|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
1-533 |
0e+00 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 885.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNIL 80
Cdd:PRK07524 1 MTTCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 81 TAMAQAYADSIPMLVISSVNERARLAHGNGYLHELPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIE 160
Cdd:PRK07524 81 TAMGQAYADSIPMLVISSVNRRASLGKGRGKLHELPDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 161 LPLDVITAPAEHLALRPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALTINAKGLL 240
Cdd:PRK07524 161 IPLDVLAAPADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAAALRALAERLDAPVALTINAKGLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 241 PADHPLLLGSNQSCVPVRELAAEADVVLAIGTELGETDYDVVFDGGFALDGELIRIDIDPQQLMRNYTPSLAIHSDARLA 320
Cdd:PRK07524 241 PAGHPLLLGASQSLPAVRALIAEADVVLAVGTELGETDYDVYFDGGFPLPGELIRIDIDPDQLARNYPPALALVGDARAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 321 MRVLLAELPGGEASPDsPGARRAAAVRQRLAEDFAGWSH-YRQLFAAILAEWPDARFVGDSTQTVYSGNHLVDLDEPRRW 399
Cdd:PRK07524 321 LEALLARLPGQAAAAD-WGAARVAALRQALRAEWDPLTAaQVALLDTILAALPDAIFVGDSTQPVYAGNLYFDADAPRRW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 400 FNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKRYMERREITPL 479
Cdd:PRK07524 400 FNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1521190028 480 GVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA-DRPLIVEVLQAAPFHP 533
Cdd:PRK07524 480 GVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFArPGPTLIEVDQACWFAA 534
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
1-525 |
7.49e-159 |
|
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: 463.48 E-value: 7.49e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPG-SRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNI 79
Cdd:COG0028 2 KMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRqSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 80 LTAMAQAYADSIPMLVISSVNERARLahGNGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHI 159
Cdd:COG0028 82 VTGLADAYMDSVPVLAITGQVPTSLI--GRGAFQEV-DQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 160 ELPLDVITAPAEHLALRPRTLASRPAPALAP--LREAAARLRNAKKPLLLLGGGCVEAAAEARALA--AALDAPTALTIN 235
Cdd:COG0028 159 DIPKDVQAAEAEEEPAPPELRGYRPRPAPDPeaIEEAAELLAAAKRPVILAGGGARRAGAAEELRAlaERLGAPVVTTLM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 236 AKGLLPADHPLLLGS--NQSCVPVRELAAEADVVLAIGTELGETDYDVVfdGGFALDGELIRIDIDPQQLMRNYTPSLAI 313
Cdd:COG0028 239 GKGAFPEDHPLYLGMlgMHGTPAANEALAEADLVLAVGARFDDRVTGNW--DEFAPDAKIIHIDIDPAEIGKNYPVDLPI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 314 HSDARLAMRVLLAELPGGEASPDSPGARRAAAVRQRLAEDFAGWS--HYRQLFAAILAEWP-DARFVGDSTQTVYSGNHL 390
Cdd:COG0028 317 VGDAKAVLAALLEALEPRADDRAAWLARIAAWRAEYLAAYAADDGpiKPQRVIAALREALPdDAIVVTDVGQHQMWAARY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 391 VDLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKRY 470
Cdd:COG0028 397 LRFRRPRRFLT-SGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQW 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1521190028 471 MERR-EITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGA-PADRPLIVEV 525
Cdd:COG0028 476 QELFyGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEAlASDGPALIDV 532
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-525 |
1.75e-115 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 352.01 E-value: 1.75e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTcGEFLVKQLEAWGVETVFGIPGVHTVELYRGL--PGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTN 78
Cdd:PRK08266 4 MTG-GEAIVAGLVAHGVDTVFGLPGAQLYWLFDALykAGDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 79 ILTAMAQAYADSIPMLVISSVNERARLAHGNGYLHELPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVH 158
Cdd:PRK08266 83 AGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHLHEMPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 159 IELPLDVITAPAEHLALRPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALTINAKG 238
Cdd:PRK08266 163 LEMPWDVFGQRAPVAAAPPLRPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRSGRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 239 LLPADHPLLLgsnqSCVPVRELAAEADVVLAIGTELgetdYDVVFDGGFALDG-ELIRIDIDPQQlMRNYTPSLAIHSDA 317
Cdd:PRK08266 243 IVSDRHPLGL----NFAAAYELWPQTDVVIGIGSRL----ELPTFRWPWRPDGlKVIRIDIDPTE-MRRLKPDVAIVADA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 318 RLAMRVLLAELPGgeASPDSPG-ARRAAAVRQRLAEDFAGWSHYRQLFAAILAEWP-DARFVGDSTQTVYSGNHLVDLDE 395
Cdd:PRK08266 314 KAGTAALLDALSK--AGSKRPSrRAELRELKAAARQRIQAVQPQASYLRAIREALPdDGIFVDELSQVGFASWFAFPVYA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 396 PRRWFnaSTGY-GTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKRYMER- 473
Cdd:PRK08266 392 PRTFV--TCGYqGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRr 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1521190028 474 ---REItplGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA-DRPLIVEV 525
Cdd:PRK08266 470 fggRVV---ASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAhGGPVLIEV 522
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
3-532 |
5.20e-86 |
|
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: 276.22 E-value: 5.20e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 3 TCGEFLVKQLEAWGVETVFGIPGVHTVELYRGL-PGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILT 81
Cdd:TIGR00118 2 SGAEAIIESLKDEGVKTVFGYPGGAILPIYDALyNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 82 AMAQAYADSIPMLVISSvnERARLAHGNGYLHELpnqrNLVG---NVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVH 158
Cdd:TIGR00118 82 GIATAYMDSIPMVVFTG--QVPTSLIGSDAFQEA----DILGitmPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 159 IELPLDVITA-----PAEHLAL---RPRTLASRpapalAPLREAAARLRNAKKPLLLLGGGCV--EAAAEARALAAALDA 228
Cdd:TIGR00118 156 VDLPKDVTTAeieypYPEKVNLpgyRPTVKGHP-----LQIKKAAELINLAKKPVILVGGGVIiaGASEELKELAERIQI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 229 PTALTINAKGLLPADHPLLLG--SNQSCVPVRELAAEADVVLAIGTEL-----GETDYdvvfdggFALDGELIRIDIDPQ 301
Cdd:TIGR00118 231 PVTTTLMGLGSFPEDHPLSLGmlGMHGTKTANLAVHECDLIIAVGARFddrvtGNLAK-------FAPNAKIIHIDIDPA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 302 QLMRNYTPSLAIHSDARLAMRVLLAELpGGEASPDSpgaRRAAAVRQRLAEDFAGWSHY-------RQLFAAILAEWPDA 374
Cdd:TIGR00118 304 EIGKNVRVDIPIVGDARNVLEELLKKL-FELKERKE---SAWLEQINKWKKEYPLKMDYteegikpQQVIEELSRVTKDE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 375 RFVG-DSTQTVYSGNHLVDLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVG 453
Cdd:TIGR00118 380 AIVTtDVGQHQMWAAQFYPFRKPRRFIT-SGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 454 IVVLLWNNHGYGEIKR-----YMERREITPLGvdiYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA-DRPLIVEVLQ 527
Cdd:TIGR00118 459 VKILILNNRYLGMVRQwqelfYEERYSHTHMG---SLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSsNEPVLLDVVV 535
|
....*
gi 1521190028 528 AAPFH 532
Cdd:TIGR00118 536 DKPEN 540
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
3-499 |
1.04e-78 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 257.33 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 3 TCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSR-IRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILT 81
Cdd:PRK08155 14 TGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 82 AMAQAYADSIPMLVISSVNERARLahGNGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIEL 161
Cdd:PRK08155 94 AIADARLDSIPLVCITGQVPASMI--GTDAFQEV-DTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 162 PLDVITAPAEHLAL-RPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAP--TALTINAKG 238
Cdd:PRK08155 171 PKDVQTAVIELEALpAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQlpTTMTLMALG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 239 LLPADHPLLLG---------SNQscvpvreLAAEADVVLAIGTE-----LGETDydvvfdgGFALDGELIRIDIDPQQLM 304
Cdd:PRK08155 251 MLPKAHPLSLGmlgmhgarsTNY-------ILQEADLLIVLGARfddraIGKTE-------QFCPNAKIIHVDIDRAELG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 305 RNYTPSLAIHSDARlamRVLLAELPGGEASPDspgarraaavrqrlaedfAGWshyRQLFAAILAEWP------------ 372
Cdd:PRK08155 317 KIKQPHVAIQADVD---DVLAQLLPLVEAQPR------------------AEW---HQLVADLQREFPcpipkaddplsh 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 373 ------DARFVGDSTQ-TVYSGNHLV------DLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQF 439
Cdd:PRK08155 373 yglinaVAACVDDNAIiTTDVGQHQMwtaqayPLNRPRQWLT-SGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMM 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1521190028 440 TLPELASAVEAKVGIVVLLWNNHGYGEIKR-----YMERREITPLGvdiYTPDFLAIARGFGCAA 499
Cdd:PRK08155 452 NIQEMATAAENQLDVKIILMNNEALGLVHQqqslfYGQRVFAATYP---GKINFMQIAAGFGLET 513
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
1-525 |
3.27e-78 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 255.30 E-value: 3.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLpGSR--IRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTN 78
Cdd:PRK07064 2 KVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAI-GRRgkIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 79 ILTAMAQAYADSIPMLVISSVNERARLAHGNGYLHELPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVH 158
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPYLDQDLGYIHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 159 IELPLDVITAPAEHLA-LRPRTLASrPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALTiNAK 237
Cdd:PRK07064 161 VEIPIDIQAAEIELPDdLAPVHVAV-PEPDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVDLGFGVVTST-QGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 238 GLLPADHPLLLGSNQSCVPVRELAAEADVVLAIGTEL--GET-DYDVvfdggfALDGELIRIDIDPQQLMRNYTPSLAIH 314
Cdd:PRK07064 239 GVVPEDHPASLGAFNNSAAVEALYKTCDLLLVVGSRLrgNETlKYSL------ALPRPLIRVDADAAADGRGYPNDLFVH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 315 SDARLAMRVLLAELPGGEASPDSPGARRAAAVRQRLAEDFAGWSHYRQLFAAILAEWP-DARFVGDSTQTVYS-GNHLVD 392
Cdd:PRK07064 313 GDAARVLARLADRLEGRLSVDPAFAADLRAAREAAVADLRKGLGPYAKLVDALRAALPrDGNWVRDVTISNSTwGNRLLP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 393 LDEPRRwfNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIK---- 468
Cdd:PRK07064 393 IFEPRA--NVHALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRniqd 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1521190028 469 -RYMERReitpLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPADR-PLIVEV 525
Cdd:PRK07064 471 aQYGGRR----YYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEgPVLVEV 525
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
1-518 |
3.13e-76 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 250.51 E-value: 3.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTcGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNIL 80
Cdd:PRK08322 1 MKA-ADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 81 TAMAQAYADSIPMLVISSVN--ERARLAHgngylHELPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVH 158
Cdd:PRK08322 80 TGVAYAQLGGMPMVAITGQKpiKRSKQGS-----FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 159 IELPLDVITAPAEHLALrPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAP--TALTINA 236
Cdd:PRK08322 155 LELPEDIAAEETDGKPL-PRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGipFFTTQMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 237 KGLLPADHPLLLGSnqscvpvrelAA------------EADVVLAIGtelgetdYDVV-FDGGF---ALDGELIRIDIDP 300
Cdd:PRK08322 234 KGVIPETHPLSLGT----------AGlsqgdyvhcaieHADLIINVG-------HDVIeKPPFFmnpNGDKKVIHINFLP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 301 QQLMRNYTPSLAIHSDARLAMRVLLAELPGGEaspdspgarraaavrqrlAEDFAGWSHYRQLFAAILAEWPD------- 373
Cdd:PRK08322 297 AEVDPVYFPQVEVVGDIANSLWQLKERLADQP------------------HWDFPRFLKIREAIEAHLEEGADddrfpmk 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 374 -ARFVGDsTQTVYSGNHLVDLDEP--RRWF---------NA---STGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQ 438
Cdd:PRK08322 359 pQRIVAD-LRKVMPDDDIVILDNGayKIWFarnyrayepNTcllDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFM 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 439 FTLPELASAVEAKVGIVVLLWNNHGYGEIKRYMERREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPAD 518
Cdd:PRK08322 438 MNSQELETAVRLGLPLVVLILNDNAYGMIRWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQ 517
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
5-525 |
1.17e-72 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 241.97 E-value: 1.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 5 GEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMA 84
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 85 QAYADSIPMLVISSvnerarlahgngylhELPNqrNLVGN--------------VCAFSHTLMSAEELPAVLARAFAVFD 150
Cdd:PRK06276 84 TAYADSSPVIALTG---------------QVPT--KLIGNdafqeidalgifmpITKHNFQIKKPEEIPEIFRAAFEIAK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 151 SERPRPVHIELPLDVITapAEHLALRPRTLASRPAPALAP--------LREAAARLRNAKKPLLLLGGGCV--EAAAEAR 220
Cdd:PRK06276 147 TGRPGPVHIDLPKDVQE--GELDLEKYPIPAKIDLPGYKPttfghplqIKKAAELIAEAERPVILAGGGVIisGASEELI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 221 ALAAALDAPTALTINAKGLLPADHPLLLG---------SNQScvpvrelAAEADVVLAIGTELGE-TDYDVvfdGGFALD 290
Cdd:PRK06276 225 ELSELVKIPVCTTLMGKGAFPEDHPLALGmvgmhgtkaANYS-------VTESDVLIAIGCRFSDrTTGDI---SSFAPN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 291 GELIRIDIDPQQLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSPGARRAAAVRQRLAE--DFAGWS-HYRQLFAAI 367
Cdd:PRK06276 295 AKIIHIDIDPAEIGKNVRVDVPIVGDAKNVLRDLLAELMKKEIKNKSEWLERVKKLKKESIPrmDFDDKPiKPQRVIKEL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 368 LAEWPDARFVGDSTQTVYSGN------HLVDLDEPRRwFNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTL 441
Cdd:PRK06276 375 MEVLREIDPSKNTIITTDVGQnqmwmaHFFKTSAPRS-FISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 442 PELASAVEAKVGIVVLLWNNHGYGEIKR-----YMERREITPLGvdiYTPDFLAIARGFGCAAERARDLEHLRELLRGA- 515
Cdd:PRK06276 454 QELATIAEYDIPVVICIFDNRTLGMVYQwqnlyYGKRQSEVHLG---ETPDFVKLAESYGVKADRVEKPDEIKEALKEAi 530
|
570
....*....|
gi 1521190028 516 PADRPLIVEV 525
Cdd:PRK06276 531 KSGEPYLLDI 540
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-526 |
2.18e-70 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 235.15 E-value: 2.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGvhtvELYrgLP-------GSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITG 73
Cdd:PRK08199 7 ARTGGQILVDALRANGVERVFCVPG----ESY--LAvldalhdETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 74 PGMTNILTAMAQAYADSIPMLVIssVNERARLAHGNGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSER 153
Cdd:PRK08199 81 PGATNASIGVHTAFQDSTPMILF--VGQVARDFREREAFQEI-DYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 154 PRPVHIELPLDVITAPAEHlALRPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGG--CVEAAAEARALAAALDAPTA 231
Cdd:PRK08199 158 PGPVVLALPEDVLSETAEV-PDAPPYRRVAAAPGAADLARLAELLARAERPLVILGGSgwTEAAVADLRAFAERWGLPVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 232 LTINAKGLLPADHP-----LLLGSNQScvpVRELAAEADVVLAIGTELGETDydvvfDGGFAL------DGELIRIDIDP 300
Cdd:PRK08199 237 CAFRRQDLFDNRHPnyagdLGLGINPA---LAARIREADLVLAVGTRLGEVT-----TQGYTLldipvpRQTLVHVHPDA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 301 QQLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSpgarraaaVRQRLAEDFAGWSHYR------QLFAAIlaEWPDA 374
Cdd:PRK08199 309 EELGRVYRPDLAIVADPAAFAAALAALEPPASPAWAE--------WTAAAHADYLAWSAPLpgpgavQLGEVM--AWLRE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 375 RFVGDSTQTVYSGNHLVdldeprrW---FNASTGYGT--------LGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPE 443
Cdd:PRK08199 379 RLPADAIITNGAGNYAT-------WlhrFFRFRRYRTqlaptsgsMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 444 LASAVEAKVGIVVLLWNNHGYGEIKRYMERReiTP---LGVDIYTPDFLAIARGFGCAAERARDLEHLRE-LLRGAPADR 519
Cdd:PRK08199 452 LATAVQYGLPIIVIVVNNGMYGTIRMHQERE--YPgrvSGTDLTNPDFAALARAYGGHGETVERTEDFAPaFERALASGK 529
|
....*..
