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Conserved domains on  [gi|1318663320|ref|NP_001346230|]
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2-hydroxyacyl-CoA lyase 2 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05858 super family cl35397
acetolactate synthase;
63-596 1.38e-120

acetolactate synthase;


The actual alignment was detected with superfamily member PRK05858:

Pssm-ID: 235629 [Multi-domain]  Cd Length: 542  Bit Score: 369.05  E-value: 1.38e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  63 HGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK05858    6 HAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK05858   86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPyfMVEKEMIPTKLPNSlmgrvvvwylqnclanlfvgaweprPEGPLPldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK05858  166 AFS--MADDDGRPGALTEL-------------------------PAGPTP------DPDALARAAGLLAEAQRPVIMAGT 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGrVLNRKSSIII 382
Cdd:PRK05858  213 DVWWGHAEA-ALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFG-VFGGTAQLVH 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 383 VNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQKEQtyRDKALM-----PvlqhLNP 457
Cdd:PRK05858  291 VDDAPPQR----AHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAETAARA--RDAAELaddrdP----IHP 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 458 VWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYS 537
Cdd:PRK05858  361 MRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFS 440
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1318663320 538 LIEFDTFVRHKVPVIALVGNDAGWtqiSREQVPR---LGSDVACSLA-YTDYHKAAMGLGAQG 596
Cdd:PRK05858  441 LMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRALGGHG 500
 
Name Accession Description Interval E-value
PRK05858 PRK05858
acetolactate synthase;
63-596 1.38e-120

acetolactate synthase;


Pssm-ID: 235629 [Multi-domain]  Cd Length: 542  Bit Score: 369.05  E-value: 1.38e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  63 HGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK05858    6 HAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK05858   86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPyfMVEKEMIPTKLPNSlmgrvvvwylqnclanlfvgaweprPEGPLPldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK05858  166 AFS--MADDDGRPGALTEL-------------------------PAGPTP------DPDALARAAGLLAEAQRPVIMAGT 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGrVLNRKSSIII 382
Cdd:PRK05858  213 DVWWGHAEA-ALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFG-VFGGTAQLVH 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 383 VNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQKEQtyRDKALM-----PvlqhLNP 457
Cdd:PRK05858  291 VDDAPPQR----AHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAETAARA--RDAAELaddrdP----IHP 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 458 VWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYS 537
Cdd:PRK05858  361 MRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFS 440
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1318663320 538 LIEFDTFVRHKVPVIALVGNDAGWtqiSREQVPR---LGSDVACSLA-YTDYHKAAMGLGAQG 596
Cdd:PRK05858  441 LMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRALGGHG 500
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
62-630 8.08e-112

Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 223107 [Multi-domain]  Cd Length: 550  Bit Score: 346.56  E-value: 8.08e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  62 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:COG0028     2 MTGAEALVEALEANGVDTVFGIPGGSILPLYDALYDSGIRHILVRHEQGAAFAADGYARATGKPGVCLVTSGPGATNLLT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 221
Cdd:COG0028    82 GLADAYMDSVPLLAITGQVPTSLIGTDAFQEVDQVGLFRPITKYNFEVRSPEDIPEVVARAFRIALSGRPGPVVVDLPKD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VLypyfmveKEMIPTKLPnslmgrvvvwylqnclanlfvGAWEPRPEGPLPldipqASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:COG0028   162 VL-------AAEAEEPGP---------------------EPAILPPYRPAP-----PPPEAIRKAAELLAEAKRPVILAG 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQALLPPTPANkLRAAVETLGVPCFLGGMSRGLLGRNHPLH-----IRQNRSA--ALKKADVVVLAGAVCDFRLSYGRVL 374
Cdd:COG0028   209 GGVRRAGASEE-LRELAEKLGAPVVTTLMGKGAVPEDHPLSlgmlgMHGTKAAneALEEADLLLAVGARFDDRVTGYSGF 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 375 NRKSSIIIVNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQmwSSDWAEELRKADQQKEQTYRDKALMPVlqh 454
Cdd:COG0028   288 APPAAIIHIDIDPAEI----GKNYPVDVPIVGDAKATLEALLEELKPE--RAAWLEELLEARAAYRDLALEELADDG--- 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:COG0028   359 IKPQYVIKVLRELLPDDAIVVTDVGQHQMWAARYFDFYRPRRFLTSGGLGTMGFGLPAAIGAKLAAPDRKVVAIAGDGGF 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLG-SDVACSLAYTDYHKAAMGLGAQGLILsrDNKDQVVKVLRE 613
Cdd:COG0028   439 MMNGQELETAVRYGLPVKIVVLNNGGYGMVRQWQELFYGgRYSGTDLGNPDFVKLAEAYGAKGIRV--ETPEELEEALEE 516
                         570
                  ....*....|....*..
gi 1318663320 614 GqqLCQDGhAVVVNILI 630
Cdd:COG0028   517 A--LASDG-PVLIDVVV 530
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
460-630 1.68e-62

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: 204.69  E-value: 1.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 460 VLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLI 539
Cdd:cd02004     4 VLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 540 EFDTFVRHKVPVIALVGNDAGWTQISREQVP--RLGSDVACSLAYTDYHKAAMGLGAQGLILSRDnkDQVVKVLREGQQL 617
Cdd:cd02004    84 ELETAVRYNLPIVVVVGNNGGWYQGLDGQQLsyGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTP--EELKPALKRALAS 161
                         170
                  ....*....|...
gi 1318663320 618 cqdGHAVVVNILI 630
Cdd:cd02004   162 ---GKPALINVII 171
acolac_catab TIGR02418
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ...
64-637 6.09e-58

acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]


Pssm-ID: 131471 [Multi-domain]  Cd Length: 539  Bit Score: 204.21  E-value: 6.09e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:TIGR02418   1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:TIGR02418  81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 YPyfMVEKEMIPtklpnslmgrvvvwylqnclanlfvgaweprpegplPLDIPQ---ASPQQVQRCVEILSRAKRPLLVL 300
Cdd:TIGR02418 161 DS--PVSVKAIP------------------------------------ASYAPKlgaAPDDAIDEVAEAIQNAKLPVLLL 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHirqnrsaalkkadvvvLAGAVCDFRLSYGRVLNRKSSI 380
Cdd:TIGR02418 203 GLRASSPETTE-AVRRLLKKTQLPVVETFQGAGAVSRELEDH----------------FFGRVGLFRNQPGDRLLKQADL 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 381 IIV-------------NRNRDDLLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQKE 440
Cdd:TIGR02418 266 VITigydpieyeprnwNSENDATIVHIDVepaqidnNYQPDLELVGDIASTLDLLAERIPGYELPPDALAILEDLKQQRE 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 441 QTYRDKAlMPVLQHLNPVWVLQQVEETLPDNALLVVDGGDF-VATAAYLVQPRgPLRWLDPGAFGTLGVGAGFALGAKLC 519
Cdd:TIGR02418 346 ALDRVPA-TLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHyIWMARYFRSYR-ARHLLISNGMQTLGVALPWAIGAALV 423
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 520 QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLIL 599
Cdd:TIGR02418 424 RPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQRSSGVDFGPIDFVKYAESFGAKGLRV 503
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 1318663320 600 srDNKDQVVKVLREGQQLcqDGhAVVVNILIgrtDFRD 637
Cdd:TIGR02418 504 --ESPDQLEPTLRQAMEV--EG-PVVVDIPV---DYSD 533
TPP_enzyme_N pfam02776
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
64-223 1.58e-57

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;


Pssm-ID: 426975 [Multi-domain]  Cd Length: 169  Bit Score: 191.30  E-value: 1.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:pfam02776   1 GAEALADVLKALGVDTVFGVPGGTILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQA-IDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 221
Cdd:pfam02776  81 LANAYVDSVPLIVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSPDEIPEVLRRAFRAAMSGRPGPVYLEIPLD 160

                  ..
gi 1318663320 222 VL 223
Cdd:pfam02776 161 VL 162
 
Name Accession Description Interval E-value
PRK05858 PRK05858
acetolactate synthase;
63-596 1.38e-120

acetolactate synthase;


Pssm-ID: 235629 [Multi-domain]  Cd Length: 542  Bit Score: 369.05  E-value: 1.38e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  63 HGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK05858    6 HAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK05858   86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPyfMVEKEMIPTKLPNSlmgrvvvwylqnclanlfvgaweprPEGPLPldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK05858  166 AFS--MADDDGRPGALTEL-------------------------PAGPTP------DPDALARAAGLLAEAQRPVIMAGT 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGrVLNRKSSIII 382
Cdd:PRK05858  213 DVWWGHAEA-ALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFG-VFGGTAQLVH 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 383 VNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQKEQtyRDKALM-----PvlqhLNP 457
Cdd:PRK05858  291 VDDAPPQR----AHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAETAARA--RDAAELaddrdP----IHP 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 458 VWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYS 537
Cdd:PRK05858  361 MRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFS 440
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1318663320 538 LIEFDTFVRHKVPVIALVGNDAGWtqiSREQVPR---LGSDVACSLA-YTDYHKAAMGLGAQG 596
Cdd:PRK05858  441 LMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRALGGHG 500
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
62-630 8.08e-112

Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 223107 [Multi-domain]  Cd Length: 550  Bit Score: 346.56  E-value: 8.08e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  62 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:COG0028     2 MTGAEALVEALEANGVDTVFGIPGGSILPLYDALYDSGIRHILVRHEQGAAFAADGYARATGKPGVCLVTSGPGATNLLT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 221
Cdd:COG0028    82 GLADAYMDSVPLLAITGQVPTSLIGTDAFQEVDQVGLFRPITKYNFEVRSPEDIPEVVARAFRIALSGRPGPVVVDLPKD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VLypyfmveKEMIPTKLPnslmgrvvvwylqnclanlfvGAWEPRPEGPLPldipqASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:COG0028   162 VL-------AAEAEEPGP---------------------EPAILPPYRPAP-----PPPEAIRKAAELLAEAKRPVILAG 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQALLPPTPANkLRAAVETLGVPCFLGGMSRGLLGRNHPLH-----IRQNRSA--ALKKADVVVLAGAVCDFRLSYGRVL 374
Cdd:COG0028   209 GGVRRAGASEE-LRELAEKLGAPVVTTLMGKGAVPEDHPLSlgmlgMHGTKAAneALEEADLLLAVGARFDDRVTGYSGF 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 375 NRKSSIIIVNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQmwSSDWAEELRKADQQKEQTYRDKALMPVlqh 454
Cdd:COG0028   288 APPAAIIHIDIDPAEI----GKNYPVDVPIVGDAKATLEALLEELKPE--RAAWLEELLEARAAYRDLALEELADDG--- 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:COG0028   359 IKPQYVIKVLRELLPDDAIVVTDVGQHQMWAARYFDFYRPRRFLTSGGLGTMGFGLPAAIGAKLAAPDRKVVAIAGDGGF 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLG-SDVACSLAYTDYHKAAMGLGAQGLILsrDNKDQVVKVLRE 613
Cdd:COG0028   439 MMNGQELETAVRYGLPVKIVVLNNGGYGMVRQWQELFYGgRYSGTDLGNPDFVKLAEAYGAKGIRV--ETPEELEEALEE 516
                         570
                  ....*....|....*..
gi 1318663320 614 GqqLCQDGhAVVVNILI 630
Cdd:COG0028   517 A--LASDG-PVLIDVVV 530
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
460-630 1.68e-62

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: 204.69  E-value: 1.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 460 VLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLI 539
Cdd:cd02004     4 VLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 540 EFDTFVRHKVPVIALVGNDAGWTQISREQVP--RLGSDVACSLAYTDYHKAAMGLGAQGLILSRDnkDQVVKVLREGQQL 617
Cdd:cd02004    84 ELETAVRYNLPIVVVVGNNGGWYQGLDGQQLsyGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTP--EELKPALKRALAS 161
                         170
                  ....*....|...
gi 1318663320 618 cqdGHAVVVNILI 630
Cdd:cd02004   162 ---GKPALINVII 171
TPP_PYR_POX_like cd07035
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ...
66-219 1.05e-58

Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.


