|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
7-555 |
0e+00 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 1074.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 7 ISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLIT 86
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 87 ALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPKD 166
Cdd:PRK08978 81 GLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 167 IQLAQVEYKAPLQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKGLGAIAHG 246
Cdd:PRK08978 161 IQLAEGELEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGAVEAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 247 TQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMDGDLRSILTQ 326
Cdd:PRK08978 241 HPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLNALLPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 327 LApQALQIAPWQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHFRRPEDHLSSAG 406
Cdd:PRK08978 321 LQ-QPLNIDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 407 LGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLFFEERYSETDLS 486
Cdd:PRK08978 400 LGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQLFFDERYSETDLS 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525103120 487 DNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWPLVPPGASNCEMMEQTE 555
Cdd:PRK08978 480 DNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDELENVWPLVPPGASNSEMLEKLS 548
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
5-550 |
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: 672.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 5 QKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYD-SQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATN 83
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRqSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 84 LITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDI 163
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 164 PKDIQLAQVEYKAPL--------QAVPDEPELDQaalaeANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVA 235
Cdd:COG0028 161 PKDVQAAEAEEEPAPpelrgyrpRPAPDPEAIEE-----AAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 236 TLKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVA 315
Cdd:COG0028 236 TLMGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 316 MDGDLRSILTQLA----PQALQIAPWQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQ 391
Cdd:COG0028 316 IVGDAKAVLAALLealePRADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAAR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 392 HMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQW 471
Cdd:COG0028 396 YLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQW 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525103120 472 QQLFFEERYSETDLSdNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNvwplvPPGASNCEM 550
Cdd:COG0028 476 QELFYGGRYSGTDLP-NPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN-----PPGATLDEM 548
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
7-550 |
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: 649.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 7 ISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALY-DSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLI 85
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYnDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 86 TALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPK 165
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 166 DIQLAQVEYKAP----LQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKGLG 241
Cdd:TIGR00118 161 DVTTAEIEYPYPekvnLPGYRPTVKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 242 AIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMDGDLR 321
Cdd:TIGR00118 241 SFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGDAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 322 SILTQLAPQALQIAP-----WQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHFR 396
Cdd:TIGR00118 321 NVLEELLKKLFELKErkesaWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 397 RPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLFF 476
Cdd:TIGR00118 401 KPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQWQELFY 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525103120 477 EERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWPLVPPGASNCEM 550
Cdd:TIGR00118 481 EERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVAPGGGLDEM 554
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-551 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 610.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 1 MEQGQKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDS-QVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGP 79
Cdd:PRK08155 7 TSTRKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQStQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 80 GATNLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPV 159
Cdd:PRK08155 87 GATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 160 LVDIPKDIQLAQVEYKA-PLQAVPDE-PELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATL 237
Cdd:PRK08155 167 WIDIPKDVQTAVIELEAlPAPAEKDAaPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 238 KGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMD 317
Cdd:PRK08155 247 MALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 318 GDLRSILTQLAPQ--ALQIAPWQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHF 395
Cdd:PRK08155 327 ADVDDVLAQLLPLveAQPRAEWHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 396 RRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLF 475
Cdd:PRK08155 407 NRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQSLF 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525103120 476 FEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWPLVPPGASNCEMM 551
Cdd:PRK08155 487 YGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYPMVPPGAANTEMI 562
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
5-551 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 606.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 5 QKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALY----DSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPG 80
Cdd:PRK07418 17 QRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYkaeaEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 81 ATNLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVL 160
Cdd:PRK07418 97 ATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 161 VDIPKDIQLAQVEYkaplqaVPDEP------------ELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQR 228
Cdd:PRK07418 177 IDIPKDVGQEEFDY------VPVEPgsvkppgyrptvKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAER 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 229 SGIPSVATLKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGK 308
Cdd:PRK07418 251 FQIPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 309 LRQPDVAMDGDLRSILTQLAPQAL------QIAPWQAEVEHLRAQHQWDYVHPGSLIYAPAML---RRLAnklpSDSVVS 379
Cdd:PRK07418 331 NRRPDVPIVGDVRKVLVKLLERSLepttppRTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLlavRDLA----PDAYYT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 380 CDVGQHQMWVAQHMHfRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILL 459
Cdd:PRK07418 407 TDVGQHQMWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVI 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 460 IDNQKLGMVKQWQQLFFEERYSETDLSDN-PDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVW 538
Cdd:PRK07418 486 INNGWQGMVRQWQESFYGERYSASNMEPGmPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRRDENCY 565
|
570
....*....|...
gi 2525103120 539 PLVPPGASNCEMM 551
Cdd:PRK07418 566 PMVPPGKSNAQMV 578
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
6-551 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 595.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 6 KISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQ-VEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNL 84
Cdd:PRK08527 2 KLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNyFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 85 ITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIP 164
Cdd:PRK08527 82 VTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 165 KDI--QLAQVEYkaplqavPDEPEL---------DQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPS 233
Cdd:PRK08527 162 KDVtaTLGEFEY-------PKEISLktykptykgNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 234 VATLKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPD 313
Cdd:PRK08527 235 VETLMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNAD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 314 VAMDGDLRSILTQLAPQALQI-----APWQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQMW 388
Cdd:PRK08527 315 YPIVGDLKNVLKEMLEELKEEnpttyKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 389 VAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMV 468
Cdd:PRK08527 395 VAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 469 KQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWPLVPPGASNC 548
Cdd:PRK08527 475 RQWQTFFYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLPMVPAGGALY 554
|
...
gi 2525103120 549 EMM 551
Cdd:PRK08527 555 NMI 557
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
2-551 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 590.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 2 EQGQKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALY----DSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATS 77
Cdd:CHL00099 5 LTLREKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELYawekKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 78 GPGATNLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPG 157
Cdd:CHL00099 85 GPGATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 158 PVLVDIPKDIQLAQVEYKAP--------LQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRS 229
Cdd:CHL00099 165 PVLIDIPKDVGLEKFDYYPPepgntiikILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 230 GIPSVATLKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKL 309
Cdd:CHL00099 245 KIPVTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 310 RQPDVAMDGDLRSILTQL---------APQALQIAPWQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLaNKLPSDSVVSC 380
Cdd:CHL00099 325 RIPQVAIVGDVKKVLQELlellknspnLLESEQTQAWRERINRWRKEYPLLIPKPSTSLSPQEVINEI-SQLAPDAYFTT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 381 DVGQHQMWVAQHMHFrRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLI 460
Cdd:CHL00099 404 DVGQHQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIII 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 461 DNQKLGMVKQWQQLFFEERYSETDLSDN-PDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWP 539
Cdd:CHL00099 483 NNKWQGMVRQWQQAFYGERYSHSNMEEGaPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDENCYP 562
|
570
....*....|..
gi 2525103120 540 LVPPGASNCEMM 551
Cdd:CHL00099 563 MVAPGKSNSQMI 574
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
4-551 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 586.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 4 GQKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQ-VEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGAT 82
Cdd:PRK07789 28 PERMTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTkVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 83 NLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVD 162
Cdd:PRK07789 108 NLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 163 IPKDIQLAQVEYKAPlqavpdePELD-----------QAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGI 231
Cdd:PRK07789 188 IPKDALQAQTTFSWP-------PRMDlpgyrpvtkphGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 232 PSVATLKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQ 311
Cdd:PRK07789 261 PVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRH 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 312 PDVAMDGDLRSILTQLAPqALQ----------IAPWQAEVEHLRAQHQWDYVHP--GSLiyAP-AMLRRLANKLPSDSVV 378
Cdd:PRK07789 341 ADVPIVGDVKEVIAELIA-ALRaehaaggkpdLTAWWAYLDGWRETYPLGYDEPsdGSL--APqYVIERLGEIAGPDAIY 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 379 SCDVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKIL 458
Cdd:PRK07789 418 VAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVA 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 459 LIDNQKLGMVKQWQQLFFEERYSETDLSDN----PDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKG-PfllhVAID- 532
Cdd:PRK07789 498 LINNGNLGMVRQWQTLFYEERYSNTDLHTHshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAINDrP----VVIDf 573
|
570 580
....*....|....*....|...
gi 2525103120 533 ----DAFnVWPLVPPGASNCEMM 551
Cdd:PRK07789 574 vvgkDAM-VWPMVAAGTSNDEIQ 595
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
4-551 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 568.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 4 GQKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALY-DSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGAT 82
Cdd:PRK09107 8 PRQMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFqQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 83 NLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVD 162
Cdd:PRK09107 88 NAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 163 IPKDIQLAQVEYKAPLQAVPD---EPEL--DQAALAEANALLAAARQPMLYV--GGGVGMAGAVEPLRAFIQRSGIPSVA 235
Cdd:PRK09107 168 IPKDVQFATGTYTPPQKAPVHvsyQPKVkgDAEAITEAVELLANAKRPVIYSggGVINSGPEASRLLRELVELTGFPITS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 236 TLKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVA 315
Cdd:PRK09107 248 TLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 316 MDGDLRSILTQL---------APQALQIAPWQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRL-ANKLPSDSVVSCDVGQH 385
Cdd:PRK09107 328 IIGDVGHVLEDMlrlwkargkKPDKEALADWWGQIARWRARNSLAYTPSDDVIMPQYAIQRLyELTKGRDTYITTEVGQH 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 386 QMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKL 465
Cdd:PRK09107 408 QMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYM 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 466 GMVKQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWPLVPPGA 545
Cdd:PRK09107 488 GMVRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFPMIPSGK 567
|
....*.
