTPQI-EAQPRDE------WRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITT 389
Cdd:PRK06965 330 VKVDIPIVGDVKEVLKELIEQLqTAEHGPDadalaqWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 390 DVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILL 469
Cdd:PRK06965 410 DVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 470 NNEALGLVHQQQSLFYqQGVFAATY-PGMINFMQIAAGFGLQTCDLNNEADPQAALQAII---DRpgPALIHVRIDAQQK 545
Cdd:PRK06965 490 NNRYLGMVRQWQEIEY-SKRYSHSYmDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALrlkDR--TVFLDFQTDPTEN 566
|
570
....*....|....*
gi 895912174 546 VYPMVPPGAANTEMV 560
Cdd:PRK06965 567 VWPMVQAGKGITEML 581
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
12-560 |
1.70e-155 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 457.07 E-value: 1.70e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 12 RFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNL 91
Cdd:PRK06882 3 KLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 92 ITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIP 171
Cdd:PRK06882 83 ITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 172 KDV--QAATIELETLPEPGERAPAPAFAPE--SVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLM 245
Cdd:PRK06882 163 KDMvnPANKFTYEYPEEVSLRSYNPTVQGHkgQIKKALKALLVAKKPVLFVGGGVItaECSEQLTQFAQKLNLPVTSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 246 ALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQG 325
Cdd:PRK06882 243 GLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 326 DVAEVLAQLTPQIEAQ-------PRDEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWT 398
Cdd:PRK06882 323 SAKNVLEEFLSLLEEEnlaksqtDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQMFA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 399 AQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVH 478
Cdd:PRK06882 403 ALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGMVK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 479 QQQSLFYqQGVFAATYPGMI-NFMQIAAGFGLQTCDLNNEADPQAAL-QAIIDRPGPALIHVRIDAQQKVYPMVPPGAAN 556
Cdd:PRK06882 483 QWQDLIY-SGRHSQVYMNSLpDFAKLAEAYGHVGIQIDTPDELEEKLtQAFSIKDKLVFVDVNVDETEHVYPMQIRGGAM 561
|
....
gi 895912174 557 TEMV 560
Cdd:PRK06882 562 NEMI 565
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
13-559 |
4.79e-152 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 448.15 E-value: 4.79e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 13 FTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLI 92
Cdd:PRK07979 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 93 TAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPK 172
Cdd:PRK07979 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 173 DVQAATIELETL-PEP-GERAPAPAFAPE--SVREAAAMINAAKRPVLYLGGGVINAP--QPIRDLAEKANLPTTMTLMA 246
Cdd:PRK07979 164 DILNPANKLPYVwPESvSMRSYNPTTQGHkgQIKRALQTLVAAKKPVVYVGGGAINAAchQQLKELVEKLNLPVVSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 247 LGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGD 326
Cdd:PRK07979 244 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 327 VAEVLAQ---LTPQIEAQP-----RDEWRQLvaDLQREFPC-AIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMW 397
Cdd:PRK07979 324 ARQVLEQmleLLSQESAHQpldeiRDWWQQI--EQWRARQClKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 398 TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLV 477
Cdd:PRK07979 402 AALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 478 HQQQSLFYqQGVFAATY-PGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGP---ALIHVRIDAQQKVYPMVPPG 553
Cdd:PRK07979 482 KQWQDMIY-SGRHSQSYmQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNnrlVFVDVTVDGSEHVYPMQIRG 560
|
....*.
gi 895912174 554 AANTEM 559
Cdd:PRK07979 561 GGMDEM 566
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
14-560 |
1.32e-130 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 393.05 E-value: 1.32e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDAL---SQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATN 90
Cdd:PRK06456 3 TGARILVDSLKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 91 LITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDI 170
Cdd:PRK06456 83 LVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 171 PKDVQAATIELETLPE----PGERAPAPAFAPESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTL 244
Cdd:PRK06456 163 PRDIFYEKMEEIKWPEkplvKGYRDFPTRIDRLALKKAAEILINAERPIILVGTGVVwsNATPEVLELAELLHIPIVSTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 245 MALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTEQFCPN-AKIIHVDIDRSELGKIKQPHVAI 323
Cdd:PRK06456 243 PGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 324 QGDVAEVLAQLTPQI----EAQPRDEWRQLVADLQREFPCAIQQESDP-LSHYGLINAVAACVDDEAIITTDVGQHQMWT 398
Cdd:PRK06456 323 YGNAKIILRELIKAItelgQKRDRSAWLKRVKEYKEYYSQFYYTEENGkLKPWKIMKTIRQALPRDAIVTTGVGQHQMWA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 399 AQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVH 478
Cdd:PRK06456 403 EVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLVR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 479 QQQSLFYQQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKVYPMVPPGAANTE 558
Cdd:PRK06456 483 QVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALPTLPPGGRLKQ 562
|
..
gi 895912174 559 MV 560
Cdd:PRK06456 563 VI 564
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
14-541 |
3.50e-114 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 349.90 E-value: 3.50e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTqIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK08322 2 KAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSS-IKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK08322 81 GVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 VQAATIELETLPEPGERAPAPAfaPESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLMALGMLP 251
Cdd:PRK08322 161 IAAEETDGKPLPRSYSRRPYAS--PKAIERAAEAIQAAKNPLILIGAGANrkTASKALTEFVDKTGIPFFTTQMGKGVIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 252 KAHPLSLGMLGMHGARSTNFILQEADLLIVLGarFDdrAIGKTEQF-CPNA--KIIHVDIDRSELGKIKQPHVAIQGDVA 328
Cdd:PRK08322 239 ETHPLSLGTAGLSQGDYVHCAIEHADLIINVG--HD--VIEKPPFFmNPNGdkKVIHINFLPAEVDPVYFPQVEVVGDIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 329 EVLAQLTPQIEAQPRDEW---RQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLN 405
Cdd:PRK08322 315 NSLWQLKERLADQPHWDFprfLKIREAIEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIWFARNYRAY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 406 RPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVH--QQQSL 483
Cdd:PRK08322 395 EPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRwkQENMG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 895912174 484 FYQQGVfaaTYpGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRID 541
Cdd:PRK08322 475 FEDFGL---DF-GNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVD 528
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
11-484 |
1.49e-109 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 339.65 E-value: 1.49e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 11 MRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTE-GKPAVCMACSGPGAT 89
Cdd:PRK11269 2 AKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 90 NLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWID 169
Cdd:PRK11269 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 170 IPKDVQAATIELetlpEPGERAPAPAFAPES----VREAAAMINAAKRPVLYLGGGVIN--APQPIRDLAEKANLPTTMT 243
Cdd:PRK11269 162 LPFDVQVAEIEF----DPDTYEPLPVYKPAAtraqIEKALEMLNAAERPLIVAGGGVINadASDLLVEFAELTGVPVIPT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 244 LMALGMLPKAHPLSLGMLGMHGA-RSTNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVA 322
Cdd:PRK11269 238 LMGWGAIPDDHPLMAGMVGLQTShRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 323 IQGDVA-------EVLAQLTPQIEAQPRDEWRQLVADLQRefpcAIQQESD-------PLSHYGLINAVaacVDDEAIIT 388
Cdd:PRK11269 318 IVSDAKaalellvEVAREWKAAGRLPDRSAWVADCQERKR----TLLRKTHfdnvpikPQRVYEEMNKA---FGRDTCYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 389 TDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIIL 468
Cdd:PRK11269 391 STIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVL 470
|
490
....*....|....*.
