|
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: 1194.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 1 MASSGTTSTRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVC 80
Cdd:PRK08155 1 MASSGTTSTRKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 81 MACSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQS 160
Cdd:PRK08155 81 MACSGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 161 GRPGPVWIDIPKDVQTAVFEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVIN--APARVRELAEKAQL 238
Cdd:PRK08155 161 GRPGPVWIDIPKDVQTAVIELEALPAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINsgAPARARELAEKAQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 239 PTTMTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQ 318
Cdd:PRK08155 241 PTTMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 319 PHVAIQADVDDVLAQLIPLVEAQPRAEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWT 398
Cdd:PRK08155 321 PHVAIQADVDDVLAQLLPLVEAQPRAEWHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQHQMWT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 399 AQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVH 478
Cdd:PRK08155 401 AQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 479 QQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAANTE 558
Cdd:PRK08155 481 QQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYPMVPPGAANTE 560
|
....
gi 1929626685 559 MVGE 562
Cdd:PRK08155 561 MIGE 564
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
14-559 |
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: 701.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:COG0028 4 TGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKD 173
Cdd:COG0028 84 GLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPKD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VQTAVFEIE-TQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTLMALGML 250
Cdd:COG0028 164 VQAAEAEEEpAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARraGAAEELRALAERLGAPVVTTLMGKGAF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 251 PKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDV 330
Cdd:COG0028 244 PEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIVGDAKAV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 331 LAQLIPLVEAQP--RAEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPR 408
Cdd:COG0028 324 LAALLEALEPRAddRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 409 QWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQG 488
Cdd:COG0028 404 RFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGR 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929626685 489 VFAATYPGkINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEkvypmVPPGAANTEM 559
Cdd:COG0028 484 YSGTDLPN-PDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEE-----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: 690.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQStQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK08978 2 NGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDG-GVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK08978 81 GLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VQTAvfEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVINAPA--RVRELAEKAQLPTTMTLMALGMLP 251
Cdd:PRK08978 161 IQLA--EGELEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAvpALREFLAATGMPAVATLKGLGAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 252 KAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDVL 331
Cdd:PRK08978 239 ADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLNALL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 332 AQLIPLVEAQPraeWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWL 411
Cdd:PRK08978 319 PALQQPLNIDA---WRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 412 TSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQGVFA 491
Cdd:PRK08978 396 TSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQLFFDERYSE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929626685 492 ATYPGKINFMQIAAGFGL--ETCDLNNEADpqASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAANTEMV 560
Cdd:PRK08978 476 TDLSDNPDFVMLASAFGIpgQTITRKDQVE--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: 648.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:TIGR00118 2 SGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKD 173
Cdd:TIGR00118 82 GIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VQTAV--FEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTLMALGM 249
Cdd:TIGR00118 162 VTTAEieYPYPEKVNLPGYRPTVKGHPLQIKKAAELINLAKKPVILVGGGVIiaGASEELKELAERIQIPVTTTLMGLGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 250 LPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDD 329
Cdd:TIGR00118 242 FPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGDARN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 330 VLAQLIPLVEAQPR---AEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNR 406
Cdd:TIGR00118 322 VLEELLKKLFELKErkeSAWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFRK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 407 PRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYE 486
Cdd:TIGR00118 402 PRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQWQELFYE 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626685 487 QGvFAATYPGKI-NFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAANTEMVGE 562
Cdd:TIGR00118 482 ER-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: 613.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 11 KRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATN 90
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 91 LVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDI 170
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 171 PKDVQTAV--FEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTLMA 246
Cdd:PRK08527 161 PKDVTATLgeFEYPKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAIlsNASEEIRELVKKTGIPAVETLMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 247 LGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQAD 326
Cdd:PRK08527 241 RGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 327 VDDVLAQLIPLVEA---QPRAEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYP 403
Cdd:PRK08527 321 LKNVLKEMLEELKEenpTTYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 404 LNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSL 483
Cdd:PRK08527 401 FNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQWQTF 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626685 484 FYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAANTEMV 560
Cdd:PRK08527 481 FYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLPMVPAGGALYNMI 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: 613.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 3 SSGTTSTRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQ---IRHILARHEQGAGFIAQGMARTDGKPAV 79
Cdd:PRK07418 9 GDSTTVTPQRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAegwLKHILVRHEQGAAHAADGYARATGKVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 80 CMACSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQ 159
Cdd:PRK07418 89 CFGTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIAS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 160 SGRPGPVWIDIPKDVQTAVFE-IETQPAMAEKAAAPAFSE---ESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELA 233
Cdd:PRK07418 169 SGRPGPVLIDIPKDVGQEEFDyVPVEPGSVKPPGYRPTVKgnpRQINAALKLIEEAERPLLYVGGGAIsaGAHAELKELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 234 EKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAEL 313
Cdd:PRK07418 249 ERFQIPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 314 GKIKQPHVAIQADVDDVLAQLIPLVE---AQPR-AEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDnAIITT 389
Cdd:PRK07418 329 GKNRRPDVPIVGDVRKVLVKLLERSLeptTPPRtQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAPD-AYYTT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 390 DVGQHQMWTAQaYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILM 469
Cdd:PRK07418 408 DVGQHQMWAAQ-FLRNGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVII 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 470 NNEALGLVHQQQSLFYEQGVFAATY-PGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYP 548
Cdd:PRK07418 487 NNGWQGMVRQWQESFYGERYSASNMePGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRRDENCYP 566
|
570
....*....|...
gi 1929626685 549 MVPPGAANTEMVG 561
Cdd:PRK07418 567 MVPPGKSNAQMVG 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: 596.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 2 ASSGTTSTRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCM 81
Cdd:PRK07789 20 AARPRIVAPERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 82 ACSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSG 161
Cdd:PRK07789 100 ATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 162 RPGPVWIDIPKDVQTAVFEIETQPAMAEKAAAPAFSEES--IRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQ 237
Cdd:PRK07789 180 RPGPVLVDIPKDALQAQTTFSWPPRMDLPGYRPVTKPHGkqIREAAKLIAAARRPVLYVGGGVIraEASAELRELAELTG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 238 LPTTMTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIK 317
Cdd:PRK07789 260 IPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 318 QPHVAIQADVDDVLAQLIPLVEAQPRA-------EWHQLVADLQREFPCPIPKACD-PLSHYGLINAVAACVDDNAIITT 389
Cdd:PRK07789 340 HADVPIVGDVKEVIAELIAALRAEHAAggkpdltAWWAYLDGWRETYPLGYDEPSDgSLAPQYVIERLGEIAGPDAIYVA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 390 DVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILM 469
Cdd:PRK07789 420 GVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALI 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 470 NNEALGLVHQQQSLFYEQ---GVFAATYPGKI-NFMQIAAGFGLETCDLNNEADPQASLQ---EIINRpgPALIHVRIDA 542
Cdd:PRK07789 500 NNGNLGMVRQWQTLFYEErysNTDLHTHSHRIpDFVKLAEAYGCVGLRCEREEDVDAVIEkarAINDR--PVVIDFVVGK 577
|
570
....*....|....*.
gi 1929626685 543 EEKVYPMVPPGAANTE 558
Cdd:PRK07789 578 DAMVWPMVAAGTSNDE 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: 592.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 6 TTSTRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQStQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSG 85
Cdd:PRK06048 1 MTGSTEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDS-DLRHILVRHEQAAAHAADGYARATGKVGVCVATSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 86 PGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGP 165
Cdd:PRK06048 80 PGATNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 166 VWIDIPKDVQTAVFEIETQPAMAEKAAAPAF--SEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTT 241
Cdd:PRK06048 160 VLIDLPKDVTTAEIDFDYPDKVELRGYKPTYkgNPQQIKRAAELIMKAERPIIYAGGGVIssNASEELVELAETIPAPVT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 242 MTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHV 321
Cdd:PRK06048 240 TTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 322 AIQADVDDVLAQLIPLVEAQPRAEWHQLVADLQREFPCPIPKACDPLSHYGLINAVA-ACVDdnAIITTDVGQHQMWTAQ 400
Cdd:PRK06048 320 PIVGDAKQVLKSLIKYVQYCDRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYeLCPD--AIIVTEVGQHQMWAAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 401 AYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQ 480
Cdd:PRK06048 398 YFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQW 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 481 QSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAANTEMV 560
Cdd:PRK06048 478 QELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSPMVPAGAAINEIL 557
|
..
gi 1929626685 561 GE 562
Cdd:PRK06048 558 DL 559
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
14-561 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 581.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDAL---SQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATN 90
Cdd:CHL00099 11 TGAFALIDSLVRHGVKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 91 LVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDI 170
Cdd:CHL00099 91 LVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 171 PKDVQTAVFEIETQPAMAEKAAAPAF------SEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTM 242
Cdd:CHL00099 171 PKDVGLEKFDYYPPEPGNTIIKILGCrpiykpTIKRIEQAAKLILQSSQPLLYVGGGAIisDAHQEITELAELYKIPVTT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 243 TLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVA 322
Cdd:CHL00099 251 TLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 323 IQADVDDVLAQLI-------PLVEAQPRAEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAAcVDDNAIITTDVGQHQ 395
Cdd:CHL00099 331 IVGDVKKVLQELLellknspNLLESEQTQAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQ-LAPDAYFTTDVGQHQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 396 MWTAQaYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALG 475
Cdd:CHL00099 410 MWAAQ-FLKCKPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQG 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 476 LVHQQQSLFYEQGvFAATY--PGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYPMVPPG 553
Cdd:CHL00099 489 MVRQWQQAFYGER-YSHSNmeEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDENCYPMVAPG 567
|
....*...
gi 1929626685 554 AANTEMVG 561
Cdd:CHL00099 568 KSNSQMIG 575
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
3-560 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 555.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 3 SSGTTSTRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMA 82
Cdd:PRK09107 1 SAQKSHMPRQMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 83 CSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGR 162
Cdd:PRK09107 81 TSGPGATNAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 163 PGPVWIDIPKDVQTAVFEI---ETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVIN----APARVRELAEK 235
Cdd:PRK09107 161 PGPVVVDIPKDVQFATGTYtppQKAPVHVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVINsgpeASRLLRELVEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 236 AQLPTTMTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGK 315
Cdd:PRK09107 241 TGFPITSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 316 IKQPHVAIQADVDDVLAQLIPLVEAQPRAEWHQLVADLQREFPCpiPKACDPLSH----------YGLINAVAACVDDNA 385
Cdd:PRK09107 321 NVRVDVPIIGDVGHVLEDMLRLWKARGKKPDKEALADWWGQIAR--WRARNSLAYtpsddvimpqYAIQRLYELTKGRDT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 386 IITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVK 465
Cdd:PRK09107 399 YITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 466 IILMNNEALGLVHQQQSLFYEQGV---FAATYPgkiNFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDA 542
Cdd:PRK09107 479 IFILNNQYMGMVRQWQQLLHGNRLshsYTEAMP---DFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVAN 555
|
570
....*....|....*...