gi 2525103120 546 SNCEMM 551
Cdd:PRK09107 568 AHNEML 573
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
2-555 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 567.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 2 EQGQKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGA 81
Cdd:PRK06048 3 GSTEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 82 TNLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLV 161
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 162 DIPKDIQLAQVEYKAP----LQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATL 237
Cdd:PRK06048 163 DLPKDVTTAEIDFDYPdkveLRGYKPTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 238 KGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMD 317
Cdd:PRK06048 243 MGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPIV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 318 GDLRSILTQL--APQALQIAPWQAEVEHLRAQHQWDYVHPGSLIyAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHF 395
Cdd:PRK06048 323 GDAKQVLKSLikYVQYCDRKEWLDKINQWKKEYPLKYKEREDVI-KPQYVIEQIYELCPDAIIVTEVGQHQMWAAQYFKY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 396 RRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLF 475
Cdd:PRK06048 402 KYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQWQELF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 476 FEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWPLVPPGASNCEMMEQTE 555
Cdd:PRK06048 482 YDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSPMVPAGAAINEILDLEE 561
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
9-545 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 560.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 9 GSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITAL 88
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 89 ADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPKDIQ 168
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 169 LAQV-EYKAPLQAVPDEPELDQAAL------AEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKGLG 241
Cdd:PRK06276 163 EGELdLEKYPIPAKIDLPGYKPTTFghplqiKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLMGKG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 242 AIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMDGD-- 319
Cdd:PRK06276 243 AFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVGDak 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 320 --LRSILTQLAPQALQ-IAPWQAEVEHLRAQH--QWDY----VHPGSLIyaPAMLRRLANKLP-SDSVVSCDVGQHQMWV 389
Cdd:PRK06276 323 nvLRDLLAELMKKEIKnKSEWLERVKKLKKESipRMDFddkpIKPQRVI--KELMEVLREIDPsKNTIITTDVGQNQMWM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 390 AQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVK 469
Cdd:PRK06276 401 AHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVY 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525103120 470 QWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAfNVWPLVPPGA 545
Cdd:PRK06276 481 QWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPA-EALPMVPPGG 555
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
3-551 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 556.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 3 QGQKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGAT 82
Cdd:PRK06725 11 QCEEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 83 NLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVD 162
Cdd:PRK06725 91 NLVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLID 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 163 IPKDIQLAQVEYKAP----LQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLK 238
Cdd:PRK06725 171 IPKDVQNEKVTSFYNevveIPGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 239 GLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMDG 318
Cdd:PRK06725 251 GLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 319 DLRSILTQLAPQAL--QIAPWQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHFR 396
Cdd:PRK06725 331 DVKKALHMLLHMSIhtQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 397 RPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLFF 476
Cdd:PRK06725 411 NPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEMFY 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525103120 477 EERYSETDLSdNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWPLVPPGASNCEMM 551
Cdd:PRK06725 491 ENRLSESKIG-SPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFPMVPPNKGNNEMI 564
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
2-550 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 537.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 2 EQGQKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGA 81
Cdd:PRK07710 11 TEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 82 TNLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLV 161
Cdd:PRK07710 91 TNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 162 DIPKDIQLAQVE--YKAPLQAVPDEP--ELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATL 237
Cdd:PRK07710 171 DIPKDMVVEEGEfcYDVQMDLPGYQPnyEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 238 KGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMD 317
Cdd:PRK07710 251 LGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 318 GDLRSILTQLAPQA----------LQIAPWQAEVEhLRAQHQWDYVHPGSLIyapAMLRRLANklpSDSVVSCDVGQHQM 387
Cdd:PRK07710 331 ADAKQALQVLLQQEgkkenhhewlSLLKNWKEKYP-LSYKRNSESIKPQKAI---EMLYEITK---GEAIVTTDVGQHQM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 388 WVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGM 467
Cdd:PRK07710 404 WAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGM 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 468 VKQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWPLVPPGASN 547
Cdd:PRK07710 484 VRQWQEEFYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMPMVAPGKGL 563
|
...
gi 2525103120 548 CEM 550
Cdd:PRK07710 564 HEM 566
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
9-546 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 537.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 9 GSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQ-VEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITA 87
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNcIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 88 LADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPKDI 167
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 168 Q--LAQVEYKAP---------LQAVPDEPELDQaalaeANALLAAARQPMLYvgGGVGMAGAVEPLRAFIQRSGIPSVAT 236
Cdd:PLN02470 175 QqqLAVPNWNQPmklpgylsrLPKPPEKSQLEQ-----IVRLISESKRPVVY--VGGGCLNSSEELREFVELTGIPVAST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 237 LKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAM 316
Cdd:PLN02470 248 LMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 317 DGD-------LRSILTQLAPQALQIAPWQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQMWV 389
Cdd:PLN02470 328 CADvklalqgLNKLLEERKAKRPDFSAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVGQHQMWA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 390 AQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVK 469
Cdd:PLN02470 408 AQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVV 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 470 QWQQLFFEERYSETDLSDN-------PDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWPLVP 542
Cdd:PLN02470 488 QWEDRFYKANRAHTYLGDPdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLPMIP 567
|
....
gi 2525103120 543 PGAS 546
Cdd:PLN02470 568 GGGT 571
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
5-556 |
1.19e-164 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 480.40 E-value: 1.19e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 5 QKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALY-DSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATN 83
Cdd:PRK06466 2 ELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFkQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 84 LITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDI 163
Cdd:PRK06466 82 AITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 164 PKDIQ--LAQVEY----KAPLQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATL 237
Cdd:PRK06466 162 PKDMTnpAEKFEYeypkKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 238 KGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMD 317
Cdd:PRK06466 242 MGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 318 GDLRSILTQL---------APQALQIAPWQAEVEHLRAQHQ-WDYVHP-GSLIYAPAMLRRLANKLPSDSVVSCDVGQHQ 386
Cdd:PRK06466 322 GPVESVLTEMlailkeigeKPDKEALAAWWKQIDEWRGRHGlFPYDKGdGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 387 MWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLG 466
Cdd:PRK06466 402 MFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 467 MVKQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFL-LHVAIDDAFNVWPLVPPGA 545
Cdd:PRK06466 482 MVRQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAMKDRLVfIDIYVDRSEHVYPMQIADG 561
|
570
....*....|..
gi 2525103120 546 SNCEM-MEQTEK 556
Cdd:PRK06466 562 SMRDMwLSKTER 573
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
8-551 |
1.52e-164 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 479.70 E-value: 1.52e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 8 SGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQ-VEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLIT 86
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEgIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 87 ALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPKD 166
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 167 IQLAQV-EYKAPLQAVPD-----EPELDQaaLAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKGL 240
Cdd:PRK07282 171 VSALETdFIYDPEVNLPSyqptlEPNDMQ--IKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 241 GAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMDGDL 320
Cdd:PRK07282 249 GTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 321 RSILTQL--APQA-LQIAPWQAEVEHLRAQHQWdYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHFRR 397
Cdd:PRK07282 329 KKALQMLlaEPTVhNNTEKWIEKVTKDKNRVRS-YDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 398 PEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLFFE 477
Cdd:PRK07282 408 ERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESFYE 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525103120 478 ERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALdEMLSAKGPFLLHVAIDDAFNVWPLVPPGASNCEMM 551
Cdd:PRK07282 488 GRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDL-EVITEDVPMLIEVDISRKEHVLPMVPAGKSNHEML 560
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
5-555 |
6.86e-164 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 478.91 E-value: 6.86e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 5 QKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALY-DSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATN 83
Cdd:PRK06965 19 ADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYkQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 84 LITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDI 163
Cdd:PRK06965 99 AVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 164 PKDIQLAQVEYKAP----LQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKG 239
Cdd:PRK06965 179 PKDVSKTPCEYEYPksveMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 240 LGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKA-KVIHLDIDAAELGKLRQPDVAMDG 318
Cdd:PRK06965 259 LGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRVKVDIPIVG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 319 DLRSILTQL---------APQALQIAPWQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQMWV 389
Cdd:PRK06965 339 DVKEVLKELieqlqtaehGPDADALAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMWA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 390 AQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVK 469
Cdd:PRK06965 419 AQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMVR 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 470 QWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKG-PFLLHVAIDDAFNVWPLVPPGASNC 548
Cdd:PRK06965 499 QWQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRLKDrTVFLDFQTDPTENVWPMVQAGKGIT 578
|
....*..
gi 2525103120 549 EMMEQTE 555
Cdd:PRK06965 579 EMLLGSE 585
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
5-556 |
4.03e-159 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 466.22 E-value: 4.03e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 5 QKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYD-SQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATN 83
Cdd:PRK08979 2 EMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEkSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 84 LITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDI 163
Cdd:PRK08979 82 TITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 164 PKDIQLAQV--EYKAP----LQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATL 237
Cdd:PRK08979 162 PKDCLNPAIlhPYEYPesikMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 238 KGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMD 317
Cdd:PRK08979 242 MGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 318 GD----LRSILTQLAPQ-----ALQIAPWQAEVEHLRAQHQWDY------VHPGSLIYApamLRRLANklpSDSVVSCDV 382
Cdd:PRK08979 322 GSadkvLDSMLALLDESgetndEAAIASWWNEIEVWRSRNCLAYdksserIKPQQVIET---LYKLTN---GDAYVASDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 383 GQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDN 462
Cdd:PRK08979 396 GQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 463 QKLGMVKQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFL-LHVAIDDAFNVWPLV 541
Cdd:PRK08979 476 RFLGMVKQWQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRLVfVDINVDETEHVYPMQ 555
|
570
....*....|....*.
gi 2525103120 542 PPGASNCEM-MEQTEK 556
Cdd:PRK08979 556 IRGGAMNEMwLSKTER 571
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
5-551 |
1.83e-154 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 454.37 E-value: 1.83e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 5 QKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYD-SQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATN 83
Cdd:PRK06882 2 KKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 84 LITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDI 163
Cdd:PRK06882 82 AITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 164 PKDIqlAQVEYKAPLQaVPDEPEL---------DQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSV 234
Cdd:PRK06882 162 PKDM--VNPANKFTYE-YPEEVSLrsynptvqgHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 235 ATLKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDV 314
Cdd:PRK06882 239 SSLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 315 AMDGDLRSILTQ---------LAPQALQIAPWQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQH 385
Cdd:PRK06882 319 PIVGSAKNVLEEflslleeenLAKSQTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 386 QMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKL 465
Cdd:PRK06882 399 QMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 466 GMVKQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFL-LHVAIDDAFNVWPLVPPG 544
Cdd:PRK06882 479 GMVKQWQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKLVfVDVNVDETEHVYPMQIRG 558
|
....*..
gi 2525103120 545 ASNCEMM 551
Cdd:PRK06882 559 GAMNEMI 565
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
7-556 |
3.39e-148 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 438.13 E-value: 3.39e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 7 ISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYD-SQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLI 85
Cdd:PRK07979 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 86 TALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPK 165
Cdd:PRK07979 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 166 DIqlAQVEYKAPLqAVPDEPEL---------DQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVAT 236
Cdd:PRK07979 164 DI--LNPANKLPY-VWPESVSMrsynpttqgHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 237 LKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAM 316
Cdd:PRK07979 241 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 317 DGDLRSILTQLAPQALQIAP---------WQAEVEHLRAQHQWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQM 387
Cdd:PRK07979 321 VGDARQVLEQMLELLSQESAhqpldeirdWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 388 WVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGM 467
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 468 VKQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVE----QALDEMLSAKGPFlLHVAIDDAFNVWPLVPP 543
Cdd:PRK07979 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELEsklsEALEQVRNNRLVF-VDVTVDGSEHVYPMQIR 559
|
570
....*....|....