gi 895912174 469 LNNEALGLVHQQQSLF 484
Cdd:PRK11269 471 VNNAYLGLIRQAQRAF 486
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
6-544 |
3.16e-108 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 334.92 E-value: 3.16e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 6 TTSNTMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSG 85
Cdd:PRK08199 1 MTSTPRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 86 PGATNLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGP 165
Cdd:PRK08199 81 PGATNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 166 VWIDIPKDVQAATIELETLPEPgeRAPAPAFAPESVREAAAMINAAKRPVLYLGGGVIN--APQPIRDLAEKANLPTTMT 243
Cdd:PRK08199 161 VVLALPEDVLSETAEVPDAPPY--RRVAAAPGAADLARLAELLARAERPLVILGGSGWTeaAVADLRAFAERWGLPVACA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 244 LMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAigkTEQF------CPNAKIIHVDIDRSELGKIK 317
Cdd:PRK08199 239 FRRQDLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVT---TQGYtlldipVPRQTLVHVHPDAEELGRVY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 318 QPHVAIQGDVAEVLAQLTpQIEAQPRDEWRQLVADLQREFpcaiQQESDPLSHYGLIN--AVAACVDD----EAIITTDV 391
Cdd:PRK08199 316 RPDLAIVADPAAFAAALA-ALEPPASPAWAEWTAAAHADY----LAWSAPLPGPGAVQlgEVMAWLRErlpaDAIITNGA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 392 GQHQMWTAQAYPLNRPRQWL--TSgglGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILL 469
Cdd:PRK08199 391 GNYATWLHRFFRFRRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 470 NNEALGLV--HQQQSlfyqqgvfaatYPGMIN--------FMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVR 539
Cdd:PRK08199 468 NNGMYGTIrmHQERE-----------YPGRVSgtdltnpdFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIR 536
|
....*
gi 895912174 540 IDAQQ 544
Cdd:PRK08199 537 IDPEA 541
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
11-540 |
1.16e-104 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 325.43 E-value: 1.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 11 MRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQST-QIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGAT 89
Cdd:PRK08266 2 TTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 90 NLITAIADARLDSIPLVCITGQVPASMIGTDAFQ--EV-DTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPV 166
Cdd:PRK08266 82 NAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 167 WIDIPKDVQAATIELETLPePGERAPAPAFAPESVREAAAMINAAKRPVLYLGGGVINAPQPIRDLAEKANLPTTMTLMA 246
Cdd:PRK08266 162 ALEMPWDVFGQRAPVAAAP-PLRPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 247 LGMLPKAHPLSLGMLGmhgARStnfILQEADLLIVLGARFDD---RAIGKTEqfcpNAKIIHVDIDRSELGKIKqPHVAI 323
Cdd:PRK08266 241 RGIVSDRHPLGLNFAA---AYE---LWPQTDVVIGIGSRLELptfRWPWRPD----GLKVIRIDIDPTEMRRLK-PDVAI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 324 QGDVAEVLAQLTPQIEAQP------RDEWRQLVADLQREFpcaiqQESDPLSHYglINAVAACVDDEAIITTDVGQHQMW 397
Cdd:PRK08266 310 VADAKAGTAALLDALSKAGskrpsrRAELRELKAAARQRI-----QAVQPQASY--LRAIREALPDDGIFVDELSQVGFA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 398 TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLV 477
Cdd:PRK08266 383 SWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNV 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 895912174 478 HQQQSLFYQQGVFAA--TYPgmiNFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRI 540
Cdd:PRK08266 463 RRDQKRRFGGRVVASdlVNP---DFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPV 524
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
14-546 |
3.35e-104 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 323.85 E-value: 3.35e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTqIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK07524 3 TCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSG-IRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITG-QVPASM-IGTDAFQEV-DTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDI 170
Cdd:PRK07524 82 AMGQAYADSIPMLVISSvNRRASLgKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 171 PKDVQAATIElETLPEPGERAPAPAFAPESVREAAAMINAAKRPVLYLGGGVINAPQPIRDLAEKANLPTTMTLMALGML 250
Cdd:PRK07524 162 PLDVLAAPAD-HLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVALTINAKGLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 251 PKAHPLSLGmlGMHGARSTNFILQEADLLIVLGARF--DDRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDVA 328
Cdd:PRK07524 241 PAGHPLLLG--ASQSLPAVRALIAEADVVLAVGTELgeTDYDVYFDGGFPLPGELIRIDIDPDQLARNYPPALALVGDAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 329 EVLAQLTPQIEAQPRDE-WRQLVADLQREfpcAIQQESDPL--SHYGLINAVAACVDDeAIITTDVGQHQMWTAQAYPLN 405
Cdd:PRK07524 319 AALEALLARLPGQAAAAdWGAARVAALRQ---ALRAEWDPLtaAQVALLDTILAALPD-AIFVGDSTQPVYAGNLYFDAD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 406 RPRQWLTSG-GLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLV--HQQQS 482
Cdd:PRK07524 395 APRRWFNAStGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIrrYMVAR 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 895912174 483 LFYQQGVFAATyPgmiNFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKV 546
Cdd:PRK07524 475 DIEPVGVDPYT-P---DFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQACWFAA 534
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
368-553 |
4.52e-98 |
|
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: 295.56 E-value: 4.52e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 368 LSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSL 447
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 448 MMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFYQQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAI 527
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|....*.
gi 895912174 528 IDRPGPALIHVRIDAQQKVYPMVPPG 553
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLPMVPPG 186
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
14-541 |
4.48e-97 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 306.01 E-value: 4.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTqIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK08617 6 YGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSG-PELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 V-----QAATIELETLPEPGeraPAPafaPESVREAAAMINAAKRPVLYLGggvINAPQP-----IRDLAEKANLPTTMT 243
Cdd:PRK08617 165 VvdapvTSKAIAPLSKPKLG---PAS---PEDINYLAELIKNAKLPVLLLG---MRASSPevtaaIRRLLERTNLPVVET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 244 LMALGMLPKAH-PLSLGMLGMHGARSTNFILQEADLLIVLGarFD----DRAIGKTEqfcPNAKIIHVDIDRSELGKIKQ 318
Cdd:PRK08617 236 FQAAGVISRELeDHFFGRVGLFRNQPGDELLKKADLVITIG--YDpieyEPRNWNSE---GDATIIHIDVLPAEIDNYYQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 319 PHVAIQGDVAEVLAQLTPQI-EAQPRDEWRQLVADLQR------EFPCAIQQE-SDPLShygLINAVAACVDDEAIITTD 390
Cdd:PRK08617 311 PERELIGDIAATLDLLAEKLdGLSLSPQSLEILEELRAqleelaERPARLEEGaVHPLR---IIRALQDIVTDDTTVTVD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 391 VGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLN 470
Cdd:PRK08617 388 VGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWN 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 895912174 471 NEALGLVHQQQSLFYQQGvfAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRID 541
Cdd:PRK08617 468 DGHYNMVEFQEEMKYGRS--SGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVD 536
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
15-541 |
1.43e-95 |
|
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: 301.67 E-value: 1.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 15 GAQLVVHLLERQGITMVSGIPGGSILPIYDALsQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLITA 94
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDAL-EDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 175 QAATIELETLpePGERAPAPAFAPE-SVREAAAMINAAKRPVLYLG--GGVINAPQPIRDLAEKANLPTTMTLMALGMLP 251
Cdd:TIGR02418 160 VDSPVSVKAI--PASYAPKLGAAPDdAIDEVAEAIQNAKLPVLLLGlrASSPETTEAVRRLLKKTQLPVVETFQGAGAVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 252 KA-HPLSLGMLGMHGARSTNFILQEADLLIVLGarFD----DRAIGKTEQFCPnakIIHVDIDRSELGKIKQPHVAIQGD 326
Cdd:TIGR02418 238 RElEDHFFGRVGLFRNQPGDRLLKQADLVITIG--YDpieyEPRNWNSENDAT---IVHIDVEPAQIDNNYQPDLELVGD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 327 VAEVLAQLTPQIEA-----QPRDEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQA 401
Cdd:TIGR02418 313 IASTLDLLAERIPGyelppDALAILEDLKQQREALDRVPATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 402 YPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQ 481
Cdd:TIGR02418 393 FRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQE 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 482 SLFYQQGvfAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRID 541
Cdd:TIGR02418 473 EMKYQRS--SGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVD 530
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
14-542 |
6.56e-92 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 293.06 E-value: 6.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDAL-SQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLI 92
Cdd:PRK08611 5 KAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 93 TAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRpGPVWIDIPK 172
Cdd:PRK08611 85 NGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVLTIPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 173 DVQAATIELETL-PEPGERAPAPAFAPESVREAAAMINAAKRPVLYLGGGVINAPQPIRDLAEKANLPTTMTLMALGMLP 251