gi 1929626685 543 EEKVYPMVPPGAANTEMV 560
Cdd:PRK09107 556 LENCFPMIPSGKAHNEML 573
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
15-562 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 552.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 15 GAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTA 94
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 95 IADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKDV 174
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 175 QTA-VFEIETQPAMAEKAAAP--AFSEES-IRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMALGML 250
Cdd:PLN02470 175 QQQlAVPNWNQPMKLPGYLSRlpKPPEKSqLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGLGAF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 251 PKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDV 330
Cdd:PLN02470 255 PASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADVKLA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 331 LAQLIPLVEAQPRA-----EWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLN 405
Cdd:PLN02470 335 LQGLNKLLEERKAKrpdfsAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 406 RPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFY 485
Cdd:PLN02470 415 EPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQWEDRFY 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 486 eQGVFAATYPGK--------INFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAANT 557
Cdd:PLN02470 495 -KANRAHTYLGDpdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLPMIPGGGTFK 573
|
....*
gi 1929626685 558 EMVGE 562
Cdd:PLN02470 574 DIITE 578
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
14-562 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 548.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQStQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK06276 2 KGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDS-DLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK06276 81 GIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VQTAVFEIETQPAMAEKAA-----APAFSEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTLMA 246
Cdd:PRK06276 161 VQEGELDLEKYPIPAKIDLpgykpTTFGHPLQIKKAAELIAEAERPVILAGGGVIisGASEELIELSELVKIPVCTTLMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 247 LGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQAD 326
Cdd:PRK06276 241 KGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 327 VDDVLAQLIP-LVEAQP--RAEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDD-----NAIITTDVGQHQMWT 398
Cdd:PRK06276 321 AKNVLRDLLAeLMKKEIknKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQMWM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 399 AQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVH 478
Cdd:PRK06276 401 AHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 479 QQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVyPMVPPGAANTE 558
Cdd:PRK06276 481 QWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAL-PMVPPGGNLTN 559
|
....
gi 1929626685 559 MVGE 562
Cdd:PRK06276 560 ILGP 563
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
14-560 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 540.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTqIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK06725 16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VQTAVFEIETQPAMAEKAAAPAFSEES--IRDAAAMINAAKRPVLYLGGGVINAPA--RVRELAEKAQLPTTMTLMALGM 249
Cdd:PRK06725 175 VQNEKVTSFYNEVVEIPGYKPEPRPDSmkLREVAKAISKAKRPLLYIGGGVIHSGGseELIEFARENRIPVVSTLMGLGA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 250 LPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDD 329
Cdd:PRK06725 255 YPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVGDVKK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 330 VLAQLIPLVEAQPRAEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQ 409
Cdd:PRK06725 335 ALHMLLHMSIHTQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 410 WLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQGv 489
Cdd:PRK06725 415 FLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEMFYENR- 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929626685 490 FAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAANTEMV 560
Cdd:PRK06725 494 LSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFPMVPPNKGNNEMI 564
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
1-561 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 537.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 1 MASSGTTSTRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQStQIRHILARHEQGAGFIAQGMARTDGKPAVC 80
Cdd:PRK07710 4 MRTMSSKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDC-GIPHILTRHEQGAIHAAEGYARISGKPGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 81 MACSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQS 160
Cdd:PRK07710 83 IATSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 161 GRPGPVWIDIPKDVQTA--VFEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVINAPA--RVRELAEKA 236
Cdd:PRK07710 163 GRPGPVLIDIPKDMVVEegEFCYDVQMDLPGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKAskELTSYAEQQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 237 QLPTTMTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKI 316
Cdd:PRK07710 243 EIPVVHTLLGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 317 KQPHVAIQADVDDVLAQLIPLVEAQPR-AEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQ 395
Cdd:PRK07710 323 VPTEIPIVADAKQALQVLLQQEGKKENhHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 396 MWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALG 475
Cdd:PRK07710 403 MWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALG 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 476 LVHQQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAA 555
Cdd:PRK07710 483 MVRQWQEEFYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMPMVAPGKG 562
|
....*.
gi 1929626685 556 NTEMVG 561
Cdd:PRK07710 563 LHEMVG 568
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
14-559 |
2.81e-178 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 515.06 E-value: 2.81e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK06466 5 SGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK06466 85 GIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPKD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VQTAV--FEIETQPAMAEKAAAPAFSEES--IRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTLMAL 247
Cdd:PRK06466 165 MTNPAekFEYEYPKKVKLRSYSPAVRGHSgqIRKAVEMLLAAKRPVIYSGGGVVlgNASALLTELAHLLNLPVTNTLMGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 248 GMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADV 327
Cdd:PRK06466 245 GGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPIVGPV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 328 DDVLAQLIPLVE---AQPRAE-----WHQLvaDLQRE----FPCPIPKAcDPLSHYGLINAVAACVDDNAIITTDVGQHQ 395
Cdd:PRK06466 325 ESVLTEMLAILKeigEKPDKEalaawWKQI--DEWRGrhglFPYDKGDG-GIIKPQQVVETLYEVTNGDAYVTSDVGQHQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 396 MWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALG 475
Cdd:PRK06466 402 MFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 476 LVHQQQSLFYEqGVFAATYPGKI-NFMQIAAGFGLETCDLNNEADPQASLQEIIN-RPGPALIHVRIDAEEKVYPMVPPG 553
Cdd:PRK06466 482 MVRQWQDMQYE-GRHSHSYMESLpDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVDRSEHVYPMQIAD 560
|
....*.
gi 1929626685 554 AANTEM 559
Cdd:PRK06466 561 GSMRDM 566
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
14-561 |
1.36e-174 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 505.51 E-value: 1.36e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VQTAVFEIETQPAMAEKAAAPAF--SEESIRDAAAMINAAKRPVLYLGGGV--INAPARVRELAEKAQLPTTMTLMALGM 249
Cdd:PRK07282 171 VSALETDFIYDPEVNLPSYQPTLepNDMQIKKILKQLSKAKKPVILAGGGInyAEAATELNAFAERYQIPVVTTLLGQGT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 250 LPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDD 329
Cdd:PRK07282 251 IATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 330 VLAQLIPLVEAQPR-AEWHQLVADLQREFPCPIPKAcDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPR 408
Cdd:PRK07282 331 ALQMLLAEPTVHNNtEKWIEKVTKDKNRVRSYDKKE-RVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNER 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 409 QWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQG 488
Cdd:PRK07282 410 QLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESFYEGR 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929626685 489 VFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLqEIINRPGPALIHVRIDAEEKVYPMVPPGAANTEMVG 561
Cdd:PRK07282 490 TSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDL-EVITEDVPMLIEVDISRKEHVLPMVPAGKSNHEMLG 561
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
11-559 |
1.92e-166 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 485.10 E-value: 1.92e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 11 KRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATN 90
Cdd:PRK08979 2 EMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 91 LVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDI 170
Cdd:PRK08979 82 TITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 171 PKDVQTAVFEIETQ-PAMAEKAA---APAFSEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTL 244
Cdd:PRK08979 162 PKDCLNPAILHPYEyPESIKMRSynpTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIisGADKQILQLAEKLNLPVVSTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 245 MALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQ 324
Cdd:PRK08979 242 MGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 325 ADVDDVLAQLIPLVEAQPR-------AEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMW 397
Cdd:PRK08979 322 GSADKVLDSMLALLDESGEtndeaaiASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQMF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 398 TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLV 477
Cdd:PRK08979 402 AALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 478 HQQQSLFYeQGVFAATYPGKI-NFMQIAAGFGLETCDLNNEADPQASLQEIIN-RPGPALIHVRIDAEEKVYPMVPPGAA 555
Cdd:PRK08979 482 KQWQDMIY-QGRHSHSYMDSVpDFAKIAEAYGHVGIRISDPDELESGLEKALAmKDRLVFVDINVDETEHVYPMQIRGGA 560
|
....
gi 1929626685 556 NTEM 559
Cdd:PRK08979 561 MNEM 564
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
3-560 |
4.81e-159 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 466.59 E-value: 4.81e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 3 SSGTTSTRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMA 82
Cdd:PRK06965 11 AESLSPPAADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 83 CSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGR 162
Cdd:PRK06965 91 TSGPGVTNAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 163 PGPVWIDIPKDV--QTAVFEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQL 238
Cdd:PRK06965 171 PGPVVVDIPKDVskTPCEYEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVIlaNASRELRQLADLLGY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 239 PTTMTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNA-KIIHVDIDRAELGKIK 317
Cdd:PRK06965 251 PVTNTLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 318 QPHVAIQADVDDVLAQLIPLV---EAQPRAE----WHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTD 390
Cdd:PRK06965 331 KVDIPIVGDVKEVLKELIEQLqtaEHGPDADalaqWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 391 VGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMN 470
Cdd:PRK06965 411 VGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLN 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 471 NEALGLVHQQQSLFYEqGVFAATYPGKI-NFMQIAAGFGLETCDLNNEADPQASLQEIIN-RPGPALIHVRIDAEEKVYP 548
Cdd:PRK06965 491 NRYLGMVRQWQEIEYS-KRYSHSYMDALpDFVKLAEAYGHVGMRIEKTSDVEPALREALRlKDRTVFLDFQTDPTENVWP 569
|
570
....*....|..