gi 2525103120 544 GASNCEM-MEQTEK 556
Cdd:PRK07979 560 GGGMDEMwLSKTER 573
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
7-551 |
6.88e-128 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 386.12 E-value: 6.88e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 7 ISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDA----LYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGAT 82
Cdd:PRK06456 2 PTGARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 83 NLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVD 162
Cdd:PRK06456 82 NLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 163 IPKDIQLAQVE-YKAPLQAV-----PDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVAT 236
Cdd:PRK06456 162 IPRDIFYEKMEeIKWPEKPLvkgyrDFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 237 LKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDR-VTGRLESFASKAKVIHLDIDAAELGKLRQPDVA 315
Cdd:PRK06456 242 FPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRtFTSYDEMVETRKKFIMVNIDPTDGEKAIKVDVG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 316 MDGDLRSILTQLAPQALQIA------PWQAEVEHLRAQHQWDYVHPGSLIYAP-AMLRRLANKLPSDSVVSCDVGQHQMW 388
Cdd:PRK06456 322 IYGNAKIILRELIKAITELGqkrdrsAWLKRVKEYKEYYSQFYYTEENGKLKPwKIMKTIRQALPRDAIVTTGVGQHQMW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 389 VAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMV 468
Cdd:PRK06456 402 AEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 469 KQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNVWPLVPPGASNC 548
Cdd:PRK06456 482 RQVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALPTLPPGGRLK 561
|
...
gi 2525103120 549 EMM 551
Cdd:PRK06456 562 QVI 564
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
9-532 |
2.14e-106 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 329.87 E-value: 2.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 9 GSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITAL 88
Cdd:PRK08322 3 AADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 89 ADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPKDIQ 168
Cdd:PRK08322 83 AYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 169 LAQVEYKaPLQAVPDEPEL-DQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKGLGAIAHGT 247
Cdd:PRK08322 163 AEETDGK-PLPRSYSRRPYaSPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVIPETH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 248 QGYLGMLGMHGNKAANLAVQQCDLLLVVGarFDdrvtgrLESFA-------SKAKVIHLDIDAAELGKLRQPDVAMDGD- 319
Cdd:PRK08322 242 PLSLGTAGLSQGDYVHCAIEHADLIINVG--HD------VIEKPpffmnpnGDKKVIHINFLPAEVDPVYFPQVEVVGDi 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 320 ---LRSILTQLAPQALQIAPWQAEV-EHLRAQHQwDYVH-------PGSLIYApamLRRLankLPSDSVVSCDVGQHQMW 388
Cdd:PRK08322 314 ansLWQLKERLADQPHWDFPRFLKIrEAIEAHLE-EGADddrfpmkPQRIVAD---LRKV---MPDDDIVILDNGAYKIW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 389 VAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMV 468
Cdd:PRK08322 387 FARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525103120 469 KqWQQ--LFFEERYseTDLSdNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAID 532
Cdd:PRK08322 467 R-WKQenMGFEDFG--LDFG-NPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVD 528
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
9-532 |
6.64e-100 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 313.35 E-value: 6.64e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 9 GSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLS-RHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITA 87
Cdd:PRK08199 10 GGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVcRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 88 LADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAE---ELVAtlyRAFEIAASGRPGPVLVDIP 164
Cdd:PRK08199 90 VHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAAripELVS---RAFHVATSGRPGPVVLALP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 165 KDI--QLAQVEYKAPLQAVPDEPELDQaaLAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKGLGA 242
Cdd:PRK08199 167 EDVlsETAEVPDAPPYRRVAAAPGAAD--LARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 243 IAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGR---LESFASKAKVIHLDIDAAELGKLRQPDVAMDGD 319
Cdd:PRK08199 245 FDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELGRVYRPDLAIVAD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 320 LRSILTQLAP-QALQIAPWQAEVEHLRAQH-QWDYVH--PGSLIYAPAMlRRLANKLPSDSVVSCDVGQHQMWVAQHMHF 395
Cdd:PRK08199 325 PAAFAAALAAlEPPASPAWAEWTAAAHADYlAWSAPLpgPGAVQLGEVM-AWLRERLPADAIITNGAGNYATWLHRFFRF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 396 RRPEDHLSSAGlGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLF 475
Cdd:PRK08199 404 RRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTIRMHQERE 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525103120 476 FEERYSETDLsDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAID 532
Cdd:PRK08199 483 YPGRVSGTDL-TNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRID 538
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
359-544 |
1.29e-99 |
|
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: 299.41 E-value: 1.29e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 359 IYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSF 438
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 439 MMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEM 518
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|....*.
gi 2525103120 519 LSAKGPFLLHVAIDDAFNVWPLVPPG 544
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLPMVPPG 186
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
6-544 |
6.01e-94 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 297.31 E-value: 6.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 6 KISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDS--QVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATN 83
Cdd:PRK08266 3 TMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAgdRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 84 LITALADALLDSVPLVAITGQVSTSVIGTDAFQ--EM-DVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVL 160
Cdd:PRK08266 83 AGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 161 VDIPKDI--QLAQVEYKAPLQAVPdEPELDQAALAEANALLAAARQPMLYVGGGVGMAGavEPLRAFIQRSGIPSVATLK 238
Cdd:PRK08266 163 LEMPWDVfgQRAPVAAAPPLRPAP-PPAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAG--EEIRELAEMLQAPVVAFRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 239 GLGAIAHGTQGYLGMLgmhgnkAANLAVQQCDLLLVVGARFDDRVTgRLESFASKAKVIHLDIDAAELGKLrQPDVAMDG 318
Cdd:PRK08266 240 GRGIVSDRHPLGLNFA------AAYELWPQTDVVIGIGSRLELPTF-RWPWRPDGLKVIRIDIDPTEMRRL-KPDVAIVA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 319 D----LRSILTQLAPQALQIAPWQAEVEHL--RAQHQWDYVHPGSliyapAMLRRLANKLPSDSVV---SCDVGqHQMWV 389
Cdd:PRK08266 312 DakagTAALLDALSKAGSKRPSRRAELRELkaAARQRIQAVQPQA-----SYLRAIREALPDDGIFvdeLSQVG-FASWF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 390 AQHMHfrRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVK 469
Cdd:PRK08266 386 AFPVY--APRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVR 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525103120 470 QWQQLFFEERYSETDLsDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAI--DDAFNVWPLVPPG 544
Cdd:PRK08266 464 RDQKRRFGGRVVASDL-VNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVprGSEASPWPFIHPA 539
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
5-538 |
5.57e-92 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 292.53 E-value: 5.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 5 QKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNL 84
Cdd:PRK08617 3 KKKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 85 ITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIP 164
Cdd:PRK08617 83 ATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 165 KDIQLAQVEYKA------PLQAVPDEPELDqaalaEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLK 238
Cdd:PRK08617 163 QDVVDAPVTSKAiaplskPKLGPASPEDIN-----YLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 239 GLGAIAHGTQG-YLGMLGMHGNKAANLAVQQCDLLLVVGarFD----DrvtGRLESFASKAKVIHLDIDAAELGKLRQPD 313
Cdd:PRK08617 238 AAGVISRELEDhFFGRVGLFRNQPGDELLKKADLVITIG--YDpieyE---PRNWNSEGDATIIHIDVLPAEIDNYYQPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 314 VAMDGDLRSILTQLAPQ--ALQIAP-WQAEVEHLRAQ----------HQWDYVHPGSLIYApamlrrLANKLPSDSVVSC 380
Cdd:PRK08617 313 RELIGDIAATLDLLAEKldGLSLSPqSLEILEELRAQleelaerparLEEGAVHPLRIIRA------LQDIVTDDTTVTV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 381 DVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLP-VKILL 459
Cdd:PRK08617 387 DVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNiVHIIW 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 460 IDNqKLGMVKqwqqlFFEE----RYSETDLSDnPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAF 535
Cdd:PRK08617 467 NDG-HYNMVE-----FQEEmkygRSSGVDFGP-VDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSD 539
|
...