gi 1521190028 520 PLIVEVL 526
Cdd:PRK08199 530 PALIEIR 536
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
8-524 |
3.42e-69 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 233.33 E-value: 3.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 8 LVKQLEAWGVETVFGIPGVHTVELYRGLPGS-RIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQA 86
Cdd:PRK07789 37 VVRSLEELGVDVVFGIPGGAILPVYDPLFDStKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVTPIADA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 87 YADSIPMLVISSvnERARLAHGNGYLHElpnqRNLVGNVCAFS-HTLM--SAEELPAVLARAFAVFDSERPRPVHIELPL 163
Cdd:PRK07789 117 NMDSVPVVAITG--QVGRGLIGTDAFQE----ADIVGITMPITkHNFLvtDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 164 DVITAPAE-----HLAL---RPRTlasrpAPALAPLREAAARLRNAKKPLLLLGGGCV--EAAAEARALAAALDAPTALT 233
Cdd:PRK07789 191 DALQAQTTfswppRMDLpgyRPVT-----KPHGKQIREAAKLIAAARRPVLYVGGGVIraEASAELRELAELTGIPVVTT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 234 INAKGLLPADHPLLLGsnqscVP-----VRELAA--EADVVLAIGTEL-----GETDydvvfdgGFALDGELIRIDIDPQ 301
Cdd:PRK07789 266 LMARGAFPDSHPQHLG-----MPgmhgtVAAVAAlqRSDLLIALGARFddrvtGKLD-------SFAPDAKVIHADIDPA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 302 QLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSPgarraaavrqrlaeDFAGWSHY----RQLFA--------AILA 369
Cdd:PRK07789 334 EIGKNRHADVPIVGDVKEVIAELIAALRAEHAAGGKP--------------DLTAWWAYldgwRETYPlgydepsdGSLA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 370 -EW----------PDARFVGDSTQTVYSGNHLVDLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQ 438
Cdd:PRK07789 400 pQYvierlgeiagPDAIYVAGVGQHQMWAAQFIDYEKPRTWLN-SGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 439 FTLPELASAVEAKVGIVVLLWNNHGYGEIKR-----YMERREITPLGV-DIYTPDFLAIARGFGCAAERARDLEHLRELL 512
Cdd:PRK07789 479 MTNQELATCAIEGIPIKVALINNGNLGMVRQwqtlfYEERYSNTDLHThSHRIPDFVKLAEAYGCVGLRCEREEDVDAVI 558
|
570
....*....|....
gi 1521190028 513 RGAPA--DRPLIVE 524
Cdd:PRK07789 559 EKARAinDRPVVID 572
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
8-525 |
6.76e-69 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 231.20 E-value: 6.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 8 LVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQAY 87
Cdd:PRK06048 14 IIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTGIATAY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 88 ADSIPMLVISSVNERARLahGNGYLHElPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIELPLDVIT 167
Cdd:PRK06048 94 MDSVPIVALTGQVPRSMI--GNDAFQE-ADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKDVTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 168 AP-----AEHLALRprtlASRPAPALAP--LREAAARLRNAKKPLLLLGGGCV--EAAAEARALAAALDAPTALTINAKG 238
Cdd:PRK06048 171 AEidfdyPDKVELR----GYKPTYKGNPqqIKRAAELIMKAERPIIYAGGGVIssNASEELVELAETIPAPVTTTLMGIG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 239 LLPADHPLLLG--SNQSCVPVRELAAEADVVLAIGTELgeTDYDVVFDGGFALDGELIRIDIDPQQLMRNYTPSLAIHSD 316
Cdd:PRK06048 247 AIPTEHPLSLGmlGMHGTKYANYAIQESDLIIAVGARF--DDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPIVGD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 317 ARLAMRVLLAELpggeaspdspgarrAAAVRQRLAEDFAGWS-----HYRQLFAAILAEW---------PDARFVGDSTQ 382
Cdd:PRK06048 325 AKQVLKSLIKYV--------------QYCDRKEWLDKINQWKkeyplKYKEREDVIKPQYvieqiyelcPDAIIVTEVGQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 383 TVYSGNHLVDLDEPRRwFNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNH 462
Cdd:PRK06048 391 HQMWAAQYFKYKYPRT-FITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNG 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1521190028 463 GYGEIKR-----YMERREITPLGvdiYTPDFLAIARGFGCAAERARDLEHLRELLRGA-PADRPLIVEV 525
Cdd:PRK06048 470 YLGMVRQwqelfYDKRYSHTCIK---GSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAvASDRPVVIDF 535
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-525 |
1.88e-64 |
|
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: 218.85 E-value: 1.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 6 EFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQ 85
Cdd:TIGR02418 3 DLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 86 AYADSIPMLVISSVNERARLAHgngYLHELPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIELPLDV 165
Cdd:TIGR02418 83 ANSEGDPVVAIGGQVKRADLLK---LTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 166 ITAPAEHLALRPRTLASRPAPALAPLREAAARLRNAKKPLLLLG--GGCVEAAAEARALAAALDAPTALTINAKGLLPAD 243
Cdd:TIGR02418 160 VDSPVSVKAIPASYAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGlrASSPETTEAVRRLLKKTQLPVVETFQGAGAVSRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 244 -HPLLLG-----SNQscvPVRELAAEADVVLAIGtelgetdYDVV-FDGGF---ALDGELIRIDIDPQQLMRNYTPSLAI 313
Cdd:TIGR02418 240 lEDHFFGrvglfRNQ---PGDRLLKQADLVITIG-------YDPIeYEPRNwnsENDATIVHIDVEPAQIDNNYQPDLEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 314 HSDARLAMRVLLAELPGGEASPDSpgarraaavrqrlAEDFAGWSHYRQLFAAILAEWPDARF-------------VGDS 380
Cdd:TIGR02418 310 VGDIASTLDLLAERIPGYELPPDA-------------LAILEDLKQQREALDRVPATLKQAHLhpleiikamqaivTDDV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 381 TQTVYSGNHLVDLDEPRRWFNA-----STGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIV 455
Cdd:TIGR02418 377 TVTVDMGSHYIWMARYFRSYRArhlliSNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIV 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1521190028 456 VLLWNNHGYGEIKRYMERREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGA-PADRPLIVEV 525
Cdd:TIGR02418 457 HIIWNDNGYNMVEFQEEMKYQRSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAmEVEGPVVVDI 527
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-526 |
1.13e-63 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 217.94 E-value: 1.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTcGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNIL 80
Cdd:PRK07525 6 MTP-SEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 81 TAMAQAYADSIPMLVISSvnERARLAHGNGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPrPVHIE 160
Cdd:PRK07525 85 TAVATAYWAHTPVVLVTP--QAGTKTIGQGGFQEA-EQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESG-PAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 161 LPLDVITAPAEHLALRPRTLaSRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALtinAKGLL 240
Cdd:PRK07525 161 IPRDYFYGVIDVEIPQPVRL-ERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPV---ACGYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 241 -----PADHPLL---LGSNQSCVPVrELAAEADVVLAIGTELG--------ETDYdvvfdggFALDGELIRIDIDPQQLM 304
Cdd:PRK07525 237 hndafPGSHPLWvgpLGYNGSKAAM-ELIAKADVVLALGTRLNpfgtlpqyGIDY-------WPKDAKIIQVDINPDRIG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 305 RNYTPSLAIHSDARLAMRVLLAELPGGEA----------------------------SPDSPGARRAAAVRQRLaedfAG 356
Cdd:PRK07525 309 LTKKVSVGICGDAKAVARELLARLAERLAgdagreerkaliaaeksaweqelsswdhEDDDPGTDWNEEARARK----PD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 357 WSHYRQLFAAILAEWP-DARFVGDSTQTVYSGNHLVDLDEPRRWFNASTgYGTLGYGLPAAIGAKLGEPGRPVVSLMGDG 435
Cdd:PRK07525 385 YMHPRQALREIQKALPeDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGS-FGNCGYAFPAIIGAKIACPDRPVVGFAGDG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 436 GLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKR----YMERREItplGVDIYT-PDFLAIARGFGCAAERARDLEHLRE 510
Cdd:PRK07525 464 AWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKnqvdFYNNRFV---GTELDNnVSYAGIAEAMGAEGVVVDTQEELGP 540
|
570 580
....*....|....*....|
gi 1521190028 511 LLRGAPADR----PLIVEVL 526
Cdd:PRK07525 541 ALKRAIDAQnegkTTVIEIM 560
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
8-513 |
1.43e-63 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 217.68 E-value: 1.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 8 LVKQLEAWGVETVFGIPGVHTVELYRGLPGS-RIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQA 86
Cdd:PLN02470 19 LVEALEREGVDTVFAYPGGASMEIHQALTRSnCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGLADA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 87 YADSIPMLVISSVNERARLahGNGYLHELPNQrNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIELPLDV- 165
Cdd:PLN02470 99 LLDSVPLVAITGQVPRRMI--GTDAFQETPIV-EVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDIq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 166 --ITAPAEHLALRPRTLASR-PAPALAPLREAAARL-RNAKKPLLLLGGGCVEAAAEARALAAALDAPTALTINAKGLLP 241
Cdd:PLN02470 176 qqLAVPNWNQPMKLPGYLSRlPKPPEKSQLEQIVRLiSESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGLGAFP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 242 ADHPL---LLGSNQScVPVRELAAEADVVLAIGtelgetdydVVFDG-------GFALDGELIRIDIDPQQLMRNYTPSL 311
Cdd:PLN02470 256 ASDELslqMLGMHGT-VYANYAVDSADLLLAFG---------VRFDDrvtgkleAFASRASIVHIDIDPAEIGKNKQPHV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 312 AIHSDARLAMRVLLAELpggEASPDSpgarraaavrqrlAEDFAGWshyRQLFAAILAEWP------------------- 372
Cdd:PLN02470 326 SVCADVKLALQGLNKLL---EERKAK-------------RPDFSAW---RAELDEQKEKFPlsyptfgdaippqyaiqvl 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 373 DARFVGDSTQTVYSGNHLV------DLDEPRRWFnASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELAS 446
Cdd:PLN02470 387 DELTDGNAIISTGVGQHQMwaaqwyKYKEPRRWL-TSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELAT 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1521190028 447 AVEAKVGIVVLLWNNHGYGEIKRYMER-----REITPLG-----VDIYtPDFLAIARGFGCAAERARDLEHLRELLR 513
Cdd:PLN02470 466 IHVENLPVKIMVLNNQHLGMVVQWEDRfykanRAHTYLGdpdaeAEIF-PDFLKFAEGCKIPAARVTRKSDLREAIQ 541
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
6-525 |
2.35e-63 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 216.50 E-value: 2.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 6 EFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSR-IRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMA 84
Cdd:PRK08527 7 QMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNyFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVTGLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 85 QAYADSIPMLVISSvnERARLAHGNGYLHELpnqrNLVG--NVCAFSHTLM-SAEELPAVLARAFAVFDSERPRPVHIEL 161
Cdd:PRK08527 87 TAYMDSIPLVLISG--QVPNSLIGTDAFQEI----DAVGisRPCVKHNYLVkSIEELPRILKEAFYIARSGRPGPVHIDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 162 PLDVITAPAEHLALRPRTLAS-RPAPALAP--LREAAARLRNAKKPLLLLGGGCV--EAAAEARALAAALDAPTALTINA 236
Cdd:PRK08527 161 PKDVTATLGEFEYPKEISLKTyKPTYKGNSrqIKKAAEAIKEAKKPLFYLGGGAIlsNASEEIRELVKKTGIPAVETLMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 237 KGLLPADHPLLLG---------SNQScvpvrelAAEADVVLAIGTEL-----GETDYdvvfdggFALDGELIRIDIDPQQ 302
Cdd:PRK08527 241 RGVLRSDDPLLLGmlgmhgsyaANMA-------MSECDLLISLGARFddrvtGKLSE-------FAKHAKIIHVDIDPSS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 303 LMRNYTPSLAIHSDARLAMRVLLAELpgGEASPdspgarraaavrqrlaEDFAGW----SHYRQLFA--------AILAE 370
Cdd:PRK08527 307 ISKIVNADYPIVGDLKNVLKEMLEEL--KEENP----------------TTYKEWreilKRYNELHPlsyedsdeVLKPQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 371 WP---DARFVGDSTQ-TVYSGNH------LVDLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFT 440
Cdd:PRK08527 369 WVierVGELLGDDAIiSTDVGQHqmwvaqFYPFNYPRQLAT-SGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMN 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 441 LPELASAVEAKVGIVVLLWNNHGYGEIKR-----YMERREITPLGVDiytPDFLAIARGFGCAAERARDLEHLRELLRGA 515
Cdd:PRK08527 448 IQELMTAVEYKIPVINIILNNNFLGMVRQwqtffYEERYSETDLSTQ---PDFVKLAESFGGIGFRVTTKEEFDKALKEA 524
|
570
....*....|.