gi 1929626685 549 MVPPGAANTEMV 560
Cdd:PRK06965 570 MVQAGKGITEML 581
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
11-560 |
2.25e-155 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 456.68 E-value: 2.25e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 11 KRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATN 90
Cdd:PRK06882 2 KKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 91 LVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDI 170
Cdd:PRK06882 82 AITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 171 PKDVQTAV----FEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTL 244
Cdd:PRK06882 162 PKDMVNPAnkftYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVItaECSEQLTQFAQKLNLPVTSSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 245 MALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQ 324
Cdd:PRK06882 242 MGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 325 ADVDDVLAQLIPLVEAQPRA-------EWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMW 397
Cdd:PRK06882 322 GSAKNVLEEFLSLLEEENLAksqtdltAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQMF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 398 TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLV 477
Cdd:PRK06882 402 AALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGMV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 478 HQQQSLFYeQGVFAATYPGKI-NFMQIAAGFGLETCDLNNEADPQASLQEIIN-RPGPALIHVRIDAEEKVYPMVPPGAA 555
Cdd:PRK06882 482 KQWQDLIY-SGRHSQVYMNSLpDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSiKDKLVFVDVNVDETEHVYPMQIRGGA 560
|
....*
gi 1929626685 556 NTEMV 560
Cdd:PRK06882 561 MNEMI 565
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
13-559 |
3.71e-148 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 438.13 E-value: 3.71e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 13 FTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLV 92
Cdd:PRK07979 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 93 TAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPK 172
Cdd:PRK07979 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 173 DVQTAVFEI----ETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVINAP--ARVRELAEKAQLPTTMTLMA 246
Cdd:PRK07979 164 DILNPANKLpyvwPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAAchQQLKELVEKLNLPVVSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 247 LGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQAD 326
Cdd:PRK07979 244 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 327 VDDVLAQLIPLVE----AQPR---AEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTA 399
Cdd:PRK07979 324 ARQVLEQMLELLSqesaHQPLdeiRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 400 QAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQ 479
Cdd:PRK07979 404 LYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 480 QQSLFYeQGVFAATYPGKI-NFMQIAAGFGLETCDLNNEADPQASLQEIINRPGP---ALIHVRIDAEEKVYPMVPPGAA 555
Cdd:PRK07979 484 WQDMIY-SGRHSQSYMQSLpDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNnrlVFVDVTVDGSEHVYPMQIRGGG 562
|
....
gi 1929626685 556 NTEM 559
Cdd:PRK07979 563 MDEM 566
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
14-560 |
9.45e-129 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 388.43 E-value: 9.45e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDAL---SQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATN 90
Cdd:PRK06456 3 TGARILVDSLKREGVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 91 LVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDI 170
Cdd:PRK06456 83 LVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 171 PKDVQTAVFEIETQPAMAEKAAAPAF----SEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTL 244
Cdd:PRK06456 163 PRDIFYEKMEEIKWPEKPLVKGYRDFptriDRLALKKAAEILINAERPIILVGTGVVwsNATPEVLELAELLHIPIVSTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 245 MALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPN-AKIIHVDIDRAELGKIKQPHVAI 323
Cdd:PRK06456 243 PGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 324 QADVDDVLAQLIPLV----EAQPRAEWHQLVADLqREFPCPIPKACDP--LSHYGLINAVAACVDDNAIITTDVGQHQMW 397
Cdd:PRK06456 323 YGNAKIILRELIKAItelgQKRDRSAWLKRVKEY-KEYYSQFYYTEENgkLKPWKIMKTIRQALPRDAIVTTGVGQHQMW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 398 TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLV 477
Cdd:PRK06456 402 AEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 478 HQQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAANT 557
Cdd:PRK06456 482 RQVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALPTLPPGGRLK 561
|
...
gi 1929626685 558 EMV 560
Cdd:PRK06456 562 QVI 564
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
14-541 |
3.43e-107 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 331.79 E-value: 3.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTqIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK08322 2 KAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSS-IKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK08322 81 GVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VqtAVFEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTLMALGMLP 251
Cdd:PRK08322 161 I--AAEETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANrkTASKALTEFVDKTGIPFFTTQMGKGVIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 252 KAHPLSLGMLGMHGVRSTNYILQEADLLIVLGarFDdrAIGKTEQF-CPNA--KIIHVDIDRAELGKIKQPHVAIQADVD 328
Cdd:PRK08322 239 ETHPLSLGTAGLSQGDYVHCAIEHADLIINVG--HD--VIEKPPFFmNPNGdkKVIHINFLPAEVDPVYFPQVEVVGDIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 329 DVLAQLIPLVEAQPRAEW-------HQLVADLQR-----EFPcPIPKAcdplshygLINAVAACVDDNAIITTDVGQHQM 396
Cdd:PRK08322 315 NSLWQLKERLADQPHWDFprflkirEAIEAHLEEgadddRFP-MKPQR--------IVADLRKVMPDDDIVILDNGAYKI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 397 WTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGL 476
Cdd:PRK08322 386 WFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGM 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626685 477 VH--QQQSLFYEQGVfaaTYpGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRID 541
Cdd:PRK08322 466 IRwkQENMGFEDFGL---DF-GNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVD 528
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
6-543 |
7.54e-107 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 331.45 E-value: 7.54e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 6 TTSTRKRfTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSG 85
Cdd:PRK08199 2 TSTPRAR-TGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 86 PGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGP 165
Cdd:PRK08199 81 PGATNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 166 VWIDIPKDVQTAVFEIETQPAMAEKAAAPafSEESIRDAAAMINAAKRPVLYLGGGVIN--APARVRELAEKAQLPTTMT 243
Cdd:PRK08199 161 VVLALPEDVLSETAEVPDAPPYRRVAAAP--GAADLARLAELLARAERPLVILGGSGWTeaAVADLRAFAERWGLPVACA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 244 LMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAigkTEQF------CPNAKIIHVDIDRAELGKIK 317
Cdd:PRK08199 239 FRRQDLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVT---TQGYtlldipVPRQTLVHVHPDAEELGRVY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 318 QPHVAIQADVDDVLAQLIPLvEAQPRAEWHQLVADLQREF-----PCPIPKacdPLSHYGLINAVAACVDDNAIITTDVG 392
Cdd:PRK08199 316 RPDLAIVADPAAFAAALAAL-EPPASPAWAEWTAAAHADYlawsaPLPGPG---AVQLGEVMAWLRERLPADAIITNGAG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 393 QHQMWTAQAYPLNRPRQWL--TSgglGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMN 470
Cdd:PRK08199 392 NYATWLHRFFRFRRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVN 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 471 NEALGLV--HQQQSlfyeqgvfaatYPGKIN--------FMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRI 540
Cdd:PRK08199 469 NGMYGTIrmHQERE-----------YPGRVSgtdltnpdFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRI 537
|
...
gi 1929626685 541 DAE 543
Cdd:PRK08199 538 DPE 540
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
11-548 |
1.47e-104 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 325.04 E-value: 1.47e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 11 KRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQST-QIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGAT 89
Cdd:PRK08266 2 TTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 90 NLVTAIADARLDSIPLICITGQVPASMIGTDAFQ--EV-DTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPV 166
Cdd:PRK08266 82 NAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 167 WIDIPKDVQTAVFEIETQPAMAEKAAAPAfSEESIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMA 246
Cdd:PRK08266 162 ALEMPWDVFGQRAPVAAAPPLRPAPPPAP-DPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 247 LGMLPKAHPLSLGMLGMHGVrstnyiLQEADLLIVLGARFDD---RAIGKTEqfcpNAKIIHVDIDRAELGKIKqPHVAI 323
Cdd:PRK08266 241 RGIVSDRHPLGLNFAAAYEL------WPQTDVVIGIGSRLELptfRWPWRPD----GLKVIRIDIDPTEMRRLK-PDVAI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 324 QADVDDVLAQLIPLVEAQP------RAEWHQLVADLQREFpcpipKACDPLSHYglINAVAACVDDNAIITTDVGQHQMW 397
Cdd:PRK08266 310 VADAKAGTAALLDALSKAGskrpsrRAELRELKAAARQRI-----QAVQPQASY--LRAIREALPDDGIFVDELSQVGFA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 398 TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLV 477
Cdd:PRK08266 383 SWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNV 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929626685 478 HQQQSLFYEqGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYP 548
Cdd:PRK08266 463 RRDQKRRFG-GRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEASP 532
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
12-484 |
3.18e-103 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 323.08 E-value: 3.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 12 RFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMART-DGKPAVCMACSGPGATN 90
Cdd:PRK11269 3 KMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRAtAGNIGVCIGTSGPAGTD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 91 LVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDI 170
Cdd:PRK11269 83 MITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 171 PKDVQTAV--FEIET-QPAMAEKAAApafSEESIRDAAAMINAAKRPVLYLGGGVINAPA--RVRELAEKAQLPTTMTLM 245
Cdd:PRK11269 163 PFDVQVAEieFDPDTyEPLPVYKPAA---TRAQIEKALEMLNAAERPLIVAGGGVINADAsdLLVEFAELTGVPVIPTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 246 ALGMLPKAHPLSLGMLGMH-GVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIq 324
Cdd:PRK11269 240 GWGAIPDDHPLMAGMVGLQtSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGI- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 325 adVDDVLAQLIPLVEA----------QPRAEWHQLVADLQREFP-------CPIpkacDPLSHYGLINAVaacVDDNAII 387
Cdd:PRK11269 319 --VSDAKAALELLVEVarewkaagrlPDRSAWVADCQERKRTLLrkthfdnVPI----KPQRVYEEMNKA---FGRDTCY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 388 TTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKII 467
Cdd:PRK11269 390 VSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHV 469
|
490
....*....|....*..
gi 1929626685 468 LMNNEALGLVHQQQSLF 484
Cdd:PRK11269 470 LVNNAYLGLIRQAQRAF 486
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
368-553 |
9.68e-101 |
|
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: 302.49 E-value: 9.68e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 368 LSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSL 447
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 448 MMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEI 527
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|....*.