gi 2525103120 536 NVW 538
Cdd:PRK08617 540 NIK 542
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
9-537 |
2.23e-91 |
|
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: 290.50 E-value: 2.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 9 GSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITAL 88
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 89 ADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPKDIQ 168
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 169 LAQVEYK------APLQAVPDEPELDQaalaeANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKGLGA 242
Cdd:TIGR02418 161 DSPVSVKaipasyAPKLGAAPDDAIDE-----VAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQGAGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 243 IAHGTQG-YLGMLGMHGNKAANLAVQQCDLLLVVGarFDD-RVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMDGDL 320
Cdd:TIGR02418 236 VSRELEDhFFGRVGLFRNQPGDRLLKQADLVITIG--YDPiEYEPRNWNSENDATIVHIDVEPAQIDNNYQPDLELVGDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 321 RSIL---------TQLAPQALQI-APWQAEVEHL---RAQHQWDYVHPGSLIyapamlRRLANKLPSDSVVSCDVGQHQM 387
Cdd:TIGR02418 314 ASTLdllaeripgYELPPDALAIlEDLKQQREALdrvPATLKQAHLHPLEII------KAMQAIVTDDVTVTVDMGSHYI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 388 WVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLP-VKILLIDNqKLG 466
Cdd:TIGR02418 388 WMARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNiVHIIWNDN-GYN 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525103120 467 MVKqWQQLFFEERYSETDLSdNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNV 537
Cdd:TIGR02418 467 MVE-FQEEMKYQRSSGVDFG-PIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYSDNP 535
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
6-544 |
4.00e-88 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 283.05 E-value: 4.00e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 6 KISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDAL--YDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATN 83
Cdd:PRK08611 3 KIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 84 LITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRpGPVLVDI 163
Cdd:PRK08611 83 LLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVLTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 164 PKDIqLAQVEYKAPLQAV----PDEPELDQAALAEANALLAAARQPMLyvGGGVGMAGAVEPLRAFIQRSGIPSVATLKG 239
Cdd:PRK08611 162 PDDL-PAQKIKDTTNKTVdtfrPTVPSPKPKDIKKAAKLINKAKKPVI--LAGLGAKHAKEELLAFAEKAKIPIIHTLPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 240 LGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRvtgrlESFASKAKVIHLDIDAAELGKLRQPDVAMDGD 319
Cdd:PRK08611 239 KGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV-----DYLPKKAKAIQIDTDPANIGKRYPVNVGLVGD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 320 LRSILTQLAP-----------QALQ--IAPWQAEVEHLRAQHQwdyvHPgslIYAPAMLRRLANKLPSDSVVSCDVGQHQ 386
Cdd:PRK08611 314 AKKALHQLTEnikhvedrrflEACQenMAKWWKWMEEDENNAS----TP---IKPERVMAAIQKIADDDAVLSVDVGTVT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 387 MWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLG 466
Cdd:PRK08611 387 VWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLA 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525103120 467 MVKQWQQLFFEERYsETDLSDnPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDafNVWPLvpPG 544
Cdd:PRK08611 467 FIKYEQQAAGELEY-AIDLSD-MDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDP--NAAPL--PG 538
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
11-517 |
1.15e-84 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 274.55 E-value: 1.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 11 EAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDS-QVEHLLSRHEQGAAFAAVGYARSS-GKTGVCLATSGPGATNLITAL 88
Cdd:PRK11269 8 DAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHgGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 89 ADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPKDIQ 168
Cdd:PRK11269 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDVQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 169 LAQVEYK----APLQavPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKGLGAIA 244
Cdd:PRK11269 168 VAEIEFDpdtyEPLP--VYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMGWGAIP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 245 HGTQGYLGMLGMH-GNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMDGDLRSI 323
Cdd:PRK11269 246 DDHPLMAGMVGLQtSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIVSDAKAA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 324 LTQL--APQALQIA-------PWQAEVEHLRA--QHQWDYVH-PgslIYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQ 391
Cdd:PRK11269 326 LELLveVAREWKAAgrlpdrsAWVADCQERKRtlLRKTHFDNvP---IKPQRVYEEMNKAFGRDTCYVSTIGLSQIAAAQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 392 HMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQW 471
Cdd:PRK11269 403 FLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQA 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2525103120 472 Q---------QLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDE 517
Cdd:PRK11269 483 QrafdmdycvQLAFENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALEQ 537
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
8-532 |
5.76e-79 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 258.22 E-value: 5.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 8 SGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITA 87
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 88 LADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRpGPVLVDIPKDI 167
Cdd:PRK06457 83 LYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 168 QLAQVEYKA----PLQAVPDEPELDQaalaeANALLAAARQPMLYvgGGVGMAGAVEPLRAFIQRSGIPSVATLKGLGAI 243
Cdd:PRK06457 162 LRKSSEYKGskntEVGKVKYSIDFSR-----AKELIKESEKPVLL--IGGGTRGLGKEINRFAEKIGAPIIYTLNGKGIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 244 AHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDdrvtgrLESFASK-AKVIHLDIDAAELGKLRQPDVAMDGDLRS 322
Cdd:PRK06457 235 PDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFP------YVNFLNKsAKVIQVDIDNSNIGKRLDVDLSYPIPVAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 323 ILtQLAPQAL----------QIAPWQAEVEHLraqhQWDYVHPgslIYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQH 392
Cdd:PRK06457 309 FL-NIDIEEKsdkfyeelkgKKEDWLDSISKQ----ENSLDKP---MKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARH 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 393 MHFRRPEDHLSSAGLGTMGFGLPAAIGAQMA-RPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKqw 471
Cdd:PRK06457 381 FRASGEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIK-- 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525103120 472 qqlfFEER---YSE--TDLSdNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAID 532
Cdd:PRK06457 459 ----FEQEvmgYPEwgVDLY-NPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVD 519
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
6-522 |
1.06e-76 |
|
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: 253.25 E-value: 1.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 6 KISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLI 85
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 86 TALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRpGPVLVDIPK 165
Cdd:TIGR03457 81 TAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 166 DIQLAQVEYKAPLQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKGLGAIAH 245
Cdd:TIGR03457 160 DYFYGEIDVEIPRPVRLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDSFPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 246 GTQGYLGMLGMHGNKAANLAVQQCDLLLVVGAR---FDDRVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMDGDLR- 321
Cdd:TIGR03457 240 SHPLWVGPLGYQGSKAAMKLISDADVVLALGTRlgpFGTLPQYGIDYWPKNAKIIQVDANAKMIGLVKKVTVGICGDAKa 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 322 ---SILTQLAPQALQI-------------APWQAEVE---HLRAQHQWDYV-----HPGSLIYAPAMLRRLANKLPSDSV 377
Cdd:TIGR03457 320 aaaEILQRLAGKAGDAnraerkakiqaerSAWEQELSemtHERDPFSLDMIveqrqEEGNWLHPRQVLRELEKAMPEDAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 378 VSCDVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKI 457
Cdd:TIGR03457 400 VSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIPVTA 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525103120 458 LLIDNQKLGMVKQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAK 522
Cdd:TIGR03457 480 VVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQ 544
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
5-529 |
5.20e-73 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 242.59 E-value: 5.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 5 QKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYD-SQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATN 83
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRrGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 84 LITALADALLDSVPLVAITGQVSTSVIGTDA--FQEM-DVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVL 160
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 161 VDIPKDIQLAQVEYKAPLQAVPDE-PELDQAALAEANALLAAARQPMLYvgGGVGMAGAVEPLRAFIQRsGIPSVATLKG 239
Cdd:PRK07064 161 VEIPIDIQAAEIELPDDLAPVHVAvPEPDAAAVAELAERLAAARRPLLW--LGGGARHAGAEVKRLVDL-GFGVVTSTQG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 240 LGAIAHGTQGYLGMLGMHgnKAANLAVQQCDLLLVVGARFDDRVTGRLEsFASKAKVIHLDIDAAELGKLRQPDVAMDGD 319
Cdd:PRK07064 238 RGVVPEDHPASLGAFNNS--AAVEALYKTCDLLLVVGSRLRGNETLKYS-LALPRPLIRVDADAAADGRGYPNDLFVHGD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 320 LRSILTQLA---PQALQIAP-WQAEVEHLRAQ---HQWDYVHPGSLIyaPAMLRRLankLPSDSVVSCDVG-QHQMWVAQ 391
Cdd:PRK07064 315 AARVLARLAdrlEGRLSVDPaFAADLRAAREAavaDLRKGLGPYAKL--VDALRAA---LPRDGNWVRDVTiSNSTWGNR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 392 HMHFRRPEDHLSSAGlGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQW 471
Cdd:PRK07064 390 LLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNI 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525103120 472 QQLFFEERYSETDLSdNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHV 529
Cdd:PRK07064 469 QDAQYGGRRYYVELH-TPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
11-535 |
1.02e-72 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 241.42 E-value: 1.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 11 EAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITALAD 90
Cdd:PRK07524 6 EALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 91 ALLDSVPLVAITGQVSTSVIGTD--AFQEM-DVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPKDI 167
Cdd:PRK07524 86 AYADSIPMLVISSVNRRASLGKGrgKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLDV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 168 QLAQVEYKAPL-QAVPDEPELDQAALAEANALLAAARQPMLyvGGGVGMAGAVEPLRAFIQRSGIPSVATLKGLGAIAHG 246
Cdd:PRK07524 166 LAAPADHLLPApPTRPARPGPAPAALAQAAERLAAARRPLI--LAGGGALAAAAALRALAERLDAPVALTINAKGLLPAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 247 TQGYLGmlGMHGNKAANLAVQQCDLLLVVG---ARFDDRVTGRlESFASKAKVIHLDIDAAELGKLRQPDVAMDGD---- 319
Cdd:PRK07524 244 HPLLLG--ASQSLPAVRALIAEADVVLAVGtelGETDYDVYFD-GGFPLPGELIRIDIDPDQLARNYPPALALVGDaraa 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 320 LRSILTQLAPQALQIAPWQAEVEHLR--AQHQWDyvhPGSLIYApAMLRRLANKLPSDSVVScDVGQhQMWVAQHMH-FR 396
Cdd:PRK07524 321 LEALLARLPGQAAAADWGAARVAALRqaLRAEWD---PLTAAQV-ALLDTILAALPDAIFVG-DSTQ-PVYAGNLYFdAD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 397 RPEDHL-SSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQwqqlF 475
Cdd:PRK07524 395 APRRWFnASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRR----Y 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525103120 476 FEERYSE---TDLSdNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAF 535
Cdd:PRK07524 471 MVARDIEpvgVDPY-TPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQACWF 532
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
5-522 |
1.79e-72 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 242.21 E-value: 1.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 5 QKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNL 84
Cdd:PRK07525 4 MKMTPSEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 85 ITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRpGPVLVDIP 164
Cdd:PRK07525 84 VTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 165 KD-------IQLAQ-VEYKAP---LQAVPDEPELdqaalaeanalLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPs 233
Cdd:PRK07525 163 RDyfygvidVEIPQpVRLERGaggEQSLAEAAEL-----------LSEAKFPVILSGAGVVLSDAIEECKALAERLDAP- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 234 VATlkglgaiahgtqGYL-------------GMLGMHGNKAANLAVQQCDLLLVVGARFDdrVTGRL-----ESFASKAK 295
Cdd:PRK07525 231 VAC------------GYLhndafpgshplwvGPLGYNGSKAAMELIAKADVVLALGTRLN--PFGTLpqygiDYWPKDAK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 296 VIHLDIDAAELGKLRQPDVAMDGDL----RSILTQLAPQ--------------ALQIAPWQAEVEHL------------- 344
Cdd:PRK07525 297 IIQVDINPDRIGLTKKVSVGICGDAkavaRELLARLAERlagdagreerkaliAAEKSAWEQELSSWdhedddpgtdwne 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 345 RAQHQW-DYVHPGSliyapaMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMA 423
Cdd:PRK07525 377 EARARKpDYMHPRQ------ALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 424 RPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGR 503
Cdd:PRK07525 451 CPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGV 530
|
570
....*....|....*....