gi 1521190028 516 -PADRPLIVEV 525
Cdd:PRK08527 525 lESDKVALIDV 535
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
9-526 |
1.46e-62 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 215.23 E-value: 1.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 9 VKQLEAWGVETVFGIPGVHTVELYRGLPGSR-IRHVTPRHEQGAGFMADGYARVT-GKPGVCFIITGPGMTNILTAMAQA 86
Cdd:PRK11269 11 VLVLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGLYSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 87 YADSIPMLVISSVNERARlahgngyLHELPNQ----RNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIELP 162
Cdd:PRK11269 91 SADSIPILCITGQAPRAR-------LHKEDFQavdiESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 163 LDVITAPAEhlaLRPRTLAS----RPAPALAPLREAAARLRNAKKPLLLLGGGCV--EAAAEARALAAALDAPTALTINA 236
Cdd:PRK11269 164 FDVQVAEIE---FDPDTYEPlpvyKPAATRAQIEKALEMLNAAERPLIVAGGGVInaDASDLLVEFAELTGVPVIPTLMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 237 KGLLPADHPLLLG----------SNQSCVpvrelaaEADVVLAIGTEL-----GETDydvVFDGGfaldGELIRIDIDPQ 301
Cdd:PRK11269 241 WGAIPDDHPLMAGmvglqtshryGNATLL-------ASDFVLGIGNRWanrhtGSVE---VYTKG----RKFVHVDIEPT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 302 QLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSPgarraaavrqrlaeDFAGWSH---------------------- 359
Cdd:PRK11269 307 QIGRVFGPDLGIVSDAKAALELLVEVAREWKAAGRLP--------------DRSAWVAdcqerkrtllrkthfdnvpikp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 360 ---YRQLFAAIlaeWPDARFVgdSTQTVY--SGNHLVDLDEPRRWFNASTGyGTLGYGLPAAIGAKLGEPGRPVVSLMGD 434
Cdd:PRK11269 373 qrvYEEMNKAF---GRDTCYV--STIGLSqiAAAQFLHVYKPRHWINCGQA-GPLGWTIPAALGVRAADPDRNVVALSGD 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 435 GGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIkRYMER------------REITPLGVDIYTPDFLAIARGFGCAAERA 502
Cdd:PRK11269 447 YDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLI-RQAQRafdmdycvqlafENINSPELNGYGVDHVKVAEGLGCKAIRV 525
|
570 580
....*....|....*....|....*....
gi 1521190028 503 RDLEHLRELLRGAPAD-----RPLIVEVL 526
Cdd:PRK11269 526 FKPEDIAPALEQAKALmaefrVPVVVEVI 554
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-525 |
4.99e-61 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 210.83 E-value: 4.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGL-PGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNI 79
Cdd:PRK08979 3 MLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALhEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 80 LTAMAQAYADSIPMLVISsvnerarlahGNgylheLPNqrNLVGN--------------VCAFSHTLMSAEELPAVLARA 145
Cdd:PRK08979 83 ITGIATAYMDSIPMVVLS----------GQ-----VPS--NLIGNdafqecdmigisrpVVKHSFLVKDAEDIPEIIKKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 146 FAVFDSERPRPVHIELPLDVITAPAEHLALRPRTLASRP-APALA----PLREAAARLRNAKKPLLLLGGGCV--EAAAE 218
Cdd:PRK08979 146 FYIASTGRPGPVVIDLPKDCLNPAILHPYEYPESIKMRSyNPTTSghkgQIKRGLQALLAAKKPVLYVGGGAIisGADKQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 219 ARALAAALDAPTALTINAKGLLPADHPLLLG--SNQSCVPVRELAAEADVVLAIGTELGETDYDVVfdGGFALDGELIRI 296
Cdd:PRK08979 226 ILQLAEKLNLPVVSTLMGLGAFPGTHKNSLGmlGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNL--EKYCPNATILHI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 297 DIDPQQLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSpgarraaAVRQRLAEDFAGWSHYRQLFAAILAEWPDARF 376
Cdd:PRK08979 304 DIDPSSISKTVRVDIPIVGSADKVLDSMLALLDESGETNDE-------AAIASWWNEIEVWRSRNCLAYDKSSERIKPQQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 377 VGDSTQTVYSGNHLV---------------DLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTL 441
Cdd:PRK08979 377 VIETLYKLTNGDAYVasdvgqhqmfaalyyPFDKPRRWIN-SGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 442 PELASAVEAKVGIVVLLWNNHGYGEIKRYMERreitplgvdIYT-----------PDFLAIARGFGCAAERARDLEHLRE 510
Cdd:PRK08979 456 QELSTALQYDIPVKIINLNNRFLGMVKQWQDM---------IYQgrhshsymdsvPDFAKIAEAYGHVGIRISDPDELES 526
|
570
....*....|....*..
gi 1521190028 511 LLRGAPA--DRPLIVEV 525
Cdd:PRK08979 527 GLEKALAmkDRLVFVDI 543
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
6-501 |
9.14e-61 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 209.35 E-value: 9.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 6 EFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQ 85
Cdd:PRK08978 5 QWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 86 AYADSIPMLVISSvnERARLAHGNGYLHELpnqrnlvgNVCAFS-----HTLM--SAEELPAVLARAFAVFDSERPRPVH 158
Cdd:PRK08978 85 ALLDSVPVVAITG--QVSSPLIGTDAFQEI--------DVLGLSlactkHSFLvqSLEELPEIMAEAFEIASSGRPGPVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 159 IELPLDVITAPAEhLALRPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALTINAKG 238
Cdd:PRK08978 155 VDIPKDIQLAEGE-LEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 239 L--LPADHPLLLG---------SNqscvpvreLAA-EADVVLAIGTElgetdydvvFD-------GGFALDGELIRIDID 299
Cdd:PRK08978 234 LgaVEADHPYYLGmlgmhgtkaAN--------LAVqECDLLIAVGAR---------FDdrvtgklNTFAPHAKVIHLDID 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 300 PQQLMRNYTPSLAIHSDARLAMRVLLAELpggeaspdspgarraaavrqrlaeDFAGWSH----YRQLFA--------AI 367
Cdd:PRK08978 297 PAEINKLRQAHVALQGDLNALLPALQQPL------------------------NIDAWRQhcaqLRAEHAwrydhpgeAI 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 368 LAEW----------PDARFVGDSTQ-TVYSGNHLvDLDEPRRwFNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGG 436
Cdd:PRK08978 353 YAPAllkqlsdrkpADTVVTTDVGQhQMWVAQHM-RFTRPEN-FITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGS 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1521190028 437 LQFTLPELASAVEAKVGIVVLLWNNHGYGEIK---------RYMErreitplgVDIY-TPDFLAIARGFGCAAER 501
Cdd:PRK08978 431 FMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRqwqqlffdeRYSE--------TDLSdNPDFVMLASAFGIPGQT 497
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
1-515 |
5.92e-60 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 207.77 E-value: 5.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRG----LPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGM 76
Cdd:PRK06456 1 MPTGARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 77 TNILTAMAQAYADSIPmlVISSVNERARLAHGNGYLHElPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRP 156
Cdd:PRK06456 81 TNLVTGLITAYWDSSP--VIAITGQVPRSVMGKMAFQE-ADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 157 VHIELPLDVITAPAEHLAL--RPRTLASRPAPALA---PLREAAARLRNAKKPLLLLGGGCV--EAAAEARALAAALDAP 229
Cdd:PRK06456 158 VVIDIPRDIFYEKMEEIKWpeKPLVKGYRDFPTRIdrlALKKAAEILINAERPIILVGTGVVwsNATPEVLELAELLHIP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 230 TALTINAKGLLPADHPLLLGS--NQSCVPVRELAAEADVVLAIGTELGE---TDYDVVFDGGfaldGELIRIDIDPQQLM 304
Cdd:PRK06456 238 IVSTFPGKTAIPHDHPLYFGPmgYYGRAEASMAALESDAMLVVGARFSDrtfTSYDEMVETR----KKFIMVNIDPTDGE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 305 RNYTPSLAIHSDARLAMRVLLAELPggeaspdspgarraaavRQRLAEDFAGW----SHYRQLFAAI--------LAEWP 372
Cdd:PRK06456 314 KAIKVDVGIYGNAKIILRELIKAIT-----------------ELGQKRDRSAWlkrvKEYKEYYSQFyyteengkLKPWK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 373 DARFV-----GDSTQTVYSGNHLV------DLDEPRRWFnASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTL 441
Cdd:PRK06456 377 IMKTIrqalpRDAIVTTGVGQHQMwaevfwEVLEPRTFL-TSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTG 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1521190028 442 PELASAVEAKVGIVVLLWNNHGYGEIKR----YMERREItplGVDI-YTPDFLAIARGFGCAAERARDLEHLRELLRGA 515
Cdd:PRK06456 456 TNLATAVDEHIPVISVIFDNRTLGLVRQvqdlFFGKRIV---GVDYgPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSA 531
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
2-525 |
1.44e-59 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 206.78 E-value: 1.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 2 TTCGEFLVKQLEAWGVETVFGIPG---VHTVELYRGLPgSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTN 78
Cdd:PRK08611 4 IKAGEALVKLLQDWGIDHVYGIPGdsiDAVVDALRKEQ-DKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 79 ILTAMAQAYADSIPMLVISSVNERARLahGNGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVH 158
Cdd:PRK08611 83 LLNGLYDAKMDHVPVLALAGQVTSDLL--GTDFFQEV-NLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 159 I---ELPLDVITAPAEHLAlrPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALTIN 235
Cdd:PRK08611 160 TipdDLPAQKIKDTTNKTV--DTFRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 236 AKGLLPADHPLLLGsNQSCV---PVRELAAEADVVLAIGTELGETDYdvvfdggFALDGELIRIDIDPQQLMRNYTPSLA 312
Cdd:PRK08611 238 AKGIIPDDHPYSLG-NLGKIgtkPAYEAMQEADLLIMVGTNYPYVDY-------LPKKAKAIQIDTDPANIGKRYPVNVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 313 IHSDARLAMRVLLAElpgGEASPDSPgarraaaVRQRLAEDFAGWSHY--------------RQLFAAILAEWP-DARF- 376
Cdd:PRK08611 310 LVGDAKKALHQLTEN---IKHVEDRR-------FLEACQENMAKWWKWmeedennastpikpERVMAAIQKIADdDAVLs 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 377 --VGdsTQTVYSGNHLvDLdEPRRWFNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGI 454
Cdd:PRK08611 380 vdVG--TVTVWSARYL-NL-GTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPI 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1521190028 455 VVLLWNNHGYGEIKrYmERREITPL--GVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGA-PADRPLIVEV 525
Cdd:PRK08611 456 VVVVLNNQQLAFIK-Y-EQQAAGELeyAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEAlAQDKPVIIDV 527
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
3-524 |
1.68e-59 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 206.36 E-value: 1.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 3 TCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTA 82
Cdd:PRK06725 16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 83 MAQAYADSIPMLVISSvNERARLAHGNGYlhelpNQRNLVG---NVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHI 159
Cdd:PRK06725 96 LADAYMDSIPLVVITG-QVATPLIGKDGF-----QEADVVGitvPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 160 ELPLDVITAPA-----EHLALRPRTLASRPAPalAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAP--TAL 232
Cdd:PRK06725 170 DIPKDVQNEKVtsfynEVVEIPGYKPEPRPDS--MKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRipVVS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 233 TINAKGLLPADHPLLLG--SNQSCVPVRELAAEADVVLAIGTElgetdYDVVFDGG---FALDGELIRIDIDPQQLMRNY 307
Cdd:PRK06725 248 TLMGLGAYPPGDPLFLGmlGMHGTYAANMAVTECDLLLALGVR-----FDDRVTGKlelFSPHSKKVHIDIDPSEFHKNV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 308 TPSLAIHSDARLAMRVLLAElpggeaspdsPGARRAAAVRQRLAEDFAGWSHYRQLFAAILAEWPDARFVGDSTQ----- 382
Cdd:PRK06725 323 AVEYPVVGDVKKALHMLLHM----------SIHTQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNgeaiv 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 383 TVYSGNH------LVDLDEPRRWFnASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVV 456
Cdd:PRK06725 393 TTEVGQHqmwaahFYKAKNPRTFL-TSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKV 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1521190028 457 LLWNNHGYGEIKRYME-----RREITPLGvdiyTPDFLAIARGFGCAAERARDLEHLRELLRGAPADR-PLIVE 524
Cdd:PRK06725 472 FIINNKFLGMVRQWQEmfyenRLSESKIG----SPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEgPVVVD 541
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
2-526 |
1.27e-57 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 201.20 E-value: 1.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 2 TTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSR-IRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNIL 80
Cdd:PRK07282 10 KSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEgIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 81 TAMAQAYADSIPMLVISSvnERARLAHGNGYLHElpnqRNLVG---NVCAFSHTLMSAEELPAVLARAFAVFDSERPRPV 157
Cdd:PRK07282 90 TGIADAMSDSVPLLVFTG--QVARAGIGKDAFQE----ADIVGitmPITKYNYQIRETADIPRIITEAVHIATTGRPGPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 158 HIELPLDV-------ITAPAEHLALRPRTLasrpAPALAPLREAAARLRNAKKPLLLLGGGC--VEAAAEARALAAALDA 228
Cdd:PRK07282 164 VIDLPKDVsaletdfIYDPEVNLPSYQPTL----EPNDMQIKKILKQLSKAKKPVILAGGGInyAEAATELNAFAERYQI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 229 PTALTINAKGLLPADHPLLLG---------SNQSCVpvrelaaEADVVLAIGTELgeTDYDVVFDGGFALDGELIRIDID 299
Cdd:PRK07282 240 PVVTTLLGQGTIATSHPLFLGmggmhgsyaANIAMT-------EADFMINIGSRF--DDRLTGNPKTFAKNAKVAHIDID 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 300 PQQLMRNYTPSLAIHSDARLAMRVLLAElpgGEASPDSPGARRAAAVRQRLAEDFAGWSHYRQLFAAIlaewpdaRFVGD 379
Cdd:PRK07282 311 PAEIGKIIKTDIPVVGDAKKALQMLLAE---PTVHNNTEKWIEKVTKDKNRVRSYDKKERVVQPQAVI-------ERIGE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 380 STQtvysGNHLV--DLDEPRRWF-------NA-----STGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELA 445
Cdd:PRK07282 381 LTN----GDAIVvtDVGQHQMWAaqyypyqNErqlvtSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 446 SAVEAKVGIVVLLWNNHGYGEIKR-----YMERREITPLGVDiytPDFLAIARGFGCAAERARDLEHLRELLRGAPADRP 520
Cdd:PRK07282 457 ILNIYKVPIKVVMLNNHSLGMVRQwqesfYEGRTSESVFDTL---PDFQLMAQAYGIKHYKFDNPETLAQDLEVITEDVP 533
|
....*.