Cdd:PRK08611 164 DLPAQKIKDTTNkTVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPAKGIIP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 252 KAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRaigkteQFCPN-AKIIHVDIDRSELGKIKQPHVAIQGDVAEV 330
Cdd:PRK08611 244 DDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPKkAKAIQIDTDPANIGKRYPVNVGLVGDAKKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 331 LAQLTPQIEaqPRDEWRQLVADLQR------EFPCAIQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPL 404
Cdd:PRK08611 318 LHQLTENIK--HVEDRRFLEACQENmakwwkWMEEDENNASTPIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 405 NRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLV-HQQQSL 483
Cdd:PRK08611 396 GTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIkYEQQAA 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 895912174 484 FYQQGVFAATYPGMINFMQIAAGFGLQTCDlNNEADP--QAALQAiiDRpgPALIHVRIDA 542
Cdd:PRK08611 476 GELEYAIDLSDMDYAKFAEACGGKGYRVEK-AEELDPafEEALAQ--DK--PVIIDVYVDP 531
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
10-529 |
1.07e-88 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 284.97 E-value: 1.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 10 TMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDaLSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGAT 89
Cdd:PRK07525 3 KMKMTPSEAFVETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 90 NLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRpGPVWID 169
Cdd:PRK07525 82 NFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 170 IPKDVQAATIELEtLPEPgERAPAPAFAPESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLMAL 247
Cdd:PRK07525 161 IPRDYFYGVIDVE-IPQP-VRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVlsDAIEECKALAERLDAPVACGYLHN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 248 GMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDdrAIGKTEQ-----FCPNAKIIHVDIDRSELGKIKQPHVA 322
Cdd:PRK07525 239 DAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLN--PFGTLPQygidyWPKDAKIIQVDINPDRIGLTKKVSVG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 323 IQGDVAEV----LAQLTPQIE------------AQPRDEWRQLVADLQRE--------FPCAIQQESDPLSHYGLINAVA 378
Cdd:PRK07525 317 ICGDAKAVarelLARLAERLAgdagreerkaliAAEKSAWEQELSSWDHEdddpgtdwNEEARARKPDYMHPRQALREIQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 379 ACVDDEAIITTDVGQHQMwTAQAYP-LNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATA 457
Cdd:PRK07525 397 KALPEDAIVSTDIGNNCS-IANSYLrFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTA 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 895912174 458 AENQLDVKIILLNNEALGLVHQQQSLFYQQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIID 529
Cdd:PRK07525 476 VRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAID 547
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
14-551 |
3.41e-88 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 282.87 E-value: 3.41e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQStQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKS-KVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRpGPVWIDIPKD 173
Cdd:PRK06457 82 GLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 VQAATIELEtlPEPGERAPAPAFAPEsVREAAAMINAAKRPVLYLGGGVINAPQPIRDLAEKANLPTTMTLMALGMLPKA 253
Cdd:PRK06457 161 ILRKSSEYK--GSKNTEVGKVKYSID-FSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 254 HPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAigkteqFCP-NAKIIHVDIDRSELGKIKQPHVAIQGDVAEVla 332
Cdd:PRK06457 238 DPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVN------FLNkSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEF-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 333 qLTPQIEAQPRDEWRQLVADLQREFPCAIQQESD---PLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRPRQ 409
Cdd:PRK06457 310 -LNIDIEEKSDKFYEELKGKKEDWLDSISKQENSldkPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 410 WLTSGGLGTMGFGLPAAIGAALA-NPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVH-QQQSLFYQQ 487
Cdd:PRK06457 389 FIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKfEQEVMGYPE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 895912174 488 GVFAATYPgmiNFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKvyPMVP 551
Cdd:PRK06457 469 WGVDLYNP---DFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNER--PMPP 527
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
12-529 |
1.88e-87 |
|
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: 281.75 E-value: 1.88e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 12 RFTGAQLVVHLLERQGITMVSGIPGGSILPIYDaLSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNL 91
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMD-LFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 92 ITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRpGPVWIDIP 171
Cdd:TIGR03457 80 VTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 172 KDVQAATIELETL-PEPGERAPApafAPESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLMALG 248
Cdd:TIGR03457 159 RDYFYGEIDVEIPrPVRLDRGAG---GATSLAQAARLLAEAKFPVIISGGGVVmgDAVEECKALAERLGAPVVNSYLHND 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 249 MLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDdrAIGKTEQ-----FCPNAKIIHVDIDRSELGKIKQPHVAI 323
Cdd:TIGR03457 236 SFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLG--PFGTLPQygidyWPKNAKIIQVDANAKMIGLVKKVTVGI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 324 QGDVAEVLAQLTPQIEA---------------QPRDEWRQLVADLQRE--------FPCAIQQESDPLSHYGLINAVAAC 380
Cdd:TIGR03457 314 CGDAKAAAAEILQRLAGkagdanraerkakiqAERSAWEQELSEMTHErdpfsldmIVEQRQEEGNWLHPRQVLRELEKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 381 VDDEAIITTDVGQHQMwTAQAYP-LNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAE 459
Cdd:TIGR03457 394 MPEDAIVSTDIGNINS-VANSYLrFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVR 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 460 NQLDVKIILLNNEALGLVHQQQSLFYQQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIID 529
Cdd:TIGR03457 473 HDIPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIA 542
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
19-540 |
7.33e-78 |
|
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: 256.30 E-value: 7.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 19 VVHLLERQGITMVSGIPGGSILPIYDALS-QSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLITAIAD 97
Cdd:TIGR02720 5 VLKVLEAWGVDHIYGIPGGSFNSTMDALSaERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 98 ARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSgRPGPVWIDIPKDVQAA 177
Cdd:TIGR02720 85 AKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYA-HNGVAVVTIPVDFGWQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 178 TIELETLPEPG--ERAP-APAFAPESVREAAAMINAAKRPVLYLGGGVINAPQPIRDLAEKANLPTTMTLMALGMLPKAH 254
Cdd:TIGR02720 164 EIPDNDYYASSvsYQTPlLPAPDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGIIEDRY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 255 PLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTeqFCPNAKIIHVDIDRSELGKIKQPHVAIQGDVAEVLAQL 334
Cdd:TIGR02720 244 PAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKA--FKNTKYFIQIDIDPAKLGKRHHTDIAVLADAKKALAAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 335 TPQIEaqPRDE---WRQLVADLQ--REFPCAIQQES-DPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRPR 408
Cdd:TIGR02720 322 LAQVE--PREStpwWQANVANVKnwRAYLASLEDKTeGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 409 QWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFYQQg 488
Cdd:TIGR02720 400 KWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQP- 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 895912174 489 VFAATYPGmINFMQIAAGFGLQTCDLNNEAD-PQAALQAIIDRPG-PALIHVRI 540
Cdd:TIGR02720 479 LIGVDFND-ADFAKIAEGVGAVGFRVNKIEQlPAVFEQAKAIKQGkPVLIDAKI 531
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
11-541 |
3.60e-76 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 251.83 E-value: 3.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 11 MRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATN 90
Cdd:PRK06546 1 MAKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 91 LITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAqSGRPGPVWIDI 170
Cdd:PRK06546 81 LINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHA-VAGGGVSVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 171 PKDV---QAATIELETLPEPGERAPAPafAPESVREAAAMINAAKRPVLYLGGGVINAPQPIRDLAEKANLPTTMTLMAL 247
Cdd:PRK06546 160 PGDIadePAPEGFAPSVISPRRPTVVP--DPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 248 GMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFddraigKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDV 327
Cdd:PRK06546 238 EWIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDF------PYDQFLPDVRTAQVDIDPEHLGRRTRVDLAVHGDV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 328 AEVLAQLTPQIEaqPRDEWR---QLVADLQREFPCAIQQESDPLSHYGLINA--VAACVD----DEAIITTDVGQHQMWT 398
Cdd:PRK06546 312 AETIRALLPLVK--EKTDRRfldRMLKKHARKLEKVVGAYTRKVEKHTPIHPeyVASILDelaaDDAVFTVDTGMCNVWA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 399 AQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVH 478
Cdd:PRK06546 390 ARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVK 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 895912174 479 QQQSLfyqQGV--FAATYPgMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRID 541
Cdd:PRK06546 470 LEMLV---DGLpdFGTDHP-PVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTD 530
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
11-542 |