gi 2525103120 504 TIYSADEVEQALDEMLSAK 522
Cdd:PRK07525 531 VVDTQEELGPALKRAIDAQ 549
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
9-534 |
1.67e-71 |
|
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: 239.35 E-value: 1.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 9 GSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQ--VEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLIT 86
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAERdrIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 87 ALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEiAASGRPGPVLVDIPKD 166
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIR-RAYAHNGVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 167 IQLAQVE----YKAPLQA-VPDEPELDQAALAEANALLAAARQPMLYvgGGVGMAGAVEPLRAFIQRSGIPSVATLKGLG 241
Cdd:TIGR02720 160 FGWQEIPdndyYASSVSYqTPLLPAPDVEAVTRAVQTLKAAERPVIY--YGIGARKAGEELEALSEKLKIPLISTGLAKG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 242 AIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDdrVTGRLESFASKAKVIHLDIDAAELGKLRQPDVAMDGD-- 319
Cdd:TIGR02720 238 IIEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYP--FAEVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADak 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 320 --LRSILTQLAPQAlQIAPWQAEVEHLRAQHQW----DYVHPGSLIYAPAMlrRLANKLPS-DSVVSCDVGQHQMWVAQH 392
Cdd:TIGR02720 316 kaLAAILAQVEPRE-STPWWQANVANVKNWRAYlaslEDKTEGPLQAYQVY--RAINKIAEdDAIYSIDVGDININSNRH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 393 MHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQwQ 472
Cdd:TIGR02720 393 LKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKD-E 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525103120 473 QLFFEERYSETDLSDnPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKG--PFLLHVAIDDA 534
Cdd:TIGR02720 472 QEDTNQPLIGVDFND-ADFAKIAEGVGAVGFRVNKIEQLPAVFEQAKAIKQgkPVLIDAKITGD 534
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
11-165 |
2.86e-70 |
|
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: 222.41 E-value: 2.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 11 EAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITALAD 90
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525103120 91 ALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPK 165
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
10-543 |
8.57e-66 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 224.79 E-value: 8.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 10 SEAVIKVLAAHGVNTVFGYPGGAIMPIYDAL--YDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITA 87
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALgrADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 88 LADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMsLSCTKHSF--MVTRAEELVATLYRAFEIAASGRpGPVLVDIPK 165
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSL-FKDVAGAFvqMVTVPEQLRHLVDRAVRTALAER-TVTAVILPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 166 DIQlaQVEYKAPLQA---------------VPDEPELDQaalaEANALLAAARQPMLyvgGGVGMAGAVEPLRAFIQRSG 230
Cdd:PRK08273 164 DVQ--ELEYEPPPHAhgtvhsgvgytrprvVPYDEDLRR----AAEVLNAGRKVAIL---VGAGALGATDEVIAVAERLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 231 iPSVAT-LKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDdrVTGRLESFAsKAKVIHLDIDAAELGkL 309
Cdd:PRK08273 235 -AGVAKaLLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFP--YSEFLPKEG-QARGVQIDIDGRMLG-L 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 310 RQP-DVAMDGDLRSILTQLAP--QALQIAPWQAEVEhlRAQHQWDYV------HPGSLIYAPAMLRRLANKLPSDSVVSC 380
Cdd:PRK08273 310 RYPmEVNLVGDAAETLRALLPllERKKDRSWRERIE--KWVARWWETlearamVPADPVNPQRVFWELSPRLPDNAILTA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 381 DVGQHQMWVAQHMHFRRP-EDHLSSaGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMN-VQELTTIKRR-----KL 453
Cdd:PRK08273 388 DSGSCANWYARDLRMRRGmMASLSG-TLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKYwrqwsDP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 454 PVKILLIDNQKLGMVkQWQQLFFE--ERYSET-DLSDNPdFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVA 530
Cdd:PRK08273 467 RLIVLVLNNRDLNQV-TWEQRVMEgdPKFEASqDLPDVP-YARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVK 544
|
570
....*....|...
gi 2525103120 531 IDdafnvwPLVPP 543
Cdd:PRK08273 545 TD------PNVPP 551
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
381-529 |
4.80e-64 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 206.28 E-value: 4.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 381 DVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLI 460
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525103120 461 DNQKLGMVKQWQQLFFEERYSETD--LSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHV 529
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSgkILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
9-173 |
5.24e-64 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 206.70 E-value: 5.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 9 GSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDS-QVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITA 87
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSpGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 88 LADALLDSVPLVAITGQVSTSVIGTDAFQ-EMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIPKD 166
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*..
gi 2525103120 167 IQLAQVE 173
Cdd:pfam02776 161 VLLEEVD 167
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-535 |
1.69e-60 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 210.00 E-value: 1.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 1 MEQGQKISGSEAVIKVLAAHGVNTVFG--YPGGAIMPIyDALYDSQVEHllsRHEQGAAFAAVGYARSSGKTGVCLATSG 78
Cdd:PRK06112 8 PGFTLNGTVAHAIARALKRHGVEQIFGqsLPSALFLAA-EAIGIRQIAY---RTENAGGAMADGYARVSGKVAVVTAQNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 79 PGATNLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGP 158
Cdd:PRK06112 84 PAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 159 VLVDIPKDIQLAQVEYKA----------PL-QAVPDEPELDQaalaeANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQ 227
Cdd:PRK06112 164 VVLLLPADLLTAAAAAPAaprsnslghfPLdRTVPAPQRLAE-----AASLLAQAQRPVVVAGGGVHISGASAALAALQS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 228 RSGIPSVATLKGLGAIAHGTQGYLGMLG--MHGNKAANLA---VQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDID 302
Cdd:PRK06112 239 LAGLPVATTNMGKGAVDETHPLSLGVVGslMGPRSPGRHLrdlVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 303 AAELGK----LRqpdvaMDGD-------LRSILTQ--LAPQALQIAPWQAEVEHLRAQHQWD----YVHPGSLIYAPAML 365
Cdd:PRK06112 319 GEEVGRnyeaLR-----LVGDarltlaaLTDALRGrdLAARAGRRAALEPAIAAGREAHREDsapvALSDASPIRPERIM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 366 RRLANKLPSDSVVSCDVGQHQMWVAQHMHFRRP-EDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQE 444
Cdd:PRK06112 394 AELQAVLTGDTIVVADASYSSIWVANFLTARRAgMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 445 LTTIKRRKLPVKILLIDNQKLGMVKQWQQLFFEERYSETDLSDnPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGP 524
Cdd:PRK06112 474 LETARRMGVPVTIVVLNNGILGFQKHAETVKFGTHTDACHFAA-VDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGP 552
|
570
....*....|..
gi 2525103120 525 FLLHVAID-DAF 535
Cdd:PRK06112 553 TLIEVITDpSAF 564
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
5-532 |
2.63e-58 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 203.41 E-value: 2.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 5 QKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNL 84
Cdd:PRK05858 3 QTGHAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 85 ITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLVDIP 164
Cdd:PRK05858 83 MSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 165 KDIQLAQVE---YKAPLQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATLKGLG 241
Cdd:PRK05858 163 MDHAFSMADddgRPGALTELPAGPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 242 AIAHGTQgylgmlgMHGNKAANLAVQQCDLLLVVGARFDDRVTgrLESFASKAKVIHLDIDAAELGKLRQPDVAMDGDLR 321
Cdd:PRK05858 243 VVPADHP-------LAFSRARGKALGEADVVLVVGVPMDFRLG--FGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 322 SILTQLAPQALQIAPWQAEVEHLRAQH-------------QWDYVHPGSlIYApamlrRLANKLPSDSVVSCDVGQHQMW 388
Cdd:PRK05858 314 AILSALAGAGGDRTDHQGWIEELRTAEtaarardaaeladDRDPIHPMR-VYG-----ELAPLLDRDAIVIGDGGDFVSY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 389 VAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMV 468
Cdd:PRK05858 388 AGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLE 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525103120 469 KQWQQLFFEerYS-ETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAID 532
Cdd:PRK05858 468 KHPMEALYG--YDvAADLRPGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTD 530
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
10-529 |
1.19e-57 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 202.14 E-value: 1.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 10 SEAVIKVLAAHGVNTVFGYPGGAIMPIYDALY-DSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITAL 88
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRrMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 89 ADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEiAASGRPGPVLVDIPKDIQ 168
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMR-KAILNRGVAVVVLPGDVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 169 LAQVEYKAPL--------QAVPDEPELDQAALaeanallaaarqpMLYVGGGVGM------AGAVEPLRAFIQRSGIPSV 234
Cdd:PRK09124 165 LKPAPERATPhwyhapqpVVTPAEEELRKLAA-------------LLNGSSNITLlcgsgcAGAHDELVALAETLKAPIV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 235 ATLKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRvtgrlESFASKAKVIHLDIDAAELGKLRQPDV 314
Cdd:PRK09124 232 HALRGKEHVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 315 AMDGDLRSILTQLAPQaLQIapwQAEVEHL--------RAQHQWDYV----HPGSLIYaPAMLRRLANKLPS-DSVVSCD 381
Cdd:PRK09124 307 GLVGDVKATLAALLPL-LEE---KTDRKFLdkalehyrKARKGLDDLavpsDGGKPIH-PQYLARQISEFAAdDAIFTCD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 382 VGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLID 461
Cdd:PRK09124 382 VGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFN 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 462 NQKLGMVKQWQQL--FFEerySETDLsDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHV 529
Cdd:PRK09124 462 NSVLGFVAMEMKAggYLT---DGTDL-HNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDV 527
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
11-532 |
2.17e-53 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 190.58 E-value: 2.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 11 EAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQ-VEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITALA 89
Cdd:PRK06546 7 EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGgIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 90 DALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEiAASGRPGPVLVDIPKDIQL 169
Cdd:PRK06546 87 DAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQ-HAVAGGGVSVVTLPGDIAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 170 AQVEYK-APLQAVPDEPEL--DQAALAEANALLAAARQPMLYvgGGVGMAGAVEPLRAFIQRSGIPSVATLKGLGAIAHG 246
Cdd:PRK06546 166 EPAPEGfAPSVISPRRPTVvpDPAEVRALADAINEAKKVTLF--AGAGVRGAHAEVLALAEKIKAPVGHSLRGKEWIQYD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 247 TQGYLGMLGMHGNKAANLAVQQCDLLLVVGARF--DDrvtgrlesFASKAKVIHLDIDAAELGKLRQPDVAMDGDLRSIL 324
Cdd:PRK06546 244 NPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFpyDQ--------FLPDVRTAQVDIDPEHLGRRTRVDLAVHGDVAETI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 325 TQLAPQALQ---------------------IAPWQAEVEHLRAqhqwdyVHPGsliYAPAMLRRLANKlpsDSVVSCDVG 383
Cdd:PRK06546 316 RALLPLVKEktdrrfldrmlkkharklekvVGAYTRKVEKHTP------IHPE---YVASILDELAAD---DAVFTVDTG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 384 QHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQ 463
Cdd:PRK06546 384 MCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNS 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525103120 464 KLGMVK-----QWQQLFfeerysETDlSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAID 532
Cdd:PRK06546 464 TLGMVKlemlvDGLPDF------GTD-HPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTD 530
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
363-531 |
3.26e-53 |
|
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: 178.22 E-value: 3.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 363 AMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNV 442
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 443 QELTTIKRRKLPVKILLIDNQKLGMVKQWQQLFFEERYSETDLSdNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAK 522
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLS-NPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAG 159
|
....*....
gi 2525103120 523 GPFLLHVAI 531
Cdd:cd00568 160 GPALIEVKT 168
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
10-171 |
3.20e-52 |
|
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: 175.43 E-value: 3.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 10 SEAVIKVLAAHGVNTVFGYPGGAIMPIYDALY-DSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITAL 88
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRrEGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 89 ADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRpGPVLVDIPKDIQ 168
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGDVQ 161
|
...