Pssm-ID: 132918 [Multi-domain]  Cd Length: 155  Bit Score: 193.90  E-value: 1.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 145
Cdd:cd07035     1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663320 146 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 219
Cdd:cd07035    81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLP 154
PRK07524 PRK07524
5-guanidino-2-oxopentanoate decarboxylase;
65-594 1.24e-58

5-guanidino-2-oxopentanoate decarboxylase;


Pssm-ID: 236041 [Multi-domain]  Cd Length: 535  Bit Score: 205.98  E-value: 1.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  65 GESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVK 144
Cdd:PRK07524    5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 145 NAQVAQSPVLLLGG--AASTLLQKRGALQAI-DQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 221
Cdd:PRK07524   85 QAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VlypyfMVEKemiptklpnslmgrvvvwylqnclanlFVGAWEPRPEGPLPldiPQASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:PRK07524  165 V-----LAAP---------------------------ADHLLPAPPTRPAR---PGPAPAALAQAAERLAAARRPLILAG 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRS-----AALKKADVVVLAG---AVCDFRLSYGRV 373
Cdd:PRK07524  210 GGAL---AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSlpavrALIAEADVVLAVGtelGETDYDVYFDGG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 LNRKSSIIIVNRNRDDLLLNsdifWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEElRKADQQKEQTYRDKALMPVLQ 453
Cdd:PRK07524  287 FPLPGELIRIDIDPDQLARN----YPPALALVGDARAALEALLARLPGQAAAADWGAA-RVAALRQALRAEWDPLTAAQV 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 454 HLnpvwvLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLD-PGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDG 532
Cdd:PRK07524  362 AL-----LDTILAALPD-AIFVGDSTQPVYAGNLYFDADAPRRWFNaSTGYGTLGYGLPAAIGAALGAPERPVVCLVGDG 435
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1318663320 533 AFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGA 594
Cdd:PRK07524  436 GLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGC 497
acolac_catab TIGR02418
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ...
64-637 6.09e-58

acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]


Pssm-ID: 131471 [Multi-domain]  Cd Length: 539  Bit Score: 204.21  E-value: 6.09e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:TIGR02418   1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:TIGR02418  81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 YPyfMVEKEMIPtklpnslmgrvvvwylqnclanlfvgaweprpegplPLDIPQ---ASPQQVQRCVEILSRAKRPLLVL 300
Cdd:TIGR02418 161 DS--PVSVKAIP------------------------------------ASYAPKlgaAPDDAIDEVAEAIQNAKLPVLLL 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHirqnrsaalkkadvvvLAGAVCDFRLSYGRVLNRKSSI 380
Cdd:TIGR02418 203 GLRASSPETTE-AVRRLLKKTQLPVVETFQGAGAVSRELEDH----------------FFGRVGLFRNQPGDRLLKQADL 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 381 IIV-------------NRNRDDLLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQKE 440
Cdd:TIGR02418 266 VITigydpieyeprnwNSENDATIVHIDVepaqidnNYQPDLELVGDIASTLDLLAERIPGYELPPDALAILEDLKQQRE 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 441 QTYRDKAlMPVLQHLNPVWVLQQVEETLPDNALLVVDGGDF-VATAAYLVQPRgPLRWLDPGAFGTLGVGAGFALGAKLC 519
Cdd:TIGR02418 346 ALDRVPA-TLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHyIWMARYFRSYR-ARHLLISNGMQTLGVALPWAIGAALV 423
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 520 QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLIL 599
Cdd:TIGR02418 424 RPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQRSSGVDFGPIDFVKYAESFGAKGLRV 503
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 1318663320 600 srDNKDQVVKVLREGQQLcqDGhAVVVNILIgrtDFRD 637
Cdd:TIGR02418 504 --ESPDQLEPTLRQAMEV--EG-PVVVDIPV---DYSD 533
TPP_enzyme_N pfam02776
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
64-223 1.58e-57

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;


Pssm-ID: 426975 [Multi-domain]  Cd Length: 169  Bit Score: 191.30  E-value: 1.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:pfam02776   1 GAEALADVLKALGVDTVFGVPGGTILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQA-IDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 221
Cdd:pfam02776  81 LANAYVDSVPLIVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSPDEIPEVLRRAFRAAMSGRPGPVYLEIPLD 160

                  ..
gi 1318663320 222 VL 223
Cdd:pfam02776 161 VL 162
PRK07525 PRK07525
sulfoacetaldehyde acetyltransferase; Validated
66-632 1.18e-55

sulfoacetaldehyde acetyltransferase; Validated


Pssm-ID: 236042 [Multi-domain]  Cd Length: 588  Bit Score: 199.07  E-value: 1.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 145
Cdd:PRK07525   10 EAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVAT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 146 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTpGPVFVELPLDvlYP 225
Cdd:PRK07525   90 AYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD--YF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 226 YFMVEKEmIPTklpnslmgrvvvwylqnclanlfvgaweprpegPLPLDIPQASPQQVQRCVEILSRAKRPLLVLG---- 301
Cdd:PRK07525  167 YGVIDVE-IPQ---------------------------------PVRLERGAGGEQSLAEAAELLSEAKFPVILSGagvv 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 -SQALlpptpaNKLRAAVETLGVPCFLGGMSRGLLGRNHPLH---IRQNRSAA----LKKADVVVLAGAvcdfRLSYGRV 373
Cdd:PRK07525  213 lSDAI------EECKALAERLDAPVACGYLHNDAFPGSHPLWvgpLGYNGSKAamelIAKADVVLALGT----RLNPFGT 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 LN--------RKSSIIIVNRNRDDLLLNsdifwKPQE-AVQGDVGSFMIKLVEGLQGQMWS---------------SDWA 429
Cdd:PRK07525  283 LPqygidywpKDAKIIQVDINPDRIGLT-----KKVSvGICGDAKAVARELLARLAERLAGdagreerkaliaaekSAWE 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 430 EELRKADQQKEQ---TYRDKALMPVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATA-AYLvQPRGPLRWLDPGAFGT 505
Cdd:PRK07525  358 QELSSWDHEDDDpgtDWNEEARARKPDYMHPRQALREIQKALPEDAIVSTDIGNNCSIAnSYL-RFEKGRKYLAPGSFGN 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 506 LGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSD-VACSL-AYT 583
Cdd:PRK07525  437 CGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRfVGTELdNNV 516
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 1318663320 584 DYHKAAMGLGAQGLILsrDNKDQVVKVLREGQQLCQDGHAVVVNILIGR 632
Cdd:PRK07525  517 SYAGIAEAMGAEGVVV--DTQEELGPALKRAIDAQNEGKTTVIEIMCNQ 563
acolac_lg TIGR00118
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ...
64-559 1.65e-55

acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 272915 [Multi-domain]  Cd Length: 558  Bit Score: 198.02  E-value: 1.65e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:TIGR00118   3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDsGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:TIGR00118  83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPYFMVEkemIPTKLpnSLMGrvvvwylqnclanlfvgaWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:TIGR00118 163 TTAEIEYP---YPEKV--NLPG------------------YRPTVKG---------HPLQIKKAAELINLAKKPVILVGG 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLN 375
Cdd:TIGR00118 211 GVIIAGASE-ELKELAERIQIPVTTTLMGLGSFPEDHPLslgmlgmHGTKTANLAVHECDLIIAVGARFDDRVT-GNLAK 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 376 RKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGL--QGQMWSSDWAEELR--KADQQKEQTYRDKALMPv 451
Cdd:TIGR00118 289 FAPNAKIIHIDIDPAEIGKNV--RVDIPIVGDARNVLEELLKKLfeLKERKESAWLEQINkwKKEYPLKMDYTEEGIKP- 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 452 lQHlnpvwVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 531
Cdd:TIGR00118 366 -QQ-----VIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGD 439
                         490       500
                  ....*....|....*....|....*...
gi 1318663320 532 GAFGYSLIEFDTFVRHKVPVIALVGNDA 559
Cdd:TIGR00118 440 GSFQMNLQELSTAVQYDIPVKILILNNR 467
PRK09259 PRK09259
putative oxalyl-CoA decarboxylase; Validated
68-578 1.70e-55

putative oxalyl-CoA decarboxylase; Validated


Pssm-ID: 236433 [Multi-domain]  Cd Length: 569  Bit Score: 197.90  E-value: 1.70e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  68 VAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQ 147
Cdd:PRK09259   16 VIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALANAT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 148 VAQSPVLLLGGAASTL---LQkRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVLY 224
Cdd:PRK09259   96 TNCFPMIMISGSSEREivdLQ-QGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVLA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 225 PYFMVEKemiptklpnslmGRVVVWylqnclanlfvgawepRPEGPLPLDIPqaSPQQVQRCVEILSRAKRPLLVLGSQA 304
Cdd:PRK09259  175 QTMDADE------------ALTSLV----------------KVVDPAPAQLP--APEAVDRALDLLKKAKRPLIILGKGA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 305 LLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGR--VLNRKSSIII 382
Cdd:PRK09259  225 AYAQADE-QIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVVLLVGARLNWLLSHGKgkTWGADKKFIQ 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 383 VnrnrddlllnsDIfwKPQEA---------VQGDVGSFMIKLVEGLQGQmW---SSDWAEEL--RKADQQKEQTYRDKAL 448
Cdd:PRK09259  304 I-----------DI--EPQEIdsnrpiaapVVGDIGSVMQALLAGLKQN-TfkaPAEWLDALaeRKEKNAAKMAEKLSTD 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 449 MPVLQHLNPVWVLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC--QPeaeVW 526
Cdd:PRK09259  370 TQPMNFYNALGAIRDVLKENPD-IYLVNEGANTLDLARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAAAVEtgKP---VV 445
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1318663320 527 CLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGwtqISR--EQVPRLGSDVAC 578
Cdd:PRK09259  446 AIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGG---IYRgdDVNLSGAGDPSP 496
PRK08527 PRK08527
acetolactate synthase large subunit;
64-558 2.15e-52

acetolactate synthase large subunit;


Pssm-ID: 181458 [Multi-domain]  Cd Length: 563  Bit Score: 189.54  E-value: 2.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHIspLLVACE---KLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 140
Cdd:PRK08527    5 GSQMVCEALKEEGVKVVFGYPGGAI--LNIYDEiykQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 141 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:PRK08527   83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DV-------LYPyfmvEKEMIPTKLPNslmgrvvvwYLQNclanlfvgaweprpegplpldipqasPQQVQRCVEILSRA 293
Cdd:PRK08527  163 DVtatlgefEYP----KEISLKTYKPT---------YKGN--------------------------SRQIKKAAEAIKEA 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 294 KRPLLVLGSQALLpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDF 366
Cdd:PRK08527  204 KKPLFYLGGGAIL-SNASEEIRELVKKTGIPAVETLMARGVLRSDDPLllgmlgmHGSYAANMAMSECDLLISLGARFDD 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 367 RLSyGRV--LNRKSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDVGSFMIKLVEGLQGQMWS--SDWAEELRKADQQKE 440
Cdd:PRK08527  283 RVT-GKLseFAKHAKIIHVDIDPSSIskIVNADY------PIVGDLKNVLKEMLEELKEENPTtyKEWREILKRYNELHP 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 441 QTYRDKALMpvlqhLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQ 520
Cdd:PRK08527  356 LSYEDSDEV-----LKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAV 430
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1318663320 521 PEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 558
Cdd:PRK08527  431 PDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNN 468
PRK08617 PRK08617
acetolactate synthase AlsS;
62-637 2.40e-50

acetolactate synthase AlsS;


Pssm-ID: 236312 [Multi-domain]  Cd Length: 552  Bit Score: 183.52  E-value: 2.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  62 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:PRK08617    5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 221
Cdd:PRK08617   85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VLYPyfmvekemiPTKLPNslmgrvvvwylqnclanlfVGAWEPRPEGPlpldipqASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:PRK08617  165 VVDA---------PVTSKA-------------------IAPLSKPKLGP-------ASPEDINYLAELIKNAKLPVLLLG 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQALLPPTpANKLRAAVETLGVPCF-----LGGMSRGL---------LGRNHP---LhirqnrsaaLKKADVVVLAGavc 364
Cdd:PRK08617  210 MRASSPEV-TAAIRRLLERTNLPVVetfqaAGVISRELedhffgrvgLFRNQPgdeL---------LKKADLVITIG--- 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 365 dfrlsYG------RVLNRKSSIIIVnrNRDDLLLNSDIFWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQ 438
Cdd:PRK08617  277 -----YDpieyepRNWNSEGDATII--HIDVLPAEIDNYYQPERELIGDIAATLDLLAEKLDGLSLSPQSLEILEELRAQ 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 439 KEQTYRDKALMPVlQHLNPVWVLQQVEETLPDNALLVVDGGDF---VATAAYLVQPRGPLrwldpgaFG----TLGVGAG 511
Cdd:PRK08617  350 LEELAERPARLEE-GAVHPLRIIRALQDIVTDDTTVTVDVGSHyiwMARYFRSYEPRHLL-------FSngmqTLGVALP 421
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 512 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMG 591
Cdd:PRK08617  422 WAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMKYGRSSGVDFGPVDFVKYAES 501
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 1318663320 592 LGAQGliLSRDNKDQVVKVLREGqqLCQDGhAVVVNILIgrtDFRD 637
Cdd:PRK08617  502 FGAKG--LRVTSPDELEPVLREA--LATDG-PVVIDIPV---DYSD 539
PRK08266 PRK08266
hypothetical protein; Provisional
64-596 3.82e-49

hypothetical protein; Provisional


Pssm-ID: 181337 [Multi-domain]  Cd Length: 542  Bit Score: 179.82  E-value: 3.82e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:PRK08266    6 GGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGG--AASTLLQKRGALQAI-DQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVEL 218
Cdd:PRK08266   86 ALLTAYGCNSPVLCLTGqiPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALEM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 219 PLDVLYpyfMVEKEMIPTKLpnslmgrvvvwylqnclanlfvgawepRPEGPLPLDipqasPQQVQRCVEILSRAKRPLL 298
Cdd:PRK08266  166 PWDVFG---QRAPVAAAPPL---------------------------RPAPPPAPD-----PDAIAAAAALIAAAKNPMI 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 299 VLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHirQNRSAA---LKKADVVVLAGAVCDFRLSYGRVLN 375
Cdd:PRK08266  211 FVGGGAA---GAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLG--LNFAAAyelWPQTDVVIGIGSRLELPTFRWPWRP 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 376 RKSSIIIVNRNRDDLllnsdIFWKPQEAVQGDVGSFMIKLVEGLQGQM-WSSDWAEELRKADQQKEQtyRDKALMPVLQH 454
Cdd:PRK08266  286 DGLKVIRIDIDPTEM-----RRLKPDVAIVADAKAGTAALLDALSKAGsKRPSRRAELRELKAAARQ--RIQAVQPQASY 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNpvwvlqQVEETLPDNAlLVVDGGDFVATAAYLVQP-RGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGA 533
Cdd:PRK08266  359 LR------AIREALPDDG-IFVDELSQVGFASWFAFPvYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGG 431
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663320 534 FGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRL-GSDVACSLAYTDYHKAAMGLGAQG 596
Cdd:PRK08266  432 FMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFgGRVVASDLVNPDFVKLAESFGVAA 495
PRK08322 PRK08322
acetolactate synthase large subunit;
72-625 1.93e-48

acetolactate synthase large subunit;