4.70e-76 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 250.68 E-value: 4.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 11 MRFTGAQLVVHLLERQGITMVSGIPggSI--LPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGA 88
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVI--SIhnMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 89 TNLITAIADARLDSIPLVCITGQVPASMIGTDA--FQEV-DTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGP 165
Cdd:PRK07064 79 GNAAGALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 166 VWIDIPKDVQAATIELETLPEPgERAPAPAFAPESVREAAAMINAAKRPVLYLGGGVINAPQPIRDLAEkANLPTTMTLM 245
Cdd:PRK07064 159 VSVEIPIDIQAAEIELPDDLAP-VHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVD-LGFGVVTSTQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 246 ALGMLPKAHPLSLGMLGMHGARSTnfILQEADLLIVLGARFDDRAIGKTEQFCPnAKIIHVDIDRSELGKIKQPHVAIQG 325
Cdd:PRK07064 237 GRGVVPEDHPASLGAFNNSAAVEA--LYKTCDLLLVVGSRLRGNETLKYSLALP-RPLIRVDADAAADGRGYPNDLFVHG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 326 DVAEVLAQLTPQIEAQPR--DEWrqlVADLQREFPCAIQQESDPLSHYGLIN-AVAACVDDEAIITTDVG-QHQMWTAQA 401
Cdd:PRK07064 314 DAARVLARLADRLEGRLSvdPAF---AADLRAAREAAVADLRKGLGPYAKLVdALRAALPRDGNWVRDVTiSNSTWGNRL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 402 YPLNRPRQWLTSGGlGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQ 481
Cdd:PRK07064 391 LPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNIQ 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 895912174 482 SLFY---QQGVFAATyPgmiNFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDA 542
Cdd:PRK07064 470 DAQYggrRYYVELHT-P---DFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVDMLS 529
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-548 |
5.36e-68 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 230.42 E-value: 5.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 1 MASSGTTSNTmrfTGAQLVVHLLERQGITMVSG--IPGGSILPiydalSQSTQIRHILARHEQGAGFIAQGMARTEGKPA 78
Cdd:PRK06112 5 LSAPGFTLNG---TVAHAIARALKRHGVEQIFGqsLPSALFLA-----AEAIGIRQIAYRTENAGGAMADGYARVSGKVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 79 VCMACSGPGATNLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKhnyLVRDIAElPQVISD----A 154
Cdd:PRK06112 77 VVTAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTK---WVRRVTV-AERIDDyvdqA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 155 FRIAQSGRPGPVWIDIPKDVQAATIELETLPEPGERAPAP----AFAPESVREAAAMINAAKRPVLYLGGGV--INAPQP 228
Cdd:PRK06112 153 FTAATSGRPGPVVLLLPADLLTAAAAAPAAPRSNSLGHFPldrtVPAPQRLAEAASLLAQAQRPVVVAGGGVhiSGASAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 229 IRDLAEKANLPTTMTLMALGMLPKAHPLSLGMLG-MHGARS----TNFILQEADLLIVLGARFDDRAIGKTEQFCPNAKI 303
Cdd:PRK06112 233 LAALQSLAGLPVATTNMGKGAVDETHPLSLGVVGsLMGPRSpgrhLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 304 IHVDIDRSELGKiKQPHVAIQGDVAEVLAQLT---------------PQIEAQPRDEWRQLVADLQRefpcAIQQESDPL 368
Cdd:PRK06112 313 IHIDVDGEEVGR-NYEALRLVGDARLTLAALTdalrgrdlaaragrrAALEPAIAAGREAHREDSAP----VALSDASPI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 369 SHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRPRQ-WLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSL 447
Cdd:PRK06112 388 RPERIMAELQAVLTGDTIVVADASYSSIWVANFLTARRAGMrFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 448 MMNIQEMATAAENQLDVKIILLNNEALGL-VHQQQSLFyqqGVF-AATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQ 525
Cdd:PRK06112 468 AHVWAELETARRMGVPVTIVVLNNGILGFqKHAETVKF---GTHtDACHFAAVDHAAIARACGCDGVRVEDPAELAQALA 544
|
570 580
....*....|....*....|...
gi 895912174 526 AIIDRPGPALIHVRIDaqQKVYP 548
Cdd:PRK06112 545 AAMAAPGPTLIEVITD--PSAFP 565
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
11-548 |
3.21e-67 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 227.95 E-value: 3.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 11 MRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATN 90
Cdd:PRK09124 1 MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 91 LITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRpGPVWIDI 170
Cdd:PRK09124 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNR-GVAVVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 171 PKDVQaatieLETLPEPGERAPAPAFAP------ESVREAAAMINAAKRPVLYLGGGVINAPQPIRDLAEKANLPTTMTL 244
Cdd:PRK09124 160 PGDVA-----LKPAPERATPHWYHAPQPvvtpaeEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 245 MALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRaigkteQFCP-NAKIIHVDIDRSELGKIKQPHVAI 323
Cdd:PRK09124 235 RGKEHVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR------QFYPtDAKIIQIDINPGSLGRRSPVDLGL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 324 QGDVAEVLAQLTPQIeaQPRDEWRQLvaDLQREFPCAIQQESDPLS-----------HY--GLINAVAAcvdDEAIITTD 390
Cdd:PRK09124 309 VGDVKATLAALLPLL--EEKTDRKFL--DKALEHYRKARKGLDDLAvpsdggkpihpQYlaRQISEFAA---DDAIFTCD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 391 VGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLN 470
Cdd:PRK09124 382 VGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 471 NEALGLVhqqqSLFYQQGVFAATYPGMIN--FMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDAQQKVYP 548
Cdd:PRK09124 462 NSVLGFV----AMEMKAGGYLTDGTDLHNpdFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMP 537
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
15-548 |
4.29e-66 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 224.21 E-value: 4.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 15 GAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTqIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLITA 94
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 175 QAATIELETLPEPGERAP-APAFAPESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLMALGMLP 251
Cdd:PRK05858 166 AFSMADDDGRPGALTELPaGPTPDPDALARAAGLLAEAQRPVIMAGTDVWwgHAEAALLRLAEELGIPVLMNGMGRGVVP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 252 KAHPLSLgmlgmhgARSTNFILQEADLLIVLGARFDDR-AIGkteQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDVAEV 330
Cdd:PRK05858 246 ADHPLAF-------SRARGKALGEADVVLVVGVPMDFRlGFG---VFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 331 LAQLTPQieAQPRDEWRQLVADLQREFPCAIQQ-------ESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYP 403
Cdd:PRK05858 316 LSALAGA--GGDRTDHQGWIEELRTAETAARARdaaeladDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 404 LNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSL 483
Cdd:PRK05858 394 PYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKHPMEA 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 895912174 484 FYQQGVFAATYPGMiNFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRIDaQQKVYP 548
Cdd:PRK05858 474 LYGYDVAADLRPGT-RYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTD-PSVAYP 536
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
17-172 |
1.11e-63 |
|
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: 205.46 E-value: 1.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 17 QLVVHLLERQGITMVSGIPGGSILPIYDALSQStQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLITAIA 96
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARS-GIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 895912174 97 DARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPK 172
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
14-541 |
2.55e-62 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 214.85 E-value: 2.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGgsiLPIYD--ALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNL 91
Cdd:PRK09259 11 DGFHLVIDALKLNGIDTIYGVVG---IPITDlaRLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 92 ITAIADARLDSIPLVCITGQVPASMIGTDA--FQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWID 169
Cdd:PRK09259 88 LTALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 170 IPKDVQAATIELE----TLPEPGERAPAPAFAPESVREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMT 243
Cdd:PRK09259 168 LPAKVLAQTMDADealtSLVKVVDPAPAQLPAPEAVDRALDLLKKAKRPLIILGKGAAyaQADEQIREFVEKTGIPFLPM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 244 LMALGMLPKAHPLSLGmlgmhGARStnFILQEADLLIVLGARFD-DRAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVA 322
Cdd:PRK09259 248 SMAKGLLPDTHPQSAA-----AARS--LALANADVVLLVGARLNwLLSHGKGKTWGADKKFIQIDIEPQEIDSNRPIAAP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 323 IQGDVAEVLAQLTPQIEA---QPRDEWRQLVADlQRE-----FPCAIQQESDPLSHYGLINAVAACVDD-EAIITTDVGq 393
Cdd:PRK09259 321 VVGDIGSVMQALLAGLKQntfKAPAEWLDALAE-RKEknaakMAEKLSTDTQPMNFYNALGAIRDVLKEnPDIYLVNEG- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 394 hqmwtAQAYPLNR-------PRQWLTSGGLGTMGFGLPAAIGAALANpQRKVICFSGDGSLMMNIQEMATAAENQLDVKI 466
Cdd:PRK09259 399 -----ANTLDLARniidmykPRHRLDCGTWGVMGIGMGYAIAAAVET-GKPVVAIEGDSAFGFSGMEVETICRYNLPVTV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 467 ILLNNEALglvhqqqslfYQ---QGVFAATYPGMINFM------QIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIH 537
Cdd:PRK09259 473 VIFNNGGI----------YRgddVNLSGAGDPSPTVLVhharydKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLIN 542
|
....
gi 895912174 538 VRID 541
Cdd:PRK09259 543 VVID 546
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
15-182 |
2.94e-62 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 202.08 E-value: 2.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 15 GAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLITA 94
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 95 IADARLDSIPLVCITGQVPASMIGTDAFQ-EVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*....