gi 1929626685 528 INRPGPALIHVRIDAEEKVYPMVPPG 553
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLPMVPPG 186
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
14-538 |
4.12e-98 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 308.06 E-value: 4.12e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTqIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK07524 3 TCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSG-IRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITG-QVPASM-IGTDAFQEV-DTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDI 170
Cdd:PRK07524 82 AMGQAYADSIPMLVISSvNRRASLgKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 171 PKDVQTAVFEiETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMALGML 250
Cdd:PRK07524 162 PLDVLAAPAD-HLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVALTINAKGLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 251 PKAHPLSLGmlGMHGVRSTNYILQEADLLIVLGARF--DDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVD 328
Cdd:PRK07524 241 PAGHPLLLG--ASQSLPAVRALIAEADVVLAVGTELgeTDYDVYFDGGFPLPGELIRIDIDPDQLARNYPPALALVGDAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 329 DVLAQLIPLVEAQPRAE-WHQL-VADLQREfpcpIPKACDPL--SHYGLINAVAACVDDnAIITTDVGQHQMWTAQAYPL 404
Cdd:PRK07524 319 AALEALLARLPGQAAAAdWGAArVAALRQA----LRAEWDPLtaAQVALLDTILAALPD-AIFVGDSTQPVYAGNLYFDA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 405 NRPRQWLTSG-GLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLV--HQQQ 481
Cdd:PRK07524 394 DAPRRWFNAStGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIrrYMVA 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626685 482 SLFYEQGVFAATyPgkiNFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHV 538
Cdd:PRK07524 474 RDIEPVGVDPYT-P---DFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
9-541 |
5.10e-92 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 292.53 E-value: 5.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 9 TRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTqIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGA 88
Cdd:PRK08617 1 TDKKKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSG-PELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 89 TNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWI 168
Cdd:PRK08617 80 SNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 169 DIPKDVQTAvfEIETQPAMAEKAAAP-AFSEESIRDAAAMINAAKRPVLYLG--GGVINAPARVRELAEKAQLPTTMTLM 245
Cdd:PRK08617 160 SLPQDVVDA--PVTSKAIAPLSKPKLgPASPEDINYLAELIKNAKLPVLLLGmrASSPEVTAAIRRLLERTNLPVVETFQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 246 ALGMLPKAH-PLSLGMLGMHGVRSTNYILQEADLLIVLGarFD----DRAIGKTEqfcPNAKIIHVDIDRAELGKIKQPH 320
Cdd:PRK08617 238 AAGVISRELeDHFFGRVGLFRNQPGDELLKKADLVITIG--YDpieyEPRNWNSE---GDATIIHIDVLPAEIDNYYQPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 321 VA----IQADVDDVLAQLIPL-VEAQPRAEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQ 395
Cdd:PRK08617 313 REligdIAATLDLLAEKLDGLsLSPQSLEILEELRAQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSHY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 396 MWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALG 475
Cdd:PRK08617 393 IWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYN 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929626685 476 LVHQQQSLFYEQGvfAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRID 541
Cdd:PRK08617 473 MVEFQEEMKYGRS--SGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVD 536
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
15-541 |
1.30e-90 |
|
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: 288.57 E-value: 1.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 15 GAEFIVHFLEQQGIKIVTGIPGGSILPVYDALsQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTA 94
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDAL-EDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 95 IADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKDV 174
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 175 QTAVFEIETQPAMAEKAAAPAfSEESIRDAAAMINAAKRPVLYLG--GGVINAPARVRELAEKAQLPTTMTLMALGMLPK 252
Cdd:TIGR02418 160 VDSPVSVKAIPASYAPKLGAA-PDDAIDEVAEAIQNAKLPVLLLGlrASSPETTEAVRRLLKKTQLPVVETFQGAGAVSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 253 A-HPLSLGMLGMHGVRSTNYILQEADLLIVLGarFD----DRAIGKTEQFCPnakIIHVDIDRAELGKIKQPHVAIQADV 327
Cdd:TIGR02418 239 ElEDHFFGRVGLFRNQPGDRLLKQADLVITIG--YDpieyEPRNWNSENDAT---IVHIDVEPAQIDNNYQPDLELVGDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 328 D---DVLAQLIPLVEAQPRAEwhQLVADLQREFPC----PIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQ 400
Cdd:TIGR02418 314 AstlDLLAERIPGYELPPDAL--AILEDLKQQREAldrvPATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMAR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 401 AYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQ 480
Cdd:TIGR02418 392 YFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQ 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929626685 481 QSLFYEQGvfAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRID 541
Cdd:TIGR02418 472 EEMKYQRS--SGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVD 530
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
14-544 |
4.83e-90 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 288.44 E-value: 4.83e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDAL-SQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLV 92
Cdd:PRK08611 5 KAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 93 TAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRpGPVWIDIPK 172
Cdd:PRK08611 85 NGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVLTIPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 173 DVQTAVFEIETQ-PAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMALGMLP 251
Cdd:PRK08611 164 DLPAQKIKDTTNkTVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPAKGIIP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 252 KAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRaigkteQFCPN-AKIIHVDIDRAELGKIKQPHVAIQADVDDV 330
Cdd:PRK08611 244 DDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPKkAKAIQIDTDPANIGKRYPVNVGLVGDAKKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 331 LAQL---IPLVEAQPRAE---------WHQLVADLQrefpcpipKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWT 398
Cdd:PRK08611 318 LHQLtenIKHVEDRRFLEacqenmakwWKWMEEDEN--------NASTPIKPERVMAAIQKIADDDAVLSVDVGTVTVWS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 399 AQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVH 478
Cdd:PRK08611 390 ARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIK 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929626685 479 qqqslfYEQGVFA----ATYPGKINFMQIA-----AGFGLETcdlNNEADPqaSLQEIINRPGPALIHVRIDAEE 544
Cdd:PRK08611 470 ------YEQQAAGeleyAIDLSDMDYAKFAeacggKGYRVEK---AEELDP--AFEEALAQDKPVIIDVYVDPNA 533
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
14-551 |
4.87e-84 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 271.70 E-value: 4.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQStQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKS-KVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRpGPVWIDIPKD 173
Cdd:PRK06457 82 GLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VQTAVFEIEtqPAMAEKAAAPAFSEEsIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMALGMLPKA 253
Cdd:PRK06457 161 ILRKSSEYK--GSKNTEVGKVKYSID-FSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 254 HPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAigkteqFCP-NAKIIHVDIDRAELGKIKQPHVAIQADVDDVLA 332
Cdd:PRK06457 238 DPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVN------FLNkSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 333 qliPLVEAQPRAEWHQLVADLQREFPCPIPKACD---PLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQ 409
Cdd:PRK06457 312 ---IDIEEKSDKFYEELKGKKEDWLDSISKQENSldkPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 410 WLTSGGLGTMGFGLPAAIGAALA-NPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHqqqslfYEQG 488
Cdd:PRK06457 389 FIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIK------FEQE 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929626685 489 VFAatYPG------KINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKvyPMVP 551
Cdd:PRK06457 463 VMG--YPEwgvdlyNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNER--PMPP 527
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
12-543 |
1.21e-83 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 271.87 E-value: 1.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 12 RFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDaLSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNL 91
Cdd:PRK07525 5 KMTPSEAFVETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 92 VTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRpGPVWIDIP 171
Cdd:PRK07525 84 VTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 172 KDVQTAVFEIET-QPAMAEKAAApafSEESIRDAAAMINAAKRPVLYLGGGVINAPAR--VRELAEKAQLPTTMTLMALG 248
Cdd:PRK07525 163 RDYFYGVIDVEIpQPVRLERGAG---GEQSLAEAAELLSEAKFPVILSGAGVVLSDAIeeCKALAERLDAPVACGYLHND 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 249 MLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDdrAIGKTEQ-----FCPNAKIIHVDIDRAELGKIKQPHVAI 323
Cdd:PRK07525 240 AFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLN--PFGTLPQygidyWPKDAKIIQVDINPDRIGLTKKVSVGI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 324 QADVDDV----LAQLIPLVE------------AQPRAEWHQLVADLQREFPCP----IPKA----CDPLSHYGLINAVAA 379
Cdd:PRK07525 318 CGDAKAVarelLARLAERLAgdagreerkaliAAEKSAWEQELSSWDHEDDDPgtdwNEEArarkPDYMHPRQALREIQK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 380 CVDDNAIITTDVGQHQMwTAQAYP-LNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATAS 458
Cdd:PRK07525 398 ALPEDAIVSTDIGNNCS-IANSYLrFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 459 ENQLDVKIILMNNEALGLVHQQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEII---NRPGPAL 535
Cdd:PRK07525 477 RHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIdaqNEGKTTV 556
|
....*...
gi 1929626685 536 IHVRIDAE 543
Cdd:PRK07525 557 IEIMCNQE 564
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
12-543 |
2.71e-82 |
|
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: 268.27 E-value: 2.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 12 RFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDaLSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNL 91
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMD-LFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 92 VTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRpGPVWIDIP 171
Cdd:TIGR03457 80 VTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 172 KDVQTAvfEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTLMALGM 249
Cdd:TIGR03457 159 RDYFYG--EIDVEIPRPVRLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVmgDAVEECKALAERLGAPVVNSYLHNDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 250 LPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDdrAIGKTEQ-----FCPNAKIIHVDIDRAELGKIKQPHVAIQ 324
Cdd:TIGR03457 237 FPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLG--PFGTLPQygidyWPKNAKIIQVDANAKMIGLVKKVTVGIC 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 325 ADVDDVLAQLIPLVEA---------------QPRAEWHQLVADLQREFPCPIPKAC--------DPLSHYGLINAVAACV 381
Cdd:TIGR03457 315 GDAKAAAAEILQRLAGkagdanraerkakiqAERSAWEQELSEMTHERDPFSLDMIveqrqeegNWLHPRQVLRELEKAM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 382 DDNAIITTDVGQHQMwTAQAYP-LNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASEN 460
Cdd:TIGR03457 395 PEDAIVSTDIGNINS-VANSYLrFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 461 QLDVKIILMNNEALGLVHQQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEII---NRPGPALIH 537
Cdd:TIGR03457 474 DIPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIaaqAEGKTTVIE 553
|
....*.