Pssm-ID: 236239 [Multi-domain]  Cd Length: 547  Bit Score: 178.10  E-value: 1.93e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  72 LRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQS 151
Cdd:PRK08322   11 LENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 152 PVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVrDIVPTL-RTAIAAAQSGTPGPVFVELPLDVlypyfmve 230
Cdd:PRK08322   91 PMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSP-DNIPEVvREAFRLAEEERPGAVHLELPEDI-------- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 231 kemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPLD---IPQASPQQVQRCVEILSRAKRPLLVLGSQALLP 307
Cdd:PRK08322  162 -------------------------------AAEETDGKPLPRSysrRPYASPKAIERAAEAIQAAKNPLILIGAGANRK 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 308 PTpANKLRAAVETLGVPCFLGGMSRGLLGRNHP-------LHIRQNRSAALKKADVVVLAGavcdfrlsYGRV------L 374
Cdd:PRK08322  211 TA-SKALTEFVDKTGIPFFTTQMGKGVIPETHPlslgtagLSQGDYVHCAIEHADLIINVG--------HDVIekppffM 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 375 NRKSSIIIVNRNRDDLLLNSDIFwkPQEAVQGDVGSFMIKLVEGL-QGQMWSSDWAEELRKADQQKEQTYRDKALMPVLq 453
Cdd:PRK08322  282 NPNGDKKVIHINFLPAEVDPVYF--PQVEVVGDIANSLWQLKERLaDQPHWDFPRFLKIREAIEAHLEEGADDDRFPMK- 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 454 hlnPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGA 533
Cdd:PRK08322  359 ---PQRIVADLRKVMPDDDIVILDNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGG 435
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 534 FGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILSRDnkDQVVKVLRE 613
Cdd:PRK08322  436 FMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESA--DDLLPTLEE 513
                         570
                  ....*....|..
gi 1318663320 614 GqqLCQDGHAVV 625
Cdd:PRK08322  514 A--LAQPGVHVI 523
PRK06276 PRK06276
acetolactate synthase large subunit;
64-555 1.08e-47

acetolactate synthase large subunit;


Pssm-ID: 235766 [Multi-domain]  Cd Length: 586  Bit Score: 176.87  E-value: 1.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:PRK06276    3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:PRK06276   83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 YPYFMVEKEMIPTKLPnsLMGrvvvwylqnclanlfvgaWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGSQ 303
Cdd:PRK06276  163 EGELDLEKYPIPAKID--LPG------------------YKPTTFG---------HPLQIKKAAELIAEAERPVILAGGG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 304 ALLppTPANK-LRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGavCDFRlsyGRVLN 375
Cdd:PRK06276  214 VII--SGASEeLIELSELVKIPVCTTLMGKGAFPEDHPLalgmvgmHGTKAANYSVTESDVLIAIG--CRFS---DRTTG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 376 RKSS------IIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEGLQGQMWSSD--WAEELR--KADQQKEQTYRD 445
Cdd:PRK06276  287 DISSfapnakIIHIDIDPAEIGKNVRV----DVPIVGDAKNVLRDLLAELMKKEIKNKseWLERVKklKKESIPRMDFDD 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 446 KALMPvlQHLnpVWVLQQV--EETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEA 523
Cdd:PRK06276  363 KPIKP--QRV--IKELMEVlrEIDPSKNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDA 438
                         490       500       510
                  ....*....|....*....|....*....|..
gi 1318663320 524 EVWCLFGDGAFGYSLIEFDTFVRHKVPVIALV 555
Cdd:PRK06276  439 NVIAITGDGGFLMNSQELATIAEYDIPVVICI 470
PRK06048 PRK06048
acetolactate synthase large subunit;
64-632 2.01e-46

acetolactate synthase large subunit;


Pssm-ID: 180368 [Multi-domain]  Cd Length: 561  Bit Score: 172.65  E-value: 2.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:PRK06048   10 GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTGI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:PRK06048   90 ATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKDVT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 -------YPyfmvEKEMIPtklpnslmgrvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRP 296
Cdd:PRK06048  170 taeidfdYP----DKVELR--------------------------GYKPTYKG---------NPQQIKRAAELIMKAERP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 297 LL-----VLGSQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI-------RQNRSAALKKADVVVLAGAVC 364
Cdd:PRK06048  211 IIyagggVISSNA------SEELVELAETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAIQESDLIIAVGARF 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 365 DFRLSyGRVLNRKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQgqmwSSDWAEELRKADQQKEQ--- 441
Cdd:PRK06048  285 DDRVT-GKLASFAPNAKIIHIDIDPAEISKNV--KVDVPIVGDAKQVLKSLIKYVQ----YCDRKEWLDKINQWKKEypl 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 442 --TYRDKALMpvlqhlnPVWVLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC 519
Cdd:PRK06048  358 kyKEREDVIK-------PQYVIEQIYELCPD-AIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVG 429
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 520 QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQISREQvpRLGSdvACSLAYTDYHKAAMGLG 593
Cdd:PRK06048  430 KPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGylgmvrQWQELFYDK--RYSH--TCIKGSVDFVKLAEAYG 505
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 1318663320 594 AQGLILSRDNkdQVVKVLREGQQLcqdGHAVVVNILIGR 632
Cdd:PRK06048  506 ALGLRVEKPS--EVRPAIEEAVAS---DRPVVIDFIVEC 539
PRK06154 PRK06154
thiamine pyrophosphate-requiring protein;
54-632 8.91e-46

thiamine pyrophosphate-requiring protein;


Pssm-ID: 235718 [Multi-domain]  Cd Length: 565  Bit Score: 170.76  E-value: 8.91e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  54 HKVDKTSIRHGGESVAAVLRAHGVRFVFtlvGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTG--TVGVAAVT 131
Cdd:PRK06154   12 HLPAEAKTMKVAEAVAEILKEEGVELLF---GFPVNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 132 AGPGLTNTVTAVKNAQVAQSPVLLLGGAASTllqkrgALQAID----QMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQ 207
Cdd:PRK06154   89 YGPGAENAFGGVAQAYGDSVPVLFLPTGYPR------GSTDVApnfeSLRNYRHITKWCEQVTLPDEVPELMRRAFTRLR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 208 SGTPGPVFVELPLDVLYpyfmvekemipTKLPNSlmgrvvvwylqnclanlfvgawePRPEGPLPLDIPQASPQQVQRCV 287
Cdd:PRK06154  163 NGRPGPVVLELPVDVLA-----------EELDEL-----------------------PLDHRPSRRSRPGADPVEVVEAA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 288 EILSRAKRPLLVLGsQALLPPTPANKLRAAVETLGVPCF--LGGMSRglLGRNHPLHIRQNRSAA-------LKKADVVV 358
Cdd:PRK06154  209 ALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMttLNGKSA--FPEDHPLALGSGGRARpatvahfLREADVLF 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 359 LAGavCDF-RLSYGRVLNRKSSIIIVnrNRDDLLLNSDIFWKpqEAVQGDVGSFMIKLVEGLQGQMW-----SSDWAEEL 432
Cdd:PRK06154  286 GIG--CSLtRSYYGLPMPEGKTIIHS--TLDDADLNKDYPID--HGLVGDAALVLKQMIEELRRRVGpdrgrAQQVAAEI 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 433 RKADQQKEQTYRDKaLMPVLQHLNPVWVLQQVEETL-PDNALLVVDGG---DFVATAAYLVQPRGPLRWldpGAFGTLGV 508
Cdd:PRK06154  360 EAVRAAWLAKWMPK-LTSDSTPINPYRVVWELQHAVdIKTVIITHDAGsprDQLSPFYVASRPGSYLGW---GKTTQLGY 435
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 509 GAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDaGWTQISREQVPRLGSDVACSLAYTDYHKA 588
Cdd:PRK06154  436 GLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNN-FSMGGYDKVMPVSTTKYRATDISGDYAAI 514
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 1318663320 589 AMGLGAQGLILSRdnKDQVVKVLREGQQLCQDGHAVVVNILIGR 632
Cdd:PRK06154  515 ARALGGYGERVED--PEMLVPALLRALRKVKEGTPALLEVITSE 556
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
64-561 1.61e-45

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 169.79  E-value: 1.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK07064    5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGkIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAAST--LLQKRGAL-QAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 219
Cdd:PRK07064   85 LVEALTAGTPLLHITGQIETpyLDQDLGYIhEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 220 LDvlypyfmvekemiptklpnsLMGRVVVWylqnclanlfvgawePRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLV 299
Cdd:PRK07064  165 ID--------------------IQAAEIEL---------------PDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLW 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 300 LGSQALlppTPANKLRAAVEtLGVPCFLGGMSRGLLGRNHPLHIRQ-NRSAA----LKKADVVVLAGAvcDFR----LSY 370
Cdd:PRK07064  210 LGGGAR---HAGAEVKRLVD-LGFGVVTSTQGRGVVPEDHPASLGAfNNSAAvealYKTCDLLLVVGS--RLRgnetLKY 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 371 GRVLNRKSSIIIVNRNRDDLLLNSDIFwkpqeaVQGDVGSFMIKLVEGLQGQMW-SSDWAEELRKADQQKEQTYRDKalm 449
Cdd:PRK07064  284 SLALPRPLIRVDADAAADGRGYPNDLF------VHGDAARVLARLADRLEGRLSvDPAFAADLRAAREAAVADLRKG--- 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 450 pvlqhLNPVWVL-QQVEETLPDNALLVVDGGdfVATAAY---LVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEV 525
Cdd:PRK07064  355 -----LGPYAKLvDALRAALPRDGNWVRDVT--ISNSTWgnrLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKT 426
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1318663320 526 WCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGW 561
Cdd:PRK07064  427 VGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGY 462
PRK06725 PRK06725
acetolactate synthase large subunit;
64-625 9.00e-45

acetolactate synthase large subunit;


Pssm-ID: 180672 [Multi-domain]  Cd Length: 570  Bit Score: 168.22  E-value: 9.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:PRK06725   17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:PRK06725   97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVQ 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 ---YPYFMVEKEMIPTKLPnslmgrvvvwylqnclanlfvgawEPRPEgplpldipqasPQQVQRCVEILSRAKRPLLVL 300
Cdd:PRK06725  177 nekVTSFYNEVVEIPGYKP------------------------EPRPD-----------SMKLREVAKAISKAKRPLLYI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRV 373
Cdd:PRK06725  222 GG-GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLflgmlgmHGTYAANMAVTECDLLLALGVRFDDRVT-GKL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 --LNRKSSIIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEgLQGQMWSSDWAEELRKADQQKEQTYRDKAlmpv 451
Cdd:PRK06725  300 elFSPHSKKVHIDIDPSEFHKNVAV----EYPVVGDVKKALHMLLH-MSIHTQTDEWLQKVKTWKEEYPLSYKQKE---- 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 452 lQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 531
Cdd:PRK06725  371 -SELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGD 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 532 GAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQI---SREQVPRLGSdvacslayTDYHKAAMGLGAQGliLSRD 602
Cdd:PRK06725  450 ASFQMNIQELQTIAENNIPVKVFIINNKflgmvrQWQEMfyeNRLSESKIGS--------PDFVKVAEAYGVKG--LRAT 519
                         570       580
                  ....*....|....*....|...
gi 1318663320 603 NKDQVVKVLREGqqLCQDGHAVV 625
Cdd:PRK06725  520 NSTEAKQVMLEA--FAHEGPVVV 540
PRK06965 PRK06965
acetolactate synthase 3 catalytic subunit; Validated
64-617 6.11e-44

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 180780 [Multi-domain]  Cd Length: 587  Bit Score: 166.13  E-value: 6.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 140
Cdd:PRK06965   23 GAEILMKALAAEGVEFIWGYPGGavlYIYDELYKQDK--IQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 141 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:PRK06965  101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DvlypyfmVEKEMIPTKLPNSLmgrvvvwylqnclanlfvgawEPRPEGPlpldIPQASPQQVQRCVEILSRAKRPLLVL 300
Cdd:PRK06965  181 D-------VSKTPCEYEYPKSV---------------------EMRSYNP----VTKGHSGQIRKAVSLLLSAKRPYIYT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSQALLpPTPANKLRAAVETLGVPCF-----LGGMSR------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDfrls 369
Cdd:PRK06965  229 GGGVIL-ANASRELRQLADLLGYPVTntlmgLGAYPAsdkkflGMLG----MHGTYEANMAMQHCDVLIAIGARFD---- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 370 yGRVLNRKSSIIIVNRNrddlLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQ-----------GQMWSSdwAEE 431
Cdd:PRK06965  300 -DRVIGNPAHFASRPRK----IIHIDIdpssiskRVKVDIPIVGDVKEVLKELIEQLQtaehgpdadalAQWWKQ--IEG 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 432 LRKADQQKEQTYRDKalmpvlqhLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAG 511
Cdd:PRK06965  373 WRSRDCLKYDRESEI--------IKPQYVVEKLWELTDGDAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLP 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 512 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV--IAL----VGNDAGWTQIsrEQVPRLGSDVACSLAytDY 585
Cdd:PRK06965  445 YAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVkiISLnnryLGMVRQWQEI--EYSKRYSHSYMDALP--DF 520
                         570       580       590
                  ....*....|....*....|....*....|..
gi 1318663320 586 HKAAMGLGAQGLILSRdnKDQVVKVLREGQQL 617
Cdd:PRK06965  521 VKLAEAYGHVGMRIEK--TSDVEPALREALRL 550
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
64-601 3.14e-42