gi 1521190028 521 LIVEVL 526
Cdd:PRK07282 534 MLIEVD 539
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-525 |
1.28e-57 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 201.51 E-value: 1.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGL-PGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNI 79
Cdd:PRK06466 3 LLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALfKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 80 LTAMAQAYADSIPMLVISSvnerarlahgngylhELPNqrNLVGNVcAFSHTLM---------------SAEELPAVLAR 144
Cdd:PRK06466 83 ITGIATAYMDSIPMVVLSG---------------QVPS--TLIGED-AFQETDMvgisrpivkhsfmvkHASEIPEIIKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 145 AFAVFDSERPRPVHIELPLDvITAPAEHLALR-PRTLASRP-APAL----APLREAAARLRNAKKPLLLLGGGCVEAAAE 218
Cdd:PRK06466 145 AFYIAQSGRPGPVVVDIPKD-MTNPAEKFEYEyPKKVKLRSySPAVrghsGQIRKAVEMLLAAKRPVIYSGGGVVLGNAS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 219 ARALAAALDAPTALTINAKGL--LPADHPLLLG--SNQSCVPVRELAAEADVVLAIGTELGetdyDVVFDG--GFALDGE 292
Cdd:PRK06466 224 ALLTELAHLLNLPVTNTLMGLggFPGTDRQFLGmlGMHGTYEANMAMHHADVILAVGARFD----DRVTNGpaKFCPNAK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 293 LIRIDIDPQQLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSPgarraaaVRQRLAEDFAGWSHYRQLF-------- 364
Cdd:PRK06466 300 IIHIDIDPASISKTIKADIPIVGPVESVLTEMLAILKEIGEKPDKE-------ALAAWWKQIDEWRGRHGLFpydkgdgg 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 365 -----AAILAEWP----DARFVGDSTQTVYSGNHLVDLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDG 435
Cdd:PRK06466 373 iikpqQVVETLYEvtngDAYVTSDVGQHQMFAAQYYKFNKPNRWIN-SGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 436 GLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKR-------------YMERreitplgvdiyTPDFLAIARGFGCAAERA 502
Cdd:PRK06466 452 SIQMNIQELSTCLQYGLPVKIINLNNGALGMVRQwqdmqyegrhshsYMES-----------LPDFVKLAEAYGHVGIRI 520
|
570 580
....*....|....*....|....*
gi 1521190028 503 RDLEHLRELLRGAPA--DRPLIVEV 525
Cdd:PRK06466 521 TDLKDLKPKLEEAFAmkDRLVFIDI 545
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
3-525 |
1.43e-57 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 202.20 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 3 TCGEFLVKQLEAWGVETVFGIPGVHTV----ELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTN 78
Cdd:PRK07418 20 TGAYALMDSLKRHGVKHIFGYPGGAILpiydELYKAEAEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 79 ILTAMAQAYADSIPMLVISSvnERARLAHGNGYLHE-------LPnqrnlvgnVCAFSHTLMSAEELPAVLARAFAVFDS 151
Cdd:PRK07418 100 LVTGIATAQMDSVPMVVITG--QVPRPAIGTDAFQEtdifgitLP--------IVKHSYVVRDPSDMARIVAEAFHIASS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 152 ERPRPVHIELPLDVIT-----APAEHLALRPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAAL 226
Cdd:PRK07418 170 GRPGPVLIDIPKDVGQeefdyVPVEPGSVKPPGYRPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 227 DAP--TALTINAKGLLPADHPLLLG---------SNQScvpvrelAAEADVVLAIGTElgetdydvvFD-------GGFA 288
Cdd:PRK07418 250 RFQipVTTTLMGKGAFDEHHPLSVGmlgmhgtayANFA-------VTECDLLIAVGAR---------FDdrvtgklDEFA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 289 LDGELIRIDIDPQQLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSpgarraaavrQRLAEDFAGWSHYRQLFA--- 365
Cdd:PRK07418 314 SRAKVIHIDIDPAEVGKNRRPDVPIVGDVRKVLVKLLERSLEPTTPPRT----------QAWLERINRWKQDYPLVVppy 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 366 -----------AILAEWPDARFVGDSTQ-TVYSGNHLvdLDEPRRWFnASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMG 433
Cdd:PRK07418 384 egeiypqevllAVRDLAPDAYYTTDVGQhQMWAAQFL--RNGPRRWI-SSAGLGTMGFGMPAAMGVKVALPDEEVICIAG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 434 DGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKR-----YMERREITPLGVDIytPDFLAIARGFGCAAERARDLEHL 508
Cdd:PRK07418 461 DASFLMNIQELGTLAQYGINVKTVIINNGWQGMVRQwqesfYGERYSASNMEPGM--PDFVKLAEAFGVKGMVISERDQL 538
|
570
....*....|....*...
gi 1521190028 509 RELLRGAPA-DRPLIVEV 525
Cdd:PRK07418 539 KDAIAEALAhDGPVLIDV 556
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
5-171 |
3.57e-57 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 188.21 E-value: 3.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 5 GEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGS-RIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAM 83
Cdd:pfam02776 2 AEALADVLKALGVDTVFGVPGGHILPLLDALAKSpGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 84 AQAYADSIPMLVISSVNERARLAHgnGYLHELPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIELPL 163
Cdd:pfam02776 82 ANAYVDSVPLLVISGQRPRSLVGR--GALQQELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPL 159
|
....*...
gi 1521190028 164 DVITAPAE 171
Cdd:pfam02776 160 DVLLEEVD 167
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
1-526 |
4.02e-57 |
|
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: 200.47 E-value: 4.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTcGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNIL 80
Cdd:TIGR03457 2 MTP-SEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 81 TAMAQAYADSIPMLVISSvnERARLAHGNGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPrPVHIE 160
Cdd:TIGR03457 81 TAIAAAYWAHTPVVIVTP--EAGTKTIGLGGFQEA-DQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREMG-PAQLN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 161 LPLDVITAPAEHLALRPRTLaSRPAPALAPLREAAARLRNAKKPLLLLGGGCV--EAAAEARALAAALDAPTALTINAKG 238
Cdd:TIGR03457 157 IPRDYFYGEIDVEIPRPVRL-DRGAGGATSLAQAARLLAEAKFPVIISGGGVVmgDAVEECKALAERLGAPVVNSYLHND 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 239 LLPADHPLLLG--SNQSCVPVRELAAEADVVLAIGTELGE----TDYDVVFdggFALDGELIRIDIDPQQLMRNYTPSLA 312
Cdd:TIGR03457 236 SFPASHPLWVGplGYQGSKAAMKLISDADVVLALGTRLGPfgtlPQYGIDY---WPKNAKIIQVDANAKMIGLVKKVTVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 313 IHSDARLAMRVLLAELPG--GEAS-------------------------PDSPGARRAAAVRQRLAEdfagWSHYRQLFA 365
Cdd:TIGR03457 313 ICGDAKAAAAEILQRLAGkaGDANraerkakiqaersaweqelsemtheRDPFSLDMIVEQRQEEGN----WLHPRQVLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 366 AILAEWP-DARFVGDSTQTVYSGNHLVDLDEPRRWFNASTgYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPEL 444
Cdd:TIGR03457 389 ELEKAMPeDAIVSTDIGNINSVANSYLRFEKPRKFLAPMS-FGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 445 ASAVEAKVGIVVLLWNNHGYGEIKR----YMERREItplGVDIYTP-DFLAIARGFGCAAERARDLEHLRELLRGAPADR 519
Cdd:TIGR03457 468 MTAVRHDIPVTAVVFRNRQWGAEKKnqvdFYNNRFV---GTELESElSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQ 544
|
570
....*....|.
gi 1521190028 520 ----PLIVEVL 526
Cdd:TIGR03457 545 aegkTTVIEIV 555
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
5-528 |
7.24e-57 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 199.27 E-value: 7.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 5 GEFLVKQLEAWGVETVFGIPGVHtveLYRGLPGSRIRHVTPRHEQGAGFMADGYARVTG--KPGVCFIITGPGMTNILTA 82
Cdd:PRK06154 23 AEAVAEILKEEGVELLFGFPVNE---LFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAFGG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 83 MAQAYADSIPMLVISSVNERARLahgngylHELPNQRNLV--GNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIE 160
Cdd:PRK06154 100 VAQAYGDSVPVLFLPTGYPRGST-------DVAPNFESLRnyRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 161 LPLDVITAPAEHLALRPR-TLASRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAA--EARALAAALDAPTALTINAK 237
Cdd:PRK06154 173 LPVDVLAEELDELPLDHRpSRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQAtpELKELAELLEIPVMTTLNGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 238 GLLPADHPLLLGSNQSCVP--VRELAAEADVVLAIGTELGETDYDVVFDGGfaldGELIRIDIDPQQLMRNYTPSLAIHS 315
Cdd:PRK06154 253 SAFPEDHPLALGSGGRARPatVAHFLREADVLFGIGCSLTRSYYGLPMPEG----KTIIHSTLDDADLNKDYPIDHGLVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 316 DARLAMRVLLAELpGGEASPDsPGARRAAAvrqrlaedfagwSHYRQLFAAILAEWPDA-----------RFVGDSTQTV 384
Cdd:PRK06154 329 DAALVLKQMIEEL-RRRVGPD-RGRAQQVA------------AEIEAVRAAWLAKWMPKltsdstpinpyRVVWELQHAV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 385 YSGNHLV--DLDEPRR----WFNAST-----GYGT---LGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEA 450
Cdd:PRK06154 395 DIKTVIIthDAGSPRDqlspFYVASRpgsylGWGKttqLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 451 KVGIVVLLWNNHGYGEIKRYMERREITPLGVDIyTPDFLAIARGFGCAAERARDLEHLRELLRGA----PADRPLIVEVL 526
Cdd:PRK06154 475 RIPILTILLNNFSMGGYDKVMPVSTTKYRATDI-SGDYAAIARALGGYGERVEDPEMLVPALLRAlrkvKEGTPALLEVI 553
|
..