gi 1929626685 538 VRIDAE 543
Cdd:TIGR03457 554 IVCTRE 559
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
23-540 |
4.83e-76 |
|
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: 251.68 E-value: 4.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 23 LEQQGIKIVTGIPGGSILPVYDALS-QSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTAIADARLD 101
Cdd:TIGR02720 9 LEAWGVDHIYGIPGGSFNSTMDALSaERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYDAKED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 102 SIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSgRPGPVWIDIPKDVQTAvfEI 181
Cdd:TIGR02720 89 HVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYA-HNGVAVVTIPVDFGWQ--EI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 182 ETQPAMAEKAAAPAF-----SEESIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMALGMLPKAHPL 256
Cdd:TIGR02720 166 PDNDYYASSVSYQTPllpapDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGIIEDRYPA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 257 SLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTeqFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDVLAQLIP 336
Cdd:TIGR02720 246 YLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKA--FKNTKYFIQIDIDPAKLGKRHHTDIAVLADAKKALAAILA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 337 LVEAQPRAEWHQL-VADLQ--REFPCPIP-KACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLT 412
Cdd:TIGR02720 324 QVEPRESTPWWQAnVANVKnwRAYLASLEdKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNKWIT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 413 SGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSlFYEQGVFAA 492
Cdd:TIGR02720 404 SNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQE-DTNQPLIGV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1929626685 493 TYPgKINFMQIAAGFGLETCDLNNEAD-PQASLQEIINRPG-PALIHVRI 540
Cdd:TIGR02720 483 DFN-DADFAKIAEGVGAVGFRVNKIEQlPAVFEQAKAIKQGkPVLIDAKI 531
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
14-542 |
9.71e-76 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 249.91 E-value: 9.71e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPggSI--LPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNL 91
Cdd:PRK07064 4 TVGELIAAFLEQCGVKTAFGVI--SIhnMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 92 VTAIADARLDSIPLICITGQVPASMIGTDA--FQEV-DTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWI 168
Cdd:PRK07064 82 AGALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 169 DIPKDVQTAVFEIETqPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEkAQLPTTMTLMALG 248
Cdd:PRK07064 162 EIPIDIQAAEIELPD-DLAPVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVD-LGFGVVTSTQGRG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 249 MLPKAHPLSLGMLGMH-GVRStnyILQEADLLIVLGARFDDRAIGKTEQFCPnAKIIHVDIDRAELGKIKQPHVAIQADV 327
Cdd:PRK07064 240 VVPEDHPASLGAFNNSaAVEA---LYKTCDLLLVVGSRLRGNETLKYSLALP-RPLIRVDADAAADGRGYPNDLFVHGDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 328 DDVLAQLIPLVEAQPR--AEWHQLVADLQREFPCPIPKACDPlshYGLIN-AVAACVDDNAIITTDVG-QHQMWTAQAYP 403
Cdd:PRK07064 316 ARVLARLADRLEGRLSvdPAFAADLRAAREAAVADLRKGLGP---YAKLVdALRAALPRDGNWVRDVTiSNSTWGNRLLP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 404 LNRPRQWLTSGGlGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSL 483
Cdd:PRK07064 393 IFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNIQDA 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1929626685 484 FYEqGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDA 542
Cdd:PRK07064 472 QYG-GRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVDMLS 529
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
16-541 |
1.57e-71 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 239.50 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 16 AEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTAI 95
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 96 ADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAqSGRPGPVWIDIPKDVq 175
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHA-VAGGGVSVVTLPGDI- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 176 tAVFEIETQPAMAEKAAAPAF---SEESIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMALGMLPK 252
Cdd:PRK06546 164 -ADEPAPEGFAPSVISPRRPTvvpDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGKEWIQY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 253 AHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFddraigKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDVLA 332
Cdd:PRK06546 243 DNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDF------PYDQFLPDVRTAQVDIDPEHLGRRTRVDLAVHGDVAETIR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 333 QLIPLVEAQP-RAEWHQLVADLQREFPCPIPKACDPLSHYGLINA--VAACVD----DNAIITTDVGQHQMWTAQAYPLN 405
Cdd:PRK06546 317 ALLPLVKEKTdRRFLDRMLKKHARKLEKVVGAYTRKVEKHTPIHPeyVASILDelaaDDAVFTVDTGMCNVWAARYITPN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 406 RPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLfy 485
Cdd:PRK06546 397 GRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMLV-- 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1929626685 486 eQGV--FAATYPgKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRID 541
Cdd:PRK06546 475 -DGLpdFGTDHP-PVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTD 530
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
14-548 |
1.10e-65 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 224.10 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK09124 4 TVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRpGPVWIDIPKD 173
Cdd:PRK09124 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNR-GVAVVVLPGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VQTAVFEIETQPAMAEKAAAPAF-SEESIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMALGMLPK 252
Cdd:PRK09124 163 VALKPAPERATPHWYHAPQPVVTpAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRGKEHVEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 253 AHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRaigkteQFCP-NAKIIHVDIDRAELGKIKQPHVAIQADVDDVL 331
Cdd:PRK09124 243 DNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR------QFYPtDAKIIQIDINPGSLGRRSPVDLGLVGDVKATL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 332 AQLIPLVeaQPRAEWHQLVADLQR-----------EFPCPIPKACDPLSHYGLINAVAAcvdDNAIITTDVGQHQMWTAQ 400
Cdd:PRK09124 317 AALLPLL--EEKTDRKFLDKALEHyrkarkglddlAVPSDGGKPIHPQYLARQISEFAA---DDAIFTCDVGTPTVWAAR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 401 AYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLV--H 478
Cdd:PRK09124 392 YLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVamE 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 479 QQQSLFYEQGvfaaTYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYP 548
Cdd:PRK09124 472 MKAGGYLTDG----TDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMP 537
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
17-172 |
3.79e-65 |
|
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: 209.31 E-value: 3.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 17 EFIVHFLEQQGIKIVTGIPGGSILPVYDALSQStQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTAIA 96
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARS-GIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929626685 97 DARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPK 172
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
15-177 |
9.47e-63 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 203.62 E-value: 9.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 15 GAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTA 94
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 95 IADARLDSIPLICITGQVPASMIGTDAFQ-EVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKD 173
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....
gi 1929626685 174 VQTA 177
Cdd:pfam02776 161 VLLE 164
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
2-548 |
2.01e-60 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 210.00 E-value: 2.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 2 ASSGTTSTRKRFTGAEFIVHFLEQQGIKIVTG--IPGGSILPvydalSQSTQIRHILARHEQGAGFIAQGMARTDGKPAV 79
Cdd:PRK06112 3 KPLSAPGFTLNGTVAHAIARALKRHGVEQIFGqsLPSALFLA-----AEAIGIRQIAYRTENAGGAMADGYARVSGKVAV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 80 CMACSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKhnyLVRHI---EELPQVMSDAFR 156
Cdd:PRK06112 78 VTAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTK---WVRRVtvaERIDDYVDQAFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 157 IAQSGRPGPVWIDIPKDVQTAVfeiETQPAMAEKAAAPAF-------SEESIRDAAAMINAAKRPVLYLGGGV--INAPA 227
Cdd:PRK06112 155 AATSGRPGPVVLLLPADLLTAA---AAAPAAPRSNSLGHFpldrtvpAPQRLAEAASLLAQAQRPVVVAGGGVhiSGASA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 228 RVRELAEKAQLPTTMTLMALGMLPKAHPLSLGMLG-MHGVRS----TNYILQEADLLIVLGARFDDRAIGKTEQFCPNAK 302
Cdd:PRK06112 232 ALAALQSLAGLPVATTNMGKGAVDETHPLSLGVVGsLMGPRSpgrhLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 303 IIHVDIDRAELGK-------IKQPHVAIQAdVDDVLAQLIPLVEAQPRAEWHQLVADLQREFPCPIPKACD----PLSHY 371
Cdd:PRK06112 312 YIHIDVDGEEVGRnyealrlVGDARLTLAA-LTDALRGRDLAARAGRRAALEPAIAAGREAHREDSAPVALsdasPIRPE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 372 GLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQ-WLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMN 450
Cdd:PRK06112 391 RIMAELQAVLTGDTIVVADASYSSIWVANFLTARRAGMrFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 451 IQEMATASENQLDVKIILMNNEALGL-VHQQQSLFyeqGVF-AATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEII 528
Cdd:PRK06112 471 WAELETARRMGVPVTIVVLNNGILGFqKHAETVKF---GTHtDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAM 547
|
570 580
....*....|....*....|
gi 1929626685 529 NRPGPALIHVRIDaeEKVYP 548
Cdd:PRK06112 548 AAPGPTLIEVITD--PSAFP 565
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
390-538 |
3.09e-59 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 193.57 E-value: 3.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 390 DVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILM 469
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929626685 470 NNEALGLVHQQQSLFYEQGVFAATYPG--KINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHV 538
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGKIlpPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
15-496 |
1.53e-57 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 201.49 E-value: 1.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 15 GAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTqIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTA 94
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 95 IADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKDV 174
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 175 QTAVFEIETQPAMAEKAAAPAFSE-ESIRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTLMALGMLP 251
Cdd:PRK05858 166 AFSMADDDGRPGALTELPAGPTPDpDALARAAGLLAEAQRPVIMAGTDVWwgHAEAALLRLAEELGIPVLMNGMGRGVVP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 252 KAHPLSLgmlgmhgVRSTNYILQEADLLIVLGARFDDR-AIGkteQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDV 330
Cdd:PRK05858 246 ADHPLAF-------SRARGKALGEADVVLVVGVPMDFRlGFG---VFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 331 LAQLipLVEAQPRAEWHQLVADLQREFPCPIPK-------ACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYP 403
Cdd:PRK05858 316 LSAL--AGAGGDRTDHQGWIEELRTAETAARARdaaeladDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 404 LNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSL 483
Cdd:PRK05858 394 PYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKHPMEA 473
|
490
....*....|...
gi 1929626685 484 FYEQGVFAATYPG 496
Cdd:PRK05858 474 LYGYDVAADLRPG 486
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
11-475 |
2.55e-57 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 201.19 E-value: 2.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 11 KRFTGAEFIVHFLEQQGIKIVTGIPggsILPVYDAlSQSTQIRHILARHEQGAGFIAQGMAR-TDGKP-AVCMACSGPGA 88
Cdd:PRK06154 18 KTMKVAEAVAEILKEEGVELLFGFP---VNELFDA-AAAAGIRPVIARTERVAVHMADGYARaTSGERvGVFAVQYGPGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 89 TNLVTAIADARLDSIPLICITGQVPASMIGTDA-FQEVDTYGisiPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVW 167
Cdd:PRK06154 94 ENAFGGVAQAYGDSVPVLFLPTGYPRGSTDVAPnFESLRNYR---HITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 168 IDIPKDVQTAVFEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVINAPA--RVRELAEKAQLPTTMTLM 245
Cdd:PRK06154 171 LELPVDVLAEELDELPLDHRPSRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQAtpELKELAELLEIPVMTTLN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 246 ALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTeqfCPNAK-IIHVDIDRAELGKIKQPHVAIQ 324
Cdd:PRK06154 251 GKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYGLP---MPEGKtIIHSTLDDADLNKDYPIDHGLV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 325 ADVDDVLAQLIPLVE----------AQPRAEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDD-NAIITTDVGQ 393
Cdd:PRK06154 328 GDAALVLKQMIEELRrrvgpdrgraQQVAAEIEAVRAAWLAKWMPKLTSDSTPINPYRVVWELQHAVDIkTVIITHDAGS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 394 HQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEA 473
Cdd:PRK06154 408 PRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNFS 487
|
..