gi 895912174 174 VQAATIELE 182
Cdd:pfam02776 161 VLLEEVDED 169
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
11-552 |
1.78e-61 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 213.23 E-value: 1.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 11 MRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQS-TQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGAT 89
Cdd:PRK08273 1 MSQTVADFILERLREWGVRRVFGYPGDGINGLLGALGRAdDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 90 NLITAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGisipitkhnyLVRDIA-----------ELPQVISDAFRIA 158
Cdd:PRK08273 81 HLLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQS----------LFKDVAgafvqmvtvpeQLRHLVDRAVRTA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 159 QSGRpGPVWIDIPKDVQaatiELETLPEP----------GERAPAPAFAPESVREAAAMINAAKRPVLYLGGGVINAPQP 228
Cdd:PRK08273 151 LAER-TVTAVILPNDVQ----ELEYEPPPhahgtvhsgvGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 229 IRDLAEKANLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFddraigKTEQFCP---NAKIIH 305
Cdd:PRK08273 226 VIAVAERLGAGVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSF------PYSEFLPkegQARGVQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 306 VDIDRSELGkIKQP-HVAIQGDVAEVLAQLTPQIEAQPRDEWRQL----VADLQREFPCAIQQESDPLSHYGLINAVAAC 380
Cdd:PRK08273 300 IDIDGRMLG-LRYPmEVNLVGDAAETLRALLPLLERKKDRSWRERiekwVARWWETLEARAMVPADPVNPQRVFWELSPR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 381 VDDEAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMN-IQEMATAAE 459
Cdd:PRK08273 379 LPDNAILTADSGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 460 NQLDVK-----IILLNNEALGLVHQQQSLFYQQGVFAAT-----YPgminFMQIAAGFGLQTCDLNNEADPQAALQAIID 529
Cdd:PRK08273 459 YWRQWSdprliVLVLNNRDLNQVTWEQRVMEGDPKFEASqdlpdVP----YARFAELLGLKGIRVDDPEQLGAAWDEALA 534
|
570 580
....*....|....*....|...
gi 895912174 530 RPGPALIHVRIDaqqkvyPMVPP 552
Cdd:PRK08273 535 ADRPVVLEVKTD------PNVPP 551
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
8-475 |
4.41e-59 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 205.82 E-value: 4.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 8 SNTMRftGAQLVVHLLERQGITMVSGIPggsILPIYDAlSQSTQIRHILARHEQGAGFIAQGMAR-TEGKP-AVCMACSG 85
Cdd:PRK06154 17 AKTMK--VAEAVAEILKEEGVELLFGFP---VNELFDA-AAAAGIRPVIARTERVAVHMADGYARaTSGERvGVFAVQYG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 86 PGATNLITAIADARLDSIPLVCITGQVPASMIGTDA-FQEVDTYGisiPITKHNYLVRDIAELPQVISDAFRIAQSGRPG 164
Cdd:PRK06154 91 PGAENAFGGVAQAYGDSVPVLFLPTGYPRGSTDVAPnFESLRNYR---HITKWCEQVTLPDEVPELMRRAFTRLRNGRPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 165 PVWIDIPKDVQAAtiELETLPEPGERAPA--PAFAPESVREAAAMINAAKRPVLYLGGGVINA---PQpIRDLAEKANLP 239
Cdd:PRK06154 168 PVVLELPVDVLAE--ELDELPLDHRPSRRsrPGADPVEVVEAAALLLAAERPVIYAGQGVLYAqatPE-LKELAELLEIP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 240 TTMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADLLIVLGARFDDRAIGKTeqfCPNAK-IIHVDIDRSELGKIKQ 318
Cdd:PRK06154 245 VMTTLNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYGLP---MPEGKtIIHSTLDDADLNKDYP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 319 PHVAIQGDVAEVLAQLTPQIE----------AQPRDEWRQLVADLQREFPCAIQQESDPLSHYGLINAVAACVDDE-AII 387
Cdd:PRK06154 322 IDHGLVGDAALVLKQMIEELRrrvgpdrgraQQVAAEIEAVRAAWLAKWMPKLTSDSTPINPYRVVWELQHAVDIKtVII 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 388 TTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKII 467
Cdd:PRK06154 402 THDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTI 481
|
....*...
gi 895912174 468 LLNNEALG 475
Cdd:PRK06154 482 LLNNFSMG 489
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
390-538 |
4.71e-59 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 193.19 E-value: 4.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 390 DVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILL 469
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 895912174 470 NNEALGLVHQQQSLFYQQGVFAATYPGM--INFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHV 538
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGKILppVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
10-541 |
5.73e-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: 191.53 E-value: 5.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 10 TMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMAcSGPGAT 89
Cdd:COG3961 2 PMTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTT-YGVGEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 90 NLITAIADARLDSIPLVCITGqVPAS-----------MIGT-------DAFQEVDTYGISIpiTKHNYlvrdIAELPQVI 151
Cdd:COG3961 81 SAINGIAGAYAERVPVVHIVG-APGTraqrrgpllhhTLGDgdfdhflRMFEEVTVAQAVL--TPENA----AAEIDRVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 152 SDAFRIAQsgrpgPVWIDIPKDVQAATIELetlPEPGERAPAPAFAPES----VREAAAMINAAKRPVLyLGG------G 221
Cdd:COG3961 154 AAALREKR-----PVYIELPRDVADAPIEP---PEAPLPLPPPASDPAAlaaaVAAAAERLAKAKRPVI-LAGvevhrfG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 222 VINApqpIRDLAEKANLPTTMTLMALGMLPKAHPLSLGMLGmhGARST----NFIlQEADLLIVLGARFDDRAIGKTEQF 297
Cdd:COG3961 225 LQEE---LLALAEKTGIPVATTLLGKSVLDESHPQFIGTYA--GAASSpevrEYV-ENADCVLCLGVVFTDTNTGGFTAQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 298 CPNAKIIHVDIDRSELGKIKQPHVAIqGDVAEVLAQLTPqieaqPRDEWRQLVADLQREFPcaiQQESDPLSHYGLINAV 377
Cdd:COG3961 299 LDPERTIDIQPDSVRVGGHIYPGVSL-ADFLEALAELLK-----KRSAPLPAPAPPPPPPP---AAPDAPLTQDRLWQRL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 378 AACVDDEAIITTDVGQhQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATA 457
Cdd:COG3961 370 QAFLDPGDIVVADTGT-SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTM 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 458 AENQLDVKIILLNNEALG----LVHQQQSlfYQQgvfaatypgmI---NFMQIAAGFG---LQTCDLNNEADPQAALQAI 527
Cdd:COG3961 449 LRYGLKPIIFVLNNDGYTieraIHGPDGP--YND----------IanwDYAKLPEAFGggnALGFRVTTEGELEEALAAA 516
|
570
....*....|....*
gi 895912174 528 I-DRPGPALIHVRID 541
Cdd:COG3961 517 EaNTDRLTLIEVVLD 531
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
201-334 |
1.10e-53 |
|
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: 178.53 E-value: 1.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 201 VREAAAMINAAKRPVLYLGGGVI--NAPQPIRDLAEKANLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNFILQEADL 278
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRrsGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 895912174 279 LIVLGARFDD-RAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDVAEVLAQL 334
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
10-541 |
7.92e-53 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 189.06 E-value: 7.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 10 TMRFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRH-----ILARHEQGAGFIAQGMARTEGKPAVCMACS 84
Cdd:PRK08327 4 LTMYTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGRplpefVICPHEIVAISMAHGYALVTGKPQAVMVHV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 85 GPGATNLITAIADARLDSIPLVCITGQVPASMIGT----DAF----QEV-DTYGISIPITKHNYLVRDIAELPQVISDAF 155
Cdd:PRK08327 84 DVGTANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrNTRihwtQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 156 RIAQSGRPGPVWIDIPKDVQAATIELETLPEPGERAPA-PAFAPESVREAAAMINAAKRPVLYL--GGGVINAPQPIRDL 232
Cdd:PRK08327 164 QIAMSEPKGPVYLTLPREVLAEEVPEVKADAGRQMAPApPAPDPEDIARAAEMLAAAERPVIITwrAGRTAEGFASLRRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 233 AEKANLP------TTMTLmalgmlPKAHPLSLGMlgmhgarSTNFILQEADLLIVLGArfDDRAIGKTEQFCPNAKIIHV 306
Cdd:PRK08327 244 AEELAIPvveyagEVVNY------PSDHPLHLGP-------DPRADLAEADLVLVVDS--DVPWIPKKIRPDADARVIQI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 307 DIDRSelgKIKQP------HVAIQGDVAEVLAQL----------TPQIEAQPRDEWRQLVADLQREFPCAIQQESDPlsh 370
Cdd:PRK08327 309 DVDPL---KSRIPlwgfpcDLCIQADTSTALDQLeerlkslasaERRRARRRRAAVRELRIRQEAAKRAEIERLKDR--- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 371 yGLINA--VAACV----DDEAIITTDVG--QHQMwtaqayPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFS 442
Cdd:PRK08327 383 -GPITPayLSYCLgevaDEYDAIVTEYPfvPRQA------RLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 443 GDGSLMMNIQEMA--TAAENQLDVKIILLNNEALGLVHQQQSLFYQQGVFAA--TYPGM-----INFMQIAAGFGLQTCD 513
Cdd:PRK08327 456 GDGSFIFGVPEAAhwVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPEGYAARkgTFPGTdfdprPDFAKIAEAFGGYGER 535
|
570 580 590
....*....|....*....|....*....|..
