|
Name |
Accession |
Description |
Interval |
E-value |
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
55-637 |
1.84e-132 |
|
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: 399.92 E-value: 1.84e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 55 KRHGGELVASVLKAHDVEEIFVLCGGHISPILVA-AEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNT 133
Cdd:COG0028 2 KMTGADALVEALEAEGVETVFGVPGGAILPLYDAlRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 134 ITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFP 213
Cdd:COG0028 82 VTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 214 VDVLYpyelvvKEIGFNPnakgfiqralnfylrchvsrqfgnawAPQTITPLPTNiPMPKSEKIQEIVQLVKSAKRPVLL 293
Cdd:COG0028 162 KDVQA------AEAEEEP--------------------------APPELRGYRPR-PAPDPEAIEEAAELLAAAKRPVIL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 294 IG-----SQATlppvkpADLVKAVEALGCPVFLGGMARGLLGKDHPLQM-------RQVRRDALKDADLTILAGTVCDFR 361
Cdd:COG0028 209 AGggarrAGAA------EELRALAERLGAPVVTTLMGKGAFPEDHPLYLgmlgmhgTPAANEALAEADLVLAVGARFDDR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 362 LSYG-RTLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGAnHTTTPTEWVKSLREKDDEKESANA 440
Cdd:COG0028 283 VTGNwDEFAPDAKIIHIDIDPAEIGKNYPV----DLPIVGDAKAVLAALLEALEP-RADDRAAWLARIAAWRAEYLAAYA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 441 KkmeqklTNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKR 520
Cdd:COG0028 358 A------DDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 521 PVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQS-SVAVDLARTRYDNVAKSLGSWGETIdES 599
Cdd:COG0028 432 PVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGrYSGTDLPNPDFAKLAEAFGAKGERV-ET 510
|
570 580 590
....*....|....*....|....*....|....*...
gi 17542570 600 NADsarkiLDEALAVCRSGEQSALVNVLIGKTDFREGS 637
Cdd:COG0028 511 PEE-----LEAALEEALASDGPALIDVRVDPEENPPGA 543
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
52-632 |
7.44e-131 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 395.63 E-value: 7.44e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 52 EKSKRHGGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLT 131
Cdd:PRK05858 1 PAQTGHAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 132 NTITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVE 211
Cdd:PRK05858 81 NGMSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 212 FPVDVLYPyelvVKEIGFNPnakgfiqralnfylrchvsrqfgnawAPQTITPLPtniPMPKSEKIQEIVQLVKSAKRPV 291
Cdd:PRK05858 161 FPMDHAFS----MADDDGRP--------------------------GALTELPAG---PTPDPDALARAAGLLAEAQRPV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 292 LLIGSQATLPPVKPAdLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVRRDALKDADLTILAGTVCDFRLSYGrTLSKK 371
Cdd:PRK05858 208 IMAGTDVWWGHAEAA-LLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFG-VFGGT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 372 SKIVALNRNSSQLTKNekafwnsdVSVQADVATSLVQVANALG--ANHTTTPTEWVKSLREKDDEKESANAKKMEQKLTN 449
Cdd:PRK05858 286 AQLVHVDDAPPQRAHH--------RPVAAGLYGDLSAILSALAgaGGDRTDHQGWIEELRTAETAARARDAAELADDRDP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 450 gfLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDG 529
Cdd:PRK05858 358 --IHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 530 SCGYSLMEYDTFARHKLPVIGIVGNDACWtqiAREQVPM---FQSSVAVDLA-RTRYDNVAKSLGSWGETIdeSNADSAR 605
Cdd:PRK05858 436 AFGFSLMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRALGGHGELV--TVPAELG 510
|
570 580
....*....|....*....|....*..
gi 17542570 606 KILDEALAvcrSGeQSALVNVLIGKTD 632
Cdd:PRK05858 511 PALERAFA---SG-VPYLVNVLTDPSV 533
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
454-628 |
4.62e-65 |
|
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: 211.62 E-value: 4.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 454 PLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGY 533
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 534 SLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMF--QSSVAVDLARTRYDNVAKSLGSWGETIDesNADSARKILDEA 611
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYglGLPVTTLLPDTRYDLVAEAFGGKGELVT--TPEELKPALKRA 158
|
170
....*....|....*..
gi 17542570 612 LAvcrSGeQSALVNVLI 628
Cdd:cd02004 159 LA---SG-KPALINVII 171
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
58-628 |
4.96e-65 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 224.09 E-value: 4.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAV 137
Cdd:PRK09259 12 GFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 138 KNAQMAESPLLLIGGAA--PTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVD 215
Cdd:PRK09259 92 ANATTNCFPMIMISGSSerEIVDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 216 VLYpyELVVKEIGfnpnakgfiQRALnfylrchvsrqfgnaWAPqtITPLPTNIPMPKSekIQEIVQLVKSAKRPVLLIG 295
Cdd:PRK09259 172 VLA--QTMDADEA---------LTSL---------------VKV--VDPAPAQLPAPEA--VDRALDLLKKAKRPLIILG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 296 SQATLPPVKpADLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVRRDALKDADLTILAGTVCDFRLSYGR--TLSKKSK 373
Cdd:PRK09259 222 KGAAYAQAD-EQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVVLLVGARLNWLLSHGKgkTWGADKK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 374 IVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHTTTPTEWVKSLREKDDekesANAKKMEQKLTN---- 449
Cdd:PRK09259 301 FIQIDIEPQEIDSNRPI----AAPVVGDIGSVMQALLAGLKQNTFKAPAEWLDALAERKE----KNAAKMAEKLSTdtqp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 450 -GFLNPLNFLRTLDQSLPdDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAkTVYPKRPVYIIWGD 528
Cdd:PRK09259 373 mNFYNALGAIRDVLKENP-DIYLVNEGANTLDLARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAA-AVETGKPVVAIEGD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 529 GSCGYSLMEYDTFARHKLPVIGIVGNDAcwtQIAR--EQVP--MFQSSVAVDLARTRYDNVAKSLGswGETIDESNADSA 604
Cdd:PRK09259 451 SAFGFSGMEVETICRYNLPVTVVIFNNG---GIYRgdDVNLsgAGDPSPTVLVHHARYDKMMEAFG--GVGYNVTTPDEL 525
|
570 580
....*....|....*....|....
gi 17542570 605 RKILDEALAvcrSGEQSaLVNVLI 628
Cdd:PRK09259 526 RHALTEAIA---SGKPT-LINVVI 545
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
58-613 |
9.07e-63 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 217.19 E-value: 9.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHI----SPILVAAEKlgIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNT 133
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFGLPGAQLywlfDALYKAGDR--IRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 134 ITAVKNAQMAESPLLLIGGAAPTLL--KGRGALQDI-DQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFV 210
Cdd:PRK08266 84 GAALLTAYGCNSPVLCLTGQIPSALigKGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 211 EFPVDVlypyelvvkeigfnpnakgFIQRAlnfylrchvsrqfgNAWAPQTITPLPTniPMPKSEKIQEIVQLVKSAKRP 290
Cdd:PRK08266 164 EMPWDV-------------------FGQRA--------------PVAAAPPLRPAPP--PAPDPDAIAAAAALIAAAKNP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 291 VLLIGSQAtlppVKPADLVKAV-EALGCPVFLGGMARGLLGKDHPLQMRQVR-RDALKDADLTILAGTVCDFRLSYGRTL 368
Cdd:PRK08266 209 MIFVGGGA----AGAGEEIRELaEMLQAPVVAFRSGRGIVSDRHPLGLNFAAaYELWPQTDVVIGIGSRLELPTFRWPWR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 369 SKKSKIVALNRNSSQLTKNEkafwnSDVSVQADVATSLVQVANALGANHTTTP--TEWVKSLREKDDEKESAnakkmeqk 446
Cdd:PRK08266 285 PDGLKVIRIDIDPTEMRRLK-----PDVAIVADAKAGTAALLDALSKAGSKRPsrRAELRELKAAARQRIQA-------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 447 ltngfLNP-LNFLRTLDQSLPDDAILVaDGGDFVGSAAYIVRP-RGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYI 524
Cdd:PRK08266 352 -----VQPqASYLRAIREALPDDGIFV-DELSQVGFASWFAFPvYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVS 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 525 IWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSS-VAVDLARTRYDNVAKSLGSWGETIDesNADS 603
Cdd:PRK08266 426 ITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFGGRvVASDLVNPDFVKLAESFGVAAFRVD--SPEE 503
|
570
....*....|
gi 17542570 604 ARKILDEALA 613
Cdd:PRK08266 504 LRAALEAALA 513
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
60-214 |
1.95e-58 |
|
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: 193.13 E-value: 1.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 60 ELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAVKN 139
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17542570 140 AQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPV 214
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
58-632 |
9.18e-56 |
|
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: 198.41 E-value: 9.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKL-GIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDsGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDV 216
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 217 L-----YPYELVVKEIGFNPNAKGfiqralnfylrchvsrqfgnawapqtiTPLptnipmpkseKIQEIVQLVKSAKRPV 291
Cdd:TIGR00118 163 TtaeieYPYPEKVNLPGYRPTVKG---------------------------HPL----------QIKKAAELINLAKKPV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 292 LLIGSQAtLPPVKPADLVKAVEALGCPVFLGGMARGLLGKDHPLQM-------RQVRRDALKDADLTILAGTVCDFRLSY 364
Cdd:TIGR00118 206 ILVGGGV-IIAGASEELKELAERIQIPVTTTLMGLGSFPEDHPLSLgmlgmhgTKTANLAVHECDLIIAVGARFDDRVTG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 365 G-RTLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHTTTPTEWVKSLREKDDEKesanAKKM 443
Cdd:TIGR00118 285 NlAKFAPNAKIIHIDIDPAEIGKNVRV----DIPIVGDARNVLEELLKKLFELKERKESAWLEQINKWKKEY----PLKM 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 444 EQklTNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVY 523
Cdd:TIGR00118 357 DY--TEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 524 IIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDAC------WTQIAREQvpmfQSSVAVDLARTRYDNVAKSLGSWGETId 597
Cdd:TIGR00118 435 CITGDGSFQMNLQELSTAVQYDIPVKILILNNRYlgmvrqWQELFYEE----RYSHTHMGSLPDFVKLAEAYGIKGIRI- 509
|
570 580 590
....*....|....*....|....*....|....*
gi 17542570 598 esnadSARKILDEALAVCRSGEQSALVNVLIGKTD 632
Cdd:TIGR00118 510 -----EKPEELDEKLKEALSSNEPVLLDVVVDKPE 539
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
58-614 |
1.39e-53 |
|
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: 192.27 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAV 137
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 138 KNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDVL 217
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 218 ypyELVVKEIGFNPnakgfiqralnfylrchvsrqfgnAWAPQtitplptnIPMPKSEKIQEIVQLVKSAKRPVLLIGSQ 297
Cdd:TIGR02418 161 ---DSPVSVKAIPA------------------------SYAPK--------LGAAPDDAIDEVAEAIQNAKLPVLLLGLR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 298 ATLPPVKPAdLVKAVEALGCPVFLGGMARGLLGKDHP--------LQMRQVRRDALKDADLTIlagTVCDFRLSYGRTLS 369
Cdd:TIGR02418 206 ASSPETTEA-VRRLLKKTQLPVVETFQGAGAVSRELEdhffgrvgLFRNQPGDRLLKQADLVI---TIGYDPIEYEPRNW 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 370 KK---SKIVALNRNSSQLTKNekafWNSDVSVQADVATSLVQVANALgaNHTTTPTEWVKSLREKDDEKESANAKKMEQK 446
Cdd:TIGR02418 282 NSendATIVHIDVEPAQIDNN----YQPDLELVGDIASTLDLLAERI--PGYELPPDALAILEDLKQQREALDRVPATLK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 447 ltNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIW 526
Cdd:TIGR02418 356 --QAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVS 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 527 GDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRYDNVAKSLGSWGETIDesNADSARK 606
Cdd:TIGR02418 434 GDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQRSSGVDFGPIDFVKYAESFGAKGLRVE--SPDQLEP 511
|
....*...
gi 17542570 607 ILDEALAV 614
Cdd:TIGR02418 512 TLRQAMEV 519
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
58-217 |
3.31e-52 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 177.04 E-value: 3.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEK-LGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGGAAPTLLKGRGALQD-IDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVD 215
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 17542570 216 VL 217
Cdd:pfam02776 161 VL 162
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
60-629 |
1.57e-51 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 187.51 E-value: 1.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 60 ELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAVKN 139
Cdd:PRK07525 10 EAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 140 AQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCpGPVFVEFPVDvlYP 219
Cdd:PRK07525 90 AYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD--YF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 220 YELVVKEIgfnPNakgfIQRalnfylrchVSRQFGNAwapqtitplptnipmpksEKIQEIVQLVKSAKRPVLLIGSQAT 299
Cdd:PRK07525 167 YGVIDVEI---PQ----PVR---------LERGAGGE------------------QSLAEAAELLSEAKFPVILSGAGVV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 300 LPPVKPaDLVKAVEALGCPVFLGGMARGLLGKDHPL------------QMRqvrrdALKDADLTILAGTvcdfRLSYGRT 367
Cdd:PRK07525 213 LSDAIE-ECKALAERLDAPVACGYLHNDAFPGSHPLwvgplgyngskaAME-----LIAKADVVLALGT----RLNPFGT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 368 LS--------KKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHT-------------TTPTEWVK 426
Cdd:PRK07525 283 LPqygidywpKDAKIIQVDINPDRIGLTKKV----SVGICGDAKAVARELLARLAERLAgdagreerkaliaAEKSAWEQ 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 427 SL----REKDDEKESANAKKMEQKltNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGT 502
Cdd:PRK07525 359 ELsswdHEDDDPGTDWNEEARARK--PDYMHPRQALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGN 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 503 LGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSS-VAVDL-ART 580
Cdd:PRK07525 437 CGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRfVGTELdNNV 516
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 17542570 581 RYDNVAKSLGSWGETIDesNADSARKILDEALAVCRSGEqSALVNVLIG 629
Cdd:PRK07525 517 SYAGIAEAMGAEGVVVD--TQEELGPALKRAIDAQNEGK-TTVIEIMCN 562
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
38-630 |
4.01e-51 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 185.79 E-value: 4.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 38 GNGQHVLSNAFQVDEKSKRHGGELVASVLKAHDVEeifVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLR- 116
Cdd:PRK06154 2 ADGTHALPNAHLPAEAKTMKVAEAVAEILKEEGVE---LLFGFPVNELFDAAAAAGIRPVIARTERVAVHMADGYARATs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 117 -QSIGVAAVTAGPGLTNTITAVKNAQMAESPLLLIGGAAPTllkgrgALQDID----QMVLFRPLCKYVARVERLRDIVP 191
Cdd:PRK06154 79 gERVGVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTGYPR------GSTDVApnfeSLRNYRHITKWCEQVTLPDEVPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 192 TVREAIKAAKSGCPGPVFVEFPVDVLYpyelvvKEIGFNPnakgfiqraLNFylrchvsrqfgnawapqtiTPLPTNIPM 271
Cdd:PRK06154 153 LMRRAFTRLRNGRPGPVVLELPVDVLA------EELDELP---------LDH-------------------RPSRRSRPG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 272 PKSEKIQEIVQLVKSAKRPVLLIGsQATLPPVKPADLVKAVEALGCPVFLGGMARGLLGKDHPLQM--------RQVRRd 343
Cdd:PRK06154 199 ADPVEVVEAAALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMTTLNGKSAFPEDHPLALgsggrarpATVAH- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 344 ALKDADLtiLAGTVCDF-RLSYGRTLSKKSKIVALNRNSSQLTKNekafWNSDVSVQADVATSLVQVANALGANHTTTPT 422
Cdd:PRK06154 277 FLREADV--LFGIGCSLtRSYYGLPMPEGKTIIHSTLDDADLNKD----YPIDHGLVGDAALVLKQMIEELRRRVGPDRG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 423 EWVKSLREKDDEKESANAKKMEqKLTNGF--LNPLNFLRTLDQSL-PDDAILVADGG---DFVGSAAYIVRPRGPLQWld 496
Cdd:PRK06154 351 RAQQVAAEIEAVRAAWLAKWMP-KLTSDStpINPYRVVWELQHAVdIKTVIITHDAGsprDQLSPFYVASRPGSYLGW-- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 497 pGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACwtqIAREQVPMfqsSVAVD 576
Cdd:PRK06154 428 -GKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNFS---MGGYDKVM---PVSTT 500
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 17542570 577 LARTR-----YDNVAKSLGSWGETIDEsnADSARKILDEALAVCRSGeQSALVNVLIGK 630
Cdd:PRK06154 501 KYRATdisgdYAAIARALGGYGERVED--PEMLVPALLRALRKVKEG-TPALLEVITSE 556
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
58-555 |
5.77e-51 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 185.30 E-value: 5.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKL-GIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:PRK08527 5 GSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQnYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDV 216
Cdd:PRK08527 85 LATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPKDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 217 -------LYPYElvVKEIGFNPNAKGfiqralNfylrchvSRQfgnawapqtitplptnipmpksekIQEIVQLVKSAKR 289
Cdd:PRK08527 165 tatlgefEYPKE--ISLKTYKPTYKG------N-------SRQ------------------------IKKAAEAIKEAKK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 290 PVLLIGSQATLPpvKPADLV-KAVEALGCPVFLGGMARGLLGKDHPLQMRQVRRD-------ALKDADLTILAGTVCDFR 361
Cdd:PRK08527 206 PLFYLGGGAILS--NASEEIrELVKKTGIPAVETLMARGVLRSDDPLLLGMLGMHgsyaanmAMSECDLLISLGARFDDR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 362 LSyGRT--LSKKSKIVALNRNSSQLTKnekaFWNSDVSVQADVATSLVQVANALGANHTTTPTEWVKSLREKDDekesan 439
Cdd:PRK08527 284 VT-GKLseFAKHAKIIHVDIDPSSISK----IVNADYPIVGDLKNVLKEMLEELKEENPTTYKEWREILKRYNE------ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 440 AKKMEQKLTNGFLNPLNFLRTLDQSLPDDAILVADGGDF-VGSAAY--IVRPRgplQWLDPGAFGTLGVGGGFALGAKTV 516
Cdd:PRK08527 353 LHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHqMWVAQFypFNYPR---QLATSGGLGTMGYGLPAALGAKLA 429
|
490 500 510
....*....|....*....|....*....|....*....
gi 17542570 517 YPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGND 555
Cdd:PRK08527 430 VPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNN 468
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
58-633 |
6.58e-50 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 183.03 E-value: 6.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAV 137
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 138 KNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDV- 216
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 217 -------LYPYELVVKEIGFNPNAKGfiqralnfylrcHvsrqfgnawapqtitPLptnipmpkseKIQEIVQLVKSAKR 289
Cdd:PRK06276 163 egeldleKYPIPAKIDLPGYKPTTFG------------H---------------PL----------QIKKAAELIAEAER 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 290 PVLLIGSQATLPPVKPaDLVKAVEALGCPVFLGGMARGLLGKDHPLQM-------RQVRRDALKDADLTILAGtvCDF-- 360
Cdd:PRK06276 206 PVILAGGGVIISGASE-ELIELSELVKIPVCTTLMGKGAFPEDHPLALgmvgmhgTKAANYSVTESDVLIAIG--CRFsd 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 361 ----RLSYgrtLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHTTTPTEWVKSLREKddEKE 436
Cdd:PRK06276 283 rttgDISS---FAPNAKIIHIDIDPAEIGKNVRV----DVPIVGDAKNVLRDLLAELMKKEIKNKSEWLERVKKL--KKE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 437 SANAKKMEQKLtngfLNPLNFLRTLDQSLPD-----DAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFAL 511
Cdd:PRK06276 354 SIPRMDFDDKP----IKPQRVIKELMEVLREidpskNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAI 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 512 GAKTVYPKRPVYIIWGDGscGYsLM---EYDTFARHKLPVIGIVGNDACWTQIAREQVPMF---QSSVAVDLArTRYDNV 585
Cdd:PRK06276 430 GAKVAKPDANVIAITGDG--GF-LMnsqELATIAEYDIPVVICIFDNRTLGMVYQWQNLYYgkrQSEVHLGET-PDFVKL 505
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 17542570 586 AKSLGSWGETIDEsnADSARKILDEALavcRSGEqSALVNVLIGKTDF 633
Cdd:PRK06276 506 AESYGVKADRVEK--PDEIKEALKEAI---KSGE-PYLLDIIIDPAEA 547
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
59-626 |
2.40e-48 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 177.47 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 59 GELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAVK 138
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 139 NAqMAES-PLLLIGG--AAPTLLKGRGALQDI-DQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPV 214
Cdd:PRK07524 85 QA-YADSiPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 215 DVLypyelvvkeigfnpnakgfiqralnfylrchvsrqfgNAWAPQTITPLPTNI--PMPKSEKIQEIVQLVKSAKRPVL 292
Cdd:PRK07524 164 DVL-------------------------------------AAPADHLLPAPPTRParPGPAPAALAQAAERLAAARRPLI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 293 LIGSQATlppVKPADLVKAVEALGCPVFLGGMARGLLGKDHPL-----QMRQVRRDALKDADLTILAGTV---CDFRLSY 364
Cdd:PRK07524 207 LAGGGAL---AAAAALRALAERLDAPVALTINAKGLLPAGHPLllgasQSLPAVRALIAEADVVLAVGTElgeTDYDVYF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 365 GRTLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALgaNHTTTPTEW----VKSLREkddekesANA 440
Cdd:PRK07524 284 DGGFPLPGELIRIDIDPDQLARNYPP----ALALVGDARAALEALLARL--PGQAAAADWgaarVAALRQ-------ALR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 441 KKMEQKltngFLNPLNFLRTLDQSLPDdAILVADGGDFVGSAAYIVRPRGPLQWLD-PGAFGTLGVGGGFALGAKTVYPK 519
Cdd:PRK07524 351 AEWDPL----TAAQVALLDTILAALPD-AIFVGDSTQPVYAGNLYFDADAPRRWFNaSTGYGTLGYGLPAAIGAALGAPE 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 520 RPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRYDNVAKSLGSWGETIDES 599
Cdd:PRK07524 426 RPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADL 505
|
570 580
....*....|....*....|....*..
gi 17542570 600 NAdsarkiLDEALAVCRSGEQSALVNV 626
Cdd:PRK07524 506 EQ------LQAALRAAFARPGPTLIEV 526
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
58-613 |
6.09e-48 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 177.08 E-value: 6.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAV 137
Cdd:PRK06725 17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 138 KNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDVL 217
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 218 ypyelvvkeigfnpnakgfIQRALNFYlrchVSRQFGNAWAPQtitplptniPMPKSEKIQEIVQLVKSAKRPVLLIGSq 297
Cdd:PRK06725 177 -------------------NEKVTSFY----NEVVEIPGYKPE---------PRPDSMKLREVAKAISKAKRPLLYIGG- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 298 ATLPPVKPADLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVRRDALKDADLTIlagTVCDFRLSYG-----------R 366
Cdd:PRK06725 224 GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLFLGMLGMHGTYAANMAV---TECDLLLALGvrfddrvtgklE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 367 TLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGanHTTTpTEWVKSLREKDDEKE-SANAKKMEq 445
Cdd:PRK06725 301 LFSPHSKKVHIDIDPSEFHKNVAV----EYPVVGDVKKALHMLLHMSI--HTQT-DEWLQKVKTWKEEYPlSYKQKESE- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 446 kltngfLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYII 525
Cdd:PRK06725 373 ------LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 526 WGDGSCGYSLMEYDTFARHKLPV-IGIVGNDacWTQIAREQVPMFQSSvavDLARTR-----YDNVAKSLGSWGetIDES 599
Cdd:PRK06725 447 AGDASFQMNIQELQTIAENNIPVkVFIINNK--FLGMVRQWQEMFYEN---RLSESKigspdFVKVAEAYGVKG--LRAT 519
|
570
....*....|....
gi 17542570 600 NADSARKILDEALA 613
Cdd:PRK06725 520 NSTEAKQVMLEAFA 533
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
58-631 |
1.11e-44 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 167.87 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPI---LVAAEKLGIKIVDT---RHEVTAVFAADAVARLRQSIGVAAVTAGPGLT 131
Cdd:PRK08327 9 AAELFLELLKELGVDYIFINSGTDYPPIieaKARARAAGRPLPEFvicPHEIVAISMAHGYALVTGKPQAVMVHVDVGTA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 132 NTITAVKNAQMAESPLLLIGGAAPTLLKGRGA--------LQDI-DQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKS 202
Cdd:PRK08327 89 NALGGVHNAARSRIPVLVFAGRSPYTEEGELGsrntrihwTQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAMS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 203 GCPGPVFVEFPVDVLypyelvvkeigfnpnakgfiqralnfylrchvSRQFGNAWAPQTItPLPTNIPMPKSEKIQEIVQ 282
Cdd:PRK08327 169 EPKGPVYLTLPREVL--------------------------------AEEVPEVKADAGR-QMAPAPPAPDPEDIARAAE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 283 LVKSAKRPVLlIGSQATLPPVKPADLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVRRDALKDADLTIlagtVCDFRL 362
Cdd:PRK08327 216 MLAAAERPVI-ITWRAGRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRADLAEADLVL----VVDSDV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 363 SYgrtlskkskIVALNRNSSQLT---------KNEKAFWN--SDVSVQADVATSLVQVANAL------GANHTTTPTEWV 425
Cdd:PRK08327 291 PW---------IPKKIRPDADARviqidvdplKSRIPLWGfpCDLCIQADTSTALDQLEERLkslasaERRRARRRRAAV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 426 KSLREKDDEKESANAKKMEQKltnGFLNPLNFLRTLDQSLPDDAILVADggdfvgsaaYIVRPR-----GPLQWLDPGAF 500
Cdd:PRK08327 362 RELRIRQEAAKRAEIERLKDR---GPITPAYLSYCLGEVADEYDAIVTE---------YPFVPRqarlnKPGSYFGDGSA 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 501 GTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSLME--YDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAV--- 575
Cdd:PRK08327 430 GGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPEGYAArkg 509
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542570 576 -----DLA-RTRYDNVAKSLGSWGETIDEsnADSARKILDEALAVCRSGEQSALVNVLIGKT 631
Cdd:PRK08327 510 tfpgtDFDpRPDFAKIAEAFGGYGERVED--PEELKGALRRALAAVRKGRRSAVLDVIVDRV 569
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
52-614 |
2.62e-44 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 166.57 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 52 EKSKRHGGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLT 131
Cdd:PRK08617 1 TDKKKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 132 NTITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVE 211
Cdd:PRK08617 81 NLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 212 FPVDVLYpyelvvkeigfnpnakgfiqralnfylrchvsrqfgnawAPQTITPLPTnIPMPK-----SEKIQEIVQLVKS 286
Cdd:PRK08617 161 LPQDVVD---------------------------------------APVTSKAIAP-LSKPKlgpasPEDINYLAELIKN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 287 AKRPVLLIGSQATLPPVKPAdLVKAVEALGCPVFLGGMARGLLgkDHPLQMRQVRR---------DA-LKDADLTILAGt 356
Cdd:PRK08617 201 AKLPVLLLGMRASSPEVTAA-IRRLLERTNLPVVETFQAAGVI--SRELEDHFFGRvglfrnqpgDElLKKADLVITIG- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 357 vcdfrlsYgrtlskkSKIvalnrnssqltKNEKAFWNSDV--------SVQA--------------DVATSLVQVANAL- 413
Cdd:PRK08617 277 -------Y-------DPI-----------EYEPRNWNSEGdatiihidVLPAeidnyyqpereligDIAATLDLLAEKLd 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 414 GANHTTTPTEWVKSLREKDDEKESANAkkmeqKLTNGFLNPLNFLRTLDQSLPDDAILVADGGDFvgsaaYI-------- 485
Cdd:PRK08617 332 GLSLSPQSLEILEELRAQLEELAERPA-----RLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSH-----YIwmaryfrs 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 486 VRPRgplQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQ 565
Cdd:PRK08617 402 YEPR---HLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQE 478
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 17542570 566 VPMFQSSVAVDLARTRYDNVAKSLGSWGETIDesNADSARKILDEALAV 614
Cdd:PRK08617 479 EMKYGRSSGVDFGPVDFVKYAESFGAKGLRVT--SPDELEPVLREALAT 525
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
58-597 |
2.80e-44 |
|
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: 166.93 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPIL--VAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTIT 135
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMdaLSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 136 AVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGcPGPVFVEFPVD 215
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAH-NGVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 216 VlypyelvvkeigfnpnakGFIQRALNFYLRCHVSRQfgnawapqtitplPTNIPMPKSEKIQEIVQLVKSAKRPVLLIG 295
Cdd:TIGR02720 160 F------------------GWQEIPDNDYYASSVSYQ-------------TPLLPAPDVEAVTRAVQTLKAAERPVIYYG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 296 SQAtlppVKPA-DLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVRRDALK-------DADLTILAGTVCDFRLSYgRT 367
Cdd:TIGR02720 209 IGA----RKAGeELEALSEKLKIPLISTGLAKGIIEDRYPAYLGSAYRVAQKpanealfQADLVLFVGNNYPFAEVS-KA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 368 LSKKSKIVALNRNSSQLTKNEKafwnSDVSVQADvATSLVQVANALGANHTTTPTeWVKSLREKDDEKESANakKMEQKl 447
Cdd:TIGR02720 284 FKNTKYFIQIDIDPAKLGKRHH----TDIAVLAD-AKKALAAILAQVEPRESTPW-WQANVANVKNWRAYLA--SLEDK- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 448 TNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWG 527
Cdd:TIGR02720 355 TEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAG 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 528 DGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRYDNVAKSLGSWGETID 597
Cdd:TIGR02720 435 DGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQPLIGVDFNDADFAKIAEGVGAVGFRVN 504
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
58-548 |
2.89e-44 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 166.21 E-value: 2.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAV 137
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 138 KNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDvl 217
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 218 ypyelvvkeigfnpnakgfIQRALNFYlrchvsrqfgnawapQTITPLPTNIPMPKSEKIQEIVQLVKSAKRPVLLIGSQ 297
Cdd:PRK08978 161 -------------------IQLAEGEL---------------EPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 298 ATlppvkpadLVKAVEAL-------GCPVF--LGGMarGLLGKDHP-----LQMRQVR--RDALKDADLTILAGTVCDFR 361
Cdd:PRK08978 207 VG--------MAGAVPALreflaatGMPAVatLKGL--GAVEADHPyylgmLGMHGTKaaNLAVQECDLLIAVGARFDDR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 362 LSyGR--TLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALganhttTPTEW---VKSLREK----- 431
Cdd:PRK08978 277 VT-GKlnTFAPHAKVIHLDIDPAEINKLRQA----HVALQGDLNALLPALQQPL------NIDAWrqhCAQLRAEhawry 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 432 DDEKESANAkkmeqkltngflnPLnFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFAL 511
Cdd:PRK08978 346 DHPGEAIYA-------------PA-LLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAI 411
|
490 500 510
....*....|....*....|....*....|....*..
gi 17542570 512 GAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPV 548
Cdd:PRK08978 412 GAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPV 448
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
60-613 |
4.63e-44 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 165.77 E-value: 4.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 60 ELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAVKN 139
Cdd:PRK08322 5 DLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 140 AQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERlRDIVPT-VREAIKAAKSGCPGPVFVEFPVDVly 218
Cdd:PRK08322 85 AQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVS-PDNIPEvVREAFRLAEEERPGAVHLELPEDI-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 219 pyelvvkeigfnpnakgfiqralnfylrchvsrqfgnAWAPQTITPLPTN---IPMPKSEKIQEIVQLVKSAKRPVLLIG 295
Cdd:PRK08322 162 -------------------------------------AAEETDGKPLPRSysrRPYASPKAIERAAEAIQAAKNPLILIG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 296 SQATLPPVKPAdLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQV---RRD----ALKDADLTIlagTVcdfrlsyGRTL 368
Cdd:PRK08322 205 AGANRKTASKA-LTEFVDKTGIPFFTTQMGKGVIPETHPLSLGTAglsQGDyvhcAIEHADLII---NV-------GHDV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 369 SKKS----------KIVALNRNSSQLtkneKAFWNSDVSVQADVATSLVQVANALGANHtTTPTEWVKSLREKDDEKESA 438
Cdd:PRK08322 274 IEKPpffmnpngdkKVIHINFLPAEV----DPVYFPQVEVVGDIANSLWQLKERLADQP-HWDFPRFLKIREAIEAHLEE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 439 NAKKmeqkltNGF-LNPLNFLRTLDQSLPDDAILVADGGdfvgsaAYIV------RPRGPLQWLDPGAFGTLGVGGGFAL 511
Cdd:PRK08322 349 GADD------DRFpMKPQRIVADLRKVMPDDDIVILDNG------AYKIwfarnyRAYEPNTCLLDNALATMGAGLPSAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 512 GAKTVYPKRPVYIIWGDGscGYsLM---EYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRYDNVAKS 588
Cdd:PRK08322 417 AAKLVHPDRKVLAVCGDG--GF-MMnsqELETAVRLGLPLVVLILNDNAYGMIRWKQENMGFEDFGLDFGNPDFVKYAES 493
|
570 580
....*....|....*....|....*
gi 17542570 589 LGSWGETIDEsnADSARKILDEALA 613
Cdd:PRK08322 494 YGAKGYRVES--ADDLLPTLEEALA 516
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
55-628 |
2.20e-43 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 164.40 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 55 KRHGGELVASVLKAHDVEEIFVLCGGHISPILVA--AEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTN 132
Cdd:PRK08611 3 KIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDAlrKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 133 TITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAksgcpgpvFVEF 212
Cdd:PRK08611 83 LLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTA--------YEKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 213 PVDVL-YPYELVVKEIGFNPNAkgfiqralnfylrchvsrqfgnawAPQTITPlptNIPMPKSEKIQEIVQLVKSAKRPV 291
Cdd:PRK08611 155 GVAVLtIPDDLPAQKIKDTTNK------------------------TVDTFRP---TVPSPKPKDIKKAAKLINKAKKPV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 292 LLIGSQAtlppvKPA--DLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVRR-------DALKDADLTILAGTvcdfrl 362
Cdd:PRK08611 208 ILAGLGA-----KHAkeELLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNLGKigtkpayEAMQEADLLIMVGT------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 363 SYGRT--LSKKSKIVALNRNSSQLTKNekafWNSDVSVQADVATSLVQVanalgaNHTTTPTEWVKSLREKDDEKESANa 440
Cdd:PRK08611 277 NYPYVdyLPKKAKAIQIDTDPANIGKR----YPVNVGLVGDAKKALHQL------TENIKHVEDRRFLEACQENMAKWW- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 441 KKMEQKLTNGF--LNPLNFLRTLDQSLPDDAILVADGG----------------DFVGSAayivrprgplqWLdpgafGT 502
Cdd:PRK08611 346 KWMEEDENNAStpIKPERVMAAIQKIADDDAVLSVDVGtvtvwsarylnlgtnqKFIISS-----------WL-----GT 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 503 LGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRY 582
Cdd:PRK08611 410 MGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELEYAIDLSDMDY 489
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 17542570 583 DNVAKSLGSWGETIdESNADsarkiLDEALAVCRSGEQSALVNVLI 628
Cdd:PRK08611 490 AKFAEACGGKGYRV-EKAEE-----LDPAFEEALAQDKPVIIDVYV 529
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
58-614 |
5.64e-43 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 162.47 E-value: 5.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVA-AEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAiGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGG--AAPTLLKGRGALQDI-DQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFP 213
Cdd:PRK07064 85 LVEALTAGTPLLHITGqiETPYLDQDLGYIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 214 VDvlypyelvvkeigfnpnakgfIQRALnfylrchvsrqfgNAWaPQTITPLPTNIPMPKSEKIQEIVQLVKSAKRPVLL 293
Cdd:PRK07064 165 ID---------------------IQAAE-------------IEL-PDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 294 IGSQAtlppVKPADLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVR-----RDALKDADLTILAGTvcdfRLSYGRTL 368
Cdd:PRK07064 210 LGGGA----RHAGAEVKRLVDLGFGVVTSTQGRGVVPEDHPASLGAFNnsaavEALYKTCDLLLVVGS----RLRGNETL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 369 SKKskiVALNRNSSQLTKNEKAF---WNSDVSVQADVATSLVQVANALGANHTTTPtEWVKSLREKDDEKESAnakkmeq 445
Cdd:PRK07064 282 KYS---LALPRPLIRVDADAAADgrgYPNDLFVHGDAARVLARLADRLEGRLSVDP-AFAADLRAAREAAVAD------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 446 kLTNGfLNPL-NFLRTLDQSLPDDAILVAD---GGDFVGSAayIVRPRGPLQWLDPGAfGTLGVGGGFALGAKTVYPKRP 521
Cdd:PRK07064 351 -LRKG-LGPYaKLVDALRAALPRDGNWVRDvtiSNSTWGNR--LLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRK 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 522 VYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVA-VDLARTRYDNVAKSLG--SWgetiDE 598
Cdd:PRK07064 426 TVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNIQDAQYGGRRYyVELHTPDFALLAASLGlpHW----RV 501
|
570
....*....|....*.
gi 17542570 599 SNADSARKILDEALAV 614
Cdd:PRK07064 502 TSADDFEAVLREALAK 517
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
58-628 |
6.93e-42 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 159.87 E-value: 6.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLG-IKIVDTRHEVTAVFAADAVARlrqSIGVAAV---TAGPGLTNT 133
Cdd:PRK08155 15 GAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMAR---TTGKPAVcmaCSGPGATNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 134 ITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKY---VARVERLRDIVPtvrEAIKAAKSGCPGPVFV 210
Cdd:PRK08155 92 VTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHnylVRDIEELPQVIS---DAFRIAQSGRPGPVWI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 211 EFPVDVlypyELVVKEIGfnpnakgfiqralnfylrchvsrqfgnAWAPqtiTPLPTNIPMPKSEKIQEIVQLVKSAKRP 290
Cdd:PRK08155 169 DIPKDV----QTAVIELE---------------------------ALPA---PAEKDAAPAFDEESIRDAAAMINAAKRP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 291 VLLIG-----SQAtlppvkPADLVKAVEALGCPVFLGGMARGLLGKDHPLQ-----MRQVRRD--ALKDADLTILAGTVC 358
Cdd:PRK08155 215 VLYLGggvinSGA------PARARELAEKAQLPTTMTLMALGMLPKAHPLSlgmlgMHGARSTnyILQEADLLIVLGARF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 359 DFRlSYGRT--LSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHTTtptEW---VKSLRekdd 433
Cdd:PRK08155 289 DDR-AIGKTeqFCPNAKIIHVDIDRAELGKIKQP----HVAIQADVDDVLAQLLPLVEAQPRA---EWhqlVADLQ---- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 434 ekesaNAKKMEQKLTNGFLNPLNFLRTLDQSLPDDAILVADGGD---FVGSAAYIVRPRgplQWLDPGAFGTLGVGGGFA 510
Cdd:PRK08155 357 -----REFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQhqmWTAQAYPLNRPR---QWLTSGGLGTMGFGLPAA 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 511 LGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRYDNVAKSLG 590
Cdd:PRK08155 429 IGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQSLFYGQRVFAATYPGKINFMQIAAG 508
|
570 580 590
....*....|....*....|....*....|....*...
gi 17542570 591 SWGETIDESNADSARKILDEALAvcRSGeqSALVNVLI 628
Cdd:PRK08155 509 FGLETCDLNNEADPQAALQEAIN--RPG--PALIHVRI 542
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
55-556 |
4.14e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 157.63 E-value: 4.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 55 KRHGGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTI 134
Cdd:PRK06048 7 KMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 135 TAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPV 214
Cdd:PRK06048 87 TGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 215 DVL-------YPYELVVKeiGFNPNAKGFIQralnfylrchvsrqfgnawapqtitplptnipmpkseKIQEIVQLVKSA 287
Cdd:PRK06048 167 DVTtaeidfdYPDKVELR--GYKPTYKGNPQ-------------------------------------QIKRAAELIMKA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 288 KRPVLL-----IGSQATlppvkpADLVKAVEALGCPVFLGGMARGLLGKDHPLQM-------RQVRRDALKDADLTILAG 355
Cdd:PRK06048 208 ERPIIYagggvISSNAS------EELVELAETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAIQESDLIIAVG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 356 TVCDFRLSyGRTLS--KKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHTTTPTEWVKSLREKdd 433
Cdd:PRK06048 282 ARFDDRVT-GKLASfaPNAKIIHIDIDPAEISKNVKV----DVPIVGDAKQVLKSLIKYVQYCDRKEWLDKINQWKKE-- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 434 ekesanaKKMEQKLTNGFLNPLNFLRTLDQSLPdDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGA 513
Cdd:PRK06048 355 -------YPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGA 426
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 17542570 514 KTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDA 556
Cdd:PRK06048 427 KVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNG 469
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
58-628 |
5.66e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 157.90 E-value: 5.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPI---LVAAEKLG-IKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNT 133
Cdd:PRK07418 21 GAYALMDSLKRHGVKHIFGYPGGAILPIydeLYKAEAEGwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 134 ITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCK--YVARveRLRDIVPTVREAIKAAKSGCPGPVFVE 211
Cdd:PRK07418 101 VTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKhsYVVR--DPSDMARIVAEAFHIASSGRPGPVLID 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 212 FPVDV---LYPYELV----VKEIGFNPNAKGfiqralnfylrchvsrqfgnawapqtitplptnipmpKSEKIQEIVQLV 284
Cdd:PRK07418 179 IPKDVgqeEFDYVPVepgsVKPPGYRPTVKG-------------------------------------NPRQINAALKLI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 285 KSAKRPVLLIGSQATLPPVKpADLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVRRD-------ALKDADLTILAGTV 357
Cdd:PRK07418 222 EEAERPLLYVGGGAISAGAH-AELKELAERFQIPVTTTLMGKGAFDEHHPLSVGMLGMHgtayanfAVTECDLLIAVGAR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 358 CDFRLSyGR--TLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHTTTPT-EWVkslrekdde 434
Cdd:PRK07418 301 FDDRVT-GKldEFASRAKVIHIDIDPAEVGKNRRP----DVPIVGDVRKVLVKLLERSLEPTTPPRTqAWL--------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 435 kESANAKKMEQKLT----NGFLNPLNFLRTLDQSLPdDAILVADGGDFVGSAAYIVRpRGPLQWLDPGAFGTLGVGGGFA 510
Cdd:PRK07418 367 -ERINRWKQDYPLVvppyEGEIYPQEVLLAVRDLAP-DAYYTTDVGQHQMWAAQFLR-NGPRRWISSAGLGTMGFGMPAA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 511 LGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPV-IGIVGNDacWTQIAREqvpmFQSSVAVDlartRYDN----- 584
Cdd:PRK07418 444 MGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVkTVIINNG--WQGMVRQ----WQESFYGE----RYSAsnmep 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 17542570 585 -------VAKSLGSWGETIDEsnadsaRKILDEALAVCRSGEQSALVNVLI 628
Cdd:PRK07418 514 gmpdfvkLAEAFGVKGMVISE------RDQLKDAIAEALAHDGPVLIDVHV 558
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
55-628 |
4.06e-40 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 154.65 E-value: 4.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 55 KRHGGELVASVLKAHDVEEIFVLCGGHISPILVA-AEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNT 133
Cdd:PRK08199 7 ARTGGQILVDALRANGVERVFCVPGESYLAVLDAlHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 134 ITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFP 213
Cdd:PRK08199 87 SIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 214 VDVLYpyelvvkEIGFNPNAKGFIQRAlnfylrchvsrqfgnawapqtitplptniPMPKSEKIQEIVQLVKSAKRPVLL 293
Cdd:PRK08199 167 EDVLS-------ETAEVPDAPPYRRVA-----------------------------AAPGAADLARLAELLARAERPLVI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 294 IG-----SQATlppvkpADLVKAVEALGCPVFLGGMARGLLGKDHP-------LQMRQVRRDALKDADLTILAGTvcdfR 361
Cdd:PRK08199 211 LGgsgwtEAAV------ADLRAFAERWGLPVACAFRRQDLFDNRHPnyagdlgLGINPALAARIREADLVLAVGT----R 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 362 LS----YGRTL----SKKSKIVALNRNSSQLTKnekaFWNSDVSVQADVATSLVQVAnALGANHTTTPTEWVKSLREkDD 433
Cdd:PRK08199 281 LGevttQGYTLldipVPRQTLVHVHPDAEELGR----VYRPDLAIVADPAAFAAALA-ALEPPASPAWAEWTAAAHA-DY 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 434 EKESAnAKKMEQKLTNGflnplNFLRTLDQSLPDDAILVADGGDFvgsAAYIVRP---RGPLQWLDPGAfGTLGVGGGFA 510
Cdd:PRK08199 355 LAWSA-PLPGPGAVQLG-----EVMAWLRERLPADAIITNGAGNY---ATWLHRFfrfRRYRTQLAPTS-GSMGYGLPAA 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 511 LGAKTVYPKRPVYIIWGDGsCgySLM---EYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSV-AVDLARTRYDNVA 586
Cdd:PRK08199 425 IAAKLLFPERTVVAFAGDG-C--FLMngqELATAVQYGLPIIVIVVNNGMYGTIRMHQEREYPGRVsGTDLTNPDFAALA 501
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 17542570 587 KSLGSWGETIdESNADSArkildEALAVCRSGEQSALVNVLI 628
Cdd:PRK08199 502 RAYGGHGETV-ERTEDFA-----PAFERALASGKPALIEIRI 537
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
58-614 |
4.41e-40 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 154.59 E-value: 4.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAA-EKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALhEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDV 216
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 217 L-------YPYELVVKEIGFNPNA---KGFIQRALnfylrchvsrqfgnawapqtitplptnipmpksekiqeivQLVKS 286
Cdd:PRK08979 166 LnpailhpYEYPESIKMRSYNPTTsghKGQIKRGL----------------------------------------QALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 287 AKRPVLLIGSQATLPPVKpADLVKAVEALGCPVFLGGMARGLLGKDHP-----LQMRQVRRD--ALKDADLTILAGTVCD 359
Cdd:PRK08979 206 AKKPVLYVGGGAIISGAD-KQILQLAEKLNLPVVSTLMGLGAFPGTHKnslgmLGMHGRYEAnmAMHNADLIFGIGVRFD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 360 FRLSygRTLSK---KSKIVALNRNSSQLTKNEKAfwnsDV----SVQADVATSLVQVANALGANHTTTPTEWVKSLREKD 432
Cdd:PRK08979 285 DRTT--NNLEKycpNATILHIDIDPSSISKTVRV----DIpivgSADKVLDSMLALLDESGETNDEAAIASWWNEIEVWR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 433 DEKESANAKKMEQkltngfLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALG 512
Cdd:PRK08979 359 SRNCLAYDKSSER------IKPQQVIETLYKLTNGDAYVASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 513 AKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQ--------SSVAvDLARtrydn 584
Cdd:PRK08979 433 VKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMVKQWQDMIYQgrhshsymDSVP-DFAK----- 506
|
570 580 590
....*....|....*....|....*....|
gi 17542570 585 VAKSLGSWGETIdeSNADSARKILDEALAV 614
Cdd:PRK08979 507 IAEAYGHVGIRI--SDPDELESGLEKALAM 534
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
58-548 |
8.58e-40 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 154.19 E-value: 8.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLG-IKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDkIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDV 216
Cdd:PRK06965 103 IATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPKDV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 217 -----LYPYELVVKEIGFNPNAKGfiqralnfylrchvsrqfgnawapqtitplptnipmpKSEKIQEIVQLVKSAKRPV 291
Cdd:PRK06965 183 sktpcEYEYPKSVEMRSYNPVTKG-------------------------------------HSGQIRKAVSLLLSAKRPY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 292 LLIGSQATLPPVKpADLVKAVEALGCPVF-----LGGMAR------GLLGKDHPLQMRqvrrDALKDADLTILAGTVCDF 360
Cdd:PRK06965 226 IYTGGGVILANAS-RELRQLADLLGYPVTntlmgLGAYPAsdkkflGMLGMHGTYEAN----MAMQHCDVLIAIGARFDD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 361 RL--SYGRTLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHTTTPTEWVKSLREKDDEKESA 438
Cdd:PRK06965 301 RVigNPAHFASRPRKIIHIDIDPSSISKRVKV----DIPIVGDVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGWRSR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 439 NAkkMEQKLTNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYP 518
Cdd:PRK06965 377 DC--LKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHP 454
|
490 500 510
....*....|....*....|....*....|
gi 17542570 519 KRPVYIIWGDGSCGYSLMEYDTFARHKLPV 548
Cdd:PRK06965 455 DDDVVCITGEGSIQMCIQELSTCLQYDTPV 484
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
49-529 |
6.33e-39 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 151.51 E-value: 6.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 49 QVDEKSKRHGGELVASVLKAHDVEEIFVLCGGHISPILVAAEKL-GIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAG 127
Cdd:PRK07282 3 KISLESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFeGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 128 PGLTNTITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGP 207
Cdd:PRK07282 83 PGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 208 VFVEFPVDVlypYELVVKEIgFNPNAKgfiqralnfylrchvsrqfgnawapqtitpLPTNIPM--PKSEKIQEIVQLVK 285
Cdd:PRK07282 163 VVIDLPKDV---SALETDFI-YDPEVN------------------------------LPSYQPTlePNDMQIKKILKQLS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 286 SAKRPVLLIGSQATLPPVKpADLVKAVEALGCPVFLGGMARGLLGKDHPLQM-------RQVRRDALKDADLTILAGTVC 358
Cdd:PRK07282 209 KAKKPVILAGGGINYAEAA-TELNAFAERYQIPVVTTLLGQGTIATSHPLFLgmggmhgSYAANIAMTEADFMINIGSRF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 359 DFRL-SYGRTLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVAnALGANHTTTpTEWVKSLREkddEKES 437
Cdd:PRK07282 288 DDRLtGNPKTFAKNAKVAHIDIDPAEIGKIIKT----DIPVVGDAKKALQMLL-AEPTVHNNT-EKWIEKVTK---DKNR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 438 ANAKKMEQKLtngfLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVY 517
Cdd:PRK07282 359 VRSYDKKERV----VQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIAN 434
|
490
....*....|..
gi 17542570 518 PKRPVYIIWGDG 529
Cdd:PRK07282 435 PDKEVILFVGDG 446
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
58-530 |
8.79e-39 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 151.67 E-value: 8.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPI---LVAAEKLgiKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTI 134
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAILPVydpLFDSTKV--RHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 135 TAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPV 214
Cdd:PRK07789 111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 215 DVLypyelvvkeigfnpnakgfiQRALNFylrchvsrqfgnAWAPQTITPLPTNIPMPKSEKIQEIVQLVKSAKRPVLLI 294
Cdd:PRK07789 191 DAL--------------------QAQTTF------------SWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 295 G-----SQATlppvkpADLVKAVEALGCPVFLGGMARGLLGKDHPLQM---------RQVRrdALKDADLTILAGTVCDF 360
Cdd:PRK07789 239 GggvirAEAS------AELRELAELTGIPVVTTLMARGAFPDSHPQHLgmpgmhgtvAAVA--ALQRSDLLIALGARFDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 361 RLSyGR--TLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHTTTP----TEWVKSLrekDDE 434
Cdd:PRK07789 311 RVT-GKldSFAPDAKVIHADIDPAEIGKNRHA----DVPIVGDVKEVIAELIAALRAEHAAGGkpdlTAWWAYL---DGW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 435 KESANAKKMEQklTNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAK 514
Cdd:PRK07789 383 RETYPLGYDEP--SDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAK 460
|
490
....*....|....*.
gi 17542570 515 TVYPKRPVYIIWGDGS 530
Cdd:PRK07789 461 VGRPDKEVWAIDGDGC 476
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
69-554 |
2.47e-37 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 146.77 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 69 HDVEEIFVLCGGHISPI---LVAAEKLG-IKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAVKNAQMAE 144
Cdd:CHL00099 23 HGVKHIFGYPGGAILPIydeLYAWEKKGlIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 145 SPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDV---LYPYE 221
Cdd:CHL00099 103 VPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVgleKFDYY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 222 LVVKeigfnpnakgfiqralnfylrchvsrqfgnawaPQTITPLP--TNIPMPKSEKIQEIVQLVKSAKRPVLLIGSQAT 299
Cdd:CHL00099 183 PPEP---------------------------------GNTIIKILgcRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 300 LPPVKpADLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVRRD-------ALKDADLTILAGTVCDFRLSyGR--TLSK 370
Cdd:CHL00099 230 ISDAH-QEITELAELYKIPVTTTLMGKGIFDEDHPLCLGMLGMHgtayanfAVSECDLLIALGARFDDRVT-GKldEFAC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 371 KSKIVALNRNSSQLTKNEkafwNSDVSVQADVATSLVQVANALGANHTTTPTEWVKSLREKDDEKESANAKKMEQKLTNg 450
Cdd:CHL00099 308 NAQVIHIDIDPAEIGKNR----IPQVAIVGDVKKVLQELLELLKNSPNLLESEQTQAWRERINRWRKEYPLLIPKPSTS- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 451 fLNPLNFLRTLDQSLPdDAILVADGGDFVGSAAYIVRPrGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGS 530
Cdd:CHL00099 383 -LSPQEVINEISQLAP-DAYFTTDVGQHQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDAS 459
|
490 500
....*....|....*....|....*
gi 17542570 531 CGYSLMEYDTFARHKLPV-IGIVGN 554
Cdd:CHL00099 460 FQMNLQELGTIAQYNLPIkIIIINN 484
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
58-548 |
3.46e-37 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 146.43 E-value: 3.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGG---HISPILVAAEKlgIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTI 134
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGavlHIYDALFKQDK--VEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 135 TAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPV 214
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 215 DVL-------YPYELVVKEIGFNPNAKGfiqralnfylrcHvsrqfgnawapqtitplptnipmpkSEKIQEIVQLVKSA 287
Cdd:PRK06466 164 DMTnpaekfeYEYPKKVKLRSYSPAVRG------------H-------------------------SGQIRKAVEMLLAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 288 KRPVLLIGSQATLPPVKpADLVKAVEALGCPVF-----LGGMAR------GLLGKDHPLQMRQvrrdALKDADLTILAGT 356
Cdd:PRK06466 207 KRPVIYSGGGVVLGNAS-ALLTELAHLLNLPVTntlmgLGGFPGtdrqflGMLGMHGTYEANM----AMHHADVILAVGA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 357 VCDFRLSYG-RTLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHTTTPTEWVKSLREKDDEK 435
Cdd:PRK06466 282 RFDDRVTNGpAKFCPNAKIIHIDIDPASISKTIKA----DIPIVGPVESVLTEMLAILKEIGEKPDKEALAAWWKQIDEW 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 436 ESANAKKMEQKLTNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKT 515
Cdd:PRK06466 358 RGRHGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKL 437
|
490 500 510
....*....|....*....|....*....|...
gi 17542570 516 VYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPV 548
Cdd:PRK06466 438 AFPDQDVACVTGEGSIQMNIQELSTCLQYGLPV 470
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
58-616 |
1.09e-36 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 144.98 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVA----AEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNT 133
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 134 ITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFP 213
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 214 VDVLYPYelvVKEIGF--NPNAKGFiqralnfylrchvsrqfgnawapqtiTPLPTNIpmpKSEKIQEIVQLVKSAKRPV 291
Cdd:PRK06456 164 RDIFYEK---MEEIKWpeKPLVKGY--------------------------RDFPTRI---DRLALKKAAEILINAERPI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 292 LLIGSQATLPPVKPaDLVKAVEALGCPVFLGGMARGLLGKDHPLQM-------RQVRRDALKDADLTILAGTVCDFR--L 362
Cdd:PRK06456 212 ILVGTGVVWSNATP-EVLELAELLHIPIVSTFPGKTAIPHDHPLYFgpmgyygRAEASMAALESDAMLVVGARFSDRtfT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 363 SYGRTLSKKSKIVALNRNSsqlTKNEKAFwNSDVSVQADVATSLVQVANA---LGANHTTtpTEWVKSLREKDDEKEsan 439
Cdd:PRK06456 291 SYDEMVETRKKFIMVNIDP---TDGEKAI-KVDVGIYGNAKIILRELIKAiteLGQKRDR--SAWLKRVKEYKEYYS--- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 440 akKMEQKLTNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPK 519
Cdd:PRK06456 362 --QFYYTEENGKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 520 RPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVgNDACWTQIAREQVPMFQSS--VAVDLA-RTRYDNVAKSLGSWG--- 593
Cdd:PRK06456 440 KVVVDLDGDGSFLMTGTNLATAVDEHIPVISVI-FDNRTLGLVRQVQDLFFGKriVGVDYGpSPDFVKLAEAFGALGfnv 518
|
570 580
....*....|....*....|...
gi 17542570 594 ETIDESNADSARKILDEALAVCR 616
Cdd:PRK06456 519 TTYEDIEKSLKSAIKEDIPAVIR 541
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
58-555 |
1.74e-36 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 144.52 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFvlcGGHI-SPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:PRK06112 16 VAHAIARALKRHGVEQIF---GQSLpSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDV 216
Cdd:PRK06112 93 LAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLLPADL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 217 LypyelvvKEIGFNPNAkgfiQRalnfylrchvSRQFGnAWapqtitPLPTNIPMPKseKIQEIVQLVKSAKRPVLLIG- 295
Cdd:PRK06112 173 L-------TAAAAAPAA----PR----------SNSLG-HF------PLDRTVPAPQ--RLAEAASLLAQAQRPVVVAGg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 296 ----SQATlppvkpADLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQV------------RRDALKDADLTILAGTvcd 359
Cdd:PRK06112 223 gvhiSGAS------AALAALQSLAGLPVATTNMGKGAVDETHPLSLGVVgslmgprspgrhLRDLVREADVVLLVGT--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 360 fRLSYGRT-----LSKKSKIVALNRNSSQLTKNEKAfwnsdVSVQADVATSLVQVANALGANHTTTPTEWVKSLREKDDE 434
Cdd:PRK06112 294 -RTNQNGTdswslYPEQAQYIHIDVDGEEVGRNYEA-----LRLVGDARLTLAALTDALRGRDLAARAGRRAALEPAIAA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 435 KESANAKKMEQKLTNGF--LNPLNFLRTLDQSLPDDAILVADGG-DFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFAL 511
Cdd:PRK06112 368 GREAHREDSAPVALSDAspIRPERIMAELQAVLTGDTIVVADASySSIWVANFLTARRAGMRFLTPRGLAGLGWGVPMAI 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 17542570 512 GAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGND 555
Cdd:PRK06112 448 GAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNN 491
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
55-555 |
1.76e-36 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 144.29 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 55 KRHGGELVASVLKAHDVEEIFVLCGGHISPILVAAEKL-GIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNT 133
Cdd:PRK06882 3 KLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLgGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 134 ITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFP 213
Cdd:PRK06882 83 ITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 214 VDVL-----YPYEL--VVKEIGFNPNA---KGFIQRALNFYLrchvsrqfgnawapqtitplptnipmpksekiqeivql 283
Cdd:PRK06882 163 KDMVnpankFTYEYpeEVSLRSYNPTVqghKGQIKKALKALL-------------------------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 284 vkSAKRPVLLIGSQATLPPVKpADLVKAVEALGCPVF-----LGGMAR------GLLGKDHPLQMrqvrRDALKDADLTI 352
Cdd:PRK06882 205 --VAKKPVLFVGGGVITAECS-EQLTQFAQKLNLPVTsslmgLGAYPStdkqflGMLGMHGTYEA----NNAMHESDLIL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 353 LAGTVCDFRLSygRTLSK---KSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALG----ANHTTTPTEWV 425
Cdd:PRK06882 278 GIGVRFDDRTT--NNLAKycpNAKVIHIDIDPTSISKNVPA----YIPIVGSAKNVLEEFLSLLEeenlAKSQTDLTAWW 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 426 KSLREkddekesANAKK-MEQKLTNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLG 504
Cdd:PRK06882 352 QQINE-------WKAKKcLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQMFAALHYPFDKPRRWINSGGAGTMG 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 17542570 505 VGGGFALGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGND 555
Cdd:PRK06882 425 FGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
56-548 |
3.12e-36 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 143.72 E-value: 3.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 56 RHGGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLG-IKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTI 134
Cdd:PLN02470 13 RKGADILVEALEREGVDTVFAYPGGASMEIHQALTRSNcIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 135 TAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPV 214
Cdd:PLN02470 93 TGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 215 DVlyPYELVVKEIGFNPNAKGFIQRalnfylrchvsrqfgnawapqtitpLPtniPMPKSEKIQEIVQLVKSAKRPVLLI 294
Cdd:PLN02470 173 DI--QQQLAVPNWNQPMKLPGYLSR-------------------------LP---KPPEKSQLEQIVRLISESKRPVVYV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 295 GSQATlppVKPADLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVRRD-------ALKDADLTILAGTVCDFRLSyGR- 366
Cdd:PLN02470 223 GGGCL---NSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMLGMHgtvyanyAVDSADLLLAFGVRFDDRVT-GKl 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 367 -TLSKKSKIVALNRNSSQLTKNEKAFwnsdVSVQADVATSLVQVANALGANHTTTP--TEWVKSLREKdDEKESANAKKM 443
Cdd:PLN02470 299 eAFASRASIVHIDIDPAEIGKNKQPH----VSVCADVKLALQGLNKLLEERKAKRPdfSAWRAELDEQ-KEKFPLSYPTF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 444 EQKLTngflnPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVY 523
Cdd:PLN02470 374 GDAIP-----PQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVV 448
|
490 500
....*....|....*....|....*
gi 17542570 524 IIWGDGSCGYSLMEYDTFARHKLPV 548
Cdd:PLN02470 449 DIDGDGSFIMNIQELATIHVENLPV 473
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
58-554 |
2.45e-35 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 141.00 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPIL-VAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:PRK09107 13 GAEMVVQALKDQGVEHIFGYPGGAVLPIYdEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDV 216
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 217 LYpyelvvkeigfnpnAKGFIQralnfylrchvsrqfgnawAPQTITPLPTNIPMPK--SEKIQEIVQLVKSAKRPVLLI 294
Cdd:PRK09107 173 QF--------------ATGTYT-------------------PPQKAPVHVSYQPKVKgdAEAITEAVELLANAKRPVIYS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 295 GSQATLPPVKPADLVKA-VEALGCPV--FLGGMAR---------GLLGKdHPL---QMrqvrrdALKDADLTILAGTVCD 359
Cdd:PRK09107 220 GGGVINSGPEASRLLRElVELTGFPItsTLMGLGAypasgknwlGMLGM-HGTyeaNM------AMHDCDVMLCVGARFD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 360 FRLSyGRT--LSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGANHTTTPTEWVKSLREKDDEKES 437
Cdd:PRK09107 293 DRIT-GRLdaFSPNSKKIHIDIDPSSINKNVRV----DVPIIGDVGHVLEDMLRLWKARGKKPDKEALADWWGQIARWRA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 438 ANAkkMEQKLTNGFLNPLNFLRTLDQSLPD-DAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTV 516
Cdd:PRK09107 368 RNS--LAYTPSDDVIMPQYAIQRLYELTKGrDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIA 445
|
490 500 510
....*....|....*....|....*....|....*....
gi 17542570 517 YPKRPVYIIWGDGSCGYSLMEYDTFARHKLPV-IGIVGN 554
Cdd:PRK09107 446 HPDALVIDIAGDASIQMCIQEMSTAVQYNLPVkIFILNN 484
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
49-565 |
4.74e-35 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 139.90 E-value: 4.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 49 QVDEKSKRHGGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGP 128
Cdd:PRK07710 9 SKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 129 GLTNTITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPV 208
Cdd:PRK07710 89 GATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 209 FVEFPVDVL-----YPYELVVKEIGFNPNAKgfiqralnfylrchvsrqfgnawapqtitplptnipmPKSEKIQEIVQL 283
Cdd:PRK07710 169 LIDIPKDMVveegeFCYDVQMDLPGYQPNYE-------------------------------------PNLLQIRKLVQA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 284 VKSAKRPVLLIGSqATLPPVKPADLVKAVEALGCPVFLGGMARGLLGKDHPLQM-------RQVRRDALKDADLTILAGT 356
Cdd:PRK07710 212 VSVAKKPVILAGA-GVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPADHPLFLgmagmhgTYTANMALYECDLLINIGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 357 VCDFRLSYG-RTLSKKSKIVALNRNSSQLTKNEKafwnSDVSVQADVATSLVQVANALGANHTTtpTEWVKSLREKDDE- 434
Cdd:PRK07710 291 RFDDRVTGNlAYFAKEATVAHIDIDPAEIGKNVP----TEIPIVADAKQALQVLLQQEGKKENH--HEWLSLLKNWKEKy 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 435 ----KESANAKK------MEQKLTNGflnplnflrtldqslpdDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLG 504
Cdd:PRK07710 365 plsyKRNSESIKpqkaieMLYEITKG-----------------EAIVTTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMG 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542570 505 VGGGFALGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDAC------WTQIAREQ 565
Cdd:PRK07710 428 FGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEAlgmvrqWQEEFYNQ 494
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
58-549 |
6.92e-35 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 139.60 E-value: 6.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLG-IKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGgIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDV 216
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 217 L-------YPYELVVKEIGFNPNA---KGFIQRALnfylrchvsrqfgnawapqtitplptnipmpksekiqeivQLVKS 286
Cdd:PRK07979 166 LnpanklpYVWPESVSMRSYNPTTqghKGQIKRAL----------------------------------------QTLVA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 287 AKRPVLLIGSQATLPPVKpADLVKAVEALGCPVF-----LGGM------ARGLLGKDHPLQMRQvrrdALKDADLTILAG 355
Cdd:PRK07979 206 AKKPVVYVGGGAINAACH-QQLKELVEKLNLPVVsslmgLGAFpathrqSLGMLGMHGTYEANM----TMHNADVIFAVG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 356 TVCDFRLSygRTLSK---KSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGanhTTTPTEWVKSLREKD 432
Cdd:PRK07979 281 VRFDDRTT--NNLAKycpNATVLHIDIDPTSISKTVTA----DIPIVGDARQVLEQMLELLS---QESAHQPLDEIRDWW 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 433 DEKESANAKK-MEQKLTNGFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFAL 511
Cdd:PRK07979 352 QQIEQWRARQcLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAL 431
|
490 500 510
....*....|....*....|....*....|....*...
gi 17542570 512 GAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVI 549
Cdd:PRK07979 432 GVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVL 469
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
60-628 |
5.52e-33 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 133.80 E-value: 5.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 60 ELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAVKN 139
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 140 AQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGcPGPVFVEFPVDVLY- 218
Cdd:PRK06457 86 AKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISK-RGVAHINLPVDILRk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 219 --PYELVVKEIGFNPnakgfiqralnfylrcHVSRQFGNAwapqtitplptnipmpksekiqeiVQLVKSAKRPVLLIGS 296
Cdd:PRK06457 165 ssEYKGSKNTEVGKV----------------KYSIDFSRA------------------------KELIKESEKPVLLIGG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 297 QATlppVKPADLVKAVEALGCPVFLGGMARGLLGKDHPLQMRQV-------RRDALKDADLTILAGTVcdfrLSYGRTLS 369
Cdd:PRK06457 205 GTR---GLGKEINRFAEKIGAPIIYTLNGKGILPDLDPKVMGGIgllgtkpSIEAMDKADLLIMLGTS----FPYVNFLN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 370 KKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLvqvanalganhTTTPTE-----WVKSLREKDDEKESAnaKKME 444
Cdd:PRK06457 278 KSAKVIQVDIDNSNIGKRLDV----DLSYPIPVAEFL-----------NIDIEEksdkfYEELKGKKEDWLDSI--SKQE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 445 QKLTNgFLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAK-TVYPKRPVY 523
Cdd:PRK06457 341 NSLDK-PMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASfAVENKRQVI 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 524 IIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRYDNVAKSLGSWGETIDESNadS 603
Cdd:PRK06457 420 SFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMGYPEWGVDLYNPDFTKIAESIGFKGFRLEEPK--E 497
|
570 580
....*....|....*....|....*
gi 17542570 604 ARKILDEALavcrSGEQSALVNVLI 628
Cdd:PRK06457 498 AEEIIEEFL----NTKGPAVLDAIV 518
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
474-626 |
8.46e-29 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 111.91 E-value: 8.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 474 DGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVG 553
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542570 554 NDACWTQIAREQVPMFQSSVA----VDLARTRYDNVAKSLGSWGETIDesNADSARKILDEALAvcrsGEQSALVNV 626
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSgpsgKILPPVDFAKLAEAYGAKGARVE--SPEELEEALKEALE----HDGPALIDV 151
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
457-628 |
9.65e-27 |
|
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: 106.96 E-value: 9.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 457 FLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSLM 536
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 537 EYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSV-AVDLARTRYDNVAKSLGSWGETIdESNADsarkiLDEALAVC 615
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVsGTDLSNPDFAALAEAYGAKGVRV-EDPED-----LEAALAEA 155
|
170
....*....|...
gi 17542570 616 RSGEQSALVNVLI 628
Cdd:cd00568 156 LAAGGPALIEVKT 168
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
452-628 |
8.50e-25 |
|
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: 101.45 E-value: 8.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 452 LNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSC 531
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 532 GYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRYDNVAKSLGSWGETIDesNADSARKILDEA 611
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVE--DPDELEAALDEA 159
|
170
....*....|....*..
gi 17542570 612 LAVcrsgEQSALVNVLI 628
Cdd:cd02014 160 LAA----DGPVVIDVVT 172
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
59-216 |
6.82e-24 |
|
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: 98.39 E-value: 6.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 59 GELVASVLKAHDVEEIFVLCGGHISPILVAAEKLG-IKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAV 137
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGkIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 138 KNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARV---ERLRDIvptVREAIKAAKSGcPGPVFVEFPV 214
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVtspEQLPEL---LDRAIRTAIAK-RGVAVLILPG 158
|
..
gi 17542570 215 DV 216
Cdd:cd07039 159 DV 160
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
65-593 |
1.01e-23 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 105.83 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 65 VLKAHDVEEIFVLCGGHISPILVAAEKLG-IKIVDTRHEVTAVFAADAVARLRQ-SIGVAAVTAGPGLTNTITAVKNAqM 142
Cdd:PRK11269 13 VLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEGYTRATAgNIGVCIGTSGPAGTDMITGLYSA-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 143 AES-PLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVeRLRDIVPTV-REAIKAAKSGCPGPVFVEFPVDVlypy 220
Cdd:PRK11269 92 ADSiPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTV-REPALVPRVfQQAFHLMRSGRPGPVLIDLPFDV---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 221 elVVKEIGFNPNakgfiqralnfylrchvsrqfgnawapqTITPLPTNIPMPKSEKIQEIVQLVKSAKRPVLLIGSQatl 300
Cdd:PRK11269 167 --QVAEIEFDPD----------------------------TYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGGG--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 301 ppVKPAD----LVKAVEALGCPVFLGGMARGLLGKDHPLQMRQVR-RDALKDADLTILAGtvcDFRLSYGR--------- 366
Cdd:PRK11269 214 --VINADasdlLVEFAELTGVPVIPTLMGWGAIPDDHPLMAGMVGlQTSHRYGNATLLAS---DFVLGIGNrwanrhtgs 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 367 --TLSKKSKIVALNRNSSQLTKnekaFWNSDVSVQADVATSL---VQVANALGANHTT-TPTEWVKSLREKddekesana 440
Cdd:PRK11269 289 veVYTKGRKFVHVDIEPTQIGR----VFGPDLGIVSDAKAALellVEVAREWKAAGRLpDRSAWVADCQER--------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 441 KKMEQKLTNgFLN----PLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTV 516
Cdd:PRK11269 356 KRTLLRKTH-FDNvpikPQRVYEEMNKAFGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAA 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542570 517 YPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPmFQSSVAVDLArtrYDNV-AKSLGSWG 593
Cdd:PRK11269 435 DPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQAQRA-FDMDYCVQLA---FENInSPELNGYG 508
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
59-632 |
4.30e-23 |
|
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: 103.31 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 59 GELVASVLKAHDVEEIFVLCGGHISPILVAAEKL-GIKIVDTRHEVTAVFAADAVARLRqSIGVAAVTAGPGLTNTITAV 137
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHpGIRWVGCCNELNAGYAADGYARVN-GLGALVTTYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 138 KNAqMAE-SPLLLIGGAAPTLLKGRGA-----LQDID---QMVLFRPLCKYVARverlrdIVP--TVRE---AIKAAKSG 203
Cdd:COG3961 87 AGA-YAErVPVVHIVGAPGTRAQRRGPllhhtLGDGDfdhFLRMFEEVTVAQAV------LTPenAAAEidrVLAAALRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 204 CPgPVFVEFPVDVlypyelvvkeigfnpnakgfiqralnfylrchvsrqfgnAWAPQTITPLPTNIPMPKS------EKI 277
Cdd:COG3961 160 KR-PVYIELPRDV---------------------------------------ADAPIEPPEAPLPLPPPASdpaalaAAV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 278 QEIVQLVKSAKRPVLLIGSQATLPPVKPAdLVKAVEALGCPVFLGGMARGLLGKDHPL--------QMRQVRRDALKDAD 349
Cdd:COG3961 200 AAAAERLAKAKRPVILAGVEVHRFGLQEE-LLALAEKTGIPVATTLLGKSVLDESHPQfigtyagaASSPEVREYVENAD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 350 LTILAGTV-CDFRLSYGRTLSKKSKIVALNRNSSQLtkNEKAFwnSDVSVqADVATSLVQVANALGANHTTTPtewvksl 428
Cdd:COG3961 279 CVLCLGVVfTDTNTGGFTAQLDPERTIDIQPDSVRV--GGHIY--PGVSL-ADFLEALAELLKKRSAPLPAPA------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 429 rekddEKESANAKKMEQKLTNGflnplNFLRTLDQSLPDDAILVADGGD--FVGSAAYIvrPRG-----PLQWldpgafG 501
Cdd:COG3961 347 -----PPPPPPPAAPDAPLTQD-----RLWQRLQAFLDPGDIVVADTGTslFGAADLRL--PEGatfiaQPLW------G 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 502 TLGVGGGFALGAKTVYP-KRPVYIIwGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTqIarEQVPMFQSSVAVDLART 580
Cdd:COG3961 409 SIGYTLPAALGAALAAPdRRVILLV-GDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYT-I--ERAIHGPDGPYNDIANW 484
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 17542570 581 RYDNVAKSLG---SWG---ETIDEsnadsarkiLDEALAVCRSG-EQSALVNVLIGKTD 632
Cdd:COG3961 485 DYAKLPEAFGggnALGfrvTTEGE---------LEEALAAAEANtDRLTLIEVVLDKMD 534
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
452-597 |
3.51e-22 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 94.50 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 452 LNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSC 531
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542570 532 GYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSS-VAVDLARTRYDNVAKSLGSWGETID 597
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITVD 150
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
277-408 |
1.21e-21 |
|
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: 91.09 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 277 IQEIVQLVKSAKRPVLLIGSQATLPPVKPAdLVKAVEALGCPVFLGGMARGLLGKDHPLQM-------RQVRRDALKDAD 349
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEE-LRELAEKLGIPVVTTLMGKGAFPEDHPLYLgmlgmhgTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542570 350 LTILAGTVCDFRLSYG--RTLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQ 408
Cdd:pfam00205 80 LVLAVGARFDDIRTTGklPEFAPDAKIIHIDIDPAEIGKNYPV----DVPIVGDAKETLEA 136
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
61-214 |
4.45e-17 |
|
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: 78.54 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 61 LVASVLKAHDVEEIFVLCGGHISPILVAAEKL-GIKIVDTRHEVTAVFAADAVARLrQSIGVAAVTAGPGLTNTITAVKN 139
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARA-GGPPVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17542570 140 AQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGcPGPVFVEFPV 214
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
60-630 |
7.07e-16 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 81.19 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 60 ELVASVLKAHDVEEIFVLCGGHISPILVAAEKLG-IKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAVK 138
Cdd:PRK09124 7 DYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGtIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 139 NAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRP---LCKYVARVERLrdivPTVRE-AIKAAkSGCPGPVFVEFPV 214
Cdd:PRK09124 87 DCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFREcshYCELVSNPEQL----PRVLAiAMRKA-ILNRGVAVVVLPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 215 DVlypyelvvkeigfnpnakgFIQRAlnfylrchvSRQFGNAWAPqtiTPLPtnIPMPKSEKIQEIVQLVKSAKRPVLLI 294
Cdd:PRK09124 162 DV-------------------ALKPA---------PERATPHWYH---APQP--VVTPAEEELRKLAALLNGSSNITLLC 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 295 GS---QATlppvkpADLVKAVEALGCPVflggmARGLLGKDHplqmrqVRRD------------------ALKDADLTIL 353
Cdd:PRK09124 209 GSgcaGAH------DELVALAETLKAPI-----VHALRGKEH------VEYDnpydvgmtgligfssgyhAMMNCDTLLM 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 354 AGTvcDFrlSYGRTLSKKSKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVANALGAN----HTTTPTEWVKSLR 429
Cdd:PRK09124 272 LGT--DF--PYRQFYPTDAKIIQIDINPGSLGRRSPV----DLGLVGDVKATLAALLPLLEEKtdrkFLDKALEHYRKAR 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 430 EKDDEKESANAKKMEqkltngfLNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLdpGAF--GTLGVGG 507
Cdd:PRK09124 344 KGLDDLAVPSDGGKP-------IHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRRLL--GSFnhGSMANAM 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 508 GFALGAKTVYPKRPVYIIWGDGscGYSLMEYD--TFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRYDNV 585
Cdd:PRK09124 415 PQALGAQAAHPGRQVVALSGDG--GFSMLMGDflSLVQLKLPVKIVVFNNSVLGFVAMEMKAGGYLTDGTDLHNPDFAAI 492
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 17542570 586 AKSLGSWGETIDESNAdsarkiLDEALAVCRSGEQSALVNVLIGK 630
Cdd:PRK09124 493 AEACGITGIRVEKASE------LDGALQRAFAHDGPALVDVVTAK 531
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
60-613 |
1.93e-15 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 79.65 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 60 ELVASVLKAHDVEEIFVLCGGHISPILVAAEK-LGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAVK 138
Cdd:PRK06546 7 EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRtGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 139 NAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGcPGPVFVEFPVDVly 218
Cdd:PRK06546 87 DAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAG-GGVSVVTLPGDI-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 219 pyelvvkeigfnpnakgfiqralnfylrchVSRQFGNAWAPQTITPLPTNIpMPKSEKIQEIVQLVKSAKRPVLLIGSQa 298
Cdd:PRK06546 164 ------------------------------ADEPAPEGFAPSVISPRRPTV-VPDPAEVRALADAINEAKKVTLFAGAG- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 299 tlppVKPA--DLVKAVEALGCPV---------------FLGGMArGLLGKDhplqmrqVRRDALKDADLTILAGTvcDFr 361
Cdd:PRK06546 212 ----VRGAhaEVLALAEKIKAPVghslrgkewiqydnpFDVGMS-GLLGYG-------AAHEAMHEADLLILLGT--DF- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 362 lSYGRTLSKKsKIVALNRNSSQLTKNEKAfwnsDVSVQADVATSLVQVanalganhttTPTEWVKSLREKDDEKESANAK 441
Cdd:PRK06546 277 -PYDQFLPDV-RTAQVDIDPEHLGRRTRV----DLAVHGDVAETIRAL----------LPLVKEKTDRRFLDRMLKKHAR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 442 KMEQ----------KLTNgfLNPLNFLRTLDQSLPDDAILVADGG-DFVGSAAYIVrPRGPLQWLdpGAF--GTLGVGGG 508
Cdd:PRK06546 341 KLEKvvgaytrkveKHTP--IHPEYVASILDELAADDAVFTVDTGmCNVWAARYIT-PNGRRRVI--GSFrhGSMANALP 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 509 FALGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRYDNVAKS 588
Cdd:PRK06546 416 HAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMLVDGLPDFGTDHPPVDYAAIAAA 495
|
570 580
....*....|....*....|....*
gi 17542570 589 LGSWGETIdESNADsARKILDEALA 613
Cdd:PRK06546 496 LGIHAVRV-EDPKD-VRGALREAFA 518
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
454-635 |
5.85e-14 |
|
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: 70.39 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 454 PLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGY 533
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 534 SLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSSVAVDLARTRYDNVAKSLGSWGETIDEsnADSARKILDEALA 613
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIES--ADDLLPVLERALA 158
|
170 180
....*....|....*....|..
gi 17542570 614 VcrsgEQSALVNVLIgktDFRE 635
Cdd:cd02010 159 A----DGVHVIDCPV---DYSE 173
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
452-628 |
6.37e-14 |
|
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: 70.32 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 452 LNPLNFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGPLQWLDPGAfGTLGVGGGFALGAKTVYPKRPVYIIWGDGSC 531
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 532 GYSLMEYDTFARHKLPVIGIVGNDACWTQIAREQVPMFQSS------VAVDLAR--TRYDNVAKSLGSWGETIDESNAds 603
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGpgenapDGLDLLDpgIDFAAIAKAFGVEAERVETPEE-- 157
|
170 180
....*....|....*....|....*
gi 17542570 604 arkiLDEALAVCRSGEQSALVNVLI 628
Cdd:cd02002 158 ----LDEALREALAEGGPALIEVVV 178
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
452-554 |
3.59e-13 |
|
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: 68.29 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 452 LNPLNFLRTLDQSLPDDAILVADggdfVGS----AAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWG 527
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTD----VGQhqmwAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDG 76
|
90 100
....*....|....*....|....*..
gi 17542570 528 DGSCGYSLMEYDTFARHKLPVIGIVGN 554
Cdd:cd02015 77 DGSFQMNIQELATAAQYNLPVKIVILN 103
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
58-552 |
1.54e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 70.29 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 58 GGELVASVLKAHDVEEIFVLCGGHISPILVAAEKL-GIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVpRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGG--AAPTLLKGRGALQDIDQmvLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPV 214
Cdd:PRK12474 87 LHNARRAASPIVNIVGdhAVEHLQYDAPLTSDIDG--FARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 215 DVlypyelvvkeiGFNPNAkgfiqralnfyLRCHVSRQFGnawapqtitPLPTNipmpkSEKIQEIVQLVKSAKRPVLLI 294
Cdd:PRK12474 165 DV-----------AWNEAA-----------YAAQPLRGIG---------PAPVA-----AETVERIAALLRNGKKSALLL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 295 GSQATL-PPVKPADLVKAveALGCPVFLGGMA-RGLLGKDH------PLQMRQVRRdALKDADLTILAGTvcDFRLSYGR 366
Cdd:PRK12474 209 RGSALRgAPLEAAGRIQA--KTGVRLYCDTFApRIERGAGRvpieriPYFHEQITA-FLKDVEQLVLVGA--KPPVSFFA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 367 TLSKKSKIVALNRNSSQLTKNEKafwnsdvsvqaDVATSLVQVANALGAnhtttPTEWVkslrekddekesANAKKMEQK 446
Cdd:PRK12474 284 YPGKPSWGAPPGCEIVYLAQPDE-----------DLAQALQDLADAVDA-----PAEPA------------ARTPLALPA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 447 LTNGFLNPLNFLRTLDQSLPDDAIlVADGGDFVGSAAYIVRPRGPLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIW 526
Cdd:PRK12474 336 LPKGALNSLGVAQLIAHRTPDQAI-YADEALTSGLFFDMSYDRARPHTHLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQ 414
|
490 500
....*....|....*....|....*.
gi 17542570 527 GDGSCGYSLMEYDTFARHKLPVIGIV 552
Cdd:PRK12474 415 GDGGAAYTMQALWTMARENLDVTVVI 440
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
59-616 |
2.96e-12 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 69.55 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 59 GELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKI--VDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITA 136
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGRADDKPefVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 137 VKNAQMAESPLLLIGGAaptllKGRGAL-----QDIDQMVLFR----PLCKYVARVERLRDIVPtvrEAIKAAKSGcPGP 207
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQ-----QARAALgghyqQEVDLQSLFKdvagAFVQMVTVPEQLRHLVD---RAVRTALAE-RTV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 208 VFVEFPVDV-LYPYELVVKEIGFNPNAKGfiqralnfylrchvsrqfgnaWAPQTITPLPtnipmpksEKIQEIVQLVKS 286
Cdd:PRK08273 157 TAVILPNDVqELEYEPPPHAHGTVHSGVG---------------------YTRPRVVPYD--------EDLRRAAEVLNA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 287 AKRPVLLIGSQAtlppVKPADLVKAV-EALGCpvflgGMARGLLGKDhplqmrqvrrdALKDaDLTILAGTV-------- 357
Cdd:PRK08273 208 GRKVAILVGAGA----LGATDEVIAVaERLGA-----GVAKALLGKA-----------ALPD-DLPWVTGSIgllgtkps 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 358 ------CDFRL------SYGRTLSK--KSKIVALNRNSSQLTKNekafWNSDVSVQADVATSLVQVANALGANHTT---- 419
Cdd:PRK08273 267 yelmreCDTLLmvgssfPYSEFLPKegQARGVQIDIDGRMLGLR----YPMEVNLVGDAAETLRALLPLLERKKDRswre 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 420 TPTEWVKSLREKDDEKESANAKKmeqkltngfLNPLNFLRTLDQSLPDDAILVADggdfVGSAAY-----IVRPRGPLQW 494
Cdd:PRK08273 343 RIEKWVARWWETLEARAMVPADP---------VNPQRVFWELSPRLPDNAILTAD----SGSCANwyardLRMRRGMMAS 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 495 LDpGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSLM-EYDTFARH-------KLPVIGIVGND---ACWTQIAR 563
Cdd:PRK08273 410 LS-GTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNGMaELITVAKYwrqwsdpRLIVLVLNNRDlnqVTWEQRVM 488
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 17542570 564 EQVPMFQSSvaVDLARTRYDNVAKSLGSWGETIDesNADSARKILDEALAVCR 616
Cdd:PRK08273 489 EGDPKFEAS--QDLPDVPYARFAELLGLKGIRVD--DPEQLGAAWDEALAADR 537
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
108-552 |
3.46e-12 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 69.10 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 108 AADAVARLRqsiGVAAVT---AGPGLTNTITAVKNAQMAESPLLLIGGAAPTLLKGRGA-LQ-DIDQmvLFRPLCKYVAR 182
Cdd:PRK07586 54 AADGYARMA---GKPAATllhLGPGLANGLANLHNARRARTPIVNIVGDHATYHRKYDApLTsDIEA--LARPVSGWVRR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 183 VERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDVlypyelvvkeigfnpnakgfiqralnfylrchvsrqfgnAWAPQTI 262
Cdd:PRK07586 129 SESAADVAADAAAAVAAARGAPGQVATLILPADV---------------------------------------AWSEGGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 263 TPLPTNIPMPKS---EKIQEIVQLVKSAKRPVLLIGSQATLPP-VKPADLVKAveALGC----PVFLGGMARGllgKDHP 334
Cdd:PRK07586 170 PAPPPPAPAPAAvdpAAVEAAAAALRSGEPTVLLLGGRALRERgLAAAARIAA--ATGArllaETFPARMERG---AGRP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 335 LQMR-----QVRRDALKDADLTILAGT---VCDFrlSYgrtLSKKSKIVALNRNSSQLTknekafwnsdvSVQADVATSL 406
Cdd:PRK07586 245 AVERlpyfaEQALAQLAGVRHLVLVGAkapVAFF--AY---PGKPSRLVPEGCEVHTLA-----------GPGEDAAAAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 407 VQVANALGANHTTTPTewvkslrekddekesanAKKMEQKLTNGFLNPLNFLRTLDQSLPDDAILVADGGDF-VGSAAYI 485
Cdd:PRK07586 309 EALADALGAKPAAPPL-----------------AAPARPPLPTGALTPEAIAQVIAALLPENAIVVDESITSgRGFFPAT 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17542570 486 VRPRgPLQWLD-PGafGTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIV 552
Cdd:PRK07586 372 AGAA-PHDWLTlTG--GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVI 436
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
101-554 |
5.08e-10 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 62.28 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 101 HEVTAVFAADAVArlrQSIGVAAV-----TAGPG--LTNTITAVKNaqmaESPLLLIGGA-APTLLKGRGALQDIDQMVL 172
Cdd:PRK07092 56 QEAVVVGMADGYA---QATGNAAFvnlhsAAGVGnaMGNLFTAFKN----HTPLVITAGQqARSILPFEPFLAAVQAAEL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 173 FRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDvlypyelvvkeigfnpnakGFIQRALNFYLRcHVSRQ 252
Cdd:PRK07092 129 PKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYD-------------------DWDQPAEPLPAR-TVSSA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 253 FGnawapqtitplptnipmPKSEKIQEIVQLVKSAKRPVLLIGsqatlPPVKPA----DLVKAVEALGCPVFLGGMA-RG 327
Cdd:PRK07092 189 VR-----------------PDPAALARLGDALDAARRPALVVG-----PAVDRAgawdDAVRLAERHRAPVWVAPMSgRC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 328 LLGKDHPL------QMRQVRRDALKDADLTILAGTVCdFRL---SYGRTLSKKSKIValnrnssQLTKN-EKAFWnsdvs 397
Cdd:PRK07092 247 SFPEDHPLfagflpASREKISALLDGHDLVLVIGAPV-FTYhveGPGPHLPEGAELV-------QLTDDpGEAAW----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 398 vqADVATSLVqvanalgANHTTTPTEWVKSLREKDDEKESANAKKMEQKLTNGFLNPLNFLRTLDQSLPDDAILVADggd 477
Cdd:PRK07092 314 --APMGDAIV-------GDIRLALRDLLALLPPSARPAPPARPMPPPAPAPGEPLSVAFVLQTLAALRPADAIVVEE--- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 478 fVGSAayivrpRGPLQ----WLDPGAFGTLGVGG-GFAL----GAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPV 548
Cdd:PRK07092 382 -APST------RPAMQehlpMRRQGSFYTMASGGlGYGLpaavGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPV 454
|
....*.
gi 17542570 549 IGIVGN 554
Cdd:PRK07092 455 TFVILN 460
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
456-632 |
1.60e-09 |
|
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: 57.54 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 456 NFLRTLDQSLPDDAILVADGGDFVGSAAYIVRPRGpLQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSL 535
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKG-TRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 536 MEYDTFARHKLPVIGIVGNDACWTqIAREQVPMFQSSvaVDLARTRYDNVAKSLGswgetiDESNADSAR----KILDEA 611
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINNDGYT-IERAIHGPEASY--NDIANWNYTKLPEVFG------GGGGGLSFRvkteGELDEA 155
|
170 180
....*....|....*....|..
gi 17542570 612 LAVCRS-GEQSALVNVLIGKTD 632
Cdd:cd02005 156 LKDALFnRDKLSLIEVILPKDD 177
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
66-214 |
3.87e-09 |
|
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: 55.96 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 66 LKAHDVEEIFVLCGGHISPILVAAEK-LGIKIVDTRHEVTAVFAADAVARLRqSIGVAAVTAGPGLTNTITAVKNAqMAE 144
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEEnPGLRWVGNCNELNAGYAADGYARVK-GLGALVTTYGVGELSALNGIAGA-YAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 145 -SPLLLIGGAAPTLLKGRGAL-------QDID-QMVLFRPLCKYVARVERLRD----IVPTVREAIKAAKsgcpgPVFVE 211
Cdd:cd07038 85 hVPVVHIVGAPSTKAQASGLLlhhtlgdGDFDvFLKMFEEITCAAARLTDPENaaeeIDRVLRTALRESR-----PVYIE 159
|
...
gi 17542570 212 FPV 214
Cdd:cd07038 160 IPR 162
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
61-208 |
3.42e-06 |
|
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: 47.49 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 61 LVASVLKAHDVEEiFVLC-GGHISPILVAAEKLG----IKIVDTRhevTAVFAADAVARlrQSIGVAAV--TAGPGLTNT 133
Cdd:cd07037 2 ALVEELKRLGVRD-VVISpGSRSAPLALAAAEHPefrlHVRVDER---SAAFFALGLAK--ASGRPVAVvcTSGTAVANL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 134 ITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARV------ERLRDIVPTVREAIKAAKSGCPGP 207
Cdd:cd07037 76 LPAVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLpppeddDDLWYLLRLANRAVLEALSAPPGP 155
|
.
gi 17542570 208 V 208
Cdd:cd07037 156 V 156
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
484-593 |
2.27e-04 |
|
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: 42.65 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542570 484 YIVRPRgplQWLDPGAFGTLGVGGGFALGAKTVYPKRPVYIIWGDGSCGYSLMEYDTFARHKLPVIGIVGNDAcWTQIAR 563
Cdd:cd02006 43 HVYKPR---HWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNA-YLGLIR 118
|
90 100 110
....*....|....*....|....*....|.
gi 17542570 564 EQVPMFQSSVAVDLArtrYDNVAKS-LGSWG 593
Cdd:cd02006 119 QAQRAFDMDYQVNLA---FENINSSeLGGYG 146
|
|
| |