gi 1929626685 474 LG 475
Cdd:PRK06154 488 MG 489
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
14-458 |
1.29e-56 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 200.14 E-value: 1.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQS-TQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLV 92
Cdd:PRK08273 4 TVADFILERLREWGVRRVFGYPGDGINGLLGALGRAdDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 93 TAIADARLDSIPLICITGQVPASMIGTDAFQEVDTygisIPITK---HNYL--VRHIEELPQVMSDAFRIAQSGRpGPVW 167
Cdd:PRK08273 84 NGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDL----QSLFKdvaGAFVqmVTVPEQLRHLVDRAVRTALAER-TVTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 168 IDIPKDVQTAVFE--------IETQPAMAEKAAAPafSEESIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLP 239
Cdd:PRK08273 159 VILPNDVQELEYEppphahgtVHSGVGYTRPRVVP--YDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 240 TTMTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFddraigKTEQFCP---NAKIIHVDIDRAELGkI 316
Cdd:PRK08273 237 VAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSF------PYSEFLPkegQARGVQIDIDGRMLG-L 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 317 KQP-HVAIQADVDDVLAQLIPLVEAQPRAEWHQL----VADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDV 391
Cdd:PRK08273 310 RYPmEVNLVGDAAETLRALLPLLERKKDRSWRERiekwVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADS 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1929626685 392 GQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMN-IQEMATAS 458
Cdd:PRK08273 390 GSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVA 457
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
14-541 |
2.14e-54 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 193.28 E-value: 2.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGgsiLPVYD--ALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNL 91
Cdd:PRK09259 11 DGFHLVIDALKLNGIDTIYGVVG---IPITDlaRLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 92 VTAIADARLDSIPLICITGQVPASMIGTDA--FQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWID 169
Cdd:PRK09259 88 LTALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 170 IPKDVQTAVFEIE---------TQPAMAEKAaapafSEESIRDAAAMINAAKRPVLYLGGGVINAPA--RVRELAEKAQL 238
Cdd:PRK09259 168 LPAKVLAQTMDADealtslvkvVDPAPAQLP-----APEAVDRALDLLKKAKRPLIILGKGAAYAQAdeQIREFVEKTGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 239 PTTMTLMALGMLPKAHPLSLGmlgmhGVRStnYILQEADLLIVLGARFD-DRAIGKTEQFCPNAKIIHVDIDRAELGKIK 317
Cdd:PRK09259 243 PFLPMSMAKGLLPDTHPQSAA-----AARS--LALANADVVLLVGARLNwLLSHGKGKTWGADKKFIQIDIEPQEIDSNR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 318 QPHVAIQADVDDVLAQLIPLVEA---QPRAEWHQLVADlQRE-----FPCPIPKACDPLSHYGLINAVAACVDDNA-IIT 388
Cdd:PRK09259 316 PIAAPVVGDIGSVMQALLAGLKQntfKAPAEWLDALAE-RKEknaakMAEKLSTDTQPMNFYNALGAIRDVLKENPdIYL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 389 TDVGqhqmwtAQAYPLNR-------PRQWLTSGGLGTMGFGLPAAIGAALANpDRKVLCFSGDGSLMMNIQEMATASENQ 461
Cdd:PRK09259 395 VNEG------ANTLDLARniidmykPRHRLDCGTWGVMGIGMGYAIAAAVET-GKPVVAIEGDSAFGFSGMEVETICRYN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 462 LDVKIILMNNEALglvhqqqslfY---EQGVFAATYPGKINFM------QIAAGFGLETCDLNNEADPQASLQEIINRPG 532
Cdd:PRK09259 468 LPVTVVIFNNGGI----------YrgdDVNLSGAGDPSPTVLVhharydKMMEAFGGVGYNVTTPDELRHALTEAIASGK 537
|
....*....
gi 1929626685 533 PALIHVRID 541
Cdd:PRK09259 538 PTLINVVID 546
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
201-334 |
1.59e-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: 178.14 E-value: 1.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 201 IRDAAAMINAAKRPVLYLGGGVI--NAPARVRELAEKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADL 278
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRrsGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626685 279 LIVLGARFDD-RAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDVLAQL 334
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
373-540 |
2.96e-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: 173.21 E-value: 2.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 373 LINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQ 452
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 453 EMATASENQLDVKIILMNNEALGLVHQQQSLFYEqGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPG 532
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYG-GRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 1929626685 533 PALIHVRI 540
Cdd:cd00568 161 PALIEVKT 168
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
9-541 |
5.22e-49 |
|
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: 178.04 E-value: 5.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 9 TRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMAcSGPGA 88
Cdd:COG3961 1 MPMTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTT-YGVGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 89 TNLVTAIADARLDSIPLICITGqVPAS-----------MIGT-------DAFQEVDTYGISIpiTKHNYlvrhIEELPQV 150
Cdd:COG3961 80 LSAINGIAGAYAERVPVVHIVG-APGTraqrrgpllhhTLGDgdfdhflRMFEEVTVAQAVL--TPENA----AAEIDRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 151 MSDAFRIAQsgrpgPVWIDIPKDVqtAVFEIEtQPAMAEKAAAPAFSEES----IRDAAAMINAAKRPVLyLGG------ 220
Cdd:COG3961 153 LAAALREKR-----PVYIELPRDV--ADAPIE-PPEAPLPLPPPASDPAAlaaaVAAAAERLAKAKRPVI-LAGvevhrf 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 221 GVINAparVRELAEKAQLPTTMTLMALGMLPKAHPLSLGM----LGMHGVRstNYIlQEADLLIVLGARFDDRAIGKTEQ 296
Cdd:COG3961 224 GLQEE---LLALAEKTGIPVATTLLGKSVLDESHPQFIGTyagaASSPEVR--EYV-ENADCVLCLGVVFTDTNTGGFTA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 297 FCPNAKIIHVDIDRAELGKIKQPHVAIqadvDDVLAQLIPLVEaqPRAEWHQLVADLQREFPcpiPKACDPLSHYGLINA 376
Cdd:COG3961 298 QLDPERTIDIQPDSVRVGGHIYPGVSL----ADFLEALAELLK--KRSAPLPAPAPPPPPPP---AAPDAPLTQDRLWQR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 377 VAACVDDNAIITTDVGQhQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMAT 456
Cdd:COG3961 369 LQAFLDPGDIVVADTGT-SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELST 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 457 ASENQLDVKIILMNNEALG----LVHQQQSlfYEQgvfaatypgkI---NFMQIAAGFGLE---TCDLNNEADPQASLQE 526
Cdd:COG3961 448 MLRYGLKPIIFVLNNDGYTieraIHGPDGP--YND----------IanwDYAKLPEAFGGGnalGFRVTTEGELEEALAA 515
|
570
....*....|....*.
gi 1929626685 527 II-NRPGPALIHVRID 541
Cdd:COG3961 516 AEaNTDRLTLIEVVLD 531
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
2-541 |
2.76e-46 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 170.14 E-value: 2.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 2 ASSGTTSTRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQStqIRHILARHEQGAGFIAQGMARTDGKPAVCM 81
Cdd:PRK07092 1 MPKATAPAAAMTTVRDATIDLLRRFGITTVFGNPGSTELPFLRDFPDD--FRYVLGLQEAVVVGMADGYAQATGNAAFVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 82 ACSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAF-QEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQS 160
Cdd:PRK07092 79 LHSAAGVGNAMGNLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 161 GRPGPVWIDIPKD--------VQTAVFEIETQPamaekaaapafSEESIRDAAAMINAAKRPVLYLGGGVINAPA--RVR 230
Cdd:PRK07092 159 PPRGPVFVSIPYDdwdqpaepLPARTVSSAVRP-----------DPAALARLGDALDAARRPALVVGPAVDRAGAwdDAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 231 ELAEKAQLPTTMTLMA-LGMLPKAHPLSLGML--GMHGVRSTnyiLQEADLLIVLGA---RFDDRAIGktEQFCPNAKII 304
Cdd:PRK07092 228 RLAERHRAPVWVAPMSgRCSFPEDHPLFAGFLpaSREKISAL---LDGHDLVLVIGApvfTYHVEGPG--PHLPEGAELV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 305 HVDID-----RAELGKikqphvAIQADVDDVLAQLIPLVEAQPRAewhqlvADLQREFPCPIPKACDPLSHYGLINAVAA 379
Cdd:PRK07092 303 QLTDDpgeaaWAPMGD------AIVGDIRLALRDLLALLPPSARP------APPARPMPPPAPAPGEPLSVAFVLQTLAA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 380 CVDDNAII------TTDVGQHQMwtaqayPLNRPRQWLT--SGGLGtmgFGLPAAIGAALANPDRKVLCFSGDGSLMMNI 451
Cdd:PRK07092 371 LRPADAIVveeapsTRPAMQEHL------PMRRQGSFYTmaSGGLG---YGLPAAVGVALAQPGRRVIGLIGDGSAMYSI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 452 QEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQGVFAATYPGkINFMQIAAGFGLETCDLNNEADPQASLQEIINRP 531
Cdd:PRK07092 442 QALWSAAQLKLPVTFVILNNGRYGALRWFAPVFGVRDVPGLDLPG-LDFVALARGYGCEAVRVSDAAELADALARALAAD 520
|
570
....*....|
gi 1929626685 532 GPALIHVRID 541
Cdd:PRK07092 521 GPVLVEVEVA 530
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
14-541 |
6.78e-46 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 169.80 E-value: 6.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRH-----ILARHEQGAGFIAQGMARTDGKPAVCMACSGPGA 88
Cdd:PRK08327 8 TAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGRplpefVICPHEIVAISMAHGYALVTGKPQAVMVHVDVGT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 89 TNLVTAIADARLDSIPLICITGQVPASMIGT----DAF----QEV-DTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQ 159
Cdd:PRK08327 88 ANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrNTRihwtQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 160 SGRPGPVWIDIPKDVQTAVFEIETQPAMAEKAAAPA-FSEESIRDAAAMINAAKRPVLYL--GGGVINAPARVRELAEKA 236
Cdd:PRK08327 168 SEPKGPVYLTLPREVLAEEVPEVKADAGRQMAPAPPaPDPEDIARAAEMLAAAERPVIITwrAGRTAEGFASLRRLAEEL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 237 QLP------TTMTLmalgmlPKAHPLSLGMlgmhgvrSTNYILQEADLLIVLGArfDDRAIGKTEQFCPNAKIIHVDIDR 310
Cdd:PRK08327 248 AIPvveyagEVVNY------PSDHPLHLGP-------DPRADLAEADLVLVVDS--DVPWIPKKIRPDADARVIQIDVDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 311 AelgKIKQP------HVAIQADVDDVLAQL----------IPLVEAQPRAEWHQLVADLQREFPCPIPKACDPlshyGLI 374
Cdd:PRK08327 313 L---KSRIPlwgfpcDLCIQADTSTALDQLeerlkslasaERRRARRRRAAVRELRIRQEAAKRAEIERLKDR----GPI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 375 NA--VAACV----DDNAIITTDVG--QHQMwtaqayPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGS 446
Cdd:PRK08327 386 TPayLSYCLgevaDEYDAIVTEYPfvPRQA------RLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGS 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 447 LMMNIQEMA--TASENQLDVKIILMNNEALGLVHQQQSLFYEQGVFAA--TYPG-----KINFMQIAAGFG-----LETC 512
Cdd:PRK08327 460 FIFGVPEAAhwVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPEGYAARkgTFPGtdfdpRPDFAKIAEAFGgygerVEDP 539
|
570 580
....*....|....*....|....*....