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 161.08  E-value: 3.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFtlvGGHI-SPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK06112   16 VAHAIARALKRHGVEQIF---GQSLpSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVAP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFcasVRRVRD---IVPTLRTAIAAAQSGTPGPVFVELP 219
Cdd:PRK06112   93 LAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKW---VRRVTVaerIDDYVDQAFTAATSGRPGPVVLLLP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 220 LDVLypyfmvEKEMIPTKLPNSlmgrvvvwylqnclANLfvGAWeprpegplPLDIPQASPQQVQRCVEILSRAKRPLLV 299
Cdd:PRK06112  170 ADLL------TAAAAAPAAPRS--------------NSL--GHF--------PLDRTVPAPQRLAEAASLLAQAQRPVVV 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 300 LG-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI------------RQNRSAALKKADVVVLAGA 362
Cdd:PRK06112  220 AGggvhiSGA------SAALAALQSLAGLPVATTNMGKGAVDETHPLSLgvvgslmgprspGRHLRDLVREADVVLLVGT 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 363 VCDFRLSYGRVLNRKSSIII--------VNRNRDDLLLNSDifwkPQEAVQGDVGSFMIKLVEGLQGQMWS-SDWAEELR 433
Cdd:PRK06112  294 RTNQNGTDSWSLYPEQAQYIhidvdgeeVGRNYEALRLVGD----ARLTLAALTDALRGRDLAARAGRRAAlEPAIAAGR 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 434 KADQQKEQTYRDKALMPVlqhlNPVWVLQQVEETLPDNALLVVDGG-DFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGF 512
Cdd:PRK06112  370 EAHREDSAPVALSDASPI----RPERIMAELQAVLTGDTIVVADASySSIWVANFLTARRAGMRFLTPRGLAGLGWGVPM 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 513 ALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA--GWtQISREQVpRLGSDV-ACSLAYTDYHKAA 589
Cdd:PRK06112  446 AIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGF-QKHAETV-KFGTHTdACHFAAVDHAAIA 523
                         570
                  ....*....|..
gi 1318663320 590 MGLGAQGLILSR 601
Cdd:PRK06112  524 RACGCDGVRVED 535
PRK08155 PRK08155
acetolactate synthase large subunit;
64-559 1.78e-41

acetolactate synthase large subunit;


Pssm-ID: 181257 [Multi-domain]  Cd Length: 564  Bit Score: 158.72  E-value: 1.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK08155   15 GAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK08155   95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 lypyfmvekemiptklpnslmgrvvvwylQNclANLFVGAWePRPEGPLPldIPQASPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK08155  175 -----------------------------QT--AVIELEAL-PAPAEKDA--APAFDEESIRDAAAMINAAKRPVLYLGG 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRlSYGRV-- 373
Cdd:PRK08155  221 GVINSGAPARARELA-EKAQLPTTMTLMALGMLPKAHPLslgmlgmHGARSTNYILQEADLLIVLGARFDDR-AIGKTeq 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 LNRKSSIIIVNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQMwSSDWAEelRKADQQKEQTYRdkalMPVLQ 453
Cdd:PRK08155  299 FCPNAKIIHVDIDRAEL----GKIKQPHVAIQADVDDVLAQLLPLVEAQP-RAEWHQ--LVADLQREFPCP----IPKAD 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 454 H-LNPVWVLQQVEETLPDNALLVVDGGD---FVATAAYLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLF 529
Cdd:PRK08155  368 DpLSHYGLINAVAACVDDNAIITTDVGQhqmWTAQAYPLNRPR---QWLTSGGLGTMGFGLPAAIGAALANPERKVLCFS 444
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1318663320 530 GDGAFGYSLIEFDTFVRHKVPV-IALVGNDA 559
Cdd:PRK08155  445 GDGSLMMNIQEMATAAENQLDVkIILMNNEA 475
PRK08199 PRK08199
thiamine pyrophosphate protein; Validated
62-564 6.14e-41

thiamine pyrophosphate protein; Validated


Pssm-ID: 181285 [Multi-domain]  Cd Length: 557  Bit Score: 156.96  E-value: 6.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  62 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 140
Cdd:PRK08199    8 RTGGQILVDALRANGVERVFCVPGESYLAVLDALhDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNAS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 141 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:PRK08199   88 IGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DVLYpyfmvekemiptklpnslmGRVVVwylqnclanlfvgaweprPEGPlPLDIPQASP--QQVQRCVEILSRAKRPLL 298
Cdd:PRK08199  168 DVLS-------------------ETAEV------------------PDAP-PYRRVAAAPgaADLARLAELLARAERPLV 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 299 VLG-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-----NRS--AALKKADVVVLAGAvcdf 366
Cdd:PRK08199  210 ILGgsgwtEAA------VADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGDlglgiNPAlaARIREADLVLAVGT---- 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 367 RLsyGRVLNRKSSIIIVNRNRDDLL--------LNSdiFWKPQEAVQGDVGSF--MIKLVEGLQGQMWsSDWAEELRkAD 436
Cdd:PRK08199  280 RL--GEVTTQGYTLLDIPVPRQTLVhvhpdaeeLGR--VYRPDLAIVADPAAFaaALAALEPPASPAW-AEWTAAAH-AD 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 437 QQKEQTYRdkalmPVLQHLNPVWVLQQVEETLPDNALLVVDGGDFvatAAYL---VQPRGPLRWLDPGAfGTLGVGAGFA 513
Cdd:PRK08199  354 YLAWSAPL-----PGPGAVQLGEVMAWLRERLPADAIITNGAGNY---ATWLhrfFRFRRYRTQLAPTS-GSMGYGLPAA 424
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1318663320 514 LGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQI 564
Cdd:PRK08199  425 IAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTI 475
PRK08978 PRK08978
acetolactate synthase 2 catalytic subunit; Reviewed
64-557 2.21e-39

acetolactate synthase 2 catalytic subunit; Reviewed


Pssm-ID: 181601 [Multi-domain]  Cd Length: 548  Bit Score: 152.34  E-value: 2.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:PRK08978    3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:PRK08978   83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDIQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 ypyfmvekemiptklpnslmgrvvvwylqncLANLFVGAWEPRPEGPlpldiPQASPQQVQRCVEILSRAKRPLLVLG-- 301
Cdd:PRK08978  163 -------------------------------LAEGELEPHLTTVENE-----PAFPAAELEQARALLAQAKKPVLYVGgg 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 ---SQAllppTPAnkLRAAVETLGVP--CFLGGMsrGLLGRNHP-----LHIRQNRSA--ALKKADVVVLAGAVCDFRLS 369
Cdd:PRK08978  207 vgmAGA----VPA--LREFLAATGMPavATLKGL--GAVEADHPyylgmLGMHGTKAAnlAVQECDLLIAVGARFDDRVT 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 370 yGRvLNR---KSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDvgsfMIKLVEGLQGQMWSSDWAEELRKADQQKEQTYR 444
Cdd:PRK08978  279 -GK-LNTfapHAKVIHLDIDPAEInkLRQAHV------ALQGD----LNALLPALQQPLNIDAWRQHCAQLRAEHAWRYD 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 445 DKAlmpvlQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAE 524
Cdd:PRK08978  347 HPG-----EAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDT 421
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1318663320 525 VWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 557
Cdd:PRK08978  422 VICVSGDGSFMMNVQELGTIKRKQLPVkIVLLDN 455
PRK07418 PRK07418
acetolactate synthase large subunit;
64-632 2.60e-38

acetolactate synthase large subunit;


Pssm-ID: 236014 [Multi-domain]  Cd Length: 616  Bit Score: 150.20  E-value: 2.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNT 139
Cdd:PRK07418   21 GAYALMDSLKRHGVKHIFGYPGGAILPIydeLYKAEAEGwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 140 VTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 219
Cdd:PRK07418  101 VTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 220 LDV---LYPYFMVEKEMIptKLPnslmgrvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRP 296
Cdd:PRK07418  181 KDVgqeEFDYVPVEPGSV--KPP----------------------GYRPTVKG---------NPRQINAALKLIEEAERP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 297 LLVLGSQALLPPTPANkLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRL- 368
Cdd:PRK07418  228 LLYVGGGAISAGAHAE-LKELAERFQIPVTTTLMGKGAFDEHHPLsvgmlgmHGTAYANFAVTECDLLIAVGARFDDRVt 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 369 -------SYGRVLNrkssIII----VNRNRddlllnsdifwKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQ 437
Cdd:PRK07418  307 gkldefaSRAKVIH----IDIdpaeVGKNR-----------RPDVPIVGDVRKVLVKLLERSLEPTTPPRTQAWLERINR 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 438 QKEqtyrDKALM--PVLQHLNPVWVLQQVEETLPDnALLVVDGGDFVATAA-YLvqPRGPLRWLDPGAFGTLGVGAGFAL 514
Cdd:PRK07418  372 WKQ----DYPLVvpPYEGEIYPQEVLLAVRDLAPD-AYYTTDVGQHQMWAAqFL--RNGPRRWISSAGLGTMGFGMPAAM 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 515 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDaGWTQISRE-QVPRLG-----SDVACSLAytDYHKA 588
Cdd:PRK07418  445 GVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN-GWQGMVRQwQESFYGerysaSNMEPGMP--DFVKL 521
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 1318663320 589 AMGLGAQGLILSrdNKDQVVKVLREgqQLCQDGhAVVVNILIGR 632
Cdd:PRK07418  522 AEAFGVKGMVIS--ERDQLKDAIAE--ALAHDG-PVLIDVHVRR 560
PRK07282 PRK07282
acetolactate synthase large subunit;
53-557 3.19e-38

acetolactate synthase large subunit;


Pssm-ID: 180919 [Multi-domain]  Cd Length: 566  Bit Score: 149.20  E-value: 3.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  53 MHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVT 131
Cdd:PRK07282    1 MEKISLESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFeGIRHILARHEQGALHEAEGYAKSTGKLGVAVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 132 AGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTP 211
Cdd:PRK07282   81 SGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 212 GPVFVELPLDVlypyfmVEKEmipTKLPNSlmgrvvvwylqnclanlfvgaweprPEGPLPLDIPQASPQ--QVQRCVEI 289
Cdd:PRK07282  161 GPVVIDLPKDV------SALE---TDFIYD-------------------------PEVNLPSYQPTLEPNdmQIKKILKQ 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 290 LSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGA 362
Cdd:PRK07282  207 LSKAKKPVILAGG-GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLflgmggmHGSYAANIAMTEADFMINIGS 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 363 VCDFRLSyGRVLNRKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKaDQQKEQT 442
Cdd:PRK07282  286 RFDDRLT-GNPKTFAKNAKVAHIDIDPAEIGKII--KTDIPVVGDAKKALQMLLAEPTVHNNTEKWIEKVTK-DKNRVRS 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 443 YRDKALMpvlqhLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPE 522
Cdd:PRK07282  362 YDKKERV-----VQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPD 436
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1318663320 523 AEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 557
Cdd:PRK07282  437 KEVILFVGDGGFQMTNQELAILNIYKVPIkVVMLNN 472
PRK06456 PRK06456
acetolactate synthase large subunit;
64-596 3.89e-38

acetolactate synthase large subunit;


Pssm-ID: 180569 [Multi-domain]  Cd Length: 572  Bit Score: 149.22  E-value: 3.89e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVA----CEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNT 139
Cdd:PRK06456    4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 140 VTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 219
Cdd:PRK06456   84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 220 LDVLYpyfmvEKemiptklpnslMGRVVvwylqnclanlfvgaWEPRPEGPLPLDIPQ-ASPQQVQRCVEILSRAKRPLL 298
Cdd:PRK06456  164 RDIFY-----EK-----------MEEIK---------------WPEKPLVKGYRDFPTrIDRLALKKAAEILINAERPII 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 299 VLGSQALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPLHI-------RQNRSAALKKADVVVLAGAVCDFR--LS 369
Cdd:PRK06456  213 LVGTGVVWSNATPEVLELA-ELLHIPIVSTFPGKTAIPHDHPLYFgpmgyygRAEASMAALESDAMLVVGARFSDRtfTS 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 370 YGRVLNRKSSIIIVNRNRDDlllnSDIFWKPQEAVQGDVGSF---MIKLVEGLQGQMWSSDWAEELRKADQQKEQTY--- 443
Cdd:PRK06456  292 YDEMVETRKKFIMVNIDPTD----GEKAIKVDVGIYGNAKIIlreLIKAITELGQKRDRSAWLKRVKEYKEYYSQFYyte 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 444 RDKALMPvlqhlnpvW-VLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPE 522
Cdd:PRK06456  368 ENGKLKP--------WkIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPD 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 523 AEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVgNDAGWTQISReQVPRL-------GSDVACSlayTDYHKAAMGLGAQ 595
Cdd:PRK06456  440 KVVVDLDGDGSFLMTGTNLATAVDEHIPVISVI-FDNRTLGLVR-QVQDLffgkrivGVDYGPS---PDFVKLAEAFGAL 514