gi 895912174 514 LNNEAD-PQA---ALQAIIDRPGPALIHVRID 541
Cdd:PRK08327 536 VEDPEElKGAlrrALAAVRKGRRSAVLDVIVD 567
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
373-540 |
4.59e-51 |
|
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: 172.83 E-value: 4.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 373 LINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQ 452
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 453 EMATAAENQLDVKIILLNNEALGLVHQQQSLFYqQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPG 532
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFY-GGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 895912174 533 PALIHVRI 540
Cdd:cd00568 161 PALIEVKT 168
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
1-541 |
1.02e-46 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 171.29 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 1 MASSGTTSNTMrFTGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQStqIRHILARHEQGAGFIAQGMARTEGKPAVC 80
Cdd:PRK07092 1 MPKATAPAAAM-TTVRDATIDLLRRFGITTVFGNPGSTELPFLRDFPDD--FRYVLGLQEAVVVGMADGYAQATGNAAFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 81 MACSGPGATNLITAIADARLDSIPLVCITGQVPASMIGTDAF-QEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQ 159
Cdd:PRK07092 78 NLHSAAGVGNAMGNLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 160 SGRPGPVWIDIPKD--------VQAATIELETLPEPgerapapafapESVREAAAMINAAKRPVLYLGGGV--INAPQPI 229
Cdd:PRK07092 158 QPPRGPVFVSIPYDdwdqpaepLPARTVSSAVRPDP-----------AALARLGDALDAARRPALVVGPAVdrAGAWDDA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 230 RDLAEKANLPTTMTLMA-LGMLPKAHPLSLGMLgmHGAR-STNFILQEADLLIVLGA---RFDDRAIGktEQFCPNAKII 304
Cdd:PRK07092 227 VRLAERHRAPVWVAPMSgRCSFPEDHPLFAGFL--PASReKISALLDGHDLVLVIGApvfTYHVEGPG--PHLPEGAELV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 305 HVDID-----RSELGKikqphvAIQGDVAEVLAQLTPQIEAQPRDewrqlvADLQREFPCAIQQESDPLSHYGLINAVAA 379
Cdd:PRK07092 303 QLTDDpgeaaWAPMGD------AIVGDIRLALRDLLALLPPSARP------APPARPMPPPAPAPGEPLSVAFVLQTLAA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 380 CVDDEAII------TTDVGQHQMwtaqayPLNRPRQWLT--SGGLGtmgFGLPAAIGAALANPQRKVICFSGDGSLMMNI 451
Cdd:PRK07092 371 LRPADAIVveeapsTRPAMQEHL------PMRRQGSFYTmaSGGLG---YGLPAAVGVALAQPGRRVIGLIGDGSAMYSI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 452 QEMATAAENQLDVKIILLNNEALGLVHQQQSLFYQQGVFAATYPGmINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRP 531
Cdd:PRK07092 442 QALWSAAQLKLPVTFVILNNGRYGALRWFAPVFGVRDVPGLDLPG-LDFVALARGYGCEAVRVSDAAELADALARALAAD 520
|
570
....*....|
gi 895912174 532 GPALIHVRID 541
Cdd:PRK07092 521 GPVLVEVEVA 530
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
14-177 |
2.27e-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: 151.93 E-value: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRpGPVWIDIPKD 173
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGD 159
|
....
gi 895912174 174 VQAA 177
Cdd:cd07039 160 VQDA 163
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
367-552 |
7.20e-38 |
|
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: 137.66 E-value: 7.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 367 PLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGS 446
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 447 LMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFyQQGVFAATYPGmINFMQIAAGFGLQTCDLNNEADPQAALQA 526
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVM-GQPEFGVDLPN-PDFAKIAEAMGIKGIRVEDPDELEAALDE 158
|
170 180
....*....|....*....|....*.
gi 895912174 527 IIDRPGPALIHVRIDaqqkvyPMVPP 552
Cdd:cd02014 159 ALAADGPVVIDVVTD------PNEPP 178
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
373-541 |
9.03e-38 |
|
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: 137.42 E-value: 9.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 373 LINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQ 452
Cdd:cd02010 4 IVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 453 EMATAAENQLDVKIILLNNEALGLVHQQQSLFYQQgVFAATYpGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPG 532
Cdd:cd02010 84 ELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGR-DSGVDF-GNPDFVKYAESFGAKGYRIESADDLLPVLERALAADG 161
|
....*....
gi 895912174 533 PALIHVRID 541
Cdd:cd02010 162 VHVIDCPVD 170
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
14-540 |
7.04e-33 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 131.92 E-value: 7.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK12474 6 NGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK12474 86 NLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 V--QAATIELETLPEPGeraPAPaFAPESVREAAAMINAAKRPVLYLGGGVINApQPIRdLAEKANLPTTMTLMALGMLP 251
Cdd:PRK12474 166 VawNEAAYAAQPLRGIG---PAP-VAAETVERIAALLRNGKKSALLLRGSALRG-APLE-AAGRIQAKTGVRLYCDTFAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 252 K----AHPLSLGMLGMHGARSTNFiLQEADLLIVLGARfddraiGKTEQFCPNAKIIHVDIDRSELGKIKQPHvaiqGDV 327
Cdd:PRK12474 240 RiergAGRVPIERIPYFHEQITAF-LKDVEQLVLVGAK------PPVSFFAYPGKPSWGAPPGCEIVYLAQPD----EDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 328 AEVLAQLTPQIEAQprdewRQLVADLQREFPcaiQQESDPLSHYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRP 407
Cdd:PRK12474 309 AQALQDLADAVDAP-----AEPAARTPLALP---ALPKGALNSLGVAQLIAHRTPDQAIYADEALTSGLFFDMSYDRARP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 408 RQWLTSGGlGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFYQQ 487
Cdd:PRK12474 381 HTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGELQRVGAQ 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 895912174 488 GVFAATYPGM------INFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRI 540
Cdd:PRK12474 460 GAGRNALSMLdlhnpeLNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
17-172 |
1.35e-32 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 122.45 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 17 QLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTeGKPAVCMACSGPGATNLITAIA 96
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARA-GGPPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 895912174 97 DARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGrPGPVWIDIPK 172
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
14-540 |
1.49e-32 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 131.12 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 14 TGAQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLIT 93
Cdd:PRK07586 2 NGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 94 AIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIAELPQVISDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK07586 82 NLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVATLILPAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 174 VQAAtiELETLPEPGERAPAPAFAPESVREAAAMINAAKRPVLYLGGGV-----------INAPQPIRDLAEKANlpttm 242
Cdd:PRK07586 162 VAWS--EGGPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRAlrerglaaaarIAAATGARLLAETFP----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 243 TLMALGM-LPkaHPLSLGMLGMHGARstnfILQEADLLIVLGAR-----FddrAI-GKTEQFCPNAKIIHVDIDRSElgk 315
Cdd:PRK07586 235 ARMERGAgRP--AVERLPYFAEQALA----QLAGVRHLVLVGAKapvafF---AYpGKPSRLVPEGCEVHTLAGPGE--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 316 ikqphvaiqgDVAEVLAQLTPQIEAQPRDewrqlvADLQRefPCAIQQESDPLSHYGLINAVAACVDDEAI-----ITTD 390
Cdd:PRK07586 303 ----------DAAAALEALADALGAKPAA------PPLAA--PARPPLPTGALTPEAIAQVIAALLPENAIvvdesITSG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 391 VGQHqMWTAQAyplnRPRQWLTSGGlGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIILLN 470
Cdd:PRK07586 365 RGFF-PATAGA----APHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 471 NEALGLVHQQqslfyQQGVFAATyPG-----M-------INFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHV 538
Cdd:PRK07586 439 NRAYAILRGE-----LARVGAGN-PGpraldMldlddpdLDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHLIEA 512
|
..