gi 1929626685 513 DLNNEADPQAsLQEIINRPGPALIHVRID 541
Cdd:PRK08327 540 EELKGALRRA-LAAVRKGRRSAVLDVIVD 567
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
14-177 |
7.49e-46 |
|
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: 158.48 E-value: 7.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRpGPVWIDIPKD 173
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGD 159
|
....
gi 1929626685 174 VQTA 177
Cdd:cd07039 160 VQDA 163
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
367-544 |
9.00e-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: 137.28 E-value: 9.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 367 PLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGS 446
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 447 LMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFyEQGVFAATYPGkINFMQIAAGFGLETCDLNNEADPQASLQE 526
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVM-GQPEFGVDLPN-PDFAKIAEAMGIKGIRVEDPDELEAALDE 158
|
170
....*....|....*...
gi 1929626685 527 IINRPGPALIHVRIDAEE 544
Cdd:cd02014 159 ALAADGPVVIDVVTDPNE 176
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
373-544 |
4.87e-37 |
|
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: 135.49 E-value: 4.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 373 LINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQ 452
Cdd:cd02010 4 IVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 453 EMATASENQLDVKIILMNNEALGLVHQQQSLFYEQgVFAATYpGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPG 532
Cdd:cd02010 84 ELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGR-DSGVDF-GNPDFVKYAESFGAKGYRIESADDLLPVLERALAADG 161
|
170
....*....|..
gi 1929626685 533 PALIHVRIDAEE 544
Cdd:cd02010 162 VHVIDCPVDYSE 173
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
14-540 |
3.43e-33 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 133.05 E-value: 3.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK07586 2 NGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKD 173
Cdd:PRK07586 82 NLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVATLILPAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 174 VQTAvfEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVINAPAR-----------VRELAEkaQLPTTM 242
Cdd:PRK07586 162 VAWS--EGGPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLaaaariaaatgARLLAE--TFPARM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 243 T----LMALGMLPKAHPLSLGMLgmhgvrstnyilQEADLLIVLGAR-----FddrAI-GKTEQFCPNAKIIHVDIDRAE 312
Cdd:PRK07586 238 ErgagRPAVERLPYFAEQALAQL------------AGVRHLVLVGAKapvafF---AYpGKPSRLVPEGCEVHTLAGPGE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 313 lgkikqphvaiqaDVDDVLAQLIPLVEAQPRAewhqlvADLQREFPCPIPKAcdPLSHYGLINAVAACVDDNAI-----I 387
Cdd:PRK07586 303 -------------DAAAALEALADALGAKPAA------PPLAAPARPPLPTG--ALTPEAIAQVIAALLPENAIvvdesI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 388 TTDVGQHQMwTAQAyplnRPRQWLTSGGlGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKII 467
Cdd:PRK07586 362 TSGRGFFPA-TAGA----APHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTV 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 468 LMNNealglvHQQQSLFYEQGVFAATYPGK------------INFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPAL 535
Cdd:PRK07586 436 IFAN------RAYAILRGELARVGAGNPGPraldmldlddpdLDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHL 509
|
....*
gi 1929626685 536 IHVRI 540
Cdd:PRK07586 510 IEAVV 514
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
19-172 |
1.30e-31 |
|
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: 119.76 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 19 IVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTdGKPAVCMACSGPGATNLVTAIADA 98
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARA-GGPPVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929626685 99 RLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGrPGPVWIDIPK 172
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
14-540 |
1.73e-31 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 128.07 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 14 TGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVT 93
Cdd:PRK12474 6 NGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 94 AIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKhnyLVRHIEELPQVMSD---AFRIAQSGRPGPVWIDI 170
Cdd:PRK12474 86 NLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSR---WVHRSASAGAVDSDvarAVQAAQSAPGGIATLIM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 171 PKDVqtAVFEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYL-GGGVINAPArvrELAEKAQLPTTMTLMALGM 249
Cdd:PRK12474 163 PADV--AWNEAAYAAQPLRGIGPAPVAAETVERIAALLRNGKKSALLLrGSALRGAPL---EAAGRIQAKTGVRLYCDTF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 250 LPKAH------PLS-LGMLGMHGVRstnyILQEADLLIVLGARfddraiGKTEQFCPNAKIIHVDIDRAELGKIKQPH-- 320
Cdd:PRK12474 238 APRIErgagrvPIErIPYFHEQITA----FLKDVEQLVLVGAK------PPVSFFAYPGKPSWGAPPGCEIVYLAQPDed 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 321 --VAIQADVDDVLAQLIPLVEAQPRAewhqlvadlqrefPCPiPKacDPLSHYGLINAVAACVDDNAIITTDVGQHQMWT 398
Cdd:PRK12474 308 laQALQDLADAVDAPAEPAARTPLAL-------------PAL-PK--GALNSLGVAQLIAHRTPDQAIYADEALTSGLFF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 399 AQAYPLNRPRQWLTSGGlGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNealglvH 478
Cdd:PRK12474 372 DMSYDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFAN------R 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929626685 479 QQQSLFYEQGVFAATYPGK------------INFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRI 540
Cdd:PRK12474 445 SYAILNGELQRVGAQGAGRnalsmldlhnpeLNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
373-540 |
8.86e-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: 118.08 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 373 LINAVAACVDDNAII-----TTDVGQHQMWtaqayPLNRPRQWLTSGGlGTMGFGLPAAIGAALANPDRKVLCFSGDGSL 447
Cdd:cd02002 6 LAAALAAALPEDAIIvdeavTNGLPLRDQL-----PLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 448 MMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQGVFAATY-------PGkINFMQIAAGFGLETCDLNNEADP 520
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENAPdgldlldPG-IDFAAIAKAFGVEAERVETPEEL 158
|
170 180
....*....|....*....|
gi 1929626685 521 QASLQEIINRPGPALIHVRI 540
Cdd:cd02002 159 DEALREALAEGGPALIEVVV 178
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
370-541 |
6.84e-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: 6.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 370 HYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMM 449
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 450 NIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIIN 529
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 1929626685 530 RPGPALIHVRID 541
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
366-543 |
5.99e-22 |
|
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: 93.73 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 366 DPLSHYGLINAVAACVDDNAIITTDVGQHQMwTAQAYP-LNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGD 444
Cdd:cd02013 2 NPMHPRQVLRELEKAMPEDAIVSTDIGNICS-VANSYLrFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 445 GSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEqGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASL 524
Cdd:cd02013 81 GAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYN-NRFVGTELESESFAKIAEACGAKGITVDKPEDVGPAL 159
|
170 180
....*....|....*....|..
gi 1929626685 525 QEII---NRPGPALIHVRIDAE 543
Cdd:cd02013 160 QKAIammAEGKTTVIEIVCDQE 181
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
367-472 |
7.18e-20 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 87.20 E-value: 7.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 367 PLSHYGLINAVAACVDDNAIITTDVG--QHQMWTAQaypLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGD 444
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGtsWFGALDLK---LPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGD 77
|
90 100
....*....|....*....|....*...
gi 1929626685 445 GSLMMNIQEMATASENQLDVKIILMNNE 472
Cdd:cd02005 78 GSFQMTVQELSTMIRYGLNPIIFLINND 105
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
389-484 |
1.32e-16 |
|
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: 78.48 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 389 TDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIIL 468
Cdd:cd02006 29 TTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVL 108
|
90
....*....|....*.
gi 1929626685 469 MNNEALGLVHQQQSLF 484
Cdd:cd02006 109 VNNAYLGLIRQAQRAF 124
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
377-558 |
9.01e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 76.02 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 377 VAACVDDNAIITtDVG--QHQMWTAQayplNRPRQWLTsggLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEM 454
Cdd:PRK06163 23 VAKLKDEEAVIG-GIGntNFDLWAAG----QRPQNFYM---LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 455 AT-ASENQLDVKIILMNNEALGLVHQQQSLfyeqgvfaatYPGKINFMQIAAGFGLETCD-LNNEADPQASLQEIINRPG 532
Cdd:PRK06163 95 GTiAALAPKNLTIIVMDNGVYQITGGQPTL----------TSQTVDVVAIARGAGLENSHwAADEAHFEALVDQALSGPG 164
|
170 180
....*....|....*....|....*.
gi 1929626685 533 PALIHVRIDAEekvypmvpPGAANTE 558
Cdd:PRK06163 165 PSFIAVRIDDK--------PGVGTTE 182
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
374-555 |
1.04e-15 |
|
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: 75.80 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 374 INAVAACVDDNAIITTDVGQ-----HQMWTAQAyplnrPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLM 448
Cdd:cd02003 5 LGALNEAIGDDDVVINAAGSlpgdlHKLWRART-----PGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 449 MNIQEMATASENQLDVKIILMNNEALGLV-HQQQS--------LFY----EQGVFAATYPgKINFMQIAAGFGLETCDLN 515
Cdd:cd02003 80 MLHSEIVTAVQEGLKIIIVLFDNHGFGCInNLQEStgsgsfgtEFRdrdqESGQLDGALL-PVDFAANARSLGARVEKVK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1929626685 516 NEADPQASLQEIINRPGPALIHVridaeeKVYP--MVPPGAA 555
Cdd:cd02003 159 TIEELKAALAKAKASDRTTVIVI------KTDPksMTPGYGS 194
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
19-171 |
3.93e-15 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 72.92 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 19 IVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTAIADA 98
Cdd:cd07037 3 LVEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 99 RLDSIPLICITGQVPASMIGTDAFQEVDTYGISipitkHNYlVRHIEELP------------QVMSDAFRIAQSGRPGPV 166
Cdd:cd07037 83 YYSGVPLLVLTADRPPELRGTGANQTIDQVGLF-----GDY-VRWSVDLPppeddddlwyllRLANRAVLEALSAPPGPV 156
|
....*
gi 1929626685 167 WIDIP 171
Cdd:cd07037 157 HLNLP 161
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
376-540 |
1.08e-14 |
|
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: 72.73 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 376 AVAACV---DDNAII--TTDVGQHQMWTAQAYPLNR-PRQWLTSGGlgtMGFGLPAAIGAALANPDRKVLCFSGDGSLMM 449
Cdd:cd03371 4 AIEIVLsraPATAAVvsTTGMTSRELFELRDRPGGGhAQDFLTVGS---MGHASQIALGIALARPDRKVVCIDGDGAALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 450 NIQEMAT-ASENQLDVKIILMNNEALGLVHQQqslfyeqgvfaATYPGKINFMQIAAGFG----LETCDLNneaDPQASL 524
Cdd:cd03371 81 HMGGLATiGGLAPANLIHIVLNNGAHDSVGGQ-----------PTVSFDVSLPAIAKACGyravYEVPSLE---ELVAAL 146
|
170
....*....|....*.