                  .
gi 1318663320 596 G 596
Cdd:PRK06456  515 G 515
PRK08979 PRK08979
acetolactate synthase 3 large subunit;
64-551 3.97e-38

acetolactate synthase 3 large subunit;


Pssm-ID: 181602 [Multi-domain]  Cd Length: 572  Bit Score: 149.20  E-value: 3.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK08979    6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALhEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK08979   86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK08979  166 LNPAI-----LHPYEYPESIKMR----------------SYNPTTSG---------HKGQIKRGLQALLAAKKPVLYVGG 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHP-------LHIRQNRSAALKKADVVVLAGAVCDFRLSygrvln 375
Cdd:PRK08979  216 GAIISGADKQILQLA-EKLNLPVVSTLMGLGAFPGTHKnslgmlgMHGRYEANMAMHNADLIFGIGVRFDDRTT------ 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 376 rkssiiivnRNRDDLLLNSDIFW---KP---QEAVQGD---VGSF------MIKLVEGlQGQMWSSD----WAEELRKAD 436
Cdd:PRK08979  289 ---------NNLEKYCPNATILHidiDPssiSKTVRVDipiVGSAdkvldsMLALLDE-SGETNDEAaiasWWNEIEVWR 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 437 QQKEQTYRDKAlmpvlQHLNPvwvlQQVEETL----PDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGF 512
Cdd:PRK08979  359 SRNCLAYDKSS-----ERIKP----QQVIETLykltNGDAYVASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPA 429
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1318663320 513 ALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 551
Cdd:PRK08979  430 AMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPV 468
pyruv_oxi_spxB TIGR02720
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ...
64-630 4.14e-38

pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]


Pssm-ID: 213733 [Multi-domain]  Cd Length: 575  Bit Score: 149.22  E-value: 4.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLL--VACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:TIGR02720   1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMdaLSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTpGPVFVELPLD 221
Cdd:TIGR02720  81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHN-GVAVVTIPVD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 vlYPYFMVEKEMiptklpnslmgrvvvWYLQNCLANLFVgaweprpegplpldIPQASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:TIGR02720 160 --FGWQEIPDND---------------YYASSVSYQTPL--------------LPAPDVEAVTRAVQTLKAAERPVIYYG 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVvlaGAVCDFRLSYGRvlNRKSSII 381
Cdd:TIGR02720 209 IGAR---KAGEELEALSEKLKIPLISTGLAKGIIEDRYPAYLGSAYRVAQKPANEA---LFQADLVLFVGN--NYPFAEV 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 382 IVNRNRDDLLLNSDI----FWKPQE---AVQGDVGSFmIKLVEGLQGQMWSSDWAEElRKADQQKEQTYRDKALMPVLQH 454
Cdd:TIGR02720 281 SKAFKNTKYFIQIDIdpakLGKRHHtdiAVLADAKKA-LAAILAQVEPRESTPWWQA-NVANVKNWRAYLASLEDKTEGP 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:TIGR02720 359 LQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAF 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDvacsLAYTDYHKAAMGLGAQGLILsrDNKDQVVKV 610
Cdd:TIGR02720 439 SMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQedtnQPLIGVD----FNDADFAKIAEGVGAVGFRV--NKIEQLPAV 512
                         570       580
                  ....*....|....*....|
gi 1318663320 611 LREGQQLCQdGHAVVVNILI 630
Cdd:TIGR02720 513 FEQAKAIKQ-GKPVLIDAKI 531
PRK07979 PRK07979
acetolactate synthase 3 large subunit;
64-554 9.17e-38

acetolactate synthase 3 large subunit;


Pssm-ID: 181185 [Multi-domain]  Cd Length: 574  Bit Score: 148.07  E-value: 9.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK07979    6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGgIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK07979   86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK07979  166 LNPAN-----KLPYVWPESVSMR----------------SYNPTTQG---------HKGQIKRALQTLVAAKKPVVYVGG 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPAnKLRAAVETLGVPCF-----LGGM------SRGLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSYG 371
Cdd:PRK07979  216 GAINAACHQ-QLKELVEKLNLPVVsslmgLGAFpathrqSLGMLG----MHGTYEANMTMHNADVIFAVGVRFDDRTTNN 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 372 RVLNRKSSIII---VNRNRDDLLLNSDIfwkpqeAVQGDVGSFMIKLVEgLQGQMWSSDWAEELRKADQQKEQTYRDKAL 448
Cdd:PRK07979  291 LAKYCPNATVLhidIDPTSISKTVTADI------PIVGDARQVLEQMLE-LLSQESAHQPLDEIRDWWQQIEQWRARQCL 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 449 M--PVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVW 526
Cdd:PRK07979  364 KydTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVV 443
                         490       500
                  ....*....|....*....|....*...
gi 1318663320 527 CLFGDGAFGYSLIEFDTFVRHKVPVIAL 554
Cdd:PRK07979  444 CVTGDGSIQMNIQELSTALQYELPVLVL 471
PRK06466 PRK06466
acetolactate synthase 3 large subunit;
64-551 1.71e-36

acetolactate synthase 3 large subunit;


Pssm-ID: 180578 [Multi-domain]  Cd Length: 574  Bit Score: 144.12  E-value: 1.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 140
Cdd:PRK06466    6 GAEMLVRALRDEGVEYIYGYPGGavlHIYDALFKQDK--VEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 141 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:PRK06466   84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DVLYPYFMVEKEMiPTKlpnslmgrvvvwylqnclanLFVGAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLL-- 298
Cdd:PRK06466  164 DMTNPAEKFEYEY-PKK--------------------VKLRSYSPAVRG---------HSGQIRKAVEMLLAAKRPVIys 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 299 ----VLGSQALLPPTPANKLRAAVET--LGVPCFLGGMSR--GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDfrlsy 370
Cdd:PRK06466  214 gggvVLGNASALLTELAHLLNLPVTNtlMGLGGFPGTDRQflGMLG----MHGTYEANMAMHHADVILAVGARFD----- 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 371 GRVLNRKSSII----IVNRNRDDLLLNSDIFWK-----PQEAVQGDVGSFMIKLVEGLQGQMWSSDWAE--ELRKA-DQQ 438
Cdd:PRK06466  285 DRVTNGPAKFCpnakIIHIDIDPASISKTIKADipivgPVESVLTEMLAILKEIGEKPDKEALAAWWKQidEWRGRhGLF 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 439 KEQTYRDKALMPvlqhlnpvwvlQQVEETLPD----NALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFAL 514
Cdd:PRK06466  365 PYDKGDGGIIKP-----------QQVVETLYEvtngDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAM 433
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 1318663320 515 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 551
Cdd:PRK06466  434 GVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPV 470
PRK06882 PRK06882
acetolactate synthase 3 large subunit;
64-558 6.13e-36

acetolactate synthase 3 large subunit;


Pssm-ID: 168717 [Multi-domain]  Cd Length: 574  Bit Score: 142.75  E-value: 6.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK06882    6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGgIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK06882   86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK06882  166 VNPAN-----KFTYEYPEEVSLR----------------SYNPTVQG---------HKGQIKKALKALLVAKKPVLFVGG 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTpANKLRAAVETLGVPCF-----LGGMSR------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLS-- 369
Cdd:PRK06882  216 GVITAEC-SEQLTQFAQKLNLPVTsslmgLGAYPStdkqflGMLG----MHGTYEANNAMHESDLILGIGVRFDDRTTnn 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 370 ------YGRVL-----------NRKSSIIIVNRNRDDL-----LLNSDIFWKPQEAVqgdvgsfmiklveglqgqmwsSD 427
Cdd:PRK06882  291 lakycpNAKVIhididptsiskNVPAYIPIVGSAKNVLeeflsLLEEENLAKSQTDL---------------------TA 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 428 WAEELR--KADQQKEQTYRDKALMPvlqhlnpvwvlQQVEETL----PDNALLVVDGGDFVATAAYLVQPRGPLRWLDPG 501
Cdd:PRK06882  350 WWQQINewKAKKCLEFDRTSDVIKP-----------QQVVEAIyrltNGDAYVASDVGQHQMFAALHYPFDKPRRWINSG 418
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1318663320 502 AFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 558
Cdd:PRK06882  419 GAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
PRK07710 PRK07710
acetolactate synthase large subunit;
51-558 7.41e-36

acetolactate synthase large subunit;


Pssm-ID: 236076 [Multi-domain]  Cd Length: 571  Bit Score: 142.21  E-value: 7.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  51 QLMHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAV 130
Cdd:PRK07710    5 RTMSSKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 131 TAGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGT 210
Cdd:PRK07710   85 TSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 211 PGPVFVELPLDVLYP--YFMVEKEM-----IPTKLPNSLmgrvvvwylqnclanlfvgaweprpegplpldipqaspqQV 283
Cdd:PRK07710  165 PGPVLIDIPKDMVVEegEFCYDVQMdlpgyQPNYEPNLL---------------------------------------QI 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 284 QRCVEILSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADV 356
Cdd:PRK07710  206 RKLVQAVSVAKKPVILAGA-GVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPADHPLflgmagmHGTYTANMALYECDL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 357 VVLAGAVCDFRLSyGRVLNRKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKAD 436
Cdd:PRK07710  285 LINIGARFDDRVT-GNLAYFAKEATVAHIDIDPAEIGKNV--PTEIPIVADAKQALQVLLQQEGKKENHHEWLSLLKNWK 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 437 QQKEQTYRDKAlmpvlQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGA 516
Cdd:PRK07710  362 EKYPLSYKRNS-----ESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGA 436
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1318663320 517 KLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 558
Cdd:PRK07710  437 QLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNN 478
PRK07789 PRK07789
acetolactate synthase 1 catalytic subunit; Validated
64-557 6.76e-35

acetolactate synthase 1 catalytic subunit; Validated


Pssm-ID: 236098 [Multi-domain]  Cd Length: 612  Bit Score: 140.12  E-value: 6.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPL---LVACEKLgiRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 140
Cdd:PRK07789   33 GAQAVVRSLEELGVDVVFGIPGGAILPVydpLFDSTKV--RHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 141 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:PRK07789  111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DVLypyfmvEKEMiptklpnslmgrvvvwylqnclanLFvgAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVL 300
Cdd:PRK07789  191 DAL------QAQT------------------------TF--SWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-------NRSAALKKADVVVLAGAVCDfrlsyGRV 373
Cdd:PRK07789  239 GGGVIRAEASA-ELRELAELTGIPVVTTLMARGAFPDSHPQHLGMpgmhgtvAAVAALQRSDLLIALGARFD-----DRV 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 LNRKSSI-----II--------VNRNRddlllNSDIFwkpqeaVQGDVGSFMIKLVEGLQ------GQMWSSDWAEELRK 434
Cdd:PRK07789  313 TGKLDSFapdakVIhadidpaeIGKNR-----HADVP------IVGDVKEVIAELIAALRaehaagGKPDLTAWWAYLDG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 435 ADQQKEQTYRDkalmPVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFAL 514
Cdd:PRK07789  382 WRETYPLGYDE----PSDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAM 457
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1318663320 515 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 557
Cdd:PRK07789  458 GAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIkVALINN 501
ilvB CHL00099
acetohydroxyacid synthase large subunit
75-557 2.54e-34

acetohydroxyacid synthase large subunit


Pssm-ID: 214363 [Multi-domain]  Cd Length: 585  Bit Score: 137.91  E-value: 2.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  75 HGVRFVFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQ 150
Cdd:CHL00099   23 HGVKHIFGYPGGAILPIydeLYAWEKKGlIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 151 SPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV---LYPYF 227
Cdd:CHL00099  103 VPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVgleKFDYY 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 228 MVEKEMIPTKLPnslmgrvvvwylqnclanlfvgAWEPrpegplpldIPQASPQQVQRCVEILSRAKRPLLVLGSQALLP 307
Cdd:CHL00099  183 PPEPGNTIIKIL----------------------GCRP---------IYKPTIKRIEQAAKLILQSSQPLLYVGGGAIIS 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 308 PTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLNRKSSI 380
Cdd:CHL00099  232 DA-HQEITELAELYKIPVTTTLMGKGIFDEDHPLclgmlgmHGTAYANFAVSECDLLIALGARFDDRVT-GKLDEFACNA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 381 IIV-----------NRNrddlllnsdifwkPQEAVQGDVGSFMIKLVEglqgqmwSSDWAEELRKADQQ---KEQTYRDK 446
Cdd:CHL00099  310 QVIhididpaeigkNRI-------------PQVAIVGDVKKVLQELLE-------LLKNSPNLLESEQTqawRERINRWR 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 447 ALMPVL-----QHLNPVWVLQQVEETLPDnALLVVDGGDFVATAAYL--VQPRgplRWLDPGAFGTLGVGAGFALGAKLC 519
Cdd:CHL00099  370 KEYPLLipkpsTSLSPQEVINEISQLAPD-AYFTTDVGQHQMWAAQFlkCKPR---KWLSSAGLGTMGYGLPAAIGAQIA 445
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1318663320 520 QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 557
Cdd:CHL00099  446 HPNELVICISGDASFQMNLQELGTIAQYNLPIkIIIINN 484
PRK08327 PRK08327
thiamine pyrophosphate-requiring protein;
72-561 1.23e-33

thiamine pyrophosphate-requiring protein;