gi 1521190028 527 QA 528
Cdd:PRK06154 554 TS 555
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
6-525 |
1.24e-56 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 198.16 E-value: 1.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 6 EFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQ 85
Cdd:PRK08617 9 DLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLATGLVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 86 AYADSIPMLVIS-SV--NERARLAHGNgylheLPNQrNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIELP 162
Cdd:PRK08617 89 ATAEGDPVVAIGgQVkrADRLKRTHQS-----MDNV-ALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 163 LDVITAPAEHLALRPRTLASRPAPALAPLREAAARLRNAKKPLLLLG--GGCVEAAAEARALAAALDAPTALTINAKGLL 240
Cdd:PRK08617 163 QDVVDAPVTSKAIAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLGmrASSPEVTAAIRRLLERTNLPVVETFQAAGVI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 241 PADH-PLLLG-----SNQscvPVRELAAEADVVLAIGtelgetdYDVV-FDGGF---ALDGELIRIDIDPQQLMRNYTPS 310
Cdd:PRK08617 243 SRELeDHFFGrvglfRNQ---PGDELLKKADLVITIG-------YDPIeYEPRNwnsEGDATIIHIDVLPAEIDNYYQPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 311 LAIHSDARLAMRVLLAELPGGEASPDSPG-------ARRAAAVRQRLAEDFAgwSHYRQLFAAILAEWPDarfvgDSTQT 383
Cdd:PRK08617 313 RELIGDIAATLDLLAEKLDGLSLSPQSLEileelraQLEELAERPARLEEGA--VHPLRIIRALQDIVTD-----DTTVT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 384 VYSGNHLVDLDEPRRWFNA-----STGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLL 458
Cdd:PRK08617 386 VDVGSHYIWMARYFRSYEPrhllfSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHII 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1521190028 459 WNNHGYGEIKRYMERREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA-DRPLIVEV 525
Cdd:PRK08617 466 WNDGHYNMVEFQEEMKYGRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALAtDGPVVIDI 533
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
6-162 |
3.90e-56 |
|
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: 185.04 E-value: 3.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 6 EFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQ 85
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1521190028 86 AYADSIPMLVISSvnERARLAHGNGYLHELPnQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIELP 162
Cdd:cd07035 81 AYLDSIPLLVITG--QRPTAGEGRGAFQEID-QVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLP 154
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
8-530 |
9.75e-56 |
|
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: 196.60 E-value: 9.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 8 LVKQLEAWGVETVFGIPGVHTVELYRGLPGSR--IRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQ 85
Cdd:TIGR02720 5 VLKVLEAWGVDHIYGIPGGSFNSTMDALSAERdrIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 86 AYADSIPMLVIssVNERARLAHGNGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVhIELPLDV 165
Cdd:TIGR02720 85 AKEDHVPVLAL--VGQVPTTGMNMDTFQEM-NENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHNGVAV-VTIPVDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 166 ----ITAPAEHLALRPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALTINAKGLLP 241
Cdd:TIGR02720 161 gwqeIPDNDYYASSVSYQTPLLPAPDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 242 ADHPLLLGSNQSCV--PVRELAAEADVVLAIG-----TELGETDYDVVFdggfaldgeLIRIDIDPQQLMRNYTPSLAIH 314
Cdd:TIGR02720 241 DRYPAYLGSAYRVAqkPANEALFQADLVLFVGnnypfAEVSKAFKNTKY---------FIQIDIDPAKLGKRHHTDIAVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 315 SDARLAMRVLLAElpgGEASPDSPgarraaaVRQRLAEDFAGWSHY--------------RQLFAAI--LAEwPDARF-- 376
Cdd:TIGR02720 312 ADAKKALAAILAQ---VEPRESTP-------WWQANVANVKNWRAYlasledktegplqaYQVYRAInkIAE-DDAIYsi 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 377 -VGDSTQTvysGNHLVDLDEPRRWFnASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIV 455
Cdd:TIGR02720 381 dVGDININ---SNRHLKMTPKNKWI-TSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 456 VLLWNNHGYGEIKRYMERREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA---------------DRP 520
Cdd:TIGR02720 457 NIVFSNCTYGFIKDEQEDTNQPLIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAKAikqgkpvlidakitgDRP 536
|
570
....*....|
gi 1521190028 521 LIVEVLQAAP 530
Cdd:TIGR02720 537 LPVEKLRLDP 546
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-525 |
2.00e-54 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 192.67 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 6 EFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQ 85
Cdd:PRK07710 20 QMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGLAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 86 AYADSIPMLVISSvnERARLAHGNGYLHElPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIELPLDV 165
Cdd:PRK07710 100 AMIDSLPLVVFTG--QVATSVIGSDAFQE-ADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKDM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 166 ITAPAE-------HL-ALRPRTlasrpAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAP--TALTIN 235
Cdd:PRK07710 177 VVEEGEfcydvqmDLpGYQPNY-----EPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEipVVHTLL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 236 AKGLLPADHPLLLG--SNQSCVPVRELAAEADVVLAIGTElgetdYDVVFDGG---FALDGELIRIDIDPQQLMRNYTPS 310
Cdd:PRK07710 252 GLGGFPADHPLFLGmaGMHGTYTANMALYECDLLINIGAR-----FDDRVTGNlayFAKEATVAHIDIDPAEIGKNVPTE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 311 LAIHSDARLAMRVLLAElPGGEASPDSpgarraaavrqrLAEDFAGWS-----HYRQLFAAI----LAEWPDARFVGDST 381
Cdd:PRK07710 327 IPIVADAKQALQVLLQQ-EGKKENHHE------------WLSLLKNWKekyplSYKRNSESIkpqkAIEMLYEITKGEAI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 382 QTVYSGNHLV------DLDEPRRWFnASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIV 455
Cdd:PRK07710 394 VTTDVGQHQMwaaqyyPFKTPDKWV-TSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVK 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1521190028 456 VLLWNNHGYGEIKR-----YMERREITPLGVDiytPDFLAIARGFGCAAERARDLEHLRELLRGAPA-DRPLIVEV 525
Cdd:PRK07710 473 VVILNNEALGMVRQwqeefYNQRYSHSLLSCQ---PDFVKLAEAYGIKGVRIDDELEAKEQLQHAIElQEPVVIDC 545
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
1-515 |
1.48e-53 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 190.68 E-value: 1.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEF-LVKQLEAWGVETVFGIPGVHTV----ELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPG 75
Cdd:CHL00099 8 REKTGAFaLIDSLVRHGVKHIFGYPGGAILpiydELYAWEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 76 MTNILTAMAQAYADSIPMLVISSVNERARLahGNGYLHE-------LPnqrnlvgnVCAFSHTLMSAEELPAVLARAFAV 148
Cdd:CHL00099 88 ATNLVTGIATAQMDSVPLLVITGQVGRAFI--GTDAFQEvdifgitLP--------IVKHSYVVRDARDISRIVAEAFYI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 149 FDSERPRPVHIELPLDV--------ITAPAEHLAlrpRTLASRPA--PALAPLREAAARLRNAKKPLLLLGGGCV--EAA 216
Cdd:CHL00099 158 AKHGRPGPVLIDIPKDVglekfdyyPPEPGNTII---KILGCRPIykPTIKRIEQAAKLILQSSQPLLYVGGGAIisDAH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 217 AEARALAAALDAPTALTINAKGLLPADHPLLLG---------SNQScvpvrelAAEADVVLAIGTEL-----GETDydvv 282
Cdd:CHL00099 235 QEITELAELYKIPVTTTLMGKGIFDEDHPLCLGmlgmhgtayANFA-------VSECDLLIALGARFddrvtGKLD---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 283 fdgGFALDGELIRIDIDPQQLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSpgarraaavrqrlaEDFAGWSH--- 359
Cdd:CHL00099 304 ---EFACNAQVIHIDIDPAEIGKNRIPQVAIVGDVKKVLQELLELLKNSPNLLES--------------EQTQAWRErin 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 360 -----Y-------------RQLFAAILAEWPDARFVGDSTQ-TVYSGNHLVDldEPRRWFnASTGYGTLGYGLPAAIGAK 420
Cdd:CHL00099 367 rwrkeYpllipkpstslspQEVINEISQLAPDAYFTTDVGQhQMWAAQFLKC--KPRKWL-SSAGLGTMGYGLPAAIGAQ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 421 LGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKR-----YMERreitplgvdiYT--------PD 487
Cdd:CHL00099 444 IAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMVRQwqqafYGER----------YShsnmeegaPD 513
|
570 580
....*....|....*....|....*...
gi 1521190028 488 FLAIARGFGCAAERARDLEHLRELLRGA 515
Cdd:CHL00099 514 FVKLAEAYGIKGLRIKSRKDLKSSLKEA 541
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-525 |
2.30e-53 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 190.06 E-value: 2.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPG-SRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNI 79
Cdd:PRK07979 3 MLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 80 LTAMAQAYADSIPMLVISSvnERARLAHGNGYLHELpnqrNLVG---NVCAFSHTLMSAEELPAVLARAFAVFDSERPRP 156
Cdd:PRK07979 83 ITGIATAYMDSIPLVVLSG--QVATSLIGYDAFQEC----DMVGisrPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 157 VHIELPLDVITaPAEHLA-LRPRTLASRP-APAL----APLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPT 230
Cdd:PRK07979 157 VVVDLPKDILN-PANKLPyVWPESVSMRSyNPTTqghkGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 231 ALTINAKGL--LPADHPLLLG--SNQSCVPVRELAAEADVVLAIGTELGETDYDVVfdGGFALDGELIRIDIDPQQLMRN 306
Cdd:PRK07979 236 PVVSSLMGLgaFPATHRQSLGmlGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNL--AKYCPNATVLHIDIDPTSISKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 307 YTPSLAIHSDARLAMRVLLAELPGGEASPDspgarraaavrQRLAEDFagWSHYRQLF-----------------AAILA 369
Cdd:PRK07979 314 VTADIPIVGDARQVLEQMLELLSQESAHQP-----------LDEIRDW--WQQIEQWRarqclkydthsekikpqAVIET 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 370 EWPDARfvGDSTQTVYSGNHLV------DLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPE 443
Cdd:PRK07979 381 LWRLTK--GDAYVTSDVGQHQMfaalyyPFDKPRRWIN-SGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 444 LASAVEAKVGIVVLLWNNHGYGEIKRYMERreitplgvdIYT-----------PDFLAIARGF---GCAAERARDLE-HL 508
Cdd:PRK07979 458 LSTALQYELPVLVLNLNNRYLGMVKQWQDM---------IYSgrhsqsymqslPDFVRLAEAYghvGIQISHPDELEsKL 528
|
570
....*....|....*..
gi 1521190028 509 RELLRGAPADRPLIVEV 525
Cdd:PRK07979 529 SEALEQVRNNRLVFVDV 545
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
6-532 |
8.69e-53 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 188.58 E-value: 8.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 6 EFLVKQLEAWGVETVFGIPGVHTVELYRGLPG-SRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMA 84
Cdd:PRK06882 8 EMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITGIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 85 QAYADSIPMLVISSvNERARLAHGNGYlhelpNQRNLVG---NVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIEL 161
Cdd:PRK06882 88 TAYTDSVPLVILSG-QVPSNLIGTDAF-----QECDMLGisrPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 162 PLDVITAPAEHLALRPRTLASRP-APAL----APLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALTINA 236
Cdd:PRK06882 162 PKDMVNPANKFTYEYPEEVSLRSyNPTVqghkGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 237 KGL--LPADHPLLLG--SNQSCVPVRELAAEADVVLAIGTELGETDYDVVfdGGFALDGELIRIDIDPQQLMRNYTPSLA 312
Cdd:PRK06882 242 MGLgaYPSTDKQFLGmlGMHGTYEANNAMHESDLILGIGVRFDDRTTNNL--AKYCPNAKVIHIDIDPTSISKNVPAYIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 313 IHSDARLAMRVLLAELPGGEASPDSpgarraaavrqrlaEDFAGWshYRQlfaaiLAEWPDA---RFVGDST-------- 381
Cdd:PRK06882 320 IVGSAKNVLEEFLSLLEEENLAKSQ--------------TDLTAW--WQQ-----INEWKAKkclEFDRTSDvikpqqvv 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 382 QTVYS------------GNHLV------DLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPE 443
Cdd:PRK06882 379 EAIYRltngdayvasdvGQHQMfaalhyPFDKPRRWIN-SGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 444 LASAVEAKVGIVVLLWNNHGYGEIKRYMERreitplgvdIYT-----------PDFLAIARGFGCAAERARDLEHLRELL 512
Cdd:PRK06882 458 LSTAKQYDIPVVIVSLNNRFLGMVKQWQDL---------IYSgrhsqvymnslPDFAKLAEAYGHVGIQIDTPDELEEKL 528
|
570 580
....*....|....*....|..
gi 1521190028 513 RGAPA--DRPLIVEVLQAAPFH 532
Cdd:PRK06882 529 TQAFSikDKLVFVDVNVDETEH 550
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
362-527 |
7.73e-49 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 166.28 E-value: 7.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 362 QLFAAILAEWP-DARFVGDSTQTVYSGNHLVDLdEPRRWFNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFT 440
Cdd:cd00568 1 RVLAALRAALPeDAIVVNDAGNSAYWAYRYLPL-RRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 441 LPELASAVEAKVGIVVLLWNNHGYGEIKRYMERR-EITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA-D 518
Cdd:cd00568 80 GQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFyGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAaG 159
|
....*....