gi 2525103120 169 LAQ 171
Cdd:cd07039 162 DAP 164
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
359-533 |
1.94e-49 |
|
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: 168.48 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 359 IYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSF 438
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 439 MMNVQELTTIKRRKLPVKILLIDNQKLGMVKqWQQLFFEERYSETDLsDNPDFVTLASSFDIPGRTIYSADEVEQALDEM 518
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIK-WEQEVMGQPEFGVDL-PNPDFAKIAEAMGIKGIRVEDPDELEAALDEA 159
|
170
....*....|....*
gi 2525103120 519 LSAKGPFLLHVAIDD 533
Cdd:cd02014 160 LAADGPVVIDVVTDP 174
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
372-532 |
1.16e-43 |
|
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: 153.21 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 372 LPSDSVVSCDVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRR 451
Cdd:cd02010 12 MGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQELETAVRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 452 KLPVKILLIDNQKLGMVKqWQQLFFEERYSETDLsDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAI 531
Cdd:cd02010 92 KIPLVVLIWNDNGYGLIK-WKQEKEYGRDSGVDF-GNPDFVKYAESFGAKGYRIESADDLLPVLERALAADGVHVIDCPV 169
|
.
gi 2525103120 532 D 532
Cdd:cd02010 170 D 170
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
17-463 |
2.35e-41 |
|
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: 156.47 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 17 LAAHGVNTVFGYPGGAIMPIYDALYD-SQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLaTSGPGATNLITALADALLDS 95
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLDAIEAhPGIRWVGCCNELNAGYAADGYARVNGLGALVT-TYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 96 VPLVAITGQVSTSVIGT-------------DAFQEMdvlgmslscTKHsfmVT------RAEELVATLYRAFEIAASGRP 156
Cdd:COG3961 94 VPVVHIVGAPGTRAQRRgpllhhtlgdgdfDHFLRM---------FEE---VTvaqavlTPENAAAEIDRVLAAALREKR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 157 gPVLVDIPKDIQLAQVEY---KAPLQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPS 233
Cdd:COG3961 162 -PVYIELPRDVADAPIEPpeaPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 234 VATLKGLGAIAHGTQGYLGM-LGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRLESFASKAKVIHLDIDAAELGKLRQP 312
Cdd:COG3961 241 ATTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVGGHIYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 313 DVAMdgdlRSILTQLAPQALQIAPWQAEVEHLRAqhqWDYVHPGSLIYAPAMLRRLANKLPSDSVVSCDVGQhQMWVAQH 392
Cdd:COG3961 321 GVSL----ADFLEALAELLKKRSAPLPAPAPPPP---PPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGT-SLFGAAD 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525103120 393 MHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQ 463
Cdd:COG3961 393 LRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNND 463
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
3-521 |
3.21e-40 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 153.81 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 3 QGQKISGSEAVIKVLAAHGVNTVFGYPggaIMPIYDALYDSQVEHLLSRHEQGAAFAAVGYAR-SSGKT-GVCLATSGPG 80
Cdd:PRK06154 16 EAKTMKVAEAVAEILKEEGVELLFGFP---VNELFDAAAAAGIRPVIARTERVAVHMADGYARaTSGERvGVFAVQYGPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 81 ATNLITALADALLDSVPLVAITGQVSTSVigTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVL 160
Cdd:PRK06154 93 AENAFGGVAQAYGDSVPVLFLPTGYPRGS--TDVAPNFESLRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 161 VDIPKDIQLAQVEyKAPLQAVPDE---PELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVATL 237
Cdd:PRK06154 171 LELPVDVLAEELD-ELPLDHRPSRrsrPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 238 KGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDDRVTGRleSFASKAKVIHLDIDAAELGKLRQPDVAMD 317
Cdd:PRK06154 250 NGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYGL--PMPEGKTIIHSTLDDADLNKDYPIDHGLV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 318 GDLRSILTQL--------APQALQIAPWQAEVEHLRAQ--HQW-DYVHPGSLIYAP-AMLRRLANKL-PSDSVVSCDVGQ 384
Cdd:PRK06154 328 GDAALVLKQMieelrrrvGPDRGRAQQVAAEIEAVRAAwlAKWmPKLTSDSTPINPyRVVWELQHAVdIKTVIITHDAGS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 385 HQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQK 464
Cdd:PRK06154 408 PRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNFS 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525103120 465 LGMVKQWQQLfFEERYSETDLSDnpDFVTLASSFDIPGRTIYSADEVEQALDEMLSA 521
Cdd:PRK06154 488 MGGYDKVMPV-STTKYRATDISG--DYAAIARALGGYGERVEDPEMLVPALLRALRK 541
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
12-165 |
1.29e-39 |
|
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: 141.33 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 12 AVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQ-VEHLLSRHEQGAAFAAVGYARSSGKtGVCLATSGPGATNLITALAD 90
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALREGDkRIIDTVIHELGAAGAAAGYARAGGP-PVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525103120 91 ALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGrPGPVLVDIPK 165
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
220-327 |
6.56e-38 |
|
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: 136.15 E-value: 6.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 220 EPLRAFIQRSGIPSVATLKGLGAIAHGTQGYLGMLGMHGNKAANLAVQQCDLLLVVGARFDD-RVTGRLESFASKAKVIH 298
Cdd:pfam00205 29 EELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADLVLAVGARFDDiRTTGKLPEFAPDAKIIH 108
|
90 100
....*....|....*....|....*....
gi 2525103120 299 LDIDAAELGKLRQPDVAMDGDLRSILTQL 327
Cdd:pfam00205 109 IDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
7-532 |
9.06e-38 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 146.68 E-value: 9.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 7 ISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSQVEH------LLSRHEQGAAFAAVGYARSSGKTGVCLATSGPG 80
Cdd:PRK08327 7 YTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGrplpefVICPHEIVAISMAHGYALVTGKPQAVMVHVDVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 81 ATNLITALADALLDSVPLVAITGQVSTSVIGT----DAF----QEM-DVLGMSLSCTKHSFMVTRAEELVATLYRAFEIA 151
Cdd:PRK08327 87 TANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrNTRihwtQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 152 ASGRPGPVLVDIPKDIQLAQVEY-KAPL--QAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEPLRAFIQR 228
Cdd:PRK08327 167 MSEPKGPVYLTLPREVLAEEVPEvKADAgrQMAPAPPAPDPEDIARAAEMLAAAERPVIITWRAGRTAEGFASLRRLAEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 229 SGIPSVATLKGLGAIAHGTQGYLGmlgmhGNKAANLAvqQCDLLLVVGArfDDRVTGRLESFASKAKVIHLDIDAAelgK 308
Cdd:PRK08327 247 LAIPVVEYAGEVVNYPSDHPLHLG-----PDPRADLA--EADLVLVVDS--DVPWIPKKIRPDADARVIQIDVDPL---K 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 309 LRQP------DVAMDGDLRSILTQLA--------PQALQIAPWQAEVEHLRAQHQW-------DYVHPGSlIYAPAMLRR 367
Cdd:PRK08327 315 SRIPlwgfpcDLCIQADTSTALDQLEerlkslasAERRRARRRRAAVRELRIRQEAakraeieRLKDRGP-ITPAYLSYC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 368 LANKLPSDSVVSCDVGqhqmWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQE--L 445
Cdd:PRK08327 394 LGEVADEYDAIVTEYP----FVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEaaH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 446 TTIKRRKLPVKILLIDNQKLGMVKQWQQLFFEE-------RYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEM 518
Cdd:PRK08327 470 WVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPEgyaarkgTFPGTDFDPRPDFAKIAEAFGGYGERVEDPEELKGALRRA 549
|
570
....*....|....*...
gi 2525103120 519 LSA----KGPFLLHVAID 532
Cdd:PRK08327 550 LAAvrkgRRSAVLDVIVD 567
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
2-534 |
2.77e-37 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 145.51 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 2 EQGQKISGSEAVIKVLAAHGVNTVFGYPGgaiMPIYDALYDSQVEHL--LS-RHEQGAAFAAVGYARSSGKTGVCLATSG 78
Cdd:PRK09259 5 DQLQLTDGFHLVIDALKLNGIDTIYGVVG---IPITDLARLAQAEGIryIGfRHEQSAGNAAAAAGFLTQKPGVCLTVSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 79 PGATNLITALADALLDSVPLVAITGQVSTSVIGTDA--FQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRP 156
Cdd:PRK09259 82 PGFLNGLTALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 157 GPVLVDIPKDI------------QLAQVEYKAPLQAVPDEpeldqaALAEANALLAAARQPMLYVGGGVGMAGAVEPLRA 224
Cdd:PRK09259 162 GGVYLDLPAKVlaqtmdadealtSLVKVVDPAPAQLPAPE------AVDRALDLLKKAKRPLIILGKGAAYAQADEQIRE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 225 FIQRSGIP----SVAtlKGLGAIAHGtqgylgmlgmHGNKAA-NLAVQQCDLLLVVGARFDDRVT-GRLESFASKAKVIH 298
Cdd:PRK09259 236 FVEKTGIPflpmSMA--KGLLPDTHP----------QSAAAArSLALANADVVLLVGARLNWLLShGKGKTWGADKKFIQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 299 LDIDAAELGKLRQPDVAMDGDLRSILTQLAPQALQI-----APWQAEVEHLRAQHQWDYV-------HPGSLIYAPAMLR 366
Cdd:PRK09259 304 IDIEPQEIDSNRPIAAPVVGDIGSVMQALLAGLKQNtfkapAEWLDALAERKEKNAAKMAeklstdtQPMNFYNALGAIR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 367 RLANKLPSDSVVScdVGQHQMWVAQHM-HFRRPEDHLSSAGLGTMGFGLPAAIGAQMA--RPdatVVTVSGDGSFMMNVQ 443
Cdd:PRK09259 384 DVLKENPDIYLVN--EGANTLDLARNIiDMYKPRHRLDCGTWGVMGIGMGYAIAAAVEtgKP---VVAIEGDSAFGFSGM 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 444 ELTTIKRRKLPVKILLIDNQKLgmvkqwqqlffeERYSETDLSDNPD-----FVT------LASSFDIPGRTIYSADEVE 512
Cdd:PRK09259 459 EVETICRYNLPVTVVIFNNGGI------------YRGDDVNLSGAGDpsptvLVHharydkMMEAFGGVGYNVTTPDELR 526
|
570 580
....*....|....*....|..
gi 2525103120 513 QALDEMLSAKGPFLLHVAIDDA 534
Cdd:PRK09259 527 HALTEAIASGKPTLINVVIDPA 548
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
361-531 |
1.79e-34 |
|
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: 128.10 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 361 APAMLRRLANKLPSDSVVsCD--VGQHQMwVAQHMHFRRPEDHLSSAGlGTMGFGLPAAIGAQMARPDATVVTVSGDGSF 438
Cdd:cd02002 3 PEYLAAALAAALPEDAII-VDeaVTNGLP-LRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 439 MMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLFF-----EERYSETDLSD-NPDFVTLASSFDIPGRTIYSADEVE 512
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGpegpgENAPDGLDLLDpGIDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*....