gi 895912174 539 RI 540
Cdd:PRK07586 513 VV 514
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
381-540 |
2.90e-31 |
|
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: 119.62 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 381 VDDEAIITTDVGQHQMwtaqayPLNRPRQWLTSGGlGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAEN 460
Cdd:cd02002 20 IVDEAVTNGLPLRDQL------PLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALWTAARY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 461 QLDVKIILLNNEALGLVHQQQSLFYQQGVFAATYPGM------INFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPA 534
Cdd:cd02002 93 GLPVTVVILNNRGYGALRSFLKRVGPEGPGENAPDGLdlldpgIDFAAIAKAFGVEAERVETPEELDEALREALAEGGPA 172
|
....*.
gi 895912174 535 LIHVRI 540
Cdd:cd02002 173 LIEVVV 178
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
370-541 |
7.71e-30 |
|
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: 115.32 E-value: 7.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 370 HYGLINAVAACVDDEAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMM 449
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 450 NIQEMATAAENQLDVKIILLNNEALGL-VHQQQSLFYQQGVFAATYPGmINFMQIAAGFGLQTCDLNNEADPQAALQAII 528
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQgLDGQQLSYGLGLPVTTLLPD-TRYDLVAEAFGGKGELVTTPEELKPALKRAL 159
|
170
....*....|...
gi 895912174 529 DRPGPALIHVRID 541
Cdd:cd02004 160 ASGKPALINVIID 172
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
366-529 |
1.01e-21 |
|
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: 92.96 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 366 DPLSHYGLINAVAACVDDEAIITTDVGQHQMwTAQAYP-LNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGD 444
Cdd:cd02013 2 NPMHPRQVLRELEKAMPEDAIVSTDIGNICS-VANSYLrFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 445 GSLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFYqQGVFAATYPGMINFMQIAAGFGLQTCDLNNEADPQAAL 524
Cdd:cd02013 81 GAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFY-NNRFVGTELESESFAKIAEACGAKGITVDKPEDVGPAL 159
|
....*
gi 895912174 525 QAIID 529
Cdd:cd02013 160 QKAIA 164
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
367-472 |
2.83e-19 |
|
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: 85.66 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 367 PLSHYGLINAVAACVDDEAIITTDVG--QHQMWTAQaypLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGD 444
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGtsWFGALDLK---LPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGD 77
|
90 100
....*....|....*....|....*...
gi 895912174 445 GSLMMNIQEMATAAENQLDVKIILLNNE 472
Cdd:cd02005 78 GSFQMTVQELSTMIRYGLNPIIFLINND 105
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
17-171 |
3.54e-18 |
|
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: 81.78 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 17 QLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLITAIA 96
Cdd:cd07037 1 QALVEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 97 DARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVR------DIAELPQVISDAFRIAQSGRPGPVWIDI 170
Cdd:cd07037 81 EAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddDLWYLLRLANRAVLEALSAPPGPVHLNL 160
|
.
gi 895912174 171 P 171
Cdd:cd07037 161 P 161
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
374-555 |
2.74e-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: 80.43 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 374 INAVAACVDDEAIITTDVGQ-----HQMWTAQAyplnrPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLM 448
Cdd:cd02003 5 LGALNEAIGDDDVVINAAGSlpgdlHKLWRART-----PGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 449 MNIQEMATAAENQLDVKIILLNNEALGLV-HQQQS--------LFYQQGVFAATYPGM---INFMQIAAGFGLQTCDLNN 516
Cdd:cd02003 80 MLHSEIVTAVQEGLKIIIVLFDNHGFGCInNLQEStgsgsfgtEFRDRDQESGQLDGAllpVDFAANARSLGARVEKVKT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 895912174 517 EADPQAALQAIIDRPGPALIHVridaqqKVYP--MVPPGAA 555
Cdd:cd02003 160 IEELKAALAKAKASDRTTVIVI------KTDPksMTPGYGS 194
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
1-471 |
5.54e-17 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 83.98 E-value: 5.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 1 MASSGTTSNTMRFTGAQLVVHLLERQ---GITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKP 77
Cdd:PLN02573 1 QSSAPKPATPVSSSDATLGRHLARRLveiGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 78 AVCMACSgPGATNLITAIADARLDSIPLVCITGQvPAS-----------MIGTDAF-QEVDTYGisiPITKHNYLVRDIA 145
Cdd:PLN02573 81 ACVVTFT-VGGLSVLNAIAGAYSENLPVICIVGG-PNSndygtnrilhhTIGLPDFsQELRCFQ---TVTCYQAVINNLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 146 ELPQVISDAFRIAQsGRPGPVWIDIpkdvqaaTIELETLPEPG-ERAPAP-AFAPE---------SVREAAAMINAAKRP 214
Cdd:PLN02573 156 DAHELIDTAISTAL-KESKPVYISV-------SCNLAAIPHPTfSREPVPfFLTPRlsnkmsleaAVEAAAEFLNKAVKP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 215 VLyLGGG---VINAPQPIRDLAEKANLPTTMTLMALGMLPKAHPLSLGMlgMHGARSTNF---ILQEADLLIVLGARFDD 288
Cdd:PLN02573 228 VL-VGGPklrVAKACKAFVELADASGYPVAVMPSAKGLVPEHHPHFIGT--YWGAVSTPFcaeIVESADAYLFAGPIFND 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 289 RAIGKTEQFCPNAKIIHVDIDRSELGKIKQPHVAIQGDVAEVLA-QLTPQIEAQprDEWRQLVADLQREFPCaiqQESDP 367
Cdd:PLN02573 305 YSSVGYSLLLKKEKAIIVQPDRVTIGNGPAFGCVLMKDFLEALAkRVKKNTTAY--ENYKRIFVPEGEPLKS---EPGEP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 368 LSHYGLINAVAACVDDEAIITTDVGQHqmW-TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGS 446
Cdd:PLN02573 380 LRVNVLFKHIQKMLSGDTAVIAETGDS--WfNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAAPDKRVIACIGDGS 457
|
490 500
....*....|....*....|....*
gi 895912174 447 LMMNIQEMATAAENQLDVKIILLNN 471
Cdd:PLN02573 458 FQVTAQDVSTMIRCGQKSIIFLINN 482
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
389-484 |
7.00e-17 |
|
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: 79.25 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 389 TDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEMATAAENQLDVKIIL 468
Cdd:cd02006 29 TTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVL 108
|
90
....*....|....*.
gi 895912174 469 LNNEALGLVHQQQSLF 484
Cdd:cd02006 109 VNNAYLGLIRQAQRAF 124
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
377-558 |
1.60e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 78.33 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 377 VAACVDDEAIITtDVG--QHQMWTAQayplNRPRQWLTsggLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMMNIQEM 454
Cdd:PRK06163 23 VAKLKDEEAVIG-GIGntNFDLWAAG----QRPQNFYM---LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 455 AT-AAENQLDVKIILLNNEALGLVHQQQSLFYQqgvfaatypgMINFMQIAAGFGLQTCD-LNNEADPQAALQAIIDRPG 532
Cdd:PRK06163 95 GTiAALAPKNLTIIVMDNGVYQITGGQPTLTSQ----------TVDVVAIARGAGLENSHwAADEAHFEALVDQALSGPG 164
|
170 180
....*....|....*....|....*.
gi 895912174 533 PALIHVRIDAQqkvypmvpPGAANTE 558
Cdd:PRK06163 165 PSFIAVRIDDK--------PGVGTTE 182
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
416-541 |
2.71e-13 |
|
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: 68.47 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 416 LGTMGFGLPAAIGAALANPqRKVICFSGDGSLMMNIQEMAT-AAENQLDVKIILLNNEALGLVHQQQslfyqqgvfaaTY 494
Cdd:cd03372 41 LGSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGALATiAAEKPKNLIIVVLDNGAYGSTGNQP-----------TH 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 895912174 495 PGM-INFMQIAAGFGLQtcDLNNEADPQAALQAIIDR-PGPALIHVRID 541
Cdd:cd03372 109 AGKkTDLEAVAKACGLD--NVATVASEEAFEKAVEQAlDGPSFIHVKIK 155
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
376-540 |
7.55e-13 |
|
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: 67.34 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 376 AVAACVD----DEAII-TTDVGQHQMWTAQAYPLNR-PRQWLTSGGlgtMGFGLPAAIGAALANPQRKVICFSGDGSLMM 449
Cdd:cd03371 4 AIEIVLSrapaTAAVVsTTGMTSRELFELRDRPGGGhAQDFLTVGS---MGHASQIALGIALARPDRKVVCIDGDGAALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 450 NIQEMAT-AAENQLDVKIILLNNEALGLVHQQQSLfyqqgvfAATypgmINFMQIAAGFGLQTC-DLNNEADPQAALQAI 527
Cdd:cd03371 81 HMGGLATiGGLAPANLIHIVLNNGAHDSVGGQPTV-------SFD----VSLPAIAKACGYRAVyEVPSLEELVAALAKA 149
|
170
....*....|...