gi 1521190028 519 RPLIVEVLQ 527
Cdd:cd00568 160 GPALIEVKT 168
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
5-513 |
8.73e-49 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 177.69 E-value: 8.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 5 GEFLVKQLEAWGVETVFGIPGVHTVELYRGL-PGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAM 83
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELyKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 84 AQAYADSIPMLVISSVNERArlAHGNGYLHELPN---QRNLVgnvcafSHTLM--SAEELPAVLARAFAVFDSERPRPVH 158
Cdd:PRK06965 104 ATAYMDSIPMVVISGQVPTA--AIGQDAFQECDTvgiTRPIV------KHNFLvkDVRDLAETVKKAFYIARTGRPGPVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 159 IELPLDVITAPAEHLAlrPRTLASRPAPAL-----APLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALT 233
Cdd:PRK06965 176 VDIPKDVSKTPCEYEY--PKSVEMRSYNPVtkghsGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 234 INAKGL--LPADHPLLLG------------SNQSCvpvrelaaeaDVVLAIGTELgetDYDVVFD-GGFA-LDGELIRID 297
Cdd:PRK06965 254 NTLMGLgaYPASDKKFLGmlgmhgtyeanmAMQHC----------DVLIAIGARF---DDRVIGNpAHFAsRPRKIIHID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 298 IDPQQLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSpgarraaAVRQRLAEDFAGWSHYRQLFAAILAEWPDARFV 377
Cdd:PRK06965 321 IDPSSISKRVKVDIPIVGDVKEVLKELIEQLQTAEHGPDA-------DALAQWWKQIEGWRSRDCLKYDRESEIIKPQYV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 378 ---------GDSTQTVYSGNHLV------DLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLP 442
Cdd:PRK06965 394 veklweltdGDAFVCSDVGQHQMwaaqfyRFNEPRRWIN-SGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQ 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1521190028 443 ELASAVEAKVGIVVLLWNNHGYGEIKRYMErREITPLGVDIYT---PDFLAIARGFGCAA---ERARDLE-HLRELLR 513
Cdd:PRK06965 473 ELSTCLQYDTPVKIISLNNRYLGMVRQWQE-IEYSKRYSHSYMdalPDFVKLAEAYGHVGmriEKTSDVEpALREALR 549
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
3-529 |
1.50e-48 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 177.21 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 3 TCGEFLVKQLEAWGVETVFGIPGVHTVELYRGL-PGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILT 81
Cdd:PRK09107 12 TGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIfQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 82 AMAQAYADSIPMLVISSvnerarlahgngylhELPNqrNLVGNVcAFS-------------HTLM--SAEELPAVLARAF 146
Cdd:PRK09107 92 PLQDALMDSIPLVCITG---------------QVPT--HLIGSD-AFQecdtvgitrpctkHNWLvkDVNDLARVIHEAF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 147 AVFDSERPRPVHIELPLDVITAPAEHLALRPRTLASRPAPAL----APLREAAARLRNAKKPLLLLGGGCV----EAAAE 218
Cdd:PRK09107 154 HVATSGRPGPVVVDIPKDVQFATGTYTPPQKAPVHVSYQPKVkgdaEAITEAVELLANAKRPVIYSGGGVInsgpEASRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 219 ARALAAALDAPTALTINAKGLLPADHPLLLG---------SNQScvpvrelAAEADVVLAIGTEL-----GETDydvvfd 284
Cdd:PRK09107 234 LRELVELTGFPITSTLMGLGAYPASGKNWLGmlgmhgtyeANMA-------MHDCDVMLCVGARFddritGRLD------ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 285 gGFALDGELIRIDIDPQQLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSPGarraaavRQRLAEDFAGWS-----H 359
Cdd:PRK09107 301 -AFSPNSKKIHIDIDPSSINKNVRVDVPIIGDVGHVLEDMLRLWKARGKKPDKEA-------LADWWGQIARWRarnslA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 360 YRQLFAAILAEWPDARFVG-----DSTQTVYSGNH------LVDLDEPRRWFnASTGYGTLGYGLPAAIGAKLGEPGRPV 428
Cdd:PRK09107 373 YTPSDDVIMPQYAIQRLYEltkgrDTYITTEVGQHqmwaaqFFGFEEPNRWM-TSGGLGTMGYGLPAALGVQIAHPDALV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 429 VSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKRYMERREITPLGvDIYT---PDFLAIARGFGCAAERARDL 505
Cdd:PRK09107 452 IDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMGMVRQWQQLLHGNRLS-HSYTeamPDFVKLAEAYGAVGIRCEKP 530
|
570 580
....*....|....*....|....*...
gi 1521190028 506 EHL----RELLRgapADRPLIVEVLQAA 529
Cdd:PRK09107 531 GDLddaiQEMID---VDKPVIFDCRVAN 555
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-525 |
1.68e-48 |
|
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: 176.12 E-value: 1.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGL-PGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCfiIT-GPGMTN 78
Cdd:COG3961 4 TYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIeAHPGIRWVGCCNELNAGYAADGYARVNGLGALV--TTyGVGELS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 79 ILTAMAQAYADSIPMLVIS---SVNERAR--LAH---GNGYLHelpNQRNLVGNVCAfSHTLMSAEELPA----VLARAF 146
Cdd:COG3961 82 AINGIAGAYAERVPVVHIVgapGTRAQRRgpLLHhtlGDGDFD---HFLRMFEEVTV-AQAVLTPENAAAeidrVLAAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 147 avfdSERpRPVHIELPLDVITAPAE--HLALRPRTLASRPAPALAPLREAAARLRNAKKPLLLLG-----GGCVEAAAEA 219
Cdd:COG3961 158 ----REK-RPVYIELPRDVADAPIEppEAPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGvevhrFGLQEELLAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 220 RALAAALDAPtalTINAKGLLPADHPLLLG------SNQScvpVRELAAEADVVLAIGTELgeTDYDvvfDGGF--ALDG 291
Cdd:COG3961 233 AEKTGIPVAT---TLLGKSVLDESHPQFIGtyagaaSSPE---VREYVENADCVLCLGVVF--TDTN---TGGFtaQLDP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 292 ELIrIDIDPQQLmrnytpSLAIHSDARLAMRVLLAELPggEASPDSPGARRAAAVRQRLAEDFAG--------WSHYRQL 363
Cdd:COG3961 302 ERT-IDIQPDSV------RVGGHIYPGVSLADFLEALA--ELLKKRSAPLPAPAPPPPPPPAAPDapltqdrlWQRLQAF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 364 FAA---ILAEwpdarfVGDStqtVYsgnHLVDLDEPRRW-FNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQF 439
Cdd:COG3961 373 LDPgdiVVAD------TGTS---LF---GAADLRLPEGAtFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQL 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 440 TLPELASAVEAKVGIVVLLWNNHGYGeIKRYMERREITplGVDIYTPDFLAIARGFGCA---AERARDLEHLRELLRGAP 516
Cdd:COG3961 441 TAQELSTMLRYGLKPIIFVLNNDGYT-IERAIHGPDGP--YNDIANWDYAKLPEAFGGGnalGFRVTTEGELEEALAAAE 517
|
570
....*....|.
gi 1521190028 517 A--DRPLIVEV 525
Cdd:COG3961 518 AntDRLTLIEV 528
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
2-533 |
2.90e-48 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 176.10 E-value: 2.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 2 TTCGEFLVKQLEAWGVETVFG--IPGVhtveLYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNI 79
Cdd:PRK06112 14 GTVAHAIARALKRHGVEQIFGqsLPSA----LFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 80 LTAMAQAYADSIPMLVIssVNERARLAHGNGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHI 159
Cdd:PRK06112 90 VAPLAEALKASVPIVAL--VQDVNRDQTDRNAFQEL-DHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 160 ELPLDVITAPAEHLAL-RPRTLA------SRPAPALapLREAAARLRNAKKPLLLLGGG--CVEAAAEARALAAALDAPT 230
Cdd:PRK06112 167 LLPADLLTAAAAAPAApRSNSLGhfpldrTVPAPQR--LAEAASLLAQAQRPVVVAGGGvhISGASAALAALQSLAGLPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 231 ALTINAKGLLPADHPLLLGSNQSCVP-------VRELAAEADVVLAIGTELGETDYDVVfdGGFALDGELIRIDIDPQQL 303
Cdd:PRK06112 245 ATTNMGKGAVDETHPLSLGVVGSLMGprspgrhLRDLVREADVVLLVGTRTNQNGTDSW--SLYPEQAQYIHIDVDGEEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 304 MRNYTpSLAIHSDARLAMRVLLAELPGGEASPDSPGARRAAAVRQRLAEDFAGWSH-YRQLFAA------ILAEW----- 371
Cdd:PRK06112 323 GRNYE-ALRLVGDARLTLAALTDALRGRDLAARAGRRAALEPAIAAGREAHREDSApVALSDASpirperIMAELqavlt 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 372 PDARFVGD-STQTVYSGNHLVDLdEPRRWFNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEA 450
Cdd:PRK06112 402 GDTIVVADaSYSSIWVANFLTAR-RAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 451 KVGIVVLLWNNHGYGeikrYMERREITPLG-----VDIYTPDFLAIARGFGCAAERARDLEHLRELLRGA-PADRPLIVE 524
Cdd:PRK06112 481 GVPVTIVVLNNGILG----FQKHAETVKFGthtdaCHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAmAAPGPTLIE 556
|
....*....
gi 1521190028 525 VLQAAPFHP 533
Cdd:PRK06112 557 VITDPSAFP 565
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-515 |
5.54e-48 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 175.19 E-value: 5.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIR-HVTPR-----HEQGAGFMADGYARVTGKPGVCFIITGP 74
Cdd:PRK08327 6 MYTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAgRPLPEfvicpHEIVAISMAHGYALVTGKPQAVMVHVDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 75 GMTNILTAMAQAYADSIPMLVI---SSVNERARLAHGNGYLH---ELPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAV 148
Cdd:PRK08327 86 GTANALGGVHNAARSRIPVLVFagrSPYTEEGELGSRNTRIHwtqEMRDQGGLVREYVKWDYEIRRGDQIGEVVARAIQI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 149 FDSERPRPVHIELPLDVI--TAPAEHLALRPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGG-----CVEAAAEARA 221
Cdd:PRK08327 166 AMSEPKGPVYLTLPREVLaeEVPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITWRAgrtaeGFASLRRLAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 222 LAAALDAPTALTINAkglLPADHPLLLGSNQscvpvRELAAEADVVLAIgtelgetDYDVVF---DGGFALDGELIRIDI 298
Cdd:PRK08327 246 ELAIPVVEYAGEVVN---YPSDHPLHLGPDP-----RADLAEADLVLVV-------DSDVPWipkKIRPDADARVIQIDV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 299 DP---QQLMRNYTPSLAIHSDARLAMR---VLLAELPGGE-ASPDSPGARRAAAVRQRLAEDFAGWSHYRQLfAAILAEW 371
Cdd:PRK08327 311 DPlksRIPLWGFPCDLCIQADTSTALDqleERLKSLASAErRRARRRRAAVRELRIRQEAAKRAEIERLKDR-GPITPAY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 372 PDARF--VGDSTQTVYSG----NHLVDLDEPRRWFNASTGyGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPE-- 443
Cdd:PRK08327 390 LSYCLgeVADEYDAIVTEypfvPRQARLNKPGSYFGDGSA-GGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEaa 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 444 LASAVEAKVGIVVLLWNNHGYGEIKR---------YMERREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRG 514
Cdd:PRK08327 469 HWVAERYGLPVLVVVFNNGGWLAVKEavlevypegYAARKGTFPGTDFDPRPDFAKIAEAFGGYGERVEDPEELKGALRR 548
|
.
gi 1521190028 515 A 515
Cdd:PRK08327 549 A 549
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
5-472 |
2.59e-45 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 167.21 E-value: 2.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 5 GEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMA 84
Cdd:PRK05858 8 GRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 85 QAYADSIPMLVISSvneRA-RLAHGNGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVHIELPL 163
Cdd:PRK05858 88 AAQFNQSPLVVLGG---RApALRWGMGSLQEI-DHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 164 DVITAPAEHLALRPRTLASRPAPALAP--LREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALTIN--AKGL 239
Cdd:PRK05858 164 DHAFSMADDDGRPGALTELPAGPTPDPdaLARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNgmGRGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 240 LPADHPLLLGSnqscvpVRELA-AEADVVLAIGTELgetDYDVVFdGGFALDGELIRIDIDPQQLMRNYTPSLAIHSDAR 318
Cdd:PRK05858 244 VPADHPLAFSR------ARGKAlGEADVVLVVGVPM---DFRLGF-GVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 319 LAMRVlLAELPGGEASPDSPGARRAAAVRQRLAEDFAGWSH----------YRQLfAAILAEwpDARFVGDSTQTVYSGN 388
Cdd:PRK05858 314 AILSA-LAGAGGDRTDHQGWIEELRTAETAARARDAAELADdrdpihpmrvYGEL-APLLDR--DAIVIGDGGDFVSYAG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 389 HLVDLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIK 468
Cdd:PRK05858 390 RYIDPYRPGCWLD-PGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEK 468
|
....