Pssm-ID: 236243 [Multi-domain]  Cd Length: 569  Bit Score: 135.90  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  72 LRAHGVRFVFTLVGGHISPLLVACEK---LGIRVVDT---RHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 145
Cdd:PRK08327   17 LKELGVDYIFINSGTDYPPIIEAKARaraAGRPLPEFvicPHEIVAISMAHGYALVTGKPQAVMVHVDVGTANALGGVHN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 146 AQVAQSPVLLLGGAASTLlqKRGAL-----------QAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPV 214
Cdd:PRK08327   97 AARSRIPVLVFAGRSPYT--EEGELgsrntrihwtqEMRDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAMSEPKGPV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 215 FVELPLDVLypyfmVEKemiptklpnslmgrvvvwylqnclanlfVGAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAK 294
Cdd:PRK08327  175 YLTLPREVL-----AEE----------------------------VPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 295 RPLLV---LGSQALLPPTpankLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVvlagavcdfrlsyg 371
Cdd:PRK08327  222 RPVIItwrAGRTAEGFAS----LRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRADLAEADLV-------------- 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 372 rvlnrkssiiivnrnrddLLLNSDIFWKPQE------------------------------AVQGDVGSFMIKLVEGLQG 421
Cdd:PRK08327  284 ------------------LVVDSDVPWIPKKirpdadarviqidvdplksriplwgfpcdlCIQADTSTALDQLEERLKS 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 422 QMWSSDWAEELRKADQQKEQTYRDKALMPVLQHL------NPVWVLQQVEETLPDNALLVVDGGdFVATAAYLvqpRGPL 495
Cdd:PRK08327  346 LASAERRRARRRRAAVRELRIRQEAAKRAEIERLkdrgpiTPAYLSYCLGEVADEYDAIVTEYP-FVPRQARL---NKPG 421
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1318663320 496 RWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFV--RHKVPVIALVGNDAGW 561
Cdd:PRK08327  422 SYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
PRK09107 PRK09107
acetolactate synthase 3 catalytic subunit; Validated
64-551 2.29e-33

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 236380 [Multi-domain]  Cd Length: 595  Bit Score: 135.22  E-value: 2.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK09107   13 GAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIfQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK09107   93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKDV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 lypYFMVEKEMIPTKLPnslmgrvvvwylqnclanlFVGAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK09107  173 ---QFATGTYTPPQKAP-------------------VHVSYQPKVKG---------DAEAITEAVELLANAKRPVIYSGG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPANK-LRAAVETLGVP--CFLGGMSR---------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSy 370
Cdd:PRK09107  222 GVINSGPEASRlLRELVELTGFPitSTLMGLGAypasgknwlGMLG----MHGTYEANMAMHDCDVMLCVGARFDDRIT- 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 371 GRV-----LNRKSSIII----VNRN-RDDLllnsdifwkpqeAVQGDVGSFMIKLVEGLQGQMWSSD------WAEELRK 434
Cdd:PRK09107  297 GRLdafspNSKKIHIDIdpssINKNvRVDV------------PIIGDVGHVLEDMLRLWKARGKKPDkealadWWGQIAR 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 435 ADQQKEQTYR--DKALMPvlQHlnpvwVLQQVEE-TLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAG 511
Cdd:PRK09107  365 WRARNSLAYTpsDDVIMP--QY-----AIQRLYElTKGRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLP 437
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1318663320 512 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 551
Cdd:PRK09107  438 AALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPV 477
PRK11269 PRK11269
glyoxylate carboligase; Provisional
66-632 3.08e-31

glyoxylate carboligase; Provisional


Pssm-ID: 183066 [Multi-domain]  Cd Length: 591  Bit Score: 128.94  E-value: 3.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLT-GTVGVAAVTAGPGLTNTVTAV 143
Cdd:PRK11269    8 DAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:PRK11269   88 YSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDVQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 ypyfMVEKEmiptklpnslmgrvvvwylqnclanlfvgaWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSq 303
Cdd:PRK11269  168 ----VAEIE------------------------------FDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGG- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 304 ALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL----------HIRQNrsAALKKADVVVLAGAvcdfrlsygRV 373
Cdd:PRK11269  213 GVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLmagmvglqtsHRYGN--ATLLASDFVLGIGN---------RW 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 LNRKSSIIIVNRnRDDLLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQGQMWS------SDWAEEL--RKADQQ 438
Cdd:PRK11269  282 ANRHTGSVEVYT-KGRKFVHVDIeptqigrVFGPDLGIVSDAKAALELLVEVAREWKAAgrlpdrSAWVADCqeRKRTLL 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 439 KEQTYRDkalMPVlqhlNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKL 518
Cdd:PRK11269  361 RKTHFDN---VPI----KPQRVYEEMNKAFGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRA 433
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 519 CQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPrLGSDVACSLAY------------TDYH 586
Cdd:PRK11269  434 ADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQAQRA-FDMDYCVQLAFeninspelngygVDHV 512
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*..
gi 1318663320 587 KAAMGLGAQGLILSRdnKDQVVKVLREGQQLCQDGHA-VVVNILIGR 632
Cdd:PRK11269  513 KVAEGLGCKAIRVFK--PEDIAPALEQAKALMAEFRVpVVVEVILER 557
Gcl COG3960
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];
66-632 3.42e-30

Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 226469 [Multi-domain]  Cd Length: 592  Bit Score: 125.77  E-value: 3.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLT-GTVGVAAVTAGPGLTNTVTAV 143
Cdd:COG3960     8 DAAVYVLEKEGITTAFGVPGAAINPFYSALRKHGgIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:COG3960    88 YSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKWAVTVREPALVPRVLQQAFHLMRSGRPGPVLIDLPFDVQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 ypyfMVEKEmiptklpnslmgrvvvwylqnclanlfvgaWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSq 303
Cdd:COG3960   168 ----VAEIE------------------------------FDPDMYEPLPVYKPAATRVQAEKALAMLIQAERPLIVAGG- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 304 ALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-NRSAALKKADVVVLAGavcDFRLSYG-RVLNRKS-SI 380
Cdd:COG3960   213 GVINADAAALLQEFAELTGVPVIPTLMGWGCIPDDHPLMAGMvGLQTSHRYGNATLLAS---DMVFGIGnRWANRHTgSV 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 381 IIVNRNRDdlLLNSDI-------FWKPQEAVQGDVGSFMIKLVEglQGQMWSS-----DWAEELRKADQQKEQTYRDKAL 448
Cdd:COG3960   290 EVYTEGRK--FIHVDIeptqigrVFCPDLGIVSDAKAALTLLLD--VAQEWKKagklpCRKAWVADCQQRKRTLLRKTHF 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 449 MPVlqHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCL 528
Cdd:COG3960   366 DNV--PVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQFLHVFKPRHWINCGQAGPLGWTIPAALGVCAADPKRNVVAI 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 529 FGDGAFGYSLIEFDTFVRHKVPVIALVGNDAgWTQISREQVPRLGSDVACSLAY------------TDYHKAAMGLGAQG 596
Cdd:COG3960   444 SGDYDFQFLIEELAVGAQFKIPYIHVLVNNA-YLGLIRQAQRAFDMDYCVQLAFeninssevngygVDHVKVAEGLGCKA 522
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 1318663320 597 LILSRDNkdQVVKVLREGQQLCQDGHA-VVVNILIGR 632
Cdd:COG3960   523 IRVFKPE--DIAPAFEQAKALMAQHRVpVVVEVILER 557
PLN02470 PLN02470
acetolactate synthase
62-558 7.51e-29

acetolactate synthase


Pssm-ID: 215261 [Multi-domain]  Cd Length: 585  Bit Score: 121.38  E-value: 7.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  62 RHGGESVAAVLRAHGVRFVFTLVGG-----HISPLLVACeklgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGL 136
Cdd:PLN02470   13 RKGADILVEALEREGVDTVFAYPGGasmeiHQALTRSNC----IRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 137 TNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFV 216
Cdd:PLN02470   89 TNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 217 ELPLDVlypyfmvEKEM-IPT-KLPNSLMGrvvvwYLQNClanlfvgawePRPegplpldiPQASpqQVQRCVEILSRAK 294
Cdd:PLN02470  169 DIPKDI-------QQQLaVPNwNQPMKLPG-----YLSRL----------PKP--------PEKS--QLEQIVRLISESK 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 295 RPLLVLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-------NRSAALKKADVVVLAGAVCDFR 367
Cdd:PLN02470  217 RPVVYVGGGCL---NSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMlgmhgtvYANYAVDSADLLLAFGVRFDDR 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 368 LSyGRV--LNRKSSIIIVNRNRDDLLLNSdifwKPQEAVQGDVG---SFMIKLVEGLQGQMWS-SDWAEELrkaDQQKEQ 441
Cdd:PLN02470  294 VT-GKLeaFASRASIVHIDIDPAEIGKNK----QPHVSVCADVKlalQGLNKLLEERKAKRPDfSAWRAEL---DEQKEK 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 442 ---TYRDKAlmpvlQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKL 518
Cdd:PLN02470  366 fplSYPTFG-----DAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAA 440
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1318663320 519 CQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 558
Cdd:PLN02470  441 ANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
477-626 1.89e-28

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 426974 [Multi-domain]  Cd Length: 151  Bit Score: 111.14  E-value: 1.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 477 DGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVG 556
Cdd:pfam02775   1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663320 557 NDAGWTQISREQVP----RLGSDVACSLAYTDYHKAAMGLGAQGliLSRDNKDQVVKVLREGqqLCQDGHAVVV 626
Cdd:pfam02775  81 NNGGYGMTRGQQTPfgggRYSGPSGKILPPVDFAKLAEAYGAKG--ARVESPEELEEALKEA--LEHDGPALID 150
PRK06457 PRK06457
pyruvate dehydrogenase; Provisional
66-604 2.80e-26

pyruvate dehydrogenase; Provisional


Pssm-ID: 180570 [Multi-domain]  Cd Length: 549  Bit Score: 113.39  E-value: 2.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 145
Cdd:PRK06457    6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLYD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 146 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSgTPGPVFVELPLDVLYp 225
Cdd:PRK06457   86 AKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAIS-KRGVAHINLPVDILR- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 226 yfmvekemiptklpnslMGRvvvwylqnclanlfvgawEPRPEGPLPLDIPQASPQqVQRCVEILSRAKRPLLVLGSQAL 305
Cdd:PRK06457  164 -----------------KSS------------------EYKGSKNTEVGKVKYSID-FSRAKELIKESEKPVLLIGGGTR 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 306 LPPTPANKLraaVETLGVPCF----------------LGGMsrGLLGRNHPLhirqnrsAALKKADVVVLAGAVcdfrLS 369
Cdd:PRK06457  208 GLGKEINRF---AEKIGAPIIytlngkgilpdldpkvMGGI--GLLGTKPSI-------EAMDKADLLIMLGTS----FP 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 370 YGRVLNRKSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDVGSFMI--------KLVEGLQGQMwsSDWAEELRKADQQk 439
Cdd:PRK06457  272 YVNFLNKSAKVIQVDIDNSNIgkRLDVDL------SYPIPVAEFLNidieeksdKFYEELKGKK--EDWLDSISKQENS- 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 440 eqtyRDKALmpvlqhlNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC 519
Cdd:PRK06457  343 ----LDKPM-------KPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFA 411
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 520 -QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDvacsLAYTDYHKAAMGLGA 594
Cdd:PRK06457  412 vENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQevmgYPEWGVD----LYNPDFTKIAESIGF 487
                         570
                  ....*....|
gi 1318663320 595 QGLILSRDNK 604
Cdd:PRK06457  488 KGFRLEEPKE 497
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
460-626 2.51e-24

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: 100.02  E-value: 2.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 460 VLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLI 539
Cdd:cd00568     2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 540 EFDTFVRHKVPVIALVGNDAGWTQISREQVPRL-GSDVACSLAYTDYHKAAMGLGAQGLILSRDnkDQVVKVLREGQQlc 618
Cdd:cd00568    82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYgGRVSGTDLSNPDFAALAEAYGAKGVRVEDP--EDLEAALAEALA-- 157

                  ....*...
gi 1318663320 619 QDGHAVVV 626
Cdd:cd00568   158 AGGPALIE 165
TPP_Xsc_like cd02013
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ...
455-633 2.66e-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: 100.66  E-value: 2.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:cd02013     4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSD-VACSLAYTDYHKAAMGLGAQGLILsrDNKDQVVKVLRE 613
Cdd:cd02013    84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITV--DKPEDVGPALQK 161
                         170       180
                  ....*....|....*....|
gi 1318663320 614 GQQLCQDGHAVVVNILIGRT 633
Cdd:cd02013   162 AIAMMAEGKTTVIEIVCDQE 181
TPP_PYR_POX cd07039
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ...
65-222 5.68e-24

Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.