gi 2525103120 513 QALDEMLSAKGPFLLHVAI 531
Cdd:cd02002 160 EALREALAEGGPALIEVVV 178
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
10-532 |
3.55e-34 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 135.85 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 10 SEAVIKVLAAHGVNTVFGYPGGAIMPIYDALYDSqVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITALA 89
Cdd:PRK07092 15 RDATIDLLRRFGITTVFGNPGSTELPFLRDFPDD-FRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 90 DALLDSVPLVAITGQVSTSVIGTDAFqemdvlgmsLSCT----------KHSFMVTRAEELVATLYRAFEIAASGRPGPV 159
Cdd:PRK07092 94 TAFKNHTPLVITAGQQARSILPFEPF---------LAAVqaaelpkpyvKWSIEPARAEDVPAAIARAYHIAMQPPRGPV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 160 LVDIPKDIQLAQVEYKAPLQ----AVPDEPELDQAALAEANAllaaaRQPMLYVGGGVGMAGAVEPLRAFIQRSGIPS-V 234
Cdd:PRK07092 165 FVSIPYDDWDQPAEPLPARTvssaVRPDPAALARLGDALDAA-----RRPALVVGPAVDRAGAWDDAVRLAERHRAPVwV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 235 ATLKG-----------LGAIAHGTQGYLGMLGMHgnkaanlavqqcDLLLVVGAR-FDDRVTGRLESFASKAKVIHLDID 302
Cdd:PRK07092 240 APMSGrcsfpedhplfAGFLPASREKISALLDGH------------DLVLVIGAPvFTYHVEGPGPHLPEGAELVQLTDD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 303 AAELGKLRQPDvAMDGDLRSILTQL----------APQALQIAPWQAEvehlraqhqwdyvhPGSLIYAPAMLRRLANKL 372
Cdd:PRK07092 308 PGEAAWAPMGD-AIVGDIRLALRDLlallppsarpAPPARPMPPPAPA--------------PGEPLSVAFVLQTLAALR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 373 PSDSVVSCDVGQHQ--MWvaQHMHFRRPEDHLSSAGlGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKR 450
Cdd:PRK07092 373 PADAIVVEEAPSTRpaMQ--EHLPMRRQGSFYTMAS-GGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 451 RKLPVKILLIDNQKLGMVKQWQQLFFEERYSETDLSDnPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVA 530
Cdd:PRK07092 450 LKLPVTFVILNNGRYGALRWFAPVFGVRDVPGLDLPG-LDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVE 528
|
..
gi 2525103120 531 ID 532
Cdd:PRK07092 529 VA 530
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
351-521 |
1.43e-27 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 109.52 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 351 DYVHPGSLiyapamLRRLANKLPSDSVVSCDVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVV 430
Cdd:cd02013 2 NPMHPRQV------LRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 431 TVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQQLFFEERYSETDLsDNPDFVTLASSFDIPGRTIYSADE 510
Cdd:cd02013 76 AIAGDGAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTEL-ESESFAKIAEACGAKGITVDKPED 154
|
170
....*....|.
gi 2525103120 511 VEQALDEMLSA 521
Cdd:cd02013 155 VGPALQKAIAM 165
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
8-531 |
5.25e-25 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 108.39 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 8 SGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALyDS--QVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLI 85
Cdd:PRK07586 2 NGAESLVRTLVDGGVDVCFANPGTSEMHFVAAL-DRvpGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 86 TALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVlgMSLSCTKHSFM--VTRAEElVATLYRAFEIAASGRPGPVLVDI 163
Cdd:PRK07586 81 ANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDI--EALARPVSGWVrrSESAAD-VAADAAAAVAAARGAPGQVATLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 164 -PKDIQLAQVEYKAPLQAVPDEPELDQAALAEAnallaaarqpmlyvgggvgmagaveplrAFIQRSGIPSV-------- 234
Cdd:PRK07586 158 lPADVAWSEGGPPAPPPPAPAPAAVDPAAVEAA----------------------------AAALRSGEPTVlllggral 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 235 --ATLKGLGAIAHGTQ------------------------GYLGmlgmhgnKAANLAVQQCDLLLVVGARfdDRVTgrle 288
Cdd:PRK07586 210 reRGLAAAARIAAATGarllaetfparmergagrpaverlPYFA-------EQALAQLAGVRHLVLVGAK--APVA---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 289 SFASKAKVIHLDIDAAELGKLRQPDVamdgDLRSILTQLApQALQIAPWQAEVehlrAQHQWDYVHPGSLIyAPAMLRRL 368
Cdd:PRK07586 277 FFAYPGKPSRLVPEGCEVHTLAGPGE----DAAAALEALA-DALGAKPAAPPL----AAPARPPLPTGALT-PEAIAQVI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 369 ANKLPSDSVVSCDVGQHQMWVAQHMHFRRPEDHLSSAGlGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTI 448
Cdd:PRK07586 347 AALLPENAIVVDESITSGRGFFPATAGAAPHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQ 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 449 KRRKLPV----------KILLIDNQKLGMVKQWQQLFfeerySETDLSD-NPDFVTLASSFDIPGRTIYSADEVEQALDE 517
Cdd:PRK07586 426 ARENLDVttvifanrayAILRGELARVGAGNPGPRAL-----DMLDLDDpDLDWVALAEGMGVPARRVTTAEEFADALAA 500
|
570
....*....|....
gi 2525103120 518 MLSAKGPFLLHVAI 531
Cdd:PRK07586 501 ALAEPGPHLIEAVV 514
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
365-532 |
6.12e-23 |
|
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: 95.68 E-value: 6.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 365 LRRLANKLPSDSVVSCDVGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQE 444
Cdd:cd02004 5 LHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGME 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 445 LTTIKRRKLPVKILLIDNQKLGMVKQWQQLFFEERYSETDLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGP 524
Cdd:cd02004 85 LETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALASGKP 164
|
....*...
gi 2525103120 525 FLLHVAID 532
Cdd:cd02004 165 ALINVIID 172
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
4-531 |
8.06e-23 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 101.87 E-value: 8.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 4 GQKISGSEAVIKVLAAHGVNTVFGYPGGAIMPIYDALyDSQ--VEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGA 81
Cdd:PRK12474 2 GQTMNGADSVVDTLLNCGVEVCFANPGTSEMHFVAAL-DRVprMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 82 TNLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLYRAFEIAASGRPGPVLV 161
Cdd:PRK12474 81 ANGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 162 DIPKDIQLAQVEYKAPLQAVPDEPELDQAALAEANALLAAARQPMLYVGGGVGMAGAVEpLRAFIQRSgipSVATLKGLG 241
Cdd:PRK12474 161 IMPADVAWNEAAYAAQPLRGIGPAPVAAETVERIAALLRNGKKSALLLRGSALRGAPLE-AAGRIQAK---TGVRLYCDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 242 AIAHGTQGY----LGMLGMHGNKAANLaVQQCDLLLVVGARfddrvtGRLESFASKAKVIHLDIDAAELGKLRQPDVAMD 317
Cdd:PRK12474 237 FAPRIERGAgrvpIERIPYFHEQITAF-LKDVEQLVLVGAK------PPVSFFAYPGKPSWGAPPGCEIVYLAQPDEDLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 318 GDLRSILTQLAPQALQIAPWQAEVEHLraqhqwdyvhPGSLIYAPAMLRRLANKLPSDSVVSCDVGQHQMWVAQHMHFRR 397
Cdd:PRK12474 310 QALQDLADAVDAPAEPAARTPLALPAL----------PKGALNSLGVAQLIAHRTPDQAIYADEALTSGLFFDMSYDRAR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 398 PEDHLSSAGlGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDNQKLG-----MVKQWQ 472
Cdd:PRK12474 380 PHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAilngeLQRVGA 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525103120 473 QLFFEERYSETDLsDNP--DFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAI 531
Cdd:PRK12474 459 QGAGRNALSMLDL-HNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
12-164 |
1.12e-17 |
|
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: 80.24 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 12 AVIKVLAAHGVNTVFGYPGGAIMP-IYDALYDSQVEHLLSRHEQGAAFAAVGYARSSGKTGVCLATSGPGATNLITALAD 90
Cdd:cd07037 2 ALVEELKRLGVRDVVISPGSRSAPlALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 91 ALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSFMVTRAEELVATLY------RAFEIAASGRPGPVLVDIP 164
Cdd:cd07037 82 AYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLWYllrlanRAVLEALSAPPGPVHLNLP 161
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
364-463 |
5.16e-17 |
|
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: 79.12 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 364 MLRRLANKLPSDSVVSCDVGQHQMWVAQhmhFRRPED--HLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMN 441
Cdd:cd02005 7 LWQQVQNFLKPNDILVAETGTSWFGALD---LKLPKGtrFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMT 83
|
90 100
....*....|....*....|..
gi 2525103120 442 VQELTTIKRRKLPVKILLIDNQ 463
Cdd:cd02005 84 VQELSTMIRYGLNPIIFLINND 105
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
17-114 |
3.91e-15 |
|
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: 72.91 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 17 LAAHGVNTVFGYPGGAIMPIYDALYDS-QVEHLLSRHEQGAAFAAVGYARSSGkTGVCLATSGPGATNLITALADALLDS 95
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENpGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90
....*....|....*....
gi 2525103120 96 VPLVAITGQVSTSVIGTDA 114
Cdd:cd07038 86 VPVVHIVGAPSTKAQASGL 104
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
382-514 |
1.09e-14 |
|
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: 73.08 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 382 VGQHQMWVAQHMHFRRPEDHLSSAGLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLID 461
Cdd:cd02006 31 IGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVN 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2525103120 462 NQKLGMVKQWQQLFfeerysETDLSDNPDFVTLASsfdiPGRTIYSADEVEQA 514
Cdd:cd02006 111 NAYLGLIRQAQRAF------DMDYQVNLAFENINS----SELGGYGVDHVKVA 153
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
365-532 |
4.21e-14 |
|
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: 71.18 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 365 LRRLANKLPSDSVVSCDVGQ-----HQMWVAQ-----HMHFrrpedhlssaGLGTMGFGLPAAIGAQMARPDATVVTVSG 434
Cdd:cd02003 5 LGALNEAIGDDDVVINAAGSlpgdlHKLWRARtpggyHLEY----------GYSCMGYEIAAGLGAKLAKPDREVYVLVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 435 DGSFMMNVQELTTIKRRKLPVKILLIDNQKLGMVKQWQ-----QLF---FEERYSETDLSDNP----DFVTLASSFdipG 502
Cdd:cd02003 75 DGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQestgsGSFgteFRDRDQESGQLDGAllpvDFAANARSL---G 151
|
170 180 190
....*....|....*....|....*....|...