gi 1521190028 469 RYME 472
Cdd:PRK05858 469 HPME 472
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
1-463 |
2.77e-44 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 164.77 E-value: 2.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNIL 80
Cdd:PRK09259 9 LTDGFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 81 TAMAQAYADSIPMLVISSVNERA--RLAHGNgylHELPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPVH 158
Cdd:PRK09259 89 TALANATTNCFPMIMISGSSEREivDLQQGD---YEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 159 IELPLDVI--TAPAEhLALRPRTLASRPAPALAPLREAAAR----LRNAKKPLLLLGGGC------------VEAAAEAR 220
Cdd:PRK09259 166 LDLPAKVLaqTMDAD-EALTSLVKVVDPAPAQLPAPEAVDRaldlLKKAKRPLIILGKGAayaqadeqirefVEKTGIPF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 221 ALAAAldaptaltinAKGLLPADHPlllgsnQSCVPVRELA-AEADVVLAIGTEL------GETDydvvfdgGFALDGEL 293
Cdd:PRK09259 245 LPMSM----------AKGLLPDTHP------QSAAAARSLAlANADVVLLVGARLnwllshGKGK-------TWGADKKF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 294 IRIDIDPQQLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSPGARRAAAVRQRLAEDFAG--------WSHYRQLFA 365
Cdd:PRK09259 302 IQIDIEPQEIDSNRPIAAPVVGDIGSVMQALLAGLKQNTFKAPAEWLDALAERKEKNAAKMAEklstdtqpMNFYNALGA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 366 --AILAEWPDARFVGDSTQTVYSGNHLVDLDEPRRWFNASTgYGTLGYGLPAAIGAKLgEPGRPVVSLMGDGGLQFTLPE 443
Cdd:PRK09259 382 irDVLKENPDIYLVNEGANTLDLARNIIDMYKPRHRLDCGT-WGVMGIGMGYAIAAAV-ETGKPVVAIEGDSAFGFSGME 459
|
490 500
....*....|....*....|
gi 1521190028 444 LASAVEAKVGIVVLLWNNHG 463
Cdd:PRK09259 460 VETICRYNLPVTVVIFNNGG 479
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
379-525 |
2.39e-43 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 151.20 E-value: 2.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 379 DSTQTVYSGNHLVDLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLL 458
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLT-SGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1521190028 459 WNNHGYGEIKRYME----RREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA-DRPLIVEV 525
Cdd:pfam02775 80 LNNGGYGMTRGQQTpfggGRYSGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEhDGPALIDV 151
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
1-525 |
2.70e-43 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 161.28 E-value: 2.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPgSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNIL 80
Cdd:PRK07092 11 MTTVRDATIDLLRRFGITTVFGNPGSTELPFLRDFP-DDFRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 81 TAMAQAYADSIPMLVISSVNERARLAH----GNGYLHELPnqRNLVGnvcaFSHTLMSAEELPAVLARAFAVFDSERPRP 156
Cdd:PRK07092 90 GNLFTAFKNHTPLVITAGQQARSILPFepflAAVQAAELP--KPYVK----WSIEPARAEDVPAAIARAYHIAMQPPRGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 157 VHIELPLDVITAPAEHLALRPRTLASRPAPALapLREAAARLRNAKKPLLLLGG-----GCVEAAAEARALAAALDAPTA 231
Cdd:PRK07092 164 VFVSIPYDDWDQPAEPLPARTVSSAVRPDPAA--LARLGDALDAARRPALVVGPavdraGAWDDAVRLAERHRAPVWVAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 232 LTinAKGLLPADHPLLLG----SNQSCVpvrELAAEADVVLAIGTEL------GETDYdvvFDGGfaldGELIRIDIDPQ 301
Cdd:PRK07092 242 MS--GRCSFPEDHPLFAGflpaSREKIS---ALLDGHDLVLVIGAPVftyhveGPGPH---LPEG----AELVQLTDDPG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 302 QLMRnyTP-SLAIHSDARLAMRVLLAELPGGeASPDSPGARRAAAVRQRlaedfAGWSHYRQLFAAILAEWP-DARFVGD 379
Cdd:PRK07092 310 EAAW--APmGDAIVGDIRLALRDLLALLPPS-ARPAPPARPMPPPAPAP-----GEPLSVAFVLQTLAALRPaDAIVVEE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 380 STQTVYSGNHLVDLDEPRRWFNASTGygTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLW 459
Cdd:PRK07092 382 APSTRPAMQEHLPMRRQGSFYTMASG--GLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVIL 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 460 NNHGYGEIK---RYMERREITplGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGA-PADRPLIVEV 525
Cdd:PRK07092 460 NNGRYGALRwfaPVFGVRDVP--GLDLPGLDFVALARGYGCEAVRVSDAAELADALARAlAADGPVLVEV 527
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
1-512 |
4.61e-41 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 155.37 E-value: 4.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNIL 80
Cdd:PRK06457 1 MPSVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 81 TAMAQAYADSIPMLVISSVNERARLAHgnGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARafAVFDSERPRPV-HI 159
Cdd:PRK06457 81 NGLYDAKMDHAPVIALTGQVESDMIGH--DYFQEV-NLTKLFDDVAVFNQILINPENAEYIIRR--AIREAISKRGVaHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 160 ELPLDVITAPAEHlalRPRTLASRPAPALAPLREAAARLRN-AKKPLLLLGGGCVEAAAEARALAAALDAPTALTINAKG 238
Cdd:PRK06457 156 NLPVDILRKSSEY---KGSKNTEVGKVKYSIDFSRAKELIKeSEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 239 LLPADHPL------LLGSNqscvPVRELAAEADVVLAIGTELGETDYdvvfdggFALDGELIRIDIDPQQLMRNYTPSLA 312
Cdd:PRK06457 233 ILPDLDPKvmggigLLGTK----PSIEAMDKADLLIMLGTSFPYVNF-------LNKSAKVIQVDIDNSNIGKRLDVDLS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 313 IHSDARLAMRVLLAELPGGEASpDSPGARRAAAVRQRLAEDFAGWSHYRQLFAAILAE--WPDARFVGDSTQ-TVYSGNH 389
Cdd:PRK06457 302 YPIPVAEFLNIDIEEKSDKFYE-ELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQkcKKDAVIVTDTGNvTMWTARH 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 390 LVDLDEprRWFNASTGYGTLGYGLPAAIGAKLG-EPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIK 468
Cdd:PRK06457 381 FRASGE--QTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIK 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1521190028 469 RYMERREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELL 512
Cdd:PRK06457 459 FEQEVMGYPEWGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEII 502
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
389-526 |
1.21e-34 |
|
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: 128.77 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 389 HLVDLDEPRRWFNaSTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIK 468
Cdd:cd02015 33 QYYRFKKPRSWLT-SGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNNGSLGMVR 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1521190028 469 R-----YMERREITPLGvdiYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA-DRPLIVEVL 526
Cdd:cd02015 112 QwqelfYEGRYSHTTLD---SNPDFVKLAEAYGIKGLRVEKPEELEAALKEALAsDGPVLLDVL 172
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
3-169 |
3.50e-34 |
|
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: 126.51 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 3 TCGEFLVKQLEAWGVETVFGIPGvHTV-----ELYRGlpgSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMT 77
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPG-DSInglmdALRRE---GKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 78 NILTAMAQAYADSIPMLVISSVNERARLahGNGYLHELpNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERpRPV 157
Cdd:cd07039 77 HLLNGLYDAKRDRAPVLAIAGQVPTDEL--GTDYFQEV-DLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVA 152
|
170
....*....|..
gi 1521190028 158 HIELPLDVITAP 169
Cdd:cd07039 153 VLILPGDVQDAP 164
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-525 |
7.35e-33 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 132.34 E-value: 7.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPG--VHTVELYRGLPGSRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTN 78
Cdd:PRK08273 2 SQTVADFILERLREWGVRRVFGYPGdgINGLLGALGRADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 79 ILTAMAQAYADSIPMLVIssVNERARLAHGNGYLHELPNQrNLVGNVC-AFSHTLMSAEELPAVLARAFAVFDSERpRPV 157
Cdd:PRK08273 82 LLNGLYDAKLDHVPVVAI--VGQQARAALGGHYQQEVDLQ-SLFKDVAgAFVQMVTVPEQLRHLVDRAVRTALAER-TVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 158 HIELPLDVITAPAEHLALRPRTLAS-------RPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPT 230
Cdd:PRK08273 158 AVILPNDVQELEYEPPPHAHGTVHSgvgytrpRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 231 ALTINAKGLLPADHPL------LLGSNqscvPVRELAAEADVVLAIGTELGETDYDVVFDGGFAldgelIRIDIDPQQLM 304
Cdd:PRK08273 238 AKALLGKAALPDDLPWvtgsigLLGTK----PSYELMRECDTLLMVGSSFPYSEFLPKEGQARG-----VQIDIDGRMLG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 305 RNYTPSLAIHSDARLAMRVLLAELpggEASPDSPGARRAAAVRQRLAEDFAGWSHYR------QLFAAILAE--WPDARF 376
Cdd:PRK08273 309 LRYPMEVNLVGDAAETLRALLPLL---ERKKDRSWRERIEKWVARWWETLEARAMVPadpvnpQRVFWELSPrlPDNAIL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 377 VGDSTQTVysgNHLVDLDEPRRWFNA--STGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFT-LPELASAVE---- 449
Cdd:PRK08273 386 TADSGSCA---NWYARDLRMRRGMMAslSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKywrq 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 450 -AKVGIVVLLWNNHGYGEI---KRYMERREITPLGVDIytPDF--LAIARGFGCAAERARDLEHLRELLRGA-PADRPLI 522
Cdd:PRK08273 463 wSDPRLIVLVLNNRDLNQVtweQRVMEGDPKFEASQDL--PDVpyARFAELLGLKGIRVDDPEQLGAAWDEAlAADRPVV 540
|
...
gi 1521190028 523 VEV 525
Cdd:PRK08273 541 LEV 543
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
1-528 |
2.71e-32 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 130.49 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGvhtvELYRGLPGS-----RIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPG 75
Cdd:PRK09124 2 KQTVADYIAKTLEQAGVKRIWGVTG----DSLNGLSDSlrrmgTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 76 MTNILTAMAQAYADSIPMLVISsvnerarlAH------GNGYLHELPNQrNLVGNVCAFSHTLMSAEELPAVLARAFAVF 149
Cdd:PRK09124 78 NLHLINGLFDCHRNHVPVLAIA--------AHipsseiGSGYFQETHPQ-ELFRECSHYCELVSNPEQLPRVLAIAMRKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 150 DSERPRPVhIELPLDVITAPAEHLALRPRTLASRPA--PALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALD 227
Cdd:PRK09124 149 ILNRGVAV-VVLPGDVALKPAPERATPHWYHAPQPVvtPAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 228 APTALTINAKGLLPADHPL------LLGSNQSCVPVRElaaeADVVLAIGTelgetdyDVVFDGGFALDGELIRIDIDPQ 301
Cdd:PRK09124 228 APIVHALRGKEHVEYDNPYdvgmtgLIGFSSGYHAMMN----CDTLLMLGT-------DFPYRQFYPTDAKIIQIDINPG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 302 QLMRNYTPSLAIHSDARLAMRVLLAELPGGEASPDSPGARRAAAVRQRLAEDFAGWSHYR-----QLFAAILAEW--PDA 374
Cdd:PRK09124 297 SLGRRSPVDLGLVGDVKATLAALLPLLEEKTDRKFLDKALEHYRKARKGLDDLAVPSDGGkpihpQYLARQISEFaaDDA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 375 RFVGD-STQTVYSGNHLvDLDEPRRWFnASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVG 453
Cdd:PRK09124 377 IFTCDvGTPTVWAARYL-KMNGKRRLL-GSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLP 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1521190028 454 IVVLLWNNHGYGEIKRYMERREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA-DRPLIVEVLQA 528
Cdd:PRK09124 455 VKIVVFNNSVLGFVAMEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAhDGPALVDVVTA 530
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-525 |
1.06e-31 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 128.95 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 1 MTTCGEFLVKQLEAWGVETVFGIPGVH---TVELYRGLPGSRIRHVtpRHEQGAGFMADGYARVTGKPGVCFIITGPGMT 77
Cdd:PRK06546 2 AKTVAEQLVEQLVAAGVKRIYGIVGDSlnpIVDAVRRTGGIEWVHV--RHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 78 NILTAMAQAYADSIPMLVISSVNERARLahGNGYLHELPNQRnLVGNVCAFSHTLMSAEELPAVLARA--FAVfdsERPR 155
Cdd:PRK06546 80 HLINGLYDAHRSGAPVLAIASHIPSAQI--GSGFFQETHPDR-LFVECSGYCEMVSSAEQAPRVLHSAiqHAV---AGGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 156 PVHIELPLDVITAPAEHLALRPRTLASRPA--PALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAAALDAPTALT 233
Cdd:PRK06546 154 VSVVTLPGDIADEPAPEGFAPSVISPRRPTvvPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 234 INAKGLLPADHPL------LLGSNqSCvpvRELAAEADVVLAIGTELGETDydvvfdggFALDGELIRIDIDPQQLMRNY 307
Cdd:PRK06546 234 LRGKEWIQYDNPFdvgmsgLLGYG-AA---HEAMHEADLLILLGTDFPYDQ--------FLPDVRTAQVDIDPEHLGRRT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 308 TPSLAIHSDARLAMRVLLAELpggEASPDSPGARRAAAVRQRLAEDFAGwSHYRQL----------FAAILAEW--PDAR 375
Cdd:PRK06546 302 RVDLAVHGDVAETIRALLPLV---KEKTDRRFLDRMLKKHARKLEKVVG-AYTRKVekhtpihpeyVASILDELaaDDAV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 376 FVGDSTQT-VYSGNHLVDLdePRRWFNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGI 454
Cdd:PRK06546 378 FTVDTGMCnVWAARYITPN--GRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPV 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1521190028 455 VVLLWNNHGYGEIKRYMERREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA-DRPLIVEV 525
Cdd:PRK06546 456 KVVVFNNSTLGMVKLEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAhPGPALVDV 527
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
359-526 |
2.77e-29 |
|
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: 113.78 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 359 HYRQLFAAILAE-WPDARFVGDS-TQTVYSGNHLvDLDEPRRWFnASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGG 436
Cdd:cd02014 3 HPERVAAELNKRaPDDAIFTIDVgNVTVWAARHL-RMNGKQRFI-LSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 437 LQFTLPELASAVEAKVGIVVLLWNNHGYGEIKRYMERREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGA- 515
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEAl 160
|
170
....*....|.
gi 1521190028 516 PADRPLIVEVL 526
Cdd:cd02014 161 AADGPVVIDVV 171
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
359-525 |
1.43e-27 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 108.84 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 359 HYRQLFAAILAEWP-DARFVGDSTQTVYSGNHLVDLDEPRRWFNASTGYgtLGYGLPAAIGAKLGEPGRPVVSLMGDGGL 437
Cdd:cd02002 2 TPEYLAAALAAALPeDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRGGG--LGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 438 QFTLPELASAVEAKVGIVVLLWNNHGYGEIKRYMER------REITPLGVDIYTP--DFLAIARGFGCAAERARDLEHLR 509
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRvgpegpGENAPDGLDLLDPgiDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*..
gi 1521190028 510 ELLRGAPA-DRPLIVEV 525
Cdd:cd02002 160 EALREALAeGGPALIEV 176
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
6-526 |
2.13e-25 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 109.55 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 6 EFLVKQLEAWGVETVFGIPG---VHTVELYRGLPGsrIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTA 82
Cdd:PRK07586 5 ESLVRTLVDGGVDVCFANPGtseMHFVAALDRVPG--MRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 83 MAQAYADSIPMLVIssVNERARlahgngYLHELPNQRN-----LVGNVCAFSHTLMSAEELPAVLARAFAVFDSERPRPV 157
Cdd:PRK07586 83 LHNARRARTPIVNI--VGDHAT------YHRKYDAPLTsdieaLARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 158 HIELPLDVITAPAEHLAlRPRTLASRPAPALAPLREAAARLRNAKKPLLLLGGGCVEAAAEARALAaaldaptaltINAK 237
Cdd:PRK07586 155 TLILPADVAWSEGGPPA-PPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAAR----------IAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 238 G---LLPADHPLLLGSNQSCVPVRELAAEADVVLAI--GTE---LGETDYDVVFdggFALDGELIRIDIDPQQLMRNYTP 309
Cdd:PRK07586 224 TgarLLAETFPARMERGAGRPAVERLPYFAEQALAQlaGVRhlvLVGAKAPVAF---FAYPGKPSRLVPEGCEVHTLAGP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 310 slaiHSDARLAMRVLLAELPGGEASPDSPGARRAAAVRQRLAEDFAGwshyrqlfAAILAEWPDARFVGDSTQTVYSGNH 389
Cdd:PRK07586 301 ----GEDAAAALEALADALGAKPAAPPLAAPARPPLPTGALTPEAIA--------QVIAALLPENAIVVDESITSGRGFF 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 390 LVDLDEPRRWFNASTGyGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGY----G 465
Cdd:PRK07586 369 PATAGAAPHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYailrG 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1521190028 466 EIKRyMERREITP-----LGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPADR-PLIVEVL 526
Cdd:PRK07586 448 ELAR-VGAGNPGPraldmLDLDDPDLDWVALAEGMGVPARRVTTAEEFADALAAALAEPgPHLIEAV 513
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
403-525 |
5.54e-25 |
|
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: 101.60 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 403 STGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKRYMERREITPLGVD 482
Cdd:cd02010 44 SNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVD 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1521190028 483 IYTPDFLAIARGFGCAAERARDLEHLRELLRGA-PADRPLIVEV 525
Cdd:cd02010 124 FGNPDFVKYAESFGAKGYRIESADDLLPVLERAlAADGVHVIDC 167
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
360-526 |
6.17e-24 |
|
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: 98.37 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 360 YRQLFAAILAEWP-DARFVGDSTQTVYSGNHLVDLDEPRRWFNASTgYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQ 438
Cdd:cd02004 1 PYRVLHELQEALPdDAIIVSDGGNTMDWARYILRPRKPRHRLDAGT-FGTLGVGLGYAIAAALARPDKRVVLVEGDGAFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 439 FTLPELASAVEAKVGIVVLLWNNHGYGEIKRYMERRE--ITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAP 516
Cdd:cd02004 80 FSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYglGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRAL 159
|
170
....*....|.