gi 1929626685 525 QEIINRPGPALIHVRI 540
Cdd:cd03371 147 AKALAADGPAFIEVKV 162
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
23-471 |
5.91e-14 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 74.74 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 23 LEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSgPGATNLVTAIADARLDS 102
Cdd:PLN02573 26 LVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTFT-VGGLSVLNAIAGAYSEN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 103 IPLICITGQvPAS-----------MIGTDAF-QEVDTYGisiPITKHNYLVRHIEELPQVMSDAFRIAQsGRPGPVWIDI 170
Cdd:PLN02573 105 LPVICIVGG-PNSndygtnrilhhTIGLPDFsQELRCFQ---TVTCYQAVINNLEDAHELIDTAISTAL-KESKPVYISV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 171 P---KDVQTAVFEIETQPAMAEKAAAPAFSEESIRDAAA-MINAAKRPVLYlgGGVINAPARVR----ELAEKAQLPTTM 242
Cdd:PLN02573 180 ScnlAAIPHPTFSREPVPFFLTPRLSNKMSLEAAVEAAAeFLNKAVKPVLV--GGPKLRVAKACkafvELADASGYPVAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 243 TLMALGMLPKAHPLSLGMlgMHGVRSTNY---ILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQP 319
Cdd:PLN02573 258 MPSAKGLVPEHHPHFIGT--YWGAVSTPFcaeIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGNGPAF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 320 HVAIQADVDDVLAQLIplveaQPRAEWHQlvaDLQREF-PCPIPKAC---DPLSHYGLINAVAACVDDNAIITTDVGQHq 395
Cdd:PLN02573 336 GCVLMKDFLEALAKRV-----KKNTTAYE---NYKRIFvPEGEPLKSepgEPLRVNVLFKHIQKMLSGDTAVIAETGDS- 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626685 396 mW-TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNN 471
Cdd:PLN02573 407 -WfNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINN 482
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
416-541 |
4.64e-12 |
|
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: 64.62 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 416 LGTMGFGLPAAIGAALANPdRKVLCFSGDGSLMMNIQEMAT-ASENQLDVKIILMNNEALGLVHQQQslfyeqgvfaaTY 494
Cdd:cd03372 41 LGSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGALATiAAEKPKNLIIVVLDNGAYGSTGNQP-----------TH 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1929626685 495 PGK-INFMQIAAGFGLEtcDLNNEADPQASLQEIINR-PGPALIHVRID 541
Cdd:cd03372 109 AGKkTDLEAVAKACGLD--NVATVASEEAFEKAVEQAlDGPSFIHVKIK 155
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
17-171 |
2.02e-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: 62.51 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 17 EFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGkPAVCMACSGPGATNLVTAIA 96
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 97 DARLDSIPLICITGQVPASMIGT-------------DAFQEvdtygISIPITKHNYLVRHIEELPQVMSDAFRIA-QSGR 162
Cdd:cd07038 80 GAYAEHVPVVHIVGAPSTKAQASglllhhtlgdgdfDVFLK-----MFEEITCAAARLTDPENAAEEIDRVLRTAlRESR 154
|
....*....
gi 1929626685 163 pgPVWIDIP 171
Cdd:cd07038 155 --PVYIEIP 161
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
405-542 |
2.97e-09 |
|
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: 55.96 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 405 NRPRQWLTsggLGTMGFGLPAAIGAALANPdRKVLCFSGDGSLMMNIQEMATASE-NQLDVKIILMNNEALGLVHQQQsl 483
Cdd:cd02001 33 DRDGHFYM---LGSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAGEfTPLNLILVVLDNRAYGSTGGQP-- 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1929626685 484 fyeqgvfaaTYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDA 542
Cdd:cd02001 107 ---------TPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLLHAPIAP 156
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
370-538 |
2.40e-08 |
|
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: 55.15 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 370 HYGLINAVAACVD-----DNAIITTDVGQHQMwtAQAYplnrprqWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGD 444
Cdd:COG1013 21 HGIILRLLLKALDelldgDKTVVVSGIGCSSV--APGY-------FNVPGFHTLHGRAAAVATGIKLANPDLTVIVFGGD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 445 GSLM-MNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQGVFAATYPG-----KINFMQIAAGFG---LETCDLN 515
Cdd:COG1013 92 GDTYdIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYgkpepPKDPAEIAAAHGatyVARASVG 171
|
170 180
....*....|....*....|...
gi 1929626685 516 NEADPQASLQEIINRPGPALIHV 538
Cdd:COG1013 172 DPKDLKKKIKKAIEHKGFSFIEV 194
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
365-536 |
2.34e-07 |
|
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: 51.12 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 365 CDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQayPLNRprqwltSGGLGTMGFGLPAAIGAALANPDRKVLCFSGD 444
Cdd:cd02008 7 CPGCPHRPSFYALRKAFKKDSIVSGDIGCYTLGALP--PLNA------IDTCTCMGASIGVAIGMAKASEDKKVVAVIGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 445 GSLMMN-IQEMATASENQLDVKIILMNNEALGLVHQQQSLfyEQGVFAATYPGKINFMQIAAGFGLETCDLNNEAD---P 520
Cdd:cd02008 79 STFFHSgILGLINAVYNKANITVVILDNRTTAMTGGQPHP--GTGKTLTEPTTVIDIEALVRAIGVKRVVVVDPYDlkaI 156
|
170
....*....|....*.
gi 1929626685 521 QASLQEIINRPGPALI 536
Cdd:cd02008 157 REELKEALAVPGVSVI 172
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
417-476 |
1.44e-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: 49.06 E-value: 1.44e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929626685 417 GTMGFGLPAAIGAALANPDRKVLCFSGDGSlMMNI---QEMATASENqLDVKIILMNNEALGL 476
Cdd:cd03375 51 TLHGRALAVATGVKLANPDLTVIVVSGDGD-LAAIggnHFIHAARRN-IDITVIVHNNQIYGL 111
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
417-476 |
1.92e-06 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 49.84 E-value: 1.92e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929626685 417 GTMGFGLPAAIGAALANPDRKVLCFSGDGSLM---MN--IQemaTASENqLDVKIILMNNEALGL 476
Cdd:PRK11867 69 TIHGRALAIATGLKLANPDLTVIVVTGDGDALaigGNhfIH---ALRRN-IDITYILFNNQIYGL 129
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
426-541 |
9.80e-06 |
|
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: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 426 AIGAALANPDRkVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNE-----ALGLVHQQQSLFYEqgVFAAtyPGKINF 500
Cdd:cd02009 60 ALGIALATDKP-TVLLTGDLSFLHDLNGLLLGKQEPLNLTIVVINNNgggifSLLPQASFEDEFER--LFGT--PQGLDF 134
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1929626685 501 MQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRID 541
Cdd:cd02009 135 EHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
412-495 |
3.29e-05 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 45.90 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 412 TSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDG-SLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQGVF 490
Cdd:PRK11866 54 TYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGdGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVK 133
|
....*
gi 1929626685 491 AATYP 495
Cdd:PRK11866 134 TKTTP 138
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
60-126 |
1.33e-04 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 45.23 E-value: 1.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626685 60 EQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVD 126
Cdd:PLN02980 348 ERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAIN 414
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
417-476 |
1.38e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 44.10 E-value: 1.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929626685 417 GTMGFGLPAAIGAALANPDRKVLCFSGDGSLM---MNiQEMATASENqLDVKIILMNNEALGL 476
Cdd:PRK05778 70 TLHGRAIAFATGAKLANPDLEVIVVGGDGDLAsigGG-HFIHAGRRN-IDITVIVENNGIYGL 130
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
418-493 |
1.58e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 43.57 E-value: 1.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626685 418 TMGFGLPAAIGAALANPDRKVLCFSGDG-SLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQGVFAAT 493
Cdd:PRK09628 69 THGRAVAYATGIKLANPDKHVIVVSGDGdGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVT 145
|
|
| CdhB |
COG1880 |
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion]; |
204-307 |
3.88e-04 |
|
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];
Pssm-ID: 441484 Cd Length: 168 Bit Score: 41.47 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 204 AAAMINAAKRPVLYLGGGVINAP---ARVRELAEKAQLPTTMT------LMALGMLPK----AHPLS--LGMLGMHGVRS 268
Cdd:COG1880 22 AAKMIKKAKRPLLIVGPEALDDEellERAIEIAKKAGIPIAATghsikgFVERGVEPAkyinIHELTnfLKDPEWKGLDG 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1929626685 269 T-NYilqeaDLLIVLGARFD--DRAIGKTEQFCPNAKIIHVD 307
Cdd:COG1880 102 NgQY-----DLVIFLGFKYYyaSQVLSGLKHFAPHLKTIAID 138
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
423-538 |
3.41e-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: 39.07 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626685 423 LPAAIGAALANP----DRKVLCFSGDGSLM--MNIQEMATASENQLDVKIILMNNE--ALGLVHQQQSLFYEQGVfaaTY 494
Cdd:cd02007 81 ISAALGMAVARDlkgkKRKVIAVIGDGALTggMAFEALNNAGYLKSNMIVILNDNEmsISPNVGTPGNLFEELGF---RY 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1929626685 495 PGKInfmqiaagfgletcDLNNEADPQASLQEIINRPGPALIHV 538
Cdd:cd02007 158 IGPV--------------DGHNIEALIKVLKEVKDLKGPVLLHV 187
|
|
| |