Pssm-ID: 132922 [Multi-domain]  Cd Length: 164  Bit Score: 98.78  E-value: 5.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  65 GESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:cd07039     3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGkIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRR---VRDIVPT-LRTAIAaaqsgTPGPVFVELP 219
Cdd:cd07039    83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSpeqLPELLDRaIRTAIA-----KRGVAVLILP 157

                  ...
gi 1318663320 220 LDV 222
Cdd:cd07039   158 GDV 160
TPP_POX cd02014
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...
455-630 1.59e-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: 94.90  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:cd02014     2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILsrDNKDQVVKVLREG 614
Cdd:cd02014    82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRV--EDPDELEAALDEA 159
                         170
                  ....*....|....*.
gi 1318663320 615 QQlcQDGhAVVVNILI 630
Cdd:cd02014   160 LA--ADG-PVVIDVVT 172
PRK08611 PRK08611
pyruvate oxidase; Provisional
64-596 5.08e-22

pyruvate oxidase; Provisional


Pssm-ID: 181502 [Multi-domain]  Cd Length: 576  Bit Score: 100.46  E-value: 5.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC--EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:PRK08611    6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSgTPGPVFVELPLD 221
Cdd:PRK08611   86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYE-KKGVAVLTIPDD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VLypyfmVEKEMIPTKLPNSLMgrvvvwylqnclanlfvgaweprpegplPLDIPQASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:PRK08611  165 LP-----AQKIKDTTNKTVDTF----------------------------RPTVPSPKPKDIKKAAKLINKAKKPVILAG 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQAllpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-----NRSA--ALKKADVVVLAGAvcDFrlSYGRVL 374
Cdd:PRK08611  212 LGA---KHAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNlgkigTKPAyeAMQEADLLIMVGT--NY--PYVDYL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 375 NRKSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDVGSFM------IKLVE------GLQGQMwsSDWAEELRKADQQKE 440
Cdd:PRK08611  285 PKKAKAIQIDTDPANIgkRYPVNV------GLVGDAKKALhqltenIKHVEdrrfleACQENM--AKWWKWMEEDENNAS 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 441 QTYRDKALMPVLQhlnpvwvlqqveETLPDNALLVVD-GGDFVATAAYL-VQPRGPL---RWLdpgafGTLGVGAGFALG 515
Cdd:PRK08611  357 TPIKPERVMAAIQ------------KIADDDAVLSVDvGTVTVWSARYLnLGTNQKFiisSWL-----GTMGCGLPGAIA 419
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 516 AKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQ 595
Cdd:PRK08611  420 AKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELEYAIDLSDMDYAKFAEACGGK 499

                  .
gi 1318663320 596 G 596
Cdd:PRK08611  500 G 500
IolD COG3962
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ...
106-594 1.28e-21

TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];


Pssm-ID: 226471 [Multi-domain]  Cd Length: 617  Bit Score: 99.39  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 106 RHEVTAVFAADAVARLTGTVGVAAVTA--GPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMS------ 177
Cdd:COG3962    63 HNEQGMAHAAIAYAKQHRRRRIYAVTSsiGPGAANMVTAAALAHVNRLPVLLLPGDVFATRQPDPVLQQLEQFGdgtitt 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 178 --LFRPLCKFCASVRRVRDIVPTLRTAIAA-AQSGTPGPVFVELPLDVL-----YP-YFMVEKemiptklpnslmgrvvV 248
Cdd:COG3962   143 ndCFRPVSRYFDRITRPEQLMSALPRAMRVmTDPADCGPVTLALCQDVQaeaydYPeSFFEKR----------------V 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 249 WYlqnclanlfvgaweprpegplpLDIPQASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPAnKLRAAVETLGVPCFLG 328
Cdd:COG3962   207 WR----------------------IRRPPPDERELADAAALIKSAKKPLIVAGGGVLYSGARE-ALRAFAETHGIPVVET 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 329 GMSRGLLGRNHPLHI---------RQNRSAAlkKADVVVLAGA-VCDFRLSyGRVLNRKSSIIIVNRNRDDLllnsDIFW 398
Cdd:COG3962   264 QAGKSALAWDHPLNLggvgvtgtlAANRAAE--EADLVIGIGTrLQDFTTG-SKALFKNPGVKFLNLNVQPF----DAYK 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 399 KPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKAdqqkEQTYRDKALMPVLQHLNP------VWVLQQVEETLPDNA 472
Cdd:COG3962   337 HDALPLVADARAGLEALSEALGGYRTAAGWTDERERL----KAAWDAEADAPTAKNHFLntlptqTQVIGAVQRTISDDS 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 473 LLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVI 552
Cdd:COG3962   413 VVVCAAGSLPGDLHKLWRAGVPGTYHLEYGFSCMGYEIAGGLGAKAAEPDREVYVMVGDGSYMMLNSELATSVMLGKKII 492
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1318663320 553 ALVGNDAGWTQISREQVPRLGSDVACSLAYT---------DYHKAAMGLGA 594
Cdd:COG3962   493 VVLLDNRGYGCINRLQMATGGASFNNLLRDTdheeeilqvDFAAHAESYGA 543
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
68-219 4.56e-18

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: 81.62  E-value: 4.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  68 VAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNA 146
Cdd:cd06586     3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADA 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1318663320 147 QVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGtPGPVFVELP 219
Cdd:cd06586    82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLP 153
TPP_enzyme_M pfam00205
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ...
283-415 2.22e-16

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: 76.06  E-value: 2.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 283 VQRCVEILSRAKRPLLVLGSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKAD 355
Cdd:pfam00205   1 IEKAAELLKKAKRPVILAGGGVRRSGA-SEELRELAEKLGIPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALEEAD 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1318663320 356 VVVLAGAVCDFRLSYGRV--LNRKSSIIIVNRNRDDLLLNSdifwKPQEAVQGDVGSFMIKL 415
Cdd:pfam00205  80 LVLAVGARFDDIRTTGKLpeFAPDAKIIHIDIDPAEIGKNY----PVDVPIVGDAKETLEAL 137
PRK07092 PRK07092
benzoylformate decarboxylase; Reviewed
59-561 1.98e-15

benzoylformate decarboxylase; Reviewed


Pssm-ID: 235931 [Multi-domain]  Cd Length: 530  Bit Score: 79.23  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  59 TSIRHggeSVAAVLRAHGVRFVFTLVGGHISPLLVACEKlGIRVVDTRHEVTAVFAADAVARLTGTVGV----AAVTAGP 134
Cdd:PRK07092   12 TTVRD---ATIDLLRRFGITTVFGNPGSTELPFLRDFPD-DFRYVLGLQEAVVVGMADGYAQATGNAAFvnlhSAAGVGN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 135 GLTNTVTAVKNaqvaQSP-VLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGP 213
Cdd:PRK07092   88 AMGNLFTAFKN----HTPlVITAGQQARSILPFEPFLAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 214 VFVELPLDvlypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEpRPEGPLPL-DIPQA---SPQQVQRCVEI 289
Cdd:PRK07092  164 VFVSIPYD----------------------------------------DWD-QPAEPLPArTVSSAvrpDPAALARLGDA 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 290 LSRAKRPLLVLGsqALLPPTPANKLRAAV-ETLGVPCFLGGMS-RGLLGRNHPLH------IRQNRSAALKKADVVVLAG 361
Cdd:PRK07092  203 LDAARRPALVVG--PAVDRAGAWDDAVRLaERHRAPVWVAPMSgRCSFPEDHPLFagflpaSREKISALLDGHDLVLVIG 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 362 AVCdFRL---SYGRVLNRKSSIIIVNrnrDDLLLNSdifWKPQ-EAVQGDVGSFMIKLVEGLqgqmwssdwAEELRKADQ 437
Cdd:PRK07092  281 APV-FTYhveGPGPHLPEGAELVQLT---DDPGEAA---WAPMgDAIVGDIRLALRDLLALL---------PPSARPAPP 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 438 QKEQTYRDKALMPVlqhLNPVWVLQQVEETLPDNALLVVDggdfvATAAYLV-QPRgpLRWLDPGAF-----GTLGVGAG 511
Cdd:PRK07092  345 ARPMPPPAPAPGEP---LSVAFVLQTLAALRPADAIVVEE-----APSTRPAmQEH--LPMRRQGSFytmasGGLGYGLP 414
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 1318663320 512 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGW 561
Cdd:PRK07092  415 AAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRY 464
PRK06546 PRK06546
pyruvate dehydrogenase; Provisional
66-625 6.62e-15

pyruvate dehydrogenase; Provisional


Pssm-ID: 180614 [Multi-domain]  Cd Length: 578  Bit Score: 77.72  E-value: 6.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVK 144
Cdd:PRK06546    7 EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRtGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 145 NAQVAQSPVLLLggaASTLLQKR---GALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGtPGPVFVELPLD 221
Cdd:PRK06546   87 DAHRSGAPVLAI---ASHIPSAQigsGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAG-GGVSVVTLPGD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VlypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPLDIPQA------SPQQVQRCVEILSRAKR 295
Cdd:PRK06546  163 I---------------------------------------ADEPAPEGFAPSVISPRrptvvpDPAEVRALADAINEAKK 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 296 PLLVLGS---------QALlpptpANKLRAAV-ETLGVPCFLG-------GMSrGLLGRNHPlhirqnrSAALKKADVVV 358
Cdd:PRK06546  204 VTLFAGAgvrgahaevLAL-----AEKIKAPVgHSLRGKEWIQydnpfdvGMS-GLLGYGAA-------HEAMHEADLLI 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 359 LAGAvcDFrlSYGRVLNRKsSIIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQ 438
Cdd:PRK06546  271 LLGT--DF--PYDQFLPDV-RTAQVDIDPEHLGRRTRV----DLAVHGDVAETIRALLPLVKEKTDRRFLDRMLKKHARK 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 439 KEQ---TYRDKalmpVLQH--LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLdpGAF--GTLGVGAG 511
Cdd:PRK06546  342 LEKvvgAYTRK----VEKHtpIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRRRVI--GSFrhGSMANALP 415
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 512 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDVacslAYTDYHK 587
Cdd:PRK06546  416 HAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMlvdgLPDFGTDH----PPVDYAA 491
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 1318663320 588 AAMGLGAQGLILSrDNKDqVVKVLREGqqLCQDGHAVV 625
Cdd:PRK06546  492 IAAALGIHAVRVE-DPKD-VRGALREA--FAHPGPALV 525
TPP_ALS cd02010
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ...
457-626 1.57e-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: 71.94  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 457 PVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGY 536
Cdd:cd02010     1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 537 SLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILSrdNKDQVVKVLREGqq 616
Cdd:cd02010    81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIE--SADDLLPVLERA-- 156
                         170
                  ....*....|
gi 1318663320 617 LCQDGHAVVV 626
Cdd:cd02010   157 LAADGVHVID 166
PRK08273 PRK08273
thiamine pyrophosphate protein; Provisional
72-534 6.86e-14

thiamine pyrophosphate protein; Provisional


Pssm-ID: 181344 [Multi-domain]  Cd Length: 597  Bit Score: 74.56  E-value: 6.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  72 LRAHGVRFVFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVA 149
Cdd:PRK08273   13 LREWGVRRVFGYPGDGINGLLGALGRADdkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYDAKLD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 150 QSPVLLLGGAastllQKRGAL-----QAIDQMSLFR----PLCKFCASVRRVRDIVP-TLRTAIAaaqsgTPGPVFVELP 219
Cdd:PRK08273   93 HVPVVAIVGQ-----QARAALgghyqQEVDLQSLFKdvagAFVQMVTVPEQLRHLVDrAVRTALA-----ERTVTAVILP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 220 LDVL---YPYFMVEKEMIPTKLPNSlMGRVVvwylqnclanlfvgawePRPEgplpldipqaspqQVQRCVEILSRAKRP 296
Cdd:PRK08273  163 NDVQeleYEPPPHAHGTVHSGVGYT-RPRVV-----------------PYDE-------------DLRRAAEVLNAGRKV 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 297 LLVLGSQALlppTPANKLRAAVETLGvpcflGGMSRGLLGRnhplhirqnrsAALKKaDVVVLAGAVcdfrlsyGrVLNR 376
Cdd:PRK08273  212 AILVGAGAL---GATDEVIAVAERLG-----AGVAKALLGK-----------AALPD-DLPWVTGSI-------G-LLGT 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 377 KSSIIIVnRNRDDLLLNSDIF----WKPQE----AVQGDVGSFMIKL---VE-GLQG--------------QMWSSDWAE 430
Cdd:PRK08273  264 KPSYELM-RECDTLLMVGSSFpyseFLPKEgqarGVQIDIDGRMLGLrypMEvNLVGdaaetlrallplleRKKDRSWRE 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 431 ELRKADQQKEQTYRDKALMPVlQHLNPVWVLQQVEETLPDNALLVVDGGDfVAT--AAYLVQPRGPLRWLDpGAFGTLGV 508
Cdd:PRK08273  343 RIEKWVARWWETLEARAMVPA-DPVNPQRVFWELSPRLPDNAILTADSGS-CANwyARDLRMRRGMMASLS-GTLATMGP 419
                         490       500
                  ....*....|....*....|....*.
gi 1318663320 509 GAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:PRK08273  420 AVPYAIAAKFAHPDRPVIALVGDGAM 445
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
455-630 7.87e-14

Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238960 [Multi-domain]  Cd Length: 178  Bit Score: 69.93  E-value: 7.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:cd02002     1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWtQISREQVPRLGSDVACSLAY---------TDYHKAAMGLGAQGLILSRdnKD 605
Cdd:cd02002    80 MYTIQALWTAARYGLPVTVVILNNRGY-GALRSFLKRVGPEGPGENAPdgldlldpgIDFAAIAKAFGVEAERVET--PE 156
                         170       180
                  ....*....|....*....|....*
gi 1318663320 606 QVVKVLREGQqlcQDGHAVVVNILI 630
Cdd:cd02002   157 ELDEALREAL---AEGGPALIEVVV 178
PDC1 COG3961
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
76-567 1.45e-13

TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 226470 [Multi-domain]  Cd Length: 557  Bit Score: 73.52  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  76 GVRFVFTLVGGHISPLLVA-CEKLGIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNAQVAQSPVL 154
Cdd:COG3961    18 GIKSIFGVPGDYNLSLLDKiYSVPGLRWVGNANELNAAYAADGYARLNG-ISALVTTFGVGELSALNGIAGSYAEHVPVV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 155 LLGGAASTLLQKRGAL--------QAIDQMSLFRPLCkfCASV------RRVRDIVPTLRTAIAAAQsgtpgPVFVELPL 220
Cdd:COG3961    97 HIVGVPTTSAQASGLLlhhtlgdgDFKVFHRMSKEIT--CAQAmltdinTAPREIDRVIRTALKQRR-----PVYIGLPA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DVLYpyfmvekemiptklpnslmgrvvvwylQNClanlfvgawePRPEGPLPLDIPQASPQQ----VQRCVEILSRAKRP 296
Cdd:COG3961   170 DVAD---------------------------LPI----------EAPLTPLDLQLKTSDPEAlsevIDTIAELINKAKKP 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 297 LLVLGsqallPPTPANKLRAAVETL----GVPCFLGGMSRGLLGRNHPLHIRQ-NRSAALKKADVVVlagAVCDFRLSYG 371
Cdd:COG3961   213 VILAD-----ALVSRFGLEKELKKLinatGFPVATLPMGKGVIDESHPNYLGVyNGKLSEPEVREAV---ESADLILTIG 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 372 RVLNRKSSIIIVNR-NRDDLLlnsdifwkpqeavqgDVGSFMIKLVEGLQGQMWSSDWAEELRKAdqqkeQTYRDKALMP 450
Cdd:COG3961   285 VLLTDFNTGGFTYQyKPANII---------------EIHPDSVKIKDAVFTNLSMKDALQELAKK-----IDKRNLSAPP 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 451 VLQH--------------LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGpLRWLDPGAFGTLGVGAGFALGA 516
Cdd:COG3961   345 VAYPartpptpyppanepLTQEWLWNTVQNFLKPGDVIIAETGTSFFGALDIRLPKG-ATFISQPLWGSIGYTLPAALGA 423
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1318663320 517 KLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTqISRE 567
Cdd:COG3961   424 ALAAPDRRVILFIGDGSLQLTVQEISTMIRWGLKPIIFVLNNDGYT-IERA 473
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
455-557 4.15e-13

Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.


Pssm-ID: 238973 [Multi-domain]  Cd Length: 186  Bit Score: 67.91  E-value: 4.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGD---FVATAAYLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 531
Cdd:cd02015     1 IKPQEVIKELSELTPGDAIVTTDVGQhqmWAAQYYRFKKPR---SWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGD 77
                          90       100
                  ....*....|....*....|....*.
gi 1318663320 532 GAFGYSLIEFDTFVRHKVPVIALVGN 557
Cdd:cd02015    78 GSFQMNIQELATAAQYNLPVKIVILN 103
TPP_PYR_PDC_IPDC_like cd07038
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ...
72-219 2.93e-12

Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.


Pssm-ID: 132921 [Multi-domain]  Cd Length: 162  Bit Score: 64.82  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  72 LRAHGVRFVFTLVGGHISPLL-VACEKLGIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNAQVAQ 150
Cdd:cd07038     7 LKQLGVKHVFGVPGDYNLPLLdAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 151 SPVLLLGGAASTLLQKRGA-----LQAID---QMSLFRPLCkfCASVRRVRDIVPT------LRTAIAAAQsgtpgPVFV 216
Cdd:cd07038    86 VPVVHIVGAPSTKAQASGLllhhtLGDGDfdvFLKMFEEIT--CAAARLTDPENAAeeidrvLRTALRESR-----PVYI 158

                  ...
gi 1318663320 217 ELP 219
Cdd:cd07038   159 EIP 161
TPP_PDC_IPDC cd02005
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ...
459-634 1.09e-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: 63.71  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 459 WVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGpLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSL 538
Cdd:cd02005     6 RLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKG-TRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 539 IEFDTFVRHKVPVIALVGNDAGWT---QISREQVPrlgsdvacslaYTD-----YHKAAMGLGAQGLILSRD--NKDQVV 608
Cdd:cd02005    85 QELSTMIRYGLNPIIFLINNDGYTierAIHGPEAS-----------YNDianwnYTKLPEVFGGGGGGLSFRvkTEGELD 153
                         170       180
                  ....*....|....*....|....*.
gi 1318663320 609 KVLREGQQLCqdGHAVVVNILIGRTD 634
Cdd:cd02005   154 EALKDALFNR--DKLSLIEVILPKDD 177
PRK12474 PRK12474
hypothetical protein; Provisional
64-595 2.66e-11

hypothetical protein; Provisional


Pssm-ID: 139002 [Multi-domain]  Cd Length: 518  Bit Score: 66.43  E-value: 2.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK12474    7 GADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVpRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVL-LLGGAASTLLQKRGALQAiDQMSLFRPLCKFcasVRRVRD---IVPTLRTAIAAAQSGTPGPVFVEL 218
Cdd:PRK12474   87 LHNARRAASPIVnIVGDHAVEHLQYDAPLTS-DIDGFARPVSRW---VHRSASagaVDSDVARAVQAAQSAPGGIATLIM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 219 PLDVlypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPL-DIPQA--SPQQVQRCVEILSRAKR 295
Cdd:PRK12474  163 PADV---------------------------------------AWNEAAYAAQPLrGIGPApvAAETVERIAALLRNGKK 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 296 PLLVLGSQALL--PPTPANKLRAAVetlGVPCFLGGMS-RGLLGRNH-PL----HIRQNRSAALKKADVVVLAGAvcDFR 367
Cdd:PRK12474  204 SALLLRGSALRgaPLEAAGRIQAKT---GVRLYCDTFApRIERGAGRvPIeripYFHEQITAFLKDVEQLVLVGA--KPP 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 368 LSYGRVLNRKSSIIIVNRNRDDLLlnsdifwKPQEavqgdvgsfmiKLVEGLQgqmwssDWAEELrkaDQQKEQTYRDKA 447
Cdd:PRK12474  279 VSFFAYPGKPSWGAPPGCEIVYLA-------QPDE-----------DLAQALQ------DLADAV---DAPAEPAARTPL 331
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 448 LMPVLQH--LNPVWVLQQVEETLPDNAlLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEV 525
Cdd:PRK12474  332 ALPALPKgaLNSLGVAQLIAHRTPDQA-IYADEALTSGLFFDMSYDRARPHTHLPLTGGSIGQGLPLAAGAAVAAPDRKV 410
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1318663320 526 WCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREqVPRLGSDVACSLAYT---------DYHKAAMGLGAQ 595
Cdd:PRK12474  411 VCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGE-LQRVGAQGAGRNALSmldlhnpelNWMKIAEGLGVE 488
PRK07586 PRK07586
acetolactate synthase large subunit;
64-362 9.25e-11

acetolactate synthase large subunit;


Pssm-ID: 236063 [Multi-domain]  Cd Length: 514  Bit Score: 64.48  E-value: 9.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK07586    3 GAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVpGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLAN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK07586   83 LHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVATLILPADV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 lypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEP--RPEGPLPL-DIPQASPQQVQRCVEILSRAKRPLLV 299
Cdd:PRK07586  163 ---------------------------------------AWSEggPPAPPPPApAPAAVDPAAVEAAAAALRSGEPTVLL 203
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 300 LGSQALLPPTPANKLRAAVET---LGVPCFLGGMSRGlLGRNH----PLHIRQNRsAALKKADVVVLAGA 362
Cdd:PRK07586  204 LGGRALRERGLAAAARIAAATgarLLAETFPARMERG-AGRPAverlPYFAEQAL-AQLAGVRHLVLVGA 271
PRK09124 PRK09124
ubiquinone-dependent pyruvate dehydrogenase;
68-559 5.24e-10

ubiquinone-dependent pyruvate dehydrogenase;


Pssm-ID: 181661 [Multi-domain]  Cd Length: 574  Bit Score: 62.31  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  68 VAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNA 146
Cdd:PRK09124    9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGtIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 147 QVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAqSGTPGPVFVELPLDVLYpy 226
Cdd:PRK09124   89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKA-ILNRGVAVVVLPGDVAL-- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 227 fmvekEMIPTKLPnslmgrvVVWYlqnclanlfvgaweprpEGPLPLDIPQASpqQVQRCVEILSRAKRPLLVLGS---Q 303
Cdd:PRK09124  166 -----KPAPERAT-------PHWY-----------------HAPQPVVTPAEE--ELRKLAALLNGSSNITLLCGSgcaG 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 304 AllpptpANKLRAAVETLGVPC---------------FLGGMSrGLLGRNHPLHirqnrsaALKKADVVVLAGavCDFrl 368
Cdd:PRK09124  215 A------HDELVALAETLKAPIvhalrgkehveydnpYDVGMT-GLIGFSSGYH-------AMMNCDTLLMLG--TDF-- 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 369 SYGRVLNRKSSIIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEGLQgqmwssdwaeelRKADqqkeQTYRDKAL 448
Cdd:PRK09124  277 PYRQFYPTDAKIIQIDINPGSLGRRSPV----DLGLVGDVKATLAALLPLLE------------EKTD----RKFLDKAL 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 449 M----------------PVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGF 512
Cdd:PRK09124  337 EhyrkarkglddlavpsDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQ 416
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1318663320 513 ALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA 559
Cdd:PRK09124  417 ALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNS 463
MenD COG1165
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ...
72-560 6.61e-07

2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism];


Pssm-ID: 224087 [Multi-domain]  Cd Length: 566  Bit Score: 52.33  E-value: 6.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  72 LRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQ 150
Cdd:COG1165    18 LARLGVRDVVICPGSRSTPLALAAAAHdAITVHVHIDERSAGFFALGLAKASKRPVAVICTSGTAVANLYPAVIEANLSR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 151 SPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLR----TAIAAAQSGT---PGPVFVELPLDV- 222
Cdd:COG1165    98 VPLIVLTADRPPELRGCGANQAIDQTGLFGSYVRASIDLPLPEDDIEALWylrtIASAAAQQARtphAGPVHINVPFREp 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPyfmvekEMIPTKLPNSLMgrvvvwylqnclanlfvgawepRPEGPLPLDIPQASPQQVQRCVEI--LSRAKRPLLVL 300
Cdd:COG1165   178 LVP------DLEPEGAGTPWG----------------------RPLGHWWFYTGPWTVDQGPDLLSEwfFWRQKRGVIVA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSqalLPPTPANKLRAAVETLGVPCFLGGMSrGLlgRNHPLH----IRQNRSAALKKADVVVLAGAvcdfRLSYGRVLNR 376
Cdd:COG1165   230 GR---MSAQEGKGILALANTLGWPILADPLS-PL--RNYIPCydlwLANPKAAEKLRPDIVIQFGS----PPTSKRLLQW 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 377 KSS-----IIIVNRNRDdlllNSDIFWKPQEAVQGDVGSFMIKLVEGLQGQmwsSDWAEELRKADQQKEQTYRDKALMPV 451
Cdd:COG1165   300 LADtepieYWVVDPGGG----WLDPSHHATTRLSADVATWARSIHPAGRIR---KPWLDEWLALNEKARQAVRDQLAAEA 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 452 LQHLNPVWVLQqveETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDP-GAFGTLGVGAGfALGAKLCQpEAEVWCLFG 530
Cdd:COG1165   373 LTEAHLAAALA---DLLPPQDQLFVGNSMPVRDVDALGQLPAGYRVYSNrGASGIDGTVST-ALGIARAT-QKPTVALIG 447
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1318663320 531 DGAFGYSLIEFDTFVRHKVP-VIALVGNDAG 560
Cdd:COG1165   448 DLSFLHDLNGLLLLKKVPQPlTIVVVNNNGG 478
TPP_Gcl cd02006
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ...
485-632 1.05e-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: 46.89  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 485 AAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAgWTQI 564
Cdd:cd02006    38 GAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNA-YLGL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 565 SREQVPRLGSDVACSLAY------------TDYHKAAMGLGAQGLILSRDNkdQVVKVLREGQQLCQDGHA-VVVNILIG 631
Cdd:cd02006   117 IRQAQRAFDMDYQVNLAFeninsselggygVDHVKVAEGLGCKAIRVTKPE--ELAAAFEQAKKLMAEHRVpVVVEAILE 194

                  .
gi 1318663320 632 R 632
Cdd:cd02006   195 R 195
TPP_PYR_MenD cd07037
Pyrimidine (PYR) binding domain of ...
72-220 1.67e-05

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: 45.57  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320  72 LRAHGVRFVFTLVGGHISPLLVACEKLG-IRV---VDTRhevTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQ 147
Cdd:cd07037     7 LKRLGVRDVVISPGSRSAPLALAAAEHPeFRLhvrVDER---SAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEAY 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1318663320 148 VAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVR------RVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:cd07037    84 YSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddDLWYLLRLANRAVLEALSAPPGPVHLNLPF 162
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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