gi 2525103120 503 RTIYSA---DEVEQALDEMLSAKGPFLLHVAID 532
Cdd:cd02003 152 ARVEKVktiEELKAALAKAKASDRTTVIVIKTD 184
|
|
| MenD |
COG1165 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ... |
53-537 |
1.73e-13 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440779 [Multi-domain] Cd Length: 567 Bit Score: 72.89 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 53 EQGAAFAAVGYARSSGKTGVCLATSGPGATNLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSF 132
Cdd:COG1165 54 ERSAAFFALGLAKASGRPVALVCTSGTAAANYYPAVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 133 MVTRAEE-------LVATLYRAFEIAASGRPGPVLVDIP--------KDIQLAQVEYKAPLQAVPDEPELDQAALAEANA 197
Cdd:COG1165 134 DLPLPEAdpdalryLRRTINRALAAALGPPPGPVHINVPfreplypdPDEEDPLAAGGPWIRVTPPEPAPSPEALAQLAD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 198 LLAAARQPMLYVGGGVGMAGAVEPLRAFIQRSGIPSVA-TLKGL---GAIAHgtqgYLGMLGMHGNKAAnlavQQCDLLL 273
Cdd:COG1165 214 ELERAKRGLIVAGPLPPPEELAEALAALAEALGWPVLAdPLSNLrhpNVIST----YDLLLRNPEFAEL----LQPDLVI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 274 VVGARFddrVTGRLESF---ASKAKVIHLDidaaELGKLRQP----DVAMDGDLRSILTQLAPQALQIAP-----WQAEV 341
Cdd:COG1165 286 RFGGPP---VSKRLKQFlrrHPPAEHWVVD----PSGEWRDPfhslTRVIEADPEAFLEALAERLPPADSawlarWLAAE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 342 EHLRAQHQwDYVHPGSLIyAPAMLRRLANKLPSDSVV----ScdvgqhqMWV--AQHMHFRRPEDH--LSSAGL----GT 409
Cdd:COG1165 359 QKARAAID-EYLAEDPLS-EGAVARRLLEALPEGSTLfvgnS-------MPVrdLDLFARPLPKGVrvYANRGAsgidGT 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 410 mgfgLPAAIGAQMARPDATVVtVSGDGSFM--MNVqeLTTIKRRKLPVKILLIDNQKLG---M--VKQWQQLFfeERYSE 482
Cdd:COG1165 430 ----VSTALGAALASGKPTVL-LTGDLSFLhdLNG--LLLLYELPPNLTIVVVNNDGGGifsMlpGAKFEPEF--ERFFG 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2525103120 483 TdlSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAIDDAFNV 537
Cdd:COG1165 501 T--PHGLDFEHLAAMYGLDYARVSSWEELREALAEFLPSDGPRVLEVRTDREENA 553
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
364-534 |
2.67e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 68.70 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 364 MLRRLANKLPSDSVVSCDVG--QHQMWVAQHmhfrRPEDHLSsagLGTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMN 441
Cdd:PRK06163 18 LTCRLVAKLKDEEAVIGGIGntNFDLWAAGQ----RPQNFYM---LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 442 VQELTTIKRRKLP-VKILLIDN---QKLGMVKqwqqlffeeryseTDLSDNPDFVTLASSFDIpGRTIYSADEV--EQAL 515
Cdd:PRK06163 91 LGALGTIAALAPKnLTIIVMDNgvyQITGGQP-------------TLTSQTVDVVAIARGAGL-ENSHWAADEAhfEALV 156
|
170
....*....|....*....
gi 2525103120 516 DEMLSAKGPFLLHVAIDDA 534
Cdd:PRK06163 157 DQALSGPGPSFIAVRIDDK 175
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
408-469 |
1.30e-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: 1.30e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525103120 408 GTMGFGLPAAIGAQMARPDATVVTVSGDG-SFMMNVQELTTIKRRKLPVKILLIDNQKLGMVK 469
Cdd:cd03375 51 TLHGRALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTK 113
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
407-534 |
2.70e-06 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 48.05 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 407 LGTMGFGLPAAIGAQMARPDaTVVTVSGDGSFMMNVQELTTIKRRKLP-VKILLIDNQKLGmvkqwqqlffEERYSETDL 485
Cdd:cd03372 41 LGSMGLASSIGLGLALAQPR-KVIVIDGDGSLLMNLGALATIAAEKPKnLIIVVLDNGAYG----------STGNQPTHA 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2525103120 486 SDNPDFVTLASSFDIPgrTIYSADEVEQALDEM-LSAKGPFLLHVAIDDA 534
Cdd:cd03372 110 GKKTDLEAVAKACGLD--NVATVASEEAFEKAVeQALDGPSFIHVKIKPG 157
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
365-531 |
4.78e-06 |
|
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: 47.31 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 365 LRRLANKLPSDSVVSCDVG--QHQMWVAQHMHFRRPEDHLSSAGlgTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNV 442
Cdd:cd03371 5 IEIVLSRAPATAAVVSTTGmtSRELFELRDRPGGGHAQDFLTVG--SMGHASQIALGIALARPDRKVVCIDGDGAALMHM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 443 QELTTIKRRKLP-VKILLIDNQKLGMV-KQwqqlffeerysetdlsdnpdfVTLASSFDIPG----------RTIYSADE 510
Cdd:cd03371 83 GGLATIGGLAPAnLIHIVLNNGAHDSVgGQ---------------------PTVSFDVSLPAiakacgyravYEVPSLEE 141
|
170 180
....*....|....*....|.
gi 2525103120 511 VEQALDEMLSAKGPFLLHVAI 531
Cdd:cd03371 142 LVAALAKALAADGPAFIEVKV 162
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
408-469 |
5.79e-06 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 48.30 E-value: 5.79e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525103120 408 GTMGFGLPAAIGAQMARPDATVVTVSGDG---SFMMNvqelTTIK--RRKLPVKILLIDNQKLGMVK 469
Cdd:PRK11867 69 TIHGRALAIATGLKLANPDLTVIVVTGDGdalAIGGN----HFIHalRRNIDITYILFNNQIYGLTK 131
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
417-532 |
7.25e-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: 46.43 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 417 AIGAQMARPDATVVtVSGDGSFM--MNVqeLTTIKRRKLPVKILLIDNQKLG---MVKQWQQLFFEERYSETDLsdNPDF 491
Cdd:cd02009 60 ALGIALATDKPTVL-LTGDLSFLhdLNG--LLLGKQEPLNLTIVVINNNGGGifsLLPQASFEDEFERLFGTPQ--GLDF 134
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2525103120 492 VTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAID 532
Cdd:cd02009 135 EHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
53-184 |
5.52e-05 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 46.39 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 53 EQGAAFAAVGYARSSGKTGVCLATSGPGATNLITALADALLDSVPLVAITGQVSTSVIGTDAFQEMDVLGMSLSCTKHSF 132
Cdd:PLN02980 348 ERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFF 427
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525103120 133 MV------TRAEELVATLYRAFEIAASGRPGPVLVDIPkdiqlaqveYKAPLQAVPDE 184
Cdd:PLN02980 428 NLppptdlIPARMVLTTLDSAVHWATSSPCGPVHINCP---------FREPLDGSPTN 476
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
407-531 |
1.20e-04 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 42.86 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 407 LGTMGFGLPAAIGAQMARPDAtVVTVSGDGSFMMNVQELTTI-KRRKLPVKILLIDNQKlgmvkqwqqlffeerYSET-- 483
Cdd:cd02001 41 LGSMGLAGSIGLGLALGLSRK-VIVVDGDGSLLMNPGVLLTAgEFTPLNLILVVLDNRA---------------YGSTgg 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2525103120 484 --DLSDNPDFVTLASSFDIPGRTIYSADEVEQALDEMLSAKGPFLLHVAI 531
Cdd:cd02001 105 qpTPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLLHAPI 154
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
21-103 |
5.84e-04 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 42.77 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 21 GVNTVFGYPGGAIMPIYDalydsqveHLLSR---------HEQGAAFAAVGYARSSGkTGVCLATSGPGATNLITALADA 91
Cdd:PLN02573 30 GVTDVFSVPGDFNLTLLD--------HLIAEpglnligccNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGA 100
|
90
....*....|..
gi 2525103120 92 LLDSVPLVAITG 103
Cdd:PLN02573 101 YSENLPVICIVG 112
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
408-462 |
7.12e-04 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 42.38 E-value: 7.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2525103120 408 GTMGFGLPAAIGAQMARPDATVVTVSGDGSFMMNVQELTTIKRRKLPVKILLIDN 462
Cdd:PLN02573 428 GSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINN 482
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
408-469 |
8.81e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 41.40 E-value: 8.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525103120 408 GTMGFGLPAAIGAQMARPDATVVTVSGDG---SFMMNvqELTTIKRRKLPVKILLIDNQKLGMVK 469
Cdd:PRK05778 70 TLHGRAIAFATGAKLANPDLEVIVVGGDGdlaSIGGG--HFIHAGRRNIDITVIVENNGIYGLTK 132
|
|
| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
9-162 |
2.56e-03 |
|
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate.
Pssm-ID: 132917 [Multi-domain] Cd Length: 160 Bit Score: 38.64 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 9 GSEAVIKVLAAHGVNTVFGYPG---GAIMPIYDALYDS--QVEHLLSRHEQGAAFAAVGyARSSGKTGVClATSGPGATN 83
Cdd:cd07034 1 GNEAVARGALAAGVDVVAAYPItpsTEIAETLAKAVLGelGGVVVQAESEHAAAEAAIG-ASAAGARAMT-ATSGPGLNL 78
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525103120 84 LITALADALLDSVPLVAITGQ---VSTSVIGTDAfQEMdvlgMSLSCTKHSFMV---TRAEELVATLYRAFEIAA-SGRP 156
Cdd:cd07034 79 MAEALYLAAGAELPLVIVVAQrpgPSTGLPKPDQ-SDL----MAARYGGHPWPVlapSSVQEAFDLALEAFELAEkYRLP 153
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....*.
gi 2525103120 157 GPVLVD 162
Cdd:cd07034 154 VIVLSD 159
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| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
408-467 |
7.46e-03 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 38.58 E-value: 7.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525103120 408 GTMGFGLPAAIGAQMARPDATVVTVSGDG-SFMMNVQELTTIKRRKLPVKILLIDNQKLGM 467
Cdd:PRK11866 59 GIHGRVLPIATGVKWANPKLTVIGYGGDGdGYGIGLGHLPHAARRNVDITYIVSNNQVYGL 119
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