gi 1521190028 517 A-DRPLIVEVL 526
Cdd:cd02004 160 AsGKPALINVI 170
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
400-525 |
6.12e-23 |
|
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: 96.61 E-value: 6.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 400 FNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKR---------- 469
Cdd:cd02003 41 YHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNlqestgsgsf 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1521190028 470 ---YMERREITPLGVDIYTP-DFLAIARGFGCAAERARDLEHLRELLRGAPA-DRPLIVEV 525
Cdd:cd02003 121 gteFRDRDQESGQLDGALLPvDFAANARSLGARVEKVKTIEELKAALAKAKAsDRTTVIVI 181
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
6-162 |
6.11e-22 |
|
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: 92.56 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 6 EFLVKQLEAWGVETVFGIPGVHTVELYRGLPGSR-IRHVTPRHEQGAGFMADGYARVTGkPGVCFIITGPGMTNILTAMA 84
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPgLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 85 QAYADSIPMLVIS---SVNERA--RLAHgngylHELPN-----QRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERp 154
Cdd:cd07038 80 GAYAEHVPVVHIVgapSTKAQAsgLLLH-----HTLGDgdfdvFLKMFEEITCAAARLTDPENAAEEIDRVLRTALRES- 153
|
....*...
gi 1521190028 155 RPVHIELP 162
Cdd:cd07038 154 RPVYIEIP 161
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
8-162 |
1.60e-21 |
|
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: 91.25 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 8 LVKQLEAWGVETVFGIPGVHTVELYRGL-PGSRIRHVTPRHEQGAGFMADGYARVTGkPGVCFIITGPGMTNILTAMAQA 86
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALrEGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1521190028 87 YADSIPMLVISSVNERArlAHGNGyLHELPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSErPRPVHIELP 162
Cdd:cd06586 82 AAEHLPVVFLIGARGIS--AQAKQ-TFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLP 153
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
191-324 |
1.06e-20 |
|
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: 88.00 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 191 LREAAARLRNAKKPLLLLGGGCV--EAAAEARALAAALDAPTALTINAKGLLPADHPLLLGSN--QSCVPVRELAAEADV 266
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRrsGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLgmHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1521190028 267 VLAIGTELGETDYdVVFDGGFALDGELIRIDIDPQQLMRNYTPSLAIHSDARLAMRVL 324
Cdd:pfam00205 81 VLAVGARFDDIRT-TGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
357-526 |
1.17e-18 |
|
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: 84.10 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 357 WSHYRQLFAAILAEWP-DARFVGDSTQTVYSGNHLVDLDEPRRWFNASTgYGTLGYGLPAAIGAKLGEPGRPVVSLMGDG 435
Cdd:cd02013 3 PMHPRQVLRELEKAMPeDAIVSTDIGNICSVANSYLRFEKPRSFIAPLS-FGNCGYALPAIIGAKAAAPDRPVVAIAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 436 GLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKRYM----ERREitpLGVDIYTPDFLAIARGFGCAAERARDLEHLREL 511
Cdd:cd02013 82 AWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQvdfyNNRF---VGTELESESFAKIAEACGAKGITVDKPEDVGPA 158
|
170
....*....|....*....
gi 1521190028 512 LRGAPADR----PLIVEVL 526
Cdd:cd02013 159 LQKAIAMMaegkTTVIEIV 177
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
406-525 |
4.85e-18 |
|
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: 81.81 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 406 YGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYgEIKRYMERREITPlgVDIYT 485
Cdd:cd02005 49 WGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGY-TIERAIHGPEASY--NDIAN 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1521190028 486 PDFLAIARGFGCAAE----RARDLEHLRELLRGA--PADRPLIVEV 525
Cdd:cd02005 126 WNYTKLPEVFGGGGGglsfRVKTEGELDEALKDAlfNRDKLSLIEV 171
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
372-526 |
4.52e-17 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 79.63 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 372 PDARFVGDSTQTVYSGNHLVDLDEPRRWFNASTGyGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAK 451
Cdd:cd02006 23 RDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQA-GPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 452 VGIVVLLWNNHGYGEIKR-----------YMERREITPLGVDIYTPDFLAIARGFGCAAERARDLEHLRELLRGAPA--- 517
Cdd:cd02006 102 IPYIHVLVNNAYLGLIRQaqrafdmdyqvNLAFENINSSELGGYGVDHVKVAEGLGCKAIRVTKPEELAAAFEQAKKlma 181
|
170
....*....|.
gi 1521190028 518 --DRPLIVEVL 526
Cdd:cd02006 182 ehRVPVVVEAI 192
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
8-526 |
9.83e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 83.00 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 8 LVKQLEAWGVETVFGIPGVHTVELYRGLPG-SRIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQA 86
Cdd:PRK12474 11 VVDTLLNCGVEVCFANPGTSEMHFVAALDRvPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLANLHNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 87 YADSIPMLVISsvnerarlahGNGYLHELPNQRNLVGNVCAFS-------HTLMSAEELPAVLARAFAVFDSERPRPVHI 159
Cdd:PRK12474 91 RRAASPIVNIV----------GDHAVEHLQYDAPLTSDIDGFArpvsrwvHRSASAGAVDSDVARAVQAAQSAPGGIATL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 160 ELPLDVITAPAEHLALRPRTLAsrPAPALAPLREA-AARLRNAKKPLLLLGGGCVeaAAEARALAAALDAPTALTINAKG 238
Cdd:PRK12474 161 IMPADVAWNEAAYAAQPLRGIG--PAPVAAETVERiAALLRNGKKSALLLRGSAL--RGAPLEAAGRIQAKTGVRLYCDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 239 LLPADHpllLGSNQscVPVRELAAEADVvlaIGTELGETDYdVVFDGG------FALDGELIRIDIDPQQLMRNYTPsla 312
Cdd:PRK12474 237 FAPRIE---RGAGR--VPIERIPYFHEQ---ITAFLKDVEQ-LVLVGAkppvsfFAYPGKPSWGAPPGCEIVYLAQP--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 313 iHSDARLAMRVLLAELPggeaSPDSPGARRAAAVRQRLAEDFAGWShYRQLFAAILaewPDARFVGDSTQTVySGNHLVD 392
Cdd:PRK12474 305 -DEDLAQALQDLADAVD----APAEPAARTPLALPALPKGALNSLG-VAQLIAHRT---PDQAIYADEALTS-GLFFDMS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 393 LDEPRRWFNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGYGEIKRYME 472
Cdd:PRK12474 375 YDRARPHTHLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGELQ 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1521190028 473 RREITPLG------VDIYTP--DFLAIARGFGCAAERARDLEHLRELLRGAPADR-PLIVEVL 526
Cdd:PRK12474 455 RVGAQGAGrnalsmLDLHNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRgPRLIEAM 517
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
48-163 |
1.65e-10 |
|
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: 59.82 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 48 EQGAGFMADGYARVTGKPgVCFIIT-GPGMTNILTAMAQAYADSIPMLVISSVNERARLAHGNGylhELPNQRNLVGNVC 126
Cdd:cd07037 44 ERSAAFFALGLAKASGRP-VAVVCTsGTAVANLLPAVVEAYYSGVPLLVLTADRPPELRGTGAN---QTIDQVGLFGDYV 119
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1521190028 127 AFSHTLMSAEELPA------VLARAFAVFDSERPRPVHIELPL 163
Cdd:cd07037 120 RWSVDLPPPEDDDDlwyllrLANRAVLEALSAPPGPVHLNLPF 162
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
3-464 |
2.51e-09 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 59.71 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 3 TCGEFLVKQLEAWGVETVFGIPGVHTVELYRGL---PGsrIRHVTPRHEQGAGFMADGYARVTGKPGVCFIITGPGMTnI 79
Cdd:PLN02573 17 TLGRHLARRLVEIGVTDVFSVPGDFNLTLLDHLiaePG--LNLIGCCNELNAGYAADGYARARGVGACVVTFTVGGLS-V 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 80 LTAMAQAYADSIPMLVIS---SVNERA--RLAHGNGYLHELPNQRNLVGNVCAFSHTLMSAEELPAVLARAFAVFDSERp 154
Cdd:PLN02573 94 LNAIAGAYSENLPVICIVggpNSNDYGtnRILHHTIGLPDFSQELRCFQTVTCYQAVINNLEDAHELIDTAISTALKES- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 155 RPVHIELP--LDVITAPaehlalrprTLASRPAP-ALAPLR----------EAAARLRN-AKKPLLLlgGG----CVEAA 216
Cdd:PLN02573 173 KPVYISVScnLAAIPHP---------TFSREPVPfFLTPRLsnkmsleaavEAAAEFLNkAVKPVLV--GGpklrVAKAC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 217 AEARALAAALDAPTALTINAKGLLPADHPLLLGSNQSCVP---VRELAAEADVVLAIGTELgeTDYDVVfdgGFALdgeL 293
Cdd:PLN02573 242 KAFVELADASGYPVAVMPSAKGLVPEHHPHFIGTYWGAVStpfCAEIVESADAYLFAGPIF--NDYSSV---GYSL---L 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 294 IR----IDIDPQQLMRNYTPSLA--IHSD--ARLAMRVLLAE----------LPGGEASPDSPGARRAAAVRqrlaedfa 355
Cdd:PLN02573 314 LKkekaIIVQPDRVTIGNGPAFGcvLMKDflEALAKRVKKNTtayenykrifVPEGEPLKSEPGEPLRVNVL-------- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 356 gWSHYRQLFA---AILAEwpdarfVGDStqtvysgnhlvdldeprrWFN-------ASTG------YGTLGYGLPAAIGA 419
Cdd:PLN02573 386 -FKHIQKMLSgdtAVIAE------TGDS------------------WFNcqklklpEGCGyefqmqYGSIGWSVGATLGY 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1521190028 420 KLGEPGRPVVSLMGDGGLQFTLPELASAVEAKVGIVVLLWNNHGY 464
Cdd:PLN02573 441 AQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGY 485
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
400-533 |
2.98e-05 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 44.82 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 400 FNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDG-GLQFTLPELASAVEAKVGIVVLLWNNHGYGEIK-------RYM 471
Cdd:cd03375 44 FNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKgqaspttPEG 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1521190028 472 ERREITPLGVDIYTPDFLAIARGFGC---AAERARDLEHLRELLRGAPADRPL-IVEVLQAAPFHP 533
Cdd:cd03375 124 FKTKTTPYGNIEEPFNPLALALAAGAtfvARGFSGDIKQLKEIIKKAIQHKGFsFVEVLSPCPTFP 189
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
407-525 |
8.15e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 43.67 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 407 GTLGYGLPAAIGAKLGEPGRPVVSLMGDGGLQFTLPELAS-AVEAKVGIVVLLWNNHGYGeikryMERREITPLGvdiYT 485
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTiAALAPKNLTIIVMDNGVYQ-----ITGGQPTLTS---QT 128
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1521190028 486 PDFLAIARGFGCAAER-ARDLEHLRELLRGA-PADRPLIVEV 525
Cdd:PRK06163 129 VDVVAIARGAGLENSHwAADEAHFEALVDQAlSGPGPSFIAV 170
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
360-533 |
5.24e-04 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 41.11 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 360 YRQLFAAI-LAEWPDARFVGDStqtvysGNHLVDLDEPrrwFNASTGYGTLGYGLPAAIGAKLGEPGRPVVSLMGDGGlq 438
Cdd:cd02008 12 HRPSFYALrKAFKKDSIVSGDI------GCYTLGALPP---LNAIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDST-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 439 FT---LPELASAVEAKVGIVVLLWNNhgygeikRY--MERREITP-LGVDIYTP----DFLAIARGFGCAAERARDlehl 508
Cdd:cd02008 81 FFhsgILGLINAVYNKANITVVILDN-------RTtaMTGGQPHPgTGKTLTEPttviDIEALVRAIGVKRVVVVD---- 149
|
170 180
....*....|....*....|....*
gi 1521190028 509 rellrgaPADRPLIVEVLQAAPFHP 533
Cdd:cd02008 150 -------PYDLKAIREELKEALAVP 167
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
48-162 |
9.68e-03 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 39.07 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1521190028 48 EQGAGFMADGYARVTGKPGVCFIITGPGMTNILTAMAQAYADSIPMLVISSvnERARLAHGNGyLHELPNQRNLVGNVCA 127
Cdd:PLN02980 348 ERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTA--DRPPELQDAG-ANQAINQVNHFGSFVR 424
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1521190028 128 FSHTL-MSAEELPA-----VLARAFAVFDSERPRPVHIELP 162
Cdd:PLN02980 425 FFFNLpPPTDLIPArmvltTLDSAVHWATSSPCGPVHINCP 465
|
|
| |
