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Conserved domains on  [gi|515236|pdb|1PYD|A]
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Chain A, PYRUVATE DECARBOXYLASE

Protein Classification

alpha-keto acid decarboxylase family protein( domain architecture ID 11467699)

alpha-keto acid decarboxylase is a thiamine pyrophosphate enzyme that catalyzes the decarboxylation of an alpha-keto acid (or 2-oxo acid) to yield the corresponding aldehyde, such as pyruvate decarboxylase or branched-chain keto acid decarboxylase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDC1 COG3961
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
1-556 0e+00

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: 933.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELS 80
Cdd:COG3961   1 SSPITVGDYLFDRLAQLGIKSIFGVPGDYNLSLLDKIYSVPGLRWVGNANELNAAYAADGYARLNGISALVTTFGVGELS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       81 ALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQ 160
Cdd:COG3961  81 ALNGIAGSYAEHVPVVHIVGVPTTSAQASGLLLHHTLGDGDFKVFHRMSKEITCAQAMLTDINTAPREIDRVIRTALKQR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      161 RPVYLGLPANLVDLNVPAKLlqTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQF 240
Cdd:COG3961 161 RPVYIGLPADVADLPIEAPL--TPLDLQLKTSDPEALSEVIDTIAELINKAKKPVILADALVSRFGLEKELKKLINATGF 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      241 PAFVTPMGKGSISEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNAT 320
Cdd:COG3961 239 PVATLPMGKGVIDESHPNYLGVYNGKLSEPEVREAVESADLILTIGVLLTDFNTGGFTYQYKPANIIEIHPDSVKIKDAV 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      321 FPGVQMKFVLQKLLTNIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTF 400
Cdd:COG3961 319 FTNLSMKDALQELAKKIDKRNLSAPPVAYPARTPPTPYPPANEPLTQEWLWNTVQNFLKPGDVIIAETGTSFFGALDIRL 398
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      401 PNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLI 480
Cdd:COG3961 399 PKGATFISQPLWGSIGYTLPAALGAALAA----PDRRVILFIGDGSLQLTVQEISTMIRWGLKPIIFVLNNDGYTIERAI 474
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PYD_A      481 HGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIMLPVFDAPQNLVKQAKLT 556
Cdd:COG3961 475 HGPTAPYNDIQSWDYTALPEAFGAKNGEAKFRATTGEELALALDVAFANNDRIRLIEVMLPVLDAPELLIDQAKAT 550
 
Name Accession Description Interval E-value
PDC1 COG3961
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
1-556 0e+00

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: 933.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELS 80
Cdd:COG3961   1 SSPITVGDYLFDRLAQLGIKSIFGVPGDYNLSLLDKIYSVPGLRWVGNANELNAAYAADGYARLNGISALVTTFGVGELS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       81 ALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQ 160
Cdd:COG3961  81 ALNGIAGSYAEHVPVVHIVGVPTTSAQASGLLLHHTLGDGDFKVFHRMSKEITCAQAMLTDINTAPREIDRVIRTALKQR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      161 RPVYLGLPANLVDLNVPAKLlqTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQF 240
Cdd:COG3961 161 RPVYIGLPADVADLPIEAPL--TPLDLQLKTSDPEALSEVIDTIAELINKAKKPVILADALVSRFGLEKELKKLINATGF 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      241 PAFVTPMGKGSISEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNