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Conserved domains on  [gi|1622891768|ref|XP_028694323|]
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acetolactate synthase-like protein isoform X2 [Macaca mulatta]

Protein Classification

thiamine pyrophosphate-binding protein( domain architecture ID 11414520)

thiamine pyrophosphate-binding protein similar to Streptomyces clavuligerus N(2)-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway, and to Pseudomonas fluorescens benzaldehyde lyase, which catalyzes the enantioselective carboligation of two molecules of benzaldehyde to form (R)-benzoin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
2-517 5.31e-109

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: 335.21  E-value: 5.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:COG0028    61 ARATGKPGVCLVTSGPGATNLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEV 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDvlypyfmVQKEMVPAKPRKGLVGRVvswylenylanlfagawepQPEgplpldiPQA 161
Cdd:COG0028   141 LRRAFRIATSGRPGPVVLDIPKD-------VQAAEAEEEPAPPELRGY-------------------RPR-------PAP 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLtPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAAL 234
Cdd:COG0028   188 DPEAIEEAAELLAAAKRPVILAGGGARR-AGAAEELRALAERLGAPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEAL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSYG-RVLSHSSKIIIVNRNREDMllnsDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWA-PDWV 312
Cdd:COG0028   267 AEADLVLAVGARFDDRVTGNwDEFAPDAKIIHIDIDPAEI----GKNYPVDLPIVGDAKAVLAALLEALEPRADDrAAWL 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 313 EELREADRQKEQTFREKAAmpvaqHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVG 392
Cdd:COG0028   343 ARIAAWRAEYLAAYAADDG-----PIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYG 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNV-ACSLAYTEYHKA 471
Cdd:COG0028   418 LPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGRYsGTDLPNPDFAKL 497
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1622891768 472 AMGLGARGLLLsrENEDQVVKVLHDAQQQcrdGHPVVVNILIGRTD 517
Cdd:COG0028   498 AEAFGAKGERV--ETPEELEAALEEALAS---DGPALIDVRVDPEE 538
 
Name Accession Description Interval E-value
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
2-517 5.31e-109

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: 335.21  E-value: 5.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:COG0028    61 ARATGKPGVCLVTSGPGATNLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEV 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDvlypyfmVQKEMVPAKPRKGLVGRVvswylenylanlfagawepQPEgplpldiPQA 161
Cdd:COG0028   141 LRRAFRIATSGRPGPVVLDIPKD-------VQAAEAEEEPAPPELRGY-------------------RPR-------PAP 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLtPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAAL 234
Cdd:COG0028   188 DPEAIEEAAELLAAAKRPVILAGGGARR-AGAAEELRALAERLGAPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEAL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSYG-RVLSHSSKIIIVNRNREDMllnsDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWA-PDWV 312
Cdd:COG0028   267 AEADLVLAVGARFDDRVTGNwDEFAPDAKIIHIDIDPAEI----GKNYPVDLPIVGDAKAVLAALLEALEPRADDrAAWL 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 313 EELREADRQKEQTFREKAAmpvaqHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVG 392
Cdd:COG0028   343 ARIAAWRAEYLAAYAADDG-----PIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYG 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNV-ACSLAYTEYHKA 471
Cdd:COG0028   418 LPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGRYsGTDLPNPDFAKL 497
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1622891768 472 AMGLGARGLLLsrENEDQVVKVLHDAQQQcrdGHPVVVNILIGRTD 517
Cdd:COG0028   498 AEAFGAKGERV--ETPEELEAALEEALAS---DGPALIDVRVDPEE 538
PRK05858 PRK05858
acetolactate synthase;
2-512 1.31e-93

acetolactate synthase;


Pssm-ID: 235629 [Multi-domain]  Cd Length: 542  Bit Score: 295.48  E-value: 1.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK05858   62 AKLTRVPGVAVLTAGPGVTNGMSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLYpyfmvqkEMVPAKPRkglvgrvvswylenylanlfagawePQPEGPLPLDiPQA 161
Cdd:PRK05858  142 VDQALQAAVTPHRGPVFVDFPMDHAF-------SMADDDGR-------------------------PGALTELPAG-PTP 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENRSAALKKADVIV 241
Cdd:PRK05858  189 DPDALARAAGLLAEAQRPVIMAGTDVWWG-HAEAALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVL 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 242 LAGTVCDFRLSYGRVLSHSSKIIIVnrnreDMLLNSDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREAD-- 319
Cdd:PRK05858  268 VVGVPMDFRLGFGVFGGTAQLVHVD-----DAPPQRAHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAEta 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 320 -RQKEQTFREKAAMPvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALG 398
Cdd:PRK05858  343 aRARDAAELADDRDP----IHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALA 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 399 AKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWtqiSREQVPS---LGSNVACSLA-YTEYHKAAMG 474
Cdd:PRK05858  419 ARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRA 495
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1622891768 475 LGARGLLLSRENEdqvvkvLHDAQQQCRD-GHPVVVNIL 512
Cdd:PRK05858  496 LGGHGELVTVPAE------LGPALERAFAsGVPYLVNVL 528
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
340-513 3.71e-70

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: 222.02  E-value: 3.71e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 340 PVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGY 419
Cdd:cd02004     1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 420 SLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPS--LGSNVACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDA 497
Cdd:cd02004    81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSygLGLPVTTLLPDTRYDLVAEAFGGKGELV--TTPEELKPALKRA 158
                         170
                  ....*....|....*.
gi 1622891768 498 QQQcrdGHPVVVNILI 513
Cdd:cd02004   159 LAS---GKPALINVII 171
TPP_enzyme_N pfam02776
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
2-106 8.72e-32

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;


Pssm-ID: 460690 [Multi-domain]  Cd Length: 169  Bit Score: 120.03  E-value: 8.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQA-IDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:pfam02776  57 ARATGKPGVVLVTSGPGATNALTGLANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPE 136
                          90       100
                  ....*....|....*....|....*.
gi 1622891768  81 TLRAAMAAAQSGTPGPVFVELPIDVL 106
Cdd:pfam02776 137 VLRRAFRAALSGRPGPVYLEIPLDVL 162
 
Name Accession Description Interval E-value
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
2-517 5.31e-109

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: 335.21  E-value: 5.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:COG0028    61 ARATGKPGVCLVTSGPGATNLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEV 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDvlypyfmVQKEMVPAKPRKGLVGRVvswylenylanlfagawepQPEgplpldiPQA 161
Cdd:COG0028   141 LRRAFRIATSGRPGPVVLDIPKD-------VQAAEAEEEPAPPELRGY-------------------RPR-------PAP 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLtPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAAL 234
Cdd:COG0028   188 DPEAIEEAAELLAAAKRPVILAGGGARR-AGAAEELRALAERLGAPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEAL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSYG-RVLSHSSKIIIVNRNREDMllnsDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWA-PDWV 312
Cdd:COG0028   267 AEADLVLAVGARFDDRVTGNwDEFAPDAKIIHIDIDPAEI----GKNYPVDLPIVGDAKAVLAALLEALEPRADDrAAWL 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 313 EELREADRQKEQTFREKAAmpvaqHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVG 392
Cdd:COG0028   343 ARIAAWRAEYLAAYAADDG-----PIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYG 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNV-ACSLAYTEYHKA 471
Cdd:COG0028   418 LPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGRYsGTDLPNPDFAKL 497
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 1622891768 472 AMGLGARGLLLsrENEDQVVKVLHDAQQQcrdGHPVVVNILIGRTD 517
Cdd:COG0028   498 AEAFGAKGERV--ETPEELEAALEEALAS---DGPALIDVRVDPEE 538
PRK05858 PRK05858
acetolactate synthase;
2-512 1.31e-93

acetolactate synthase;


Pssm-ID: 235629 [Multi-domain]  Cd Length: 542  Bit Score: 295.48  E-value: 1.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK05858   62 AKLTRVPGVAVLTAGPGVTNGMSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLYpyfmvqkEMVPAKPRkglvgrvvswylenylanlfagawePQPEGPLPLDiPQA 161
Cdd:PRK05858  142 VDQALQAAVTPHRGPVFVDFPMDHAF-------SMADDDGR-------------------------PGALTELPAG-PTP 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENRSAALKKADVIV 241
Cdd:PRK05858  189 DPDALARAAGLLAEAQRPVIMAGTDVWWG-HAEAALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVL 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 242 LAGTVCDFRLSYGRVLSHSSKIIIVnrnreDMLLNSDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREAD-- 319
Cdd:PRK05858  268 VVGVPMDFRLGFGVFGGTAQLVHVD-----DAPPQRAHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAEta 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 320 -RQKEQTFREKAAMPvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALG 398
Cdd:PRK05858  343 aRARDAAELADDRDP----IHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALA 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 399 AKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWtqiSREQVPS---LGSNVACSLA-YTEYHKAAMG 474
Cdd:PRK05858  419 ARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRA 495
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1622891768 475 LGARGLLLSRENEdqvvkvLHDAQQQCRD-GHPVVVNIL 512
Cdd:PRK05858  496 LGGHGELVTVPAE------LGPALERAFAsGVPYLVNVL 528
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
340-513 3.71e-70

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: 222.02  E-value: 3.71e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 340 PVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGY 419
Cdd:cd02004     1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 420 SLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPS--LGSNVACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDA 497
Cdd:cd02004    81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSygLGLPVTTLLPDTRYDLVAEAFGGKGELV--TTPEELKPALKRA 158
                         170
                  ....*....|....*.
gi 1622891768 498 QQQcrdGHPVVVNILI 513
Cdd:cd02004   159 LAS---GKPALINVII 171
PRK09259 PRK09259
putative oxalyl-CoA decarboxylase; Validated
4-513 1.24e-48

putative oxalyl-CoA decarboxylase; Validated


Pssm-ID: 236433 [Multi-domain]  Cd Length: 569  Bit Score: 176.71  E-value: 1.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   4 LSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTL---LQnRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK09259   69 LTQKPGVCLTVSAPGFLNGLTALANATTNCFPMIMISGSSEREivdLQ-QGDYEELDQLNAAKPFCKAAFRVNRAEDIGI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  81 TLRAAMAAAQSGTPGPVFVELPIDVLypyfmvQKEMVPAKPRKGLVgRVVSwylenylanlfagawepqpegPLPLDIPq 160
Cdd:PRK09259  148 GVARAIRTAVSGRPGGVYLDLPAKVL------AQTMDADEALTSLV-KVVD---------------------PAPAQLP- 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 aSPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENRSAALKKADVI 240
Cdd:PRK09259  199 -APEAVDRALDLLKKAKRPLIILGKGAAYA-QADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVV 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 241 VLAGTVCDFRLSYGR--VLSHSSKIIIVNRNREDMllNSDVfwkPQEA-VQGDVGSFVLKLVEGLQGQTWAP--DWVEEL 315
Cdd:PRK09259  277 LLVGARLNWLLSHGKgkTWGADKKFIQIDIEPQEI--DSNR---PIAApVVGDIGSVMQALLAGLKQNTFKApaEWLDAL 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 316 READRQKEQTFREK--AAMPVAQHLNPVRVLQLVEETLPDnSILVVDGGDFVGTAAHLV---QPRGPlcwLDPGAFGTLG 390
Cdd:PRK09259  352 AERKEKNAAKMAEKlsTDTQPMNFYNALGAIRDVLKENPD-IYLVNEGANTLDLARNIIdmyKPRHR---LDCGTWGVMG 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 391 VGAGFALGAKLC--RPdaeVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGwtqISR--EQVPSLGSNVACS--LA 464
Cdd:PRK09259  428 IGMGYAIAAAVEtgKP---VVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGG---IYRgdDVNLSGAGDPSPTvlVH 501
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1622891768 465 YTEYHKAAMGLGARGLLLSreNEDQVVKVLHDAQQQcrdGHPVVVNILI 513
Cdd:PRK09259  502 HARYDKMMEAFGGVGYNVT--TPDELRHALTEAIAS---GKPTLINVVI 545
PRK07524 PRK07524
5-guanidino-2-oxopentanoate decarboxylase;
2-449 1.77e-45

5-guanidino-2-oxopentanoate decarboxylase;


Pssm-ID: 236041 [Multi-domain]  Cd Length: 535  Bit Score: 167.46  E-value: 1.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGG--AASTLLQNRGALQAI-DQLSLFRPLCKFCASVRRVRDI 78
Cdd:PRK07524   59 ARVSGKPGVCFIITGPGMTNIATAMGQAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  79 VPTLRAAMAAAQSGTPGPVFVELPIDVLypyfmvqkemvpAKPrkglvgrvvswylenylanlFAGAWEPQPEGPLPldi 158
Cdd:PRK07524  139 PEVLARAFAVFDSARPRPVHIEIPLDVL------------AAP--------------------ADHLLPAPPTRPAR--- 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALltpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENRS-----AA 233
Cdd:PRK07524  184 PGPAPAALAQAAERLAAARRPLILAGGGAL---AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSlpavrAL 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTV---CDFRLSY-GRVLSHSSKIII------VNRNREdmllnsdvfwkPQEAVQGDVGSFVLKLVEGLQ 303
Cdd:PRK07524  261 IAEADVVLAVGTElgeTDYDVYFdGGFPLPGELIRIdidpdqLARNYP-----------PALALVGDARAALEALLARLP 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 304 GQTWAPDWVEELREADRQKEqtfREKAAMPVAQHlnpVRVLQLVEETLPDNsILVVDGGDFVGTAAHLVQPRGPLCWLD- 382
Cdd:PRK07524  330 GQAAAADWGAARVAALRQAL---RAEWDPLTAAQ---VALLDTILAALPDA-IFVGDSTQPVYAGNLYFDADAPRRWFNa 402
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891768 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISR 449
Cdd:PRK07524  403 STGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRR 469
PRK07525 PRK07525
sulfoacetaldehyde acetyltransferase; Validated
2-515 1.11e-42

sulfoacetaldehyde acetyltransferase; Validated


Pssm-ID: 236042 [Multi-domain]  Cd Length: 588  Bit Score: 160.55  E-value: 1.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK07525   63 TRVTGRMGMVIGQNGPGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEV 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTpGPVFVELPIDvlYPYFMVQKEMvpakprkglvgrvvswylenylanlfagawePQPegpLPLDIPQA 161
Cdd:PRK07525  143 LNRVFDKAKRES-GPAQINIPRD--YFYGVIDVEI-------------------------------PQP---VRLERGAG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVP---------CFLGG--MARGLLGRNHSlhirenr 230
Cdd:PRK07525  186 GEQSLAEAAELLSEAKFPVILSGAGVVLS-DAIEECKALAERLDAPvacgylhndAFPGShpLWVGPLGYNGS------- 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 231 SAALK---KADVIVLAGTvcdfRLSYGRVLSH--------SSKIIIVNRNREDMLLNsdvfwKPQE-AVQGDVGSFVLKL 298
Cdd:PRK07525  258 KAAMEliaKADVVLALGT----RLNPFGTLPQygidywpkDAKIIQVDINPDRIGLT-----KKVSvGICGDAKAVAREL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 299 VEGLQGQTWAP---------------DWVEELREADRQKEQ---TFREKAAMPVAQHLNPVRVLQLVEETLPDNSILVVD 360
Cdd:PRK07525  329 LARLAERLAGDagreerkaliaaeksAWEQELSSWDHEDDDpgtDWNEEARARKPDYMHPRQALREIQKALPEDAIVSTD 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 361 GGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGN 440
Cdd:PRK07525  409 IGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFR 488
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891768 441 DAGWTQISREQVPSLGSN-VACSL-AYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQQCRDGHPVVVNILIGR 515
Cdd:PRK07525  489 NYQWGAEKKNQVDFYNNRfVGTELdNNVSYAGIAEAMGAEGVVV--DTQEELGPALKRAIDAQNEGKTTVIEIMCNQ 563
PRK06276 PRK06276
acetolactate synthase large subunit;
2-513 3.33e-42

acetolactate synthase large subunit;


Pssm-ID: 235766 [Multi-domain]  Cd Length: 586  Bit Score: 159.15  E-value: 3.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06276   58 ARASGKVGVCVATSGPGATNLVTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEI 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLYPYFMVQKEMVPAKPRkglvgrvvswyLENYLANLFagawepqpegplpldipqA 161
Cdd:PRK06276  138 FRAAFEIAKTGRPGPVHIDLPKDVQEGELDLEKYPIPAKID-----------LPGYKPTTF------------------G 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADkLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAAL 234
Cdd:PRK06276  189 HPLQIKKAAELIAEAERPVILAGGGVIISGASEE-LIELSELVKIPVCTTLMGKGAFPEDHPLalgmvgmHGTKAANYSV 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGtvCDF--RLSyGRVLSHS--SKIIIVNRNREDMLLNSDVfwkpQEAVQGDVGSFVLKLVEGLQGQTWAPD 310
Cdd:PRK06276  268 TESDVLIAIG--CRFsdRTT-GDISSFApnAKIIHIDIDPAEIGKNVRV----DVPIVGDAKNVLRDLLAELMKKEIKNK 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 311 --WVEELREadrqkeqtfREKAAMPVA----QHLNPVRVLQLVEETLPD-----NSILVVDGGDFVGTAAHLVQPRGPLC 379
Cdd:PRK06276  341 seWLERVKK---------LKKESIPRMdfddKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQMWMAHFFKTSAPRS 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 380 WLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALV------GNDAGWTQI---SRE 450
Cdd:PRK06276  412 FISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIfdnrtlGMVYQWQNLyygKRQ 491
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622891768 451 QVPSLGSNvacslayTEYHKAAMGLGARGLLLsrENEDQVVKVLHDAqqqCRDGHPVVVNILI 513
Cdd:PRK06276  492 SEVHLGET-------PDFVKLAESYGVKADRV--EKPDEIKEALKEA---IKSGEPYLLDIII 542
PRK08527 PRK08527
acetolactate synthase large subunit;
2-441 5.18e-42

acetolactate synthase large subunit;


Pssm-ID: 181458 [Multi-domain]  Cd Length: 563  Bit Score: 158.34  E-value: 5.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK08527   61 ARASGKVGVAIVTSGPGFTNAVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDV-------LYPyfmVQKEMVPAKPrkglvgrvvswyleNYLANlfagawepqpegpl 154
Cdd:PRK08527  141 LKEAFYIARSGRPGPVHIDIPKDVtatlgefEYP---KEISLKTYKP--------------TYKGN-------------- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 155 pldipqasPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIR 227
Cdd:PRK08527  190 --------SRQIKKAAEAIKEAKKPLFYLGGGAILS-NASEEIRELVKKTGIPAVETLMARGVLRSDDPLllgmlgmHGS 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 228 ENRSAALKKADVIVLAGTVCDFRLSyGRV--LSHSSKIIIVNRNREDM--LLNSDVfwkpqeAVQGDVGSFVLKLVEGLQ 303
Cdd:PRK08527  261 YAANMAMSECDLLISLGARFDDRVT-GKLseFAKHAKIIHVDIDPSSIskIVNADY------PIVGDLKNVLKEMLEELK 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 304 G---QTWAPdWVEELREADRQKEQTFREKAAMpvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCW 380
Cdd:PRK08527  334 EenpTTYKE-WREILKRYNELHPLSYEDSDEV-----LKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPRQL 407
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622891768 381 LDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK08527  408 ATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNN 468
PRK08322 PRK08322
acetolactate synthase large subunit;
1-446 4.04e-41

acetolactate synthase large subunit;


Pssm-ID: 236239 [Multi-domain]  Cd Length: 547  Bit Score: 155.37  E-value: 4.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   1 MA----RLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVr 76
Cdd:PRK08322   53 MAatygRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSP- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  77 DIVPTL-RAAMAAAQSGTPGPVFVELPIDVlypyfmvqkemvpakprkglvgrvvswylenylanlfagAWEPQPEGPLP 155
Cdd:PRK08322  132 DNIPEVvREAFRLAEEERPGAVHLELPEDI---------------------------------------AAEETDGKPLP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 156 LD---IPQASPQQVQRCVEILSRAKRPLMVLGSQAlLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHS-------LH 225
Cdd:PRK08322  173 RSysrRPYASPKAIERAAEAIQAAKNPLILIGAGA-NRKTASKALTEFVDKTGIPFFTTQMGKGVIPETHPlslgtagLS 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 226 IRENRSAALKKADVIVLAG-TVCDFrlSYGRVLSHSSKIII-VNRNREDMllnsDVFWKPQEAVQGDVGSFVLKLVEGL- 302
Cdd:PRK08322  252 QGDYVHCAIEHADLIINVGhDVIEK--PPFFMNPNGDKKVIhINFLPAEV----DPVYFPQVEVVGDIANSLWQLKERLa 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 303 QGQTWAPDWVEELREADRQKEQTFREKAAMPVAqhlnPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPL-CWL 381
Cdd:PRK08322  326 DQPHWDFPRFLKIREAIEAHLEEGADDDRFPMK----PQRIVADLRKVMPDDDIVILDNGAYKIWFARNYRAYEPNtCLL 401
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 382 DpGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAG-----WTQ 446
Cdd:PRK08322  402 D-NALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAygmirWKQ 470
PRK08266 PRK08266
hypothetical protein; Provisional
2-479 4.66e-39

hypothetical protein; Provisional


Pssm-ID: 181337 [Multi-domain]  Cd Length: 542  Bit Score: 149.39  E-value: 4.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGG--AASTLLQNRGALQAI-DQLSLFRPLCKFCASVRRVRDI 78
Cdd:PRK08266   63 ARSTGRPGVCSVVPGPGVLNAGAALLTAYGCNSPVLCLTGqiPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  79 VPTLRAAMAAAQSGTPGPVFVELPIDVLypyfmvqkemvpakprkGLVGRVvswylenylanlfagawEPQPEGPlPLDI 158
Cdd:PRK08266  143 PALVAEAFQQMLSGRPRPVALEMPWDVF-----------------GQRAPV-----------------AAAPPLR-PAPP 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALltpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIreNRSAA---LK 235
Cdd:PRK08266  188 PAPDPDAIAAAAALIAAAKNPMIFVGGGAA---GAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLGL--NFAAAyelWP 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 236 KADVIVLAGTVCDFRLSYGRVLSHSSKIIIVNRNREDMllnsdVFWKPQEAVQGDVGSFVLKLVEGLQGQ-TWAPDWVEE 314
Cdd:PRK08266  263 QTDVVIGIGSRLELPTFRWPWRPDGLKVIRIDIDPTEM-----RRLKPDVAIVADAKAGTAALLDALSKAgSKRPSRRAE 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 315 LREADRQKEQTFreKAAMPVAQHLNPVRvlqlveETLPDNSIlVVDGGDFVGTAAHLVQP-RGPLCWLDPGAFGTLGVGA 393
Cdd:PRK08266  338 LRELKAAARQRI--QAVQPQASYLRAIR------EALPDDGI-FVDELSQVGFASWFAFPvYAPRTFVTCGYQGTLGYGF 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 394 GFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSL-GSNVACSLAYTEYHKAA 472
Cdd:PRK08266  409 PTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFgGRVVASDLVNPDFVKLA 488

                  ....*..
gi 1622891768 473 MGLGARG 479
Cdd:PRK08266  489 ESFGVAA 495
PRK06725 PRK06725
acetolactate synthase large subunit;
2-441 2.16e-38

acetolactate synthase large subunit;


Pssm-ID: 180672 [Multi-domain]  Cd Length: 570  Bit Score: 148.19  E-value: 2.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06725   72 ARASGKVGVVFATSGPGATNLVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRI 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDvlypyfmVQKEmvpakprkglvgRVVSWYLEnylaNLFAGAWEPQpegplpldiPQA 161
Cdd:PRK06725  152 VQEAFYIAESGRPGPVLIDIPKD-------VQNE------------KVTSFYNE----VVEIPGYKPE---------PRP 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAAL 234
Cdd:PRK06725  200 DSMKLREVAKAISKAKRPLLYIGG-GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLflgmlgmHGTYAANMAV 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSyGRV--LSHSSKIIIVNRNREDMLLNSDVfwkpQEAVQGDVGSfVLKLVEGLQGQTWAPDWV 312
Cdd:PRK06725  279 TECDLLLALGVRFDDRVT-GKLelFSPHSKKVHIDIDPSEFHKNVAV----EYPVVGDVKK-ALHMLLHMSIHTQTDEWL 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 313 EELREADRQKEQTFREKAAMpvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVG 392
Cdd:PRK06725  353 QKVKTWKEEYPLSYKQKESE-----LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFG 427
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1622891768 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK06725  428 FPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINN 476
PRK06048 PRK06048
acetolactate synthase large subunit;
2-515 5.42e-38

acetolactate synthase large subunit;


Pssm-ID: 180368 [Multi-domain]  Cd Length: 561  Bit Score: 146.84  E-value: 5.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06048   65 ARATGKVGVCVATSGPGATNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVlypyfmVQKEMVPAKPRKglvgrvVSwyLENYlanlfagawEPQPEGplpldipqa 161
Cdd:PRK06048  145 IKEAFHIASTGRPGPVLIDLPKDV------TTAEIDFDYPDK------VE--LRGY---------KPTYKG--------- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADKLRAAvETLGVPCFLGGMARGLLGRNHSLHI-------RENRSAAL 234
Cdd:PRK06048  193 NPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELA-ETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAI 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSyGRVLSHSSKIIIVNRNREDMLLNSDVfwKPQEAVQGDVGSFVLKLVEGLQGQTWAPdWVEE 314
Cdd:PRK06048  272 QESDLIIAVGARFDDRVT-GKLASFAPNAKIIHIDIDPAEISKNV--KVDVPIVGDAKQVLKSLIKYVQYCDRKE-WLDK 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 315 LREADRQKEQTFREKAAMpvaqhLNPVRVLQLVEETLPDnSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAG 394
Cdd:PRK06048  348 INQWKKEYPLKYKEREDV-----IKPQYVIEQIYELCPD-AIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFP 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 395 FALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA------GWTQISREQVPSlgsnVACSLAYTEY 468
Cdd:PRK06048  422 AAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGylgmvrQWQELFYDKRYS----HTCIKGSVDF 497
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1622891768 469 HKAAMGLGARGLLLSRENEdqvvkvLHDAQQQCRD-GHPVVVNILIGR 515
Cdd:PRK06048  498 VKLAEAYGALGLRVEKPSE------VRPAIEEAVAsDRPVVIDFIVEC 539
PRK06154 PRK06154
thiamine pyrophosphate-requiring protein;
1-515 1.08e-36

thiamine pyrophosphate-requiring protein;


Pssm-ID: 235718 [Multi-domain]  Cd Length: 565  Bit Score: 143.03  E-value: 1.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   1 MARLSG--TVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAAstllqNRGaLQAID----QLSLFRPLCKFCASVRR 74
Cdd:PRK06154   73 YARATSgeRVGVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTGY-----PRG-STDVApnfeSLRNYRHITKWCEQVTL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  75 VRDIVPTLRAAMAAAQSGTPGPVFVELPIDVLYpyfmvqkEMVPAKPrkglvgrvvswylENYlanlfagawepqpeGPL 154
Cdd:PRK06154  147 PDEVPELMRRAFTRLRNGRPGPVVLELPVDVLA-------EELDELP-------------LDH--------------RPS 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 155 PLDIPQASPQQVQRCVEILSRAKRPLMVLGsQALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENRSAA- 233
Cdd:PRK06154  193 RRSRPGADPVEVVEAAALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMTTLNGKSAFPEDHPLALGSGGRARp 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 ------LKKADVIVLAGtvCDF-RLSYGRVLSHSSKIIIVNRNREDmlLNSDVFWKpqEAVQGDVGSFVLKLVEGLQG-- 304
Cdd:PRK06154  272 atvahfLREADVLFGIG--CSLtRSYYGLPMPEGKTIIHSTLDDAD--LNKDYPID--HGLVGDAALVLKQMIEELRRrv 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 305 ------------------QTWAPDWVEELREADRQkeqtfrekaampvaqhLNPVRVLQLVEETL-PDNSILVVDGGDFV 365
Cdd:PRK06154  346 gpdrgraqqvaaeieavrAAWLAKWMPKLTSDSTP----------------INPYRVVWELQHAVdIKTVIITHDAGSPR 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 366 GTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDaGWT 445
Cdd:PRK06154  410 DQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNN-FSM 488
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 446 QISREQVPSLGSNVACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQQCRDGHPVVVNILIGR 515
Cdd:PRK06154  489 GGYDKVMPVSTTKYRATDISGDYAAIARALGGYGERV--EDPEMLVPALLRALRKVKEGTPALLEVITSE 556
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
2-444 3.65e-35

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 138.58  E-value: 3.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAAST--LLQNRGAL-QAIDQLSLFRPLCKFCASVRRVRDI 78
Cdd:PRK07064   61 ARVSGGLGVALTSTGTGAGNAAGALVEALTAGTPLLHITGQIETpyLDQDLGYIhEAPDQLTMLRAVSKAAFRVRSAETA 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  79 VPTLRAAMAAAQSGTPGPVFVELPIDVLYpyfmvqkemvpakprkglvgRVVSWylenylanlfagawePQPEGPLPLDI 158
Cdd:PRK07064  141 LATIREAVRVALTAPTGPVSVEIPIDIQA--------------------AEIEL---------------PDDLAPVHVAV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALltpKSADKLRAAVEtLGVPCFLGGMARGLLGRNHSLHIRE-NRSAA---- 233
Cdd:PRK07064  186 PEPDAAAVAELAERLAAARRPLLWLGGGAR---HAGAEVKRLVD-LGFGVVTSTQGRGVVPEDHPASLGAfNNSAAveal 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTvcdfRLSYGRVLSHSSKI------IIVNRNREDMLLNSDVFwkpqeaVQGDVGSFVLKLVEGLQGQTW 307
Cdd:PRK07064  262 YKTCDLLLVVGS----RLRGNETLKYSLALprplirVDADAAADGRGYPNDLF------VHGDAARVLARLADRLEGRLS 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 308 A-PDWVEELREADRQKEQTFRekaampvaQHLNPVRVL-QLVEETLPDNSILVVDGGDFVGTAAH-LVQPRGPLCWLDPG 384
Cdd:PRK07064  332 VdPAFAADLRAAREAAVADLR--------KGLGPYAKLvDALRAALPRDGNWVRDVTISNSTWGNrLLPIFEPRANVHAL 403
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 385 AfGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGW 444
Cdd:PRK07064  404 G-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGY 462
PRK06965 PRK06965
acetolactate synthase 3 catalytic subunit; Validated
2-434 3.68e-35

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 180780 [Multi-domain]  Cd Length: 587  Bit Score: 139.17  E-value: 3.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06965   79 ARATGKVGVALVTSGPGVTNAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAET 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLY---PYFMVQK-EMVPAKP-RKGLVGrvvswylenylanlfagawepqpegplpl 156
Cdd:PRK06965  159 VKKAFYIARTGRPGPVVVDIPKDVSKtpcEYEYPKSvEMRSYNPvTKGHSG----------------------------- 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 157 dipqaspqQVQRCVEILSRAKRPLMVLGSQALLTPKSADkLRAAVETLGVPCF-----LGGMAR------GLLGrnhsLH 225
Cdd:PRK06965  210 --------QIRKAVSLLLSAKRPYIYTGGGVILANASRE-LRQLADLLGYPVTntlmgLGAYPAsdkkflGMLG----MH 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 226 IRENRSAALKKADVIVLAGTVCDFRL--SYGRVLSHSSKII--------IVNRNREDMllnsdvfwkpqeAVQGDVGSFV 295
Cdd:PRK06965  277 GTYEANMAMQHCDVLIAIGARFDDRVigNPAHFASRPRKIIhididpssISKRVKVDI------------PIVGDVKEVL 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 296 LKLVEGLQGQTWAPD------W---VEELREADRQKEQTFREKaampvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVG 366
Cdd:PRK06965  345 KELIEQLQTAEHGPDadalaqWwkqIEGWRSRDCLKYDRESEI--------IKPQYVVEKLWELTDGDAFVCSDVGQHQM 416
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622891768 367 TAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK06965  417 WAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPV 484
PRK08617 PRK08617
acetolactate synthase AlsS;
1-520 6.45e-35

acetolactate synthase AlsS;


Pssm-ID: 236312 [Multi-domain]  Cd Length: 552  Bit Score: 137.68  E-value: 6.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK08617   61 IGRLTGKPGVVLVTSGPGVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSE 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  81 TLRAAMAAAQSGTPGPVFVELPIDVLypyfmvqKEMVPAKPRKGLvgrvvswylenylanlfagawEPQPEGPlpldipq 160
Cdd:PRK08617  141 VLANAFRAAESGRPGAAFVSLPQDVV-------DAPVTSKAIAPL---------------------SKPKLGP------- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 ASPQQVQRCVEILSRAKRPLMVLGSQAlLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHslhirENRsaalkkadvi 240
Cdd:PRK08617  186 ASPEDINYLAELIKNAKLPVLLLGMRA-SSPEVTAAIRRLLERTNLPVVETFQAAGVISREL-----EDH---------- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 241 vLAGTVCDFRLSYG-RVLSHSSKIIIV------------NRNREDMLLNSDV-------FWKPQEAVQGDVGSFVLKLVE 300
Cdd:PRK08617  250 -FFGRVGLFRNQPGdELLKKADLVITIgydpieyeprnwNSEGDATIIHIDVlpaeidnYYQPERELIGDIAATLDLLAE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 301 GLQGQTWAPDWVEELreADRQKEQTFREKAAMPVAQHL-NPVRVLQLVEETLPDNSILVVDGGDF-VGTAAHL--VQPRG 376
Cdd:PRK08617  329 KLDGLSLSPQSLEIL--EELRAQLEELAERPARLEEGAvHPLRIIRALQDIVTDDTTVTVDVGSHyIWMARYFrsYEPRH 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 377 PLcwldpgaFG----TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQV 452
Cdd:PRK08617  407 LL-------FSngmqTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEE 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622891768 453 PSLGSNVACSLAYTEYHKAAMGLGARGllLSRENEDQVVKVLHDAQQQcrDGhPVVVNILIgrtDFRD 520
Cdd:PRK08617  480 MKYGRSSGVDFGPVDFVKYAESFGAKG--LRVTSPDELEPVLREALAT--DG-PVVIDIPV---DYSD 539
TPP_PYR_POX_like cd07035
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ...
2-103 6.70e-35

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: 128.42  E-value: 6.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:cd07035    54 ARATGKPGVVLVTSGPGLTNAVTGLANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEA 133
                          90       100
                  ....*....|....*....|..
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPI 103
Cdd:cd07035   134 LRRAFRIALSGRPGPVALDLPK 155
PRK08199 PRK08199
thiamine pyrophosphate protein; Validated
2-447 3.16e-33

thiamine pyrophosphate protein; Validated


Pssm-ID: 181285 [Multi-domain]  Cd Length: 557  Bit Score: 133.08  E-value: 3.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIvPT 81
Cdd:PRK08199   66 GKLTGRPGICFVTRGPGATNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARI-PE 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRA-AMAAAQSGTPGPVFVELPIDVLYpyfmvQKEMVPAKPRkglvGRVVswylenylanlfagawEPQPegplpldipq 160
Cdd:PRK08199  145 LVSrAFHVATSGRPGPVVLALPEDVLS-----ETAEVPDAPP----YRRV----------------AAAP---------- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 aSPQQVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVP----------------CFLG----GMARGLLGR 220
Cdd:PRK08199  190 -GAADLARLAELLARAERPLVILGG-SGWTEAAVADLRAFAERWGLPvacafrrqdlfdnrhpNYAGdlglGINPALAAR 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 221 nhslhIREnrsaalkkADVIVLAGTvcdfRLsyGRVLSHSSKIIIVNRNREDML--------LNSdVFwKPQEAVQGDVG 292
Cdd:PRK08199  268 -----IRE--------ADLVLAVGT----RL--GEVTTQGYTLLDIPVPRQTLVhvhpdaeeLGR-VY-RPDLAIVADPA 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 293 SFVLKL--VEGLQGQTWApDWVEELREADRQkeqtfrEKAAMPVAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAH 370
Cdd:PRK08199  327 AFAAALaaLEPPASPAWA-EWTAAAHADYLA------WSAPLPGPGAVQLGEVMAWLRERLPADAIITNGAGNYATWLHR 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891768 371 LVQPRGPLCWLDPGAfGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQI 447
Cdd:PRK08199  400 FFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTI 475
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
2-441 5.95e-33

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 132.58  E-value: 5.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFcasVRRVRD---I 78
Cdd:PRK06112   69 ARVSGKVAVVTAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKW---VRRVTVaerI 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  79 VPTLRAAMAAAQSGTPGPVFVELPIDVLypyfmVQKEMVPAKPRKglvgrvvswylenylANLfaGAWepqpegplPLDI 158
Cdd:PRK06112  146 DDYVDQAFTAATSGRPGPVVLLLPADLL-----TAAAAAPAAPRS---------------NSL--GHF--------PLDR 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------------- 224
Cdd:PRK06112  196 TVPAPQRLAEAASLLAQAQRPVVVAGGGVHIS-GASAALAALQSLAGLPVATTNMGKGAVDETHPLslgvvgslmgprsp 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 225 --HIREnrsaALKKADVIVLAGTvcdfRLSYG-----RVLSHSSKIII-------VNRNREDMLLNSDVfwkpQEAVQGd 290
Cdd:PRK06112  275 grHLRD----LVREADVVLLVGT----RTNQNgtdswSLYPEQAQYIHidvdgeeVGRNYEALRLVGDA----RLTLAA- 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 291 vgsfvLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKAAMPV---AQHLNPVRVLQLVEETLPDNSILVVDGG-DFVG 366
Cdd:PRK06112  342 -----LTDALRGRDLAARAGRRAALEPAIAAGREAHREDSAPVAlsdASPIRPERIMAELQAVLTGDTIVVADASySSIW 416
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622891768 367 TAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK06112  417 VANFLTARRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNN 491
PRK08155 PRK08155
acetolactate synthase large subunit;
1-442 3.34e-32

acetolactate synthase large subunit;


Pssm-ID: 181257 [Multi-domain]  Cd Length: 564  Bit Score: 130.21  E-value: 3.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK08155   70 MARTTGKPAVCMACSGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQ 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  81 TLRAAMAAAQSGTPGPVFVELPIDVlypyfmvqkemvpakprkglvgrvvswylenYLANLFAGAWePQPEGPLPldIPQ 160
Cdd:PRK08155  150 VISDAFRIAQSGRPGPVWIDIPKDV-------------------------------QTAVIELEAL-PAPAEKDA--APA 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 ASPQQVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAA 233
Cdd:PRK08155  196 FDEESIRDAAAMINAAKRPVLYLGG-GVINSGAPARARELAEKAQLPTTMTLMALGMLPKAHPLslgmlgmHGARSTNYI 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTVCDFRlSYGRVLSH--SSKIIIVNRNREDMllnsDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWApDW 311
Cdd:PRK08155  275 LQEADLLIVLGARFDDR-AIGKTEQFcpNAKIIHVDIDRAEL----GKIKQPHVAIQADVDDVLAQLLPLVEAQPRA-EW 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 312 VEelREADRQKEQTFrekaAMPVAQH-LNPVRVLQLVEETLPDNSILVVDGGD---FVGTAAHLVQPRGplcWLDPGAFG 387
Cdd:PRK08155  349 HQ--LVADLQREFPC----PIPKADDpLSHYGLINAVAACVDDNAIITTDVGQhqmWTAQAYPLNRPRQ---WLTSGGLG 419
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622891768 388 TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV-MALVGNDA 442
Cdd:PRK08155  420 TMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVkIILMNNEA 475
TPP_enzyme_N pfam02776
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
2-106 8.72e-32

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;


Pssm-ID: 460690 [Multi-domain]  Cd Length: 169  Bit Score: 120.03  E-value: 8.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQA-IDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:pfam02776  57 ARATGKPGVVLVTSGPGATNALTGLANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPE 136
                          90       100
                  ....*....|....*....|....*.
gi 1622891768  81 TLRAAMAAAQSGTPGPVFVELPIDVL 106
Cdd:pfam02776 137 VLRRAFRAALSGRPGPVYLEIPLDVL 162
PRK07418 PRK07418
acetolactate synthase large subunit;
2-515 1.21e-31

acetolactate synthase large subunit;


Pssm-ID: 236014 [Multi-domain]  Cd Length: 616  Bit Score: 129.01  E-value: 1.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK07418   80 ARATGKVGVCFGTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARI 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLYPYFmvqkEMVPAKPrkglvGRVVswyLENYlanlfagawEPQPEGplpldipqa 161
Cdd:PRK07418  160 VAEAFHIASSGRPGPVLIDIPKDVGQEEF----DYVPVEP-----GSVK---PPGY---------RPTVKG--------- 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQAlLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAAL 234
Cdd:PRK07418  210 NPRQINAALKLIEEAERPLLYVGGGA-ISAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLsvgmlgmHGTAYANFAV 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSyGRVLSHSS--KII---I----VNRNRedmllnsdvfwKPQEAVQGDVGSFVLKLVEGLQGQ 305
Cdd:PRK07418  289 TECDLLIAVGARFDDRVT-GKLDEFASraKVIhidIdpaeVGKNR-----------RPDVPIVGDVRKVLVKLLERSLEP 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 306 TWAP---DWVEELreadrqkeQTFREKAAMPVAQH---LNPVRVLQLVEETLPDnSILVVDGGDFVGTAAHLVQpRGPLC 379
Cdd:PRK07418  357 TTPPrtqAWLERI--------NRWKQDYPLVVPPYegeIYPQEVLLAVRDLAPD-AYYTTDVGQHQMWAAQFLR-NGPRR 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 380 WLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDaGWTQISREQVPSL---- 455
Cdd:PRK07418  427 WISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN-GWQGMVRQWQESFyger 505
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622891768 456 --GSNVACSLAytEYHKAAMGLGARGLLLSRENEdqvvkvLHDAQQQC--RDGhPVVVNILIGR 515
Cdd:PRK07418  506 ysASNMEPGMP--DFVKLAEAFGVKGMVISERDQ------LKDAIAEAlaHDG-PVLIDVHVRR 560
PRK07789 PRK07789
acetolactate synthase 1 catalytic subunit; Validated
2-440 1.48e-31

acetolactate synthase 1 catalytic subunit; Validated


Pssm-ID: 236098 [Multi-domain]  Cd Length: 612  Bit Score: 128.56  E-value: 1.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK07789   89 AQATGRVGVCMATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRV 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLypyfmvQKEMVpakprkglvgrvvswylenylanlFAgaWEPQPEGPLPLDIPQA 161
Cdd:PRK07789  169 IAEAFHIASTGRPGPVLVDIPKDAL------QAQTT------------------------FS--WPPRMDLPGYRPVTKP 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADkLRAAVETLGVPCFLGGMARGLLGRNHSLHI-------RENRSAAL 234
Cdd:PRK07789  217 HGKQIREAAKLIAAARRPVLYVGGGVIRAEASAE-LRELAELTGIPVVTTLMARGAFPDSHPQHLgmpgmhgTVAAVAAL 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSyGRVLSHS--SKIIIVN-------RNREdmllnSDVFwkpqeaVQGDVGSFVLKLVEGLQGQ 305
Cdd:PRK07789  296 QRSDLLIALGARFDDRVT-GKLDSFApdAKVIHADidpaeigKNRH-----ADVP------IVGDVKEVIAELIAALRAE 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 306 TWA---PD---WVEELREADRQKEQTFREkaamPVAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLC 379
Cdd:PRK07789  364 HAAggkPDltaWWAYLDGWRETYPLGYDE----PSDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRT 439
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622891768 380 WLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV-MALVGN 440
Cdd:PRK07789  440 WLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIkVALINN 501
PRK07282 PRK07282
acetolactate synthase large subunit;
2-441 5.11e-31

acetolactate synthase large subunit;


Pssm-ID: 180919 [Multi-domain]  Cd Length: 566  Bit Score: 126.86  E-value: 5.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK07282   68 AKSTGKLGVAVVTSGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVlypyfmvqkemvpakprkglVGRVVSWYLEnylanlfagawepqPEGPLPLDIPQA 161
Cdd:PRK07282  148 ITEAVHIATTGRPGPVVIDLPKDV--------------------SALETDFIYD--------------PEVNLPSYQPTL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQ--QVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSA 232
Cdd:PRK07282  194 EPNdmQIKKILKQLSKAKKPVILAGG-GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLflgmggmHGSYAANI 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 233 ALKKADVIVLAGTVCDFRLSyGRVLSHSSKIIIVNRNREDMLLNSDVfwKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWV 312
Cdd:PRK07282  273 AMTEADFMINIGSRFDDRLT-GNPKTFAKNAKVAHIDIDPAEIGKII--KTDIPVVGDAKKALQMLLAEPTVHNNTEKWI 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 313 EELREaDRQKEQTFREKAAMpvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVG 392
Cdd:PRK07282  350 EKVTK-DKNRVRSYDKKERV-----VQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFG 423
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1622891768 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK07282  424 IPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNN 472
PRK06456 PRK06456
acetolactate synthase large subunit;
2-438 7.54e-31

acetolactate synthase large subunit;


Pssm-ID: 180569 [Multi-domain]  Cd Length: 572  Bit Score: 126.11  E-value: 7.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06456   63 ARASGVPGVCTATSGPGTTNLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQW 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLYPyfMVQKEMVPAKPrkglvgrvvswYLENYlanlfagawepqpeGPLPLDIpqa 161
Cdd:PRK06456  143 IKNAFYIATTGRPGPVVIDIPRDIFYE--KMEEIKWPEKP-----------LVKGY--------------RDFPTRI--- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADKLRAAvETLGVPCFLGGMARGLLGRNHSLHI-------RENRSAAL 234
Cdd:PRK06456  193 DRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELA-ELLHIPIVSTFPGKTAIPHDHPLYFgpmgyygRAEASMAA 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRL--SYGRVLSHSSKIIIVNRNREDmllnSDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPD-- 310
Cdd:PRK06456  272 LESDAMLVVGARFSDRTftSYDEMVETRKKFIMVNIDPTD----GEKAIKVDVGIYGNAKIILRELIKAITELGQKRDrs 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 311 -WVEELREADRQKEQTFREKAAmpvaQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTL 389
Cdd:PRK06456  348 aWLKRVKEYKEYYSQFYYTEEN----GKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTM 423
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1622891768 390 GVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALV 438
Cdd:PRK06456  424 GFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVI 472
PRK06466 PRK06466
acetolactate synthase 3 large subunit;
2-442 1.32e-29

acetolactate synthase 3 large subunit;


Pssm-ID: 180578 [Multi-domain]  Cd Length: 574  Bit Score: 122.55  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06466   62 ARATGKTGVVLVTSGPGATNAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEI 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLYPyfmVQKemvpakprkglvgrvvswYLENYLANLFAGAWEPQPEGplpldipqa 161
Cdd:PRK06466  142 IKKAFYIAQSGRPGPVVVDIPKDMTNP---AEK------------------FEYEYPKKVKLRSYSPAVRG--------- 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLM------VLGSQALLTPKSADKLRAAVET--LGVPCFLGGMAR--GLLGrnhsLHIRENRS 231
Cdd:PRK06466  192 HSGQIRKAVEMLLAAKRPVIysgggvVLGNASALLTELAHLLNLPVTNtlMGLGGFPGTDRQflGMLG----MHGTYEAN 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 232 AALKKADVIVLAGTVCDFRLSYG-RVLSHSSKIIIVNRNREDM--LLNSDVfwkpqeAVQGDVGSFVLKLVEGLQGQTWA 308
Cdd:PRK06466  268 MAMHHADVILAVGARFDDRVTNGpAKFCPNAKIIHIDIDPASIskTIKADI------PIVGPVESVLTEMLAILKEIGEK 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 309 PD------WVEELREAdRQKEQTFREKAAMPVAqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLD 382
Cdd:PRK06466  342 PDkealaaWWKQIDEW-RGRHGLFPYDKGDGGI--IKPQQVVETLYEVTNGDAYVTSDVGQHQMFAAQYYKFNKPNRWIN 418
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA 442
Cdd:PRK06466  419 SGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNG 478
PRK07979 PRK07979
acetolactate synthase 3 large subunit;
1-437 5.29e-29

acetolactate synthase 3 large subunit;


Pssm-ID: 181185 [Multi-domain]  Cd Length: 574  Bit Score: 120.73  E-value: 5.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK07979   61 LARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQ 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  81 TLRAAMAAAQSGTPGPVFVELPIDVLYPyfmvQKEMVPAKPRKglvgrvVSwyLENYlanlfagawEPQPEGplpldipq 160
Cdd:PRK07979  141 VLKKAFWLAASGRPGPVVVDLPKDILNP----ANKLPYVWPES------VS--MRSY---------NPTTQG-------- 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 aSPQQVQRCVEILSRAKRPLMVLGSQAlLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHS-------LHIRENRSAA 233
Cdd:PRK07979  192 -HKGQIKRALQTLVAAKKPVVYVGGGA-INAACHQQLKELVEKLNLPVVSSLMGLGAFPATHRqslgmlgMHGTYEANMT 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTVCDFRLSYGRVLSHSSKIII---VNRNREDMLLNSDVfwkpqeAVQGDvGSFVLKLVEGLQGQTWAPD 310
Cdd:PRK07979  270 MHNADVIFAVGVRFDDRTTNNLAKYCPNATVLhidIDPTSISKTVTADI------PIVGD-ARQVLEQMLELLSQESAHQ 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 311 WVEELREADRQKEQtFREKAAM---PVAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFG 387
Cdd:PRK07979  343 PLDEIRDWWQQIEQ-WRARQCLkydTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLG 421
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622891768 388 TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMAL 437
Cdd:PRK07979  422 TMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVL 471
PRK08978 PRK08978
acetolactate synthase 2 catalytic subunit; Reviewed
1-434 8.71e-29

acetolactate synthase 2 catalytic subunit; Reviewed


Pssm-ID: 181601 [Multi-domain]  Cd Length: 548  Bit Score: 119.99  E-value: 8.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK08978   57 YARATGKVGVCIATSGPGATNLITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  81 TLRAAMAAAQSGTPGPVFVELPIDvlypyfmVQKEMVPAKPrkglvgrvvswylenylaNLFAgawepqpegplPLDIPQ 160
Cdd:PRK08978  137 IMAEAFEIASSGRPGPVLVDIPKD-------IQLAEGELEP------------------HLTT-----------VENEPA 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 ASPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVP--CFLGGMarGLLGRNHS-----LHIRENRSA- 232
Cdd:PRK08978  181 FPAAELEQARALLAQAKKPVLYVGGGVGMA-GAVPALREFLAATGMPavATLKGL--GAVEADHPyylgmLGMHGTKAAn 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 233 -ALKKADVIVLAGTVCDFRLSyGRVLSHSS--KIIIVNRNREDM--LLNSDVfwkpqeAVQGDVGSFVLKLVEGLQGQTW 307
Cdd:PRK08978  258 lAVQECDLLIAVGARFDDRVT-GKLNTFAPhaKVIHLDIDPAEInkLRQAHV------ALQGDLNALLPALQQPLNIDAW 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 308 ApDWVEELREadrqkEQTFREKAAmpvAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFG 387
Cdd:PRK08978  331 R-QHCAQLRA-----EHAWRYDHP---GEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLG 401
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1622891768 388 TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK08978  402 TMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPV 448
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
360-511 2.13e-28

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 110.37  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 360 DGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVG 439
Cdd:pfam02775   1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622891768 440 NDAGWTQISREQVPSLGSNVAC----SLAYTEYHKAAMGLGARGllLSRENEDQVVKVLHDAQQQcrdGHPVVVNI 511
Cdd:pfam02775  81 NNGGYGMTRGQQTPFGGGRYSGpsgkILPPVDFAKLAEAYGAKG--ARVESPEELEEALKEALEH---DGPALIDV 151
PRK06882 PRK06882
acetolactate synthase 3 large subunit;
2-441 2.45e-28

acetolactate synthase 3 large subunit;


Pssm-ID: 168717 [Multi-domain]  Cd Length: 574  Bit Score: 118.86  E-value: 2.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06882   62 ARSTGKVGCVLVTSGPGATNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPST 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLYPYFMVQKEMvpakPRKglvgrvVSwyLENYLANLfagawepqpegplpldipQA 161
Cdd:PRK06882  142 IKKAFYIASTGRPGPVVIDIPKDMVNPANKFTYEY----PEE------VS--LRSYNPTV------------------QG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVPCF-----LGGMAR------GLLGrnhsLHIRENR 230
Cdd:PRK06882  192 HKGQIKKALKALLVAKKPVLFVGG-GVITAECSEQLTQFAQKLNLPVTsslmgLGAYPStdkqflGMLG----MHGTYEA 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 231 SAALKKADVIVLAGTVCDFRLS--YGRVLSHsSKIIIVNRNREDMLLNSDVFWKPQEAVQGDVGSFVLKLVEG--LQGQT 306
Cdd:PRK06882  267 NNAMHESDLILGIGVRFDDRTTnnLAKYCPN-AKVIHIDIDPTSISKNVPAYIPIVGSAKNVLEEFLSLLEEEnlAKSQT 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 307 WAPDWVEELREADRQKEQTFREKAAMpvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAF 386
Cdd:PRK06882  346 DLTAWWQQINEWKAKKCLEFDRTSDV-----IKPQQVVEAIYRLTNGDAYVASDVGQHQMFAALHYPFDKPRRWINSGGA 420
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622891768 387 GTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK06882  421 GTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
PRK08979 PRK08979
acetolactate synthase 3 large subunit;
2-434 6.63e-28

acetolactate synthase 3 large subunit;


Pssm-ID: 181602 [Multi-domain]  Cd Length: 572  Bit Score: 117.61  E-value: 6.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK08979   62 ARATGKVGVVLVTSGPGATNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEI 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLYPYFMVQKEmvpakprkglvgrvvswylenYLANLFAGAWEPQPEGplpldipqa 161
Cdd:PRK08979  142 IKKAFYIASTGRPGPVVIDLPKDCLNPAILHPYE---------------------YPESIKMRSYNPTTSG--------- 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTpkSADK-LRAAVETLGVPCFLGGMARGLLGRNHS-------LHIRENRSAA 233
Cdd:PRK08979  192 HKGQIKRGLQALLAAKKPVLYVGGGAIIS--GADKqILQLAEKLNLPVVSTLMGLGAFPGTHKnslgmlgMHGRYEANMA 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTVCDFRLSyGRVLSHSSKIIIVNRNREDMLLNSDVfwKPQEAVQGDVGSFVLKLVEGLQGQTWAPD--- 310
Cdd:PRK08979  270 MHNADLIFGIGVRFDDRTT-NNLEKYCPNATILHIDIDPSSISKTV--RVDIPIVGSADKVLDSMLALLDESGETNDeaa 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 311 ---WVEELreadrqkeQTFREKAAMpvAQHLNPVRVL-QLVEETL----PDNSILVVDGGDFVGTAAHLVQPRGPLCWLD 382
Cdd:PRK08979  347 iasWWNEI--------EVWRSRNCL--AYDKSSERIKpQQVIETLykltNGDAYVASDVGQHQMFAALYYPFDKPRRWIN 416
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622891768 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK08979  417 SGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPV 468
PLN02470 PLN02470
acetolactate synthase
2-441 3.98e-27

acetolactate synthase


Pssm-ID: 215261 [Multi-domain]  Cd Length: 585  Bit Score: 115.22  E-value: 3.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PLN02470   71 AKASGKVGVCIATSGPGATNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRV 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVlypyfmvQKEM-VP--AKPRKglvgrvvswyLENYLANLfagawePQPegplpldi 158
Cdd:PLN02470  151 IREAFFLASSGRPGPVLVDIPKDI-------QQQLaVPnwNQPMK----------LPGYLSRL------PKP-------- 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASpqQVQRCVEILSRAKRPLMVLGSQALltpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRE-------NRS 231
Cdd:PLN02470  200 PEKS--QLEQIVRLISESKRPVVYVGGGCL---NSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMlgmhgtvYAN 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 232 AALKKADVIVLAGTVCDFRLSyGRVLSHSSKIIIVNRNREDMLLNSDVfwKPQEAVQGDVgSFVLKLVEGL--QGQTWAP 309
Cdd:PLN02470  275 YAVDSADLLLAFGVRFDDRVT-GKLEAFASRASIVHIDIDPAEIGKNK--QPHVSVCADV-KLALQGLNKLleERKAKRP 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 310 DWVEELREADRQKEQ---TFREKAAMPVAQHlnpvrVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAF 386
Cdd:PLN02470  351 DFSAWRAELDEQKEKfplSYPTFGDAIPPQY-----AIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGL 425
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622891768 387 GTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PLN02470  426 GAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
PRK08327 PRK08327
thiamine pyrophosphate-requiring protein;
2-444 6.52e-26

thiamine pyrophosphate-requiring protein;


Pssm-ID: 236243 [Multi-domain]  Cd Length: 569  Bit Score: 111.25  E-value: 6.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLlqNRGAL-----------QAIDQLSLFRPLCKFCA 70
Cdd:PRK08327   70 ALVTGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYT--EEGELgsrntrihwtqEMRDQGGLVREYVKWDY 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  71 SVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPIDVLypyfmVQKemvpakprkglVGRVvswylenylanlfagawEPQP 150
Cdd:PRK08327  148 EIRRGDQIGEVVARAIQIAMSEPKGPVYLTLPREVL-----AEE-----------VPEV-----------------KADA 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 151 EGPLPLDIPQASPQQVQRCVEILSRAKRPLmVLGSQALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENR 230
Cdd:PRK08327  195 GRQMAPAPPAPDPEDIARAAEMLAAAERPV-IITWRAGRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDP 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 231 SAALKKADVIVLAGTVCDFRLSYGRvLSHSSKIIIVNrnrEDMLLNSDVFWK-PQE-AVQGDVGSFVLKLVEGLQGQTWA 308
Cdd:PRK08327  274 RADLAEADLVLVVDSDVPWIPKKIR-PDADARVIQID---VDPLKSRIPLWGfPCDlCIQADTSTALDQLEERLKSLASA 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 309 PDWVEELREADRQKEQTFREKAAMPVAQHL------NPVRVLQLVEETLPDNSILVVDGGdFVGTAAHLvqpRGPLCWLD 382
Cdd:PRK08327  350 ERRRARRRRAAVRELRIRQEAAKRAEIERLkdrgpiTPAYLSYCLGEVADEYDAIVTEYP-FVPRQARL---NKPGSYFG 425
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622891768 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFV--RHKIPVMALVGNDAGW 444
Cdd:PRK08327  426 DGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
PRK09107 PRK09107
acetolactate synthase 3 catalytic subunit; Validated
2-434 7.43e-26

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 236380 [Multi-domain]  Cd Length: 595  Bit Score: 111.34  E-value: 7.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK09107   69 ARSTGKPGVVLVTSGPGATNAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARV 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDVLYpyfmVQKEMVPakPRKGLVGRvvswylenylanlfagAWEPQPEGplpldipqa 161
Cdd:PRK09107  149 IHEAFHVATSGRPGPVVVDIPKDVQF----ATGTYTP--PQKAPVHV----------------SYQPKVKG--------- 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLT-PKSADKLRAAVETLGVP--CFLGGMAR---------GLLGrnhsLHIREN 229
Cdd:PRK09107  198 DAEAITEAVELLANAKRPVIYSGGGVINSgPEASRLLRELVELTGFPitSTLMGLGAypasgknwlGMLG----MHGTYE 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 230 RSAALKKADVIVLAGTVCDFRLSyGRVLS---HSSKIII------VNRNredmlLNSDVfwkpqeAVQGDVGSFVLKLVE 300
Cdd:PRK09107  274 ANMAMHDCDVMLCVGARFDDRIT-GRLDAfspNSKKIHIdidpssINKN-----VRVDV------PIIGDVGHVLEDMLR 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 301 GLQGQTWAPD------WVEELREADRQKEQTFREKAAMPVAQHlnpvRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQP 374
Cdd:PRK09107  342 LWKARGKKPDkealadWWGQIARWRARNSLAYTPSDDVIMPQY----AIQRLYELTKGRDTYITTEVGQHQMWAAQFFGF 417
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 375 RGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK09107  418 EEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPV 477
TPP_Xsc_like cd02013
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ...
338-516 3.01e-24

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: 100.28  E-value: 3.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 338 LNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:cd02013     4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 418 GYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSN-VACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHD 496
Cdd:cd02013    84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITV--DKPEDVGPALQK 161
                         170       180
                  ....*....|....*....|
gi 1622891768 497 AQQQCRDGHPVVVNILIGRT 516
Cdd:cd02013   162 AIAMMAEGKTTVIEIVCDQE 181
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
342-513 1.09e-23

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: 97.71  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 342 RVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSL 421
Cdd:cd00568     1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 422 IEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACSLAYTEYHKA-AMGLGARGLLLsrENEDQVVKVLHDAQQq 500
Cdd:cd00568    81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAAlAEAYGAKGVRV--EDPEDLEAALAEALA- 157
                         170
                  ....*....|...
gi 1622891768 501 cRDGhPVVVNILI 513
Cdd:cd00568   158 -AGG-PALIEVKT 168
ilvB CHL00099
acetohydroxyacid synthase large subunit
2-450 2.84e-23

acetohydroxyacid synthase large subunit


Pssm-ID: 214363 [Multi-domain]  Cd Length: 585  Bit Score: 103.63  E-value: 2.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:CHL00099   71 ARSTGKVGVCFATSGPGATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRI 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSGTPGPVFVELPIDV---LYPYFMVqkemVPAKPRKGLVGrvvswylenylanlfagaWEPqpegplpldI 158
Cdd:CHL00099  151 VAEAFYIAKHGRPGPVLIDIPKDVgleKFDYYPP----EPGNTIIKILG------------------CRP---------I 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIrenrsaalkkaD 238
Cdd:CHL00099  200 YKPTIKRIEQAAKLILQSSQPLLYVGGGAIIS-DAHQEITELAELYKIPVTTTLMGKGIFDEDHPLCL-----------G 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 239 VIVLAGTV--------CDFRLSYG-----RVL-------SHSSKIII------VNRNRedmllnsdvfwKPQEAVQGDVG 292
Cdd:CHL00099  268 MLGMHGTAyanfavseCDLLIALGarfddRVTgkldefaCNAQVIHIdidpaeIGKNR-----------IPQVAIVGDVK 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 293 SFVLKLVEGLQGQTWAPDwvEELREADRQKEQTFREKAAMPVAQH---LNPVRVLQLVEETLPDnSILVVDGGDFVGTAA 369
Cdd:CHL00099  337 KVLQELLELLKNSPNLLE--SEQTQAWRERINRWRKEYPLLIPKPstsLSPQEVINEISQLAPD-AYFTTDVGQHQMWAA 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 370 HL--VQPRGplcWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDaGWTQI 447
Cdd:CHL00099  414 QFlkCKPRK---WLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINN-KWQGM 489

                  ...
gi 1622891768 448 SRE 450
Cdd:CHL00099  490 VRQ 492
PRK11269 PRK11269
glyoxylate carboligase; Provisional
6-515 9.42e-23

glyoxylate carboligase; Provisional


Pssm-ID: 183066 [Multi-domain]  Cd Length: 591  Bit Score: 101.98  E-value: 9.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   6 GTVGVAAVTAGPGLTNTVTAVKNAqMAQS-PVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPTLRA 84
Cdd:PRK11269   67 GNIGVCIGTSGPAGTDMITGLYSA-SADSiPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQ 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  85 AMAAAQSGTPGPVFVELPIDvlypyfmVQKEMVpakprkglvgrvvswylenylanlfagAWEPQPEGPLPLDIPQASPQ 164
Cdd:PRK11269  146 AFHLMRSGRPGPVLIDLPFD-------VQVAEI---------------------------EFDPDTYEPLPVYKPAATRA 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 165 QVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL----------HIRENrsAAL 234
Cdd:PRK11269  192 QIEKALEMLNAAERPLIVAGG-GVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLmagmvglqtsHRYGN--ATL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRlsygrvlsHSSKIIIVNRNREdmLLNSD--------VFwKPQEAVQGDVGSFVLKLVEGLQGQT 306
Cdd:PRK11269  269 LASDFVLGIGNRWANR--------HTGSVEVYTKGRK--FVHVDieptqigrVF-GPDLGIVSDAKAALELLVEVAREWK 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 307 WA------PDWVEELREadrqkeqtfrEKAAMPVAQH-----LNPVRVLQLVEETLPDNSILV-------VDGGDFVgta 368
Cdd:PRK11269  338 AAgrlpdrSAWVADCQE----------RKRTLLRKTHfdnvpIKPQRVYEEMNKAFGRDTCYVstiglsqIAAAQFL--- 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 369 aHLVQPRGplcWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQIS 448
Cdd:PRK11269  405 -HVYKPRH---WINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIR 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 449 REQVPsLGSNVACSLAY------------TEYHKAAMGLGARGLLLSRENEdqVVKVLHDAQQQCRDGH-PVVVNILIGR 515
Cdd:PRK11269  481 QAQRA-FDMDYCVQLAFeninspelngygVDHVKVAEGLGCKAIRVFKPED--IAPALEQAKALMAEFRvPVVVEVILER 557
TPP_POX cd02014
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...
338-513 8.69e-22

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: 92.59  E-value: 8.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 338 LNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:cd02014     2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 418 GYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDA 497
Cdd:cd02014    82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRV--EDPDELEAALDEA 159
                         170
                  ....*....|....*.
gi 1622891768 498 QQQcrDGhPVVVNILI 513
Cdd:cd02014   160 LAA--DG-PVVIDVVT 172
PRK08611 PRK08611
pyruvate oxidase; Provisional
2-513 1.16e-20

pyruvate oxidase; Provisional


Pssm-ID: 181502 [Multi-domain]  Cd Length: 576  Bit Score: 95.45  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK08611   63 AKLTGKIGVCLSIGGPGAIHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSgTPGPVFVELPIDVLypyfmvqKEMVPAKPRKGlvgrvvswylenylANLFAgawepqpegplpLDIPQA 161
Cdd:PRK08611  143 VNQAIRTAYE-KKGVAVLTIPDDLP-------AQKIKDTTNKT--------------VDTFR------------PTVPSP 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQAlltpKSA-DKLRAAVETLGVPCFLGGMARGLLGRNH--SL----HIRENRS-AA 233
Cdd:PRK08611  189 KPKDIKKAAKLINKAKKPVILAGLGA----KHAkEELLAFAEKAKIPIIHTLPAKGIIPDDHpySLgnlgKIGTKPAyEA 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTvcDFrlSYGRVLSHSSKIIIVNRNREDM--LLNSDVfwkpqeAVQGDVGSFVLKLVEGLqgqtwapDW 311
Cdd:PRK08611  265 MQEADLLIMVGT--NY--PYVDYLPKKAKAIQIDTDPANIgkRYPVNV------GLVGDAKKALHQLTENI-------KH 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 312 VEELR--EADRQKEQTFREKAAMPVAQHLNPVR---VLQLVEETLPDNSILVVD-GGDFVGTAAHL-VQPRGPL---CWL 381
Cdd:PRK08611  328 VEDRRflEACQENMAKWWKWMEEDENNASTPIKperVMAAIQKIADDDAVLSVDvGTVTVWSARYLnLGTNQKFiisSWL 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 382 dpgafGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVAC 461
Cdd:PRK08611  408 -----GTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELEYAI 482
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622891768 462 SLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQQCRdghPVVVNILI 513
Cdd:PRK08611  483 DLSDMDYAKFAEACGGKGYRV--EKAEELDPAFEEALAQDK---PVIIDVYV 529
PRK06457 PRK06457
pyruvate dehydrogenase; Provisional
2-487 1.48e-18

pyruvate dehydrogenase; Provisional


Pssm-ID: 180570 [Multi-domain]  Cd Length: 549  Bit Score: 88.73  E-value: 1.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06457   59 AKITGKPSACMGTSGPGSIHLLNGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  82 LRAAMAAAQSgTPGPVFVELPIDVLypyfmvqkemvpakpRKGLvgrvvswylenylanlfagawEPQPEGPLPLDIPQA 161
Cdd:PRK06457  139 IRRAIREAIS-KRGVAHINLPVDIL---------------RKSS---------------------EYKGSKNTEVGKVKY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQqVQRCVEILSRAKRPLMVLGSQALLTPKSADKLraaVETLGVPCF----------------LGGMarGLLGRNHSLh 225
Cdd:PRK06457  182 SID-FSRAKELIKESEKPVLLIGGGTRGLGKEINRF---AEKIGAPIIytlngkgilpdldpkvMGGI--GLLGTKPSI- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 226 irenrsAALKKADVIVLAGTVcdfrLSYGRVLSHSSKIIIVNRNREDM--LLNSDVfwkpqeAVQGDVGSFV-LKLVEgl 302
Cdd:PRK06457  255 ------EAMDKADLLIMLGTS----FPYVNFLNKSAKVIQVDIDNSNIgkRLDVDL------SYPIPVAEFLnIDIEE-- 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 303 qgqtwAPDWVEElrEADRQKEQTFR--EKAAMPVAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCW 380
Cdd:PRK06457  317 -----KSDKFYE--ELKGKKEDWLDsiSKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTF 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 381 LDPGAFGTLGVGAGFALGAKLCR-PDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQ----VPSL 455
Cdd:PRK06457  390 IFSAWLGSMGIGVPGSVGASFAVeNKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQevmgYPEW 469
                         490       500       510
                  ....*....|....*....|....*....|..
gi 1622891768 456 GSNvacsLAYTEYHKAAMGLGARGLLLSRENE 487
Cdd:PRK06457  470 GVD----LYNPDFTKIAESIGFKGFRLEEPKE 497
TPP_enzyme_M pfam00205
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ...
166-298 1.21e-17

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: 79.53  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 166 VQRCVEILSRAKRPLMVLGSQALLtPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAALKKAD 238
Cdd:pfam00205   1 IEKAAELLKKAKRPVILAGGGVRR-SGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALEEAD 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622891768 239 VIVLAGTVCDFRLSYGRVLSHSS--KIIIVNRNREDMLLNSdvfwKPQEAVQGDVGSFVLKL 298
Cdd:pfam00205  80 LVLAVGARFDDIRTTGKLPEFAPdaKIIHIDIDPAEIGKNY----PVDVPIVGDAKETLEAL 137
PDC1 COG3961
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
2-517 1.81e-16

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: 82.13  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGtVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGAL--------QAIDQLSLFRPLCkfCASVR 73
Cdd:COG3961    63 ARVNG-LGALVTTYGVGELSAINGIAGAYAERVPVVHIVGAPGTRAQRRGPLlhhtlgdgDFDHFLRMFEEVT--VAQAV 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  74 -----------RVrdivptLRAAMAAAQsgtpgPVFVELPIDVlypyfmVQKEMVPakprkglvgrvvswylenylanlf 142
Cdd:COG3961   140 ltpenaaaeidRV------LAAALREKR-----PVYIELPRDV------ADAPIEP------------------------ 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 143 agawepqPEGPLPLDIPQASPQQVQRCV----EILSRAKRPLMVLGSQAL---LTpksaDKLRAAVETLGVPCFLGGMAR 215
Cdd:COG3961   179 -------PEAPLPLPPPASDPAALAAAVaaaaERLAKAKRPVILAGVEVHrfgLQ----EELLALAEKTGIPVATTLLGK 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 216 GLLGRNHSLHI--------RENRSAALKKADVIVLAGTV-CDFRLSYgrvlsHSSKIiivnrNREDMLlnsdvfwkpqea 286
Cdd:COG3961   248 SVLDESHPQFIgtyagaasSPEVREYVENADCVLCLGVVfTDTNTGG-----FTAQL-----DPERTI------------ 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 287 vqgDVGSFVLKLveglqGQTWAP-----DWVEELREADRQKEQTFREKAAMPVA------QHLNPVRVLQLVEETLPDNS 355
Cdd:COG3961   306 ---DIQPDSVRV-----GGHIYPgvslaDFLEALAELLKKRSAPLPAPAPPPPPppaapdAPLTQDRLWQRLQAFLDPGD 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 356 ILVVDGGD--FVGTAAHLvqPRG------PLcWldpgafGTLG--VGAgfALGAKLCRPDAEVWCLFGDGAFGYSLIEFD 425
Cdd:COG3961   378 IVVADTGTslFGAADLRL--PEGatfiaqPL-W------GSIGytLPA--ALGAALAAPDRRVILLVGDGAFQLTAQELS 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 426 TFVRHKIPVMALVGNDAGWTqISREQVPSLGS-NVacsLAYTEYHKAAMGLGARGLLLSR-ENEDQVVKVLHDAQQQCRd 503
Cdd:COG3961   447 TMLRYGLKPIIFVLNNDGYT-IERAIHGPDGPyND---IANWDYAKLPEAFGGGNALGFRvTTEGELEEALAAAEANTD- 521
                         570
                  ....*....|....
gi 1622891768 504 gHPVVVNILIGRTD 517
Cdd:COG3961   522 -RLTLIEVVLDKMD 534
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
338-440 4.09e-14

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: 70.60  E-value: 4.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 338 LNPVRVLQLVEETLPDNSILVVDggdfVGT----AAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFG 413
Cdd:cd02015     1 IKPQEVIKELSELTPGDAIVTTD----VGQhqmwAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDG 76
                          90       100
                  ....*....|....*....|....*..
gi 1622891768 414 DGAFGYSLIEFDTFVRHKIPVMALVGN 440
Cdd:cd02015    77 DGSFQMNIQELATAAQYNLPVKIVILN 103
TPP_ALS cd02010
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ...
340-520 4.71e-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: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 340 PVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGY 419
Cdd:cd02010     1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 420 SLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQ 499
Cdd:cd02010    81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRI--ESADDLLPVLERALA 158
                         170       180
                  ....*....|....*....|.
gi 1622891768 500 QcrDGhPVVVNILIgrtDFRD 520
Cdd:cd02010   159 A--DG-VHVIDCPV---DYSE 173
PRK08273 PRK08273
thiamine pyrophosphate protein; Provisional
2-417 5.03e-13

thiamine pyrophosphate protein; Provisional


Pssm-ID: 181344 [Multi-domain]  Cd Length: 597  Bit Score: 71.48  E-value: 5.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAastllQNRGAL-----QAIDQLSLFR----PLCKFCASV 72
Cdd:PRK08273   62 AKFTGEVGVCLATSGPGAIHLLNGLYDAKLDHVPVVAIVGQ-----QARAALgghyqQEVDLQSLFKdvagAFVQMVTVP 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  73 RRVRDIVP-TLRAAMAaaqsgTPGPVFVELPIDVlypyfmvQKEMVPAKPRK-GLVGRVVSWylenylanlfagawePQP 150
Cdd:PRK08273  137 EQLRHLVDrAVRTALA-----ERTVTAVILPNDV-------QELEYEPPPHAhGTVHSGVGY---------------TRP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 151 EgPLPldipqaSPQQVQRCVEILSRAKRPLMVLGSQALltpKSADKLRAAVETLGvpcflGGMARGLLGRnhslhirenr 230
Cdd:PRK08273  190 R-VVP------YDEDLRRAAEVLNAGRKVAILVGAGAL---GATDEVIAVAERLG-----AGVAKALLGK---------- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 231 sAALKK-----ADVIVLAGTvcdfRLSYgRVLSHSSKIIIVNRNredmllnsdvF----WKPQE----AVQGDVGSFVLK 297
Cdd:PRK08273  245 -AALPDdlpwvTGSIGLLGT----KPSY-ELMRECDTLLMVGSS----------FpyseFLPKEgqarGVQIDIDGRMLG 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 298 L---VE-GLQGQTWA------------PD--WVEELREADRQKEQTFREKAAMPvAQHLNPVRVLQLVEETLPDNSILVV 359
Cdd:PRK08273  309 LrypMEvNLVGDAAEtlrallpllerkKDrsWRERIEKWVARWWETLEARAMVP-ADPVNPQRVFWELSPRLPDNAILTA 387
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622891768 360 DGGDFVG-TAAHLVQPRGPLCWLDpGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:PRK08273  388 DSGSCANwYARDLRMRRGMMASLS-GTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAM 445
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
338-513 1.28e-12

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: 66.08  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 338 LNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAfGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:cd02002     1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 418 GYSLIEFDTFVRHKIPVMALVGNDAGWtQISREQVPSLGSNVACSLAY---------TEYHKAAMGLGARGLLLSRENEd 488
Cdd:cd02002    80 MYTIQALWTAARYGLPVTVVILNNRGY-GALRSFLKRVGPEGPGENAPdgldlldpgIDFAAIAKAFGVEAERVETPEE- 157
                         170       180
                  ....*....|....*....|....*.
gi 1622891768 489 qvvkvLHDAQQQC-RDGHPVVVNILI 513
Cdd:cd02002   158 -----LDEALREAlAEGGPALIEVVV 178
PRK07092 PRK07092
benzoylformate decarboxylase; Reviewed
11-444 2.13e-12

benzoylformate decarboxylase; Reviewed


Pssm-ID: 235931 [Multi-domain]  Cd Length: 530  Bit Score: 69.21  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  11 AAVTAGPGLTNTVTAVKNaqmaQSP-VLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPTLRAAMAAA 89
Cdd:PRK07092   81 SAAGVGNAMGNLFTAFKN----HTPlVITAGQQARSILPFEPFLAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIA 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  90 QSGTPGPVFVELPIDvlypyfmvqKEMVPAKPrkgLVGRVVSwylenylanlFAGAwepqpegplpldipqASPQQVQRC 169
Cdd:PRK07092  157 MQPPRGPVFVSIPYD---------DWDQPAEP---LPARTVS----------SAVR---------------PDPAALARL 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 170 VEILSRAKRPLMVLG-----SQAL-LTPKSADKLRAAV------------ETLgvPCFlggmaRGLLGRnhslhIRENRS 231
Cdd:PRK07092  200 GDALDAARRPALVVGpavdrAGAWdDAVRLAERHRAPVwvapmsgrcsfpEDH--PLF-----AGFLPA-----SREKIS 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 232 AALKKADVIVLAGTVCdFRL---SYGRVLSHSSKIIIVNrnrEDMLLNSdvfWKPQ-EAVQGDVGSFVLKLVEGL-QGQT 306
Cdd:PRK07092  268 ALLDGHDLVLVIGAPV-FTYhveGPGPHLPEGAELVQLT---DDPGEAA---WAPMgDAIVGDIRLALRDLLALLpPSAR 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 307 WAPDWVEELREADRQKEqtfrekaAMPVAQhlnpvrVLQLVEETLPDNSILVVDGGDFVGTaahlVQPRGPlcWLDPGAF 386
Cdd:PRK07092  341 PAPPARPMPPPAPAPGE-------PLSVAF------VLQTLAALRPADAIVVEEAPSTRPA----MQEHLP--MRRQGSF 401
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622891768 387 -----GTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGW 444
Cdd:PRK07092  402 ytmasGGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRY 464
TPP_PYR_POX cd07039
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ...
2-105 8.90e-12

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: 63.34  E-value: 8.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRR---VRDI 78
Cdd:cd07039    58 AKLTGKLGVCLGSSGPGAIHLLNGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSpeqLPEL 137
                          90       100
                  ....*....|....*....|....*...
gi 1622891768  79 VPT-LRAAMAaaqsgTPGPVFVELPIDV 105
Cdd:cd07039   138 LDRaIRTAIA-----KRGVAVLILPGDV 160
TPP_PDC_IPDC cd02005
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ...
342-517 1.34e-11

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: 63.32  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 342 RVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGpLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSL 421
Cdd:cd02005     6 RLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKG-TRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 422 IEFDTFVRHKIPVMALVGNDAGWT---QISREQVPslgsnvacslaYTE-----YHKAAMGLGARGLLLSR--ENEDQVV 491
Cdd:cd02005    85 QELSTMIRYGLNPIIFLINNDGYTierAIHGPEAS-----------YNDianwnYTKLPEVFGGGGGGLSFrvKTEGELD 153
                         170       180
                  ....*....|....*....|....*.
gi 1622891768 492 KVLHDAQQQCrdGHPVVVNILIGRTD 517
Cdd:cd02005   154 EALKDALFNR--DKLSLIEVILPKDD 177
PRK12474 PRK12474
hypothetical protein; Provisional
2-476 8.65e-10

hypothetical protein; Provisional


Pssm-ID: 139002 [Multi-domain]  Cd Length: 518  Bit Score: 61.04  E-value: 8.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVL-LLGGAASTLLQNRGALQAiDQLSLFRPLCKFcasVRRVRD--- 77
Cdd:PRK12474   63 GRIAGKPAVTLLHLGPGLANGLANLHNARRAASPIVnIVGDHAVEHLQYDAPLTS-DIDGFARPVSRW---VHRSASaga 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  78 IVPTLRAAMAAAQSGTPGPVFVELPIDVlypyfmvqkemvpakprkglvgrvvswylenylanlfagAWEPQPEGPLPL- 156
Cdd:PRK12474  139 VDSDVARAVQAAQSAPGGIATLIMPADV---------------------------------------AWNEAAYAAQPLr 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 157 DIPQA--SPQQVQRCVEILSRAKRPLMVLGSQALLTP--KSADKLRAAVetlGVPCFLGGMA-RGLLGRNHSLHIR---- 227
Cdd:PRK12474  180 GIGPApvAAETVERIAALLRNGKKSALLLRGSALRGAplEAAGRIQAKT---GVRLYCDTFApRIERGAGRVPIERipyf 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 228 -ENRSAALKKADVIVLAGT---VCDFrlSY----GRVLSHSSKIIIVNRNREDmllnsdvfwkpqeavqgdvgsfvlkLV 299
Cdd:PRK12474  257 hEQITAFLKDVEQLVLVGAkppVSFF--AYpgkpSWGAPPGCEIVYLAQPDED-------------------------LA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 300 EGLQgqtwapDWVEELREADRQKEQTFREKAAMPVAQhLNPVRVLQLVEETLPDNSIlVVDGGDFVGTAAHLVQPRGPLC 379
Cdd:PRK12474  310 QALQ------DLADAVDAPAEPAARTPLALPALPKGA-LNSLGVAQLIAHRTPDQAI-YADEALTSGLFFDMSYDRARPH 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 380 WLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAG----WTQISREQVPSL 455
Cdd:PRK12474  382 THLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSyailNGELQRVGAQGA 461
                         490       500
                  ....*....|....*....|....*
gi 1622891768 456 GSNVACSLAY----TEYHKAAMGLG 476
Cdd:PRK12474  462 GRNALSMLDLhnpeLNWMKIAEGLG 486
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
1-102 9.80e-09

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: 54.27  E-value: 9.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   1 MARLSGtVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:cd06586    54 YARAGG-PPVVIVTSGTGLLNAINGLADAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPA 132
                          90       100
                  ....*....|....*....|...
gi 1622891768  81 T-LRAAMAAAQSgtPGPVFVELP 102
Cdd:cd06586   133 GiDHAIRTAYAS--QGPVVVRLP 153
PRK07586 PRK07586
acetolactate synthase large subunit;
2-438 3.18e-06

acetolactate synthase large subunit;


Pssm-ID: 236063 [Multi-domain]  Cd Length: 514  Bit Score: 49.84  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVL-LLGGAASTLLQNRGALQAiDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK07586   59 ARMAGKPAATLLHLGPGLANGLANLHNARRARTPIVnIVGDHATYHRKYDAPLTS-DIEALARPVSGWVRRSESAADVAA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768  81 TLRAAMAAAQSGTPGPVFVELPIDVlypyfmvqkemvpakprkglvgrvvswylenylanlfagAWEP--QPEGPLPL-D 157
Cdd:PRK07586  138 DAAAAVAAARGAPGQVATLILPADV---------------------------------------AWSEggPPAPPPPApA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 158 IPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADKLRAAVET---LGVPCFLGGMARGLlGRnhsLHIR------E 228
Cdd:PRK07586  179 PAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAATgarLLAETFPARMERGA-GR---PAVErlpyfaE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 229 NRSAALKKADVIVLAGTvcdfrlsygrvlshsskiiivnrnredmllNSDVFW-----KPQEAVQGDVGsfVLKLVEGLQ 303
Cdd:PRK07586  255 QALAQLAGVRHLVLVGA------------------------------KAPVAFfaypgKPSRLVPEGCE--VHTLAGPGE 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 304 GQTWAPDWVEELREADRQKEQTFREKAAMPVAQHLNPVRVLQLVEETLPDNSILVVDGGDF-VGTAAHLVQPRgPLCWLD 382
Cdd:PRK07586  303 DAAAALEALADALGAKPAAPPLAAPARPPLPTGALTPEAIAQVIAALLPENAIVVDESITSgRGFFPATAGAA-PHDWLT 381
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891768 383 -PGafGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALV 438
Cdd:PRK07586  382 lTG--GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVI 436
TPP_Gcl cd02006
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ...
370-515 1.82e-05

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: 45.73  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 370 HLVQPRGplcWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAgWTQISR 449
Cdd:cd02006    43 HVYKPRH---WINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNA-YLGLIR 118
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622891768 450 EQVPSLGSNVACSLAY------------TEYHKAAMGLGARGLLLSRENEdqVVKVLHDAQQQCRDGH-PVVVNILIGR 515
Cdd:cd02006   119 QAQRAFDMDYQVNLAFeninsselggygVDHVKVAEGLGCKAIRVTKPEE--LAAAFEQAKKLMAEHRvPVVVEAILER 195
CdhB COG1880
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];
160-221 6.74e-05

CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];


Pssm-ID: 441484  Cd Length: 168  Bit Score: 43.40  E-value: 6.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622891768 160 QASPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADKLRAAVETLGVP-CFLGGMARGLLGRN 221
Cdd:COG1880    13 TAKAVKPEVAAKMIKKAKRPLLIVGPEALDDEELLERAIEIAKKAGIPiAATGHSIKGFVERG 75
TPP_PYR_MenD cd07037
Pyrimidine (PYR) binding domain of ...
1-103 3.01e-04

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: 41.33  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768   1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVR------R 74
Cdd:cd07037    54 LAKASGRPVAVVCTSGTAVANLLPAVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddD 133
                          90       100
                  ....*....|....*....|....*....
gi 1622891768  75 VRDIVPTLRAAMAAAQSGTPGPVFVELPI 103
Cdd:cd07037   134 LWYLLRLANRAVLEALSAPPGPVHLNLPF 162
TPP_IolD cd02003
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ...
342-511 1.42e-03

Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.


Pssm-ID: 238961 [Multi-domain]  Cd Length: 205  Bit Score: 39.98  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 342 RVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSL 421
Cdd:cd02003     3 EVLGALNEAIGDDDVVINAAGSLPGDLHKLWRARTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 422 IEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACSLAY--------------TEYHKAAMGLGARglLLSRENE 487
Cdd:cd02003    83 SEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGTEFRDrdqesgqldgallpVDFAANARSLGAR--VEKVKTI 160
                         170       180
                  ....*....|....*....|....
gi 1622891768 488 DQVVKVLHDAQQQCRdghPVVVNI 511
Cdd:cd02003   161 EELKAALAKAKASDR---TTVIVI 181
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
2-102 3.26e-03

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 40.61  E-value: 3.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768    2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP- 80
Cdd:PLN02980   359 ARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFFNLPPPTDLIPa 438
                           90       100
                   ....*....|....*....|....*..
gi 1622891768   81 -----TLRAAMAAAQSGTPGPVFVELP 102
Cdd:PLN02980   439 rmvltTLDSAVHWATSSPCGPVHINCP 465
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
389-415 4.92e-03

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 39.02  E-value: 4.92e-03
                          10        20
                  ....*....|....*....|....*..
gi 1622891768 389 LGVGAGFALGAKLCRPDAEVWCLFGDG 415
Cdd:cd02012   111 LSVAVGMALAEKLLGFDYRVYVLLGDG 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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