gi 895912174 528 IDRPGPALIHVRI 540
Cdd:cd03371 150 LAADGPAFIEVKV 162
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
21-171 |
1.05e-11 |
|
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: 63.28 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 21 HLLER---QGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGkPAVCMACSGPGATNLITAIAD 97
Cdd:cd07038 2 YLLERlkqLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 98 ARLDSIPLVCITGQVPASMIGT-------------DAFQEvdtygISIPITKHNYLVRDIAELPQVISDAFRIA-QSGRp 163
Cdd:cd07038 81 AYAEHVPVVHIVGAPSTKAQASglllhhtlgdgdfDVFLK-----MFEEITCAAARLTDPENAAEEIDRVLRTAlRESR- 154
|
....*...
gi 895912174 164 gPVWIDIP 171
Cdd:cd07038 155 -PVYIEIP 161
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
374-542 |
3.95e-10 |
|
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: 58.65 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 374 INAVAACVDDEAII-TTDVGQHQMWTAQayplNRPRQWLTsggLGTMGFGLPAAIGAALANPqRKVICFSGDGSLMMNIQ 452
Cdd:cd02001 5 IAEIIEASGDTPIVsTTGYASRELYDVQ----DRDGHFYM---LGSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 453 EMATAAE-NQLDVKIILLNNEALGLVHQQQslfyqqgvfaaTYPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRP 531
Cdd:cd02001 77 VLLTAGEfTPLNLILVVLDNRAYGSTGGQP-----------TPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATT 145
|
170
....*....|.
gi 895912174 532 GPALIHVRIDA 542
Cdd:cd02001 146 GPTLLHAPIAP 156
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
370-538 |
8.21e-09 |
|
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: 56.69 E-value: 8.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 370 HYGLINAVAACVD-----DEAIITTDVGQHQMwtAQAYplnrprqWLTSGGLGTMGFGLPAAIGAALANPQRKVICFSGD 444
Cdd:COG1013 21 HGIILRLLLKALDelldgDKTVVVSGIGCSSV--APGY-------FNVPGFHTLHGRAAAVATGIKLANPDLTVIVFGGD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 445 GSLM-MNIQEMATAAENQLDVKIILLNNEALGLVHQQQSlfyqqgvfAATYPGM-------------INFMQIAAGFGL- 509
Cdd:COG1013 92 GDTYdIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRS--------PTTPLGAkttttpygkpeppKDPAEIAAAHGAt 163
|
170 180 190
....*....|....*....|....*....|....*
gi 895912174 510 ---QTCDlnneADPQAALQAI---IDRPGPALIHV 538
Cdd:COG1013 164 yvaRASV----GDPKDLKKKIkkaIEHKGFSFIEV 194
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
370-536 |
1.44e-06 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 48.81 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 370 HYGLINAVAACVDDEAIITTDVGQHQMWTAQayPLNRprqwltSGGLGTMGFGLPAAIGAALANPQRKVICFSGDGSLMM 449
Cdd:cd02008 12 HRPSFYALRKAFKKDSIVSGDIGCYTLGALP--PLNA------IDTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTFFH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 450 N-IQEMATAAENQLDVKIILLNNEALGLVHQQQSLfyQQGVFAATYPGMINFMQIAAGFG---LQTCDLNNEADPQAALQ 525
Cdd:cd02008 84 SgILGLINAVYNKANITVVILDNRTTAMTGGQPHP--GTGKTLTEPTTVIDIEALVRAIGvkrVVVVDPYDLKAIREELK 161
|
170
....*....|.
gi 895912174 526 AIIDRPGPALI 536
Cdd:cd02008 162 EALAVPGVSVI 172
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
417-476 |
1.54e-06 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 49.84 E-value: 1.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 895912174 417 GTMGFGLPAAIGAALANPQRKVICFSGDGSLM---MN--IQematAAENQLDVKIILLNNEALGL 476
Cdd:PRK11867 69 TIHGRALAIATGLKLANPDLTVIVVTGDGDALaigGNhfIH----ALRRNIDITYILFNNQIYGL 129
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
417-476 |
4.03e-06 |
|
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: 47.52 E-value: 4.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 895912174 417 GTMGFGLPAAIGAALANPQRKVICFSGDGSlMMNI---QEMATAAENqLDVKIILLNNEALGL 476
Cdd:cd03375 51 TLHGRALAVATGVKLANPDLTVIVVSGDGD-LAAIggnHFIHAARRN-IDITVIVHNNQIYGL 111
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
426-541 |
1.15e-05 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 46.05 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 426 AIGAALANPQRkVICFSGD-------GSLMMNIQEmataaenQLDVKIILLNNE-----ALGLVHQQQSLFYQqgVFAAt 493
Cdd:cd02009 60 ALGIALATDKP-TVLLTGDlsflhdlNGLLLGKQE-------PLNLTIVVINNNgggifSLLPQASFEDEFER--LFGT- 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 895912174 494 yPGMINFMQIAAGFGLQTCDLNNEADPQAALQAIIDRPGPALIHVRID 541
Cdd:cd02009 129 -PQGLDFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
412-495 |
1.37e-05 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 47.06 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 412 TSGGLGTMGFGLPAAIGAALANPQRKVICFSGDG-SLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFYQQGVF 490
Cdd:PRK11866 54 TYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGdGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVK 133
|
....*
gi 895912174 491 AATYP 495
Cdd:PRK11866 134 TKTTP 138
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
16-126 |
1.60e-05 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 47.93 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 16 AQLVVHLLERQGITMVSGIPGGSILPIYDALSQSTQIRHILARHEQGAGFIAQGMARTEGKPAVCMACSGPGATNLITAI 95
Cdd:PLN02980 304 ASLIIEECTRLGLTYFCVAPGSRSSPLAIAASNHPLTTCIACFDERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAV 383
|
90 100 110
....*....|....*....|....*....|.
gi 895912174 96 ADARLDSIPLVCITGQVPASMIGTDAFQEVD 126
Cdd:PLN02980 384 VEASQDFVPLLLLTADRPPELQDAGANQAIN 414
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
418-493 |
3.00e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 42.80 E-value: 3.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 895912174 418 TMGFGLPAAIGAALANPQRKVICFSGDG-SLMMNIQEMATAAENQLDVKIILLNNEALGLVHQQQSLFYQQGVFAAT 493
Cdd:PRK09628 69 THGRAVAYATGIKLANPDKHVIVVSGDGdGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVT 145
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
417-476 |
1.42e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 41.02 E-value: 1.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 895912174 417 GTMGFGLPAAIGAALANPQRKVICFSGDGSLM---MNiqEMATAAENQLDVKIILLNNEALGL 476
Cdd:PRK05778 70 TLHGRAIAFATGAKLANPDLEVIVVGGDGDLAsigGG--HFIHAGRRNIDITVIVENNGIYGL 130
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
423-538 |
2.43e-03 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 39.45 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 423 LPAAIGAALANPQ----RKVICFSGDGSLM--MNIQEMATAAENQLDVKIILLNNE--ALGLVHQQQSLFYQQGVfaaTY 494
Cdd:cd02007 81 ISAALGMAVARDLkgkkRKVIAVIGDGALTggMAFEALNNAGYLKSNMIVILNDNEmsISPNVGTPGNLFEELGF---RY 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 895912174 495 PGMInfmqiaagfglqtcDLNNEADPQAALQAIIDRPGPALIHV 538
Cdd:cd02007 158 IGPV--------------DGHNIEALIKVLKEVKDLKGPVLLHV 187
|
|
| CdhB |
COG1880 |
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion]; |
203-307 |
3.06e-03 |
|
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];
Pssm-ID: 441484 Cd Length: 168 Bit Score: 38.78 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895912174 203 EAAAMINAAKRPVLYLGGGVINAPQPIR---DLAEKANLPTTMTLMALGMLPKAHPLSLGMLGMHGArsTNFILQEA--- 276
Cdd:COG1880 21 VAAKMIKKAKRPLLIVGPEALDDEELLEraiEIAKKAGIPIAATGHSIKGFVERGVEPAKYINIHEL--TNFLKDPEwkg 98
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 895912174 277 -------DLLIVLGARFD--DRAIGKTEQFCPNAKIIHVD 307
Cdd:COG1880 99 ldgngqyDLVIFLGFKYYyaSQVLSGLKHFAPHLKTIAID 138
|
|
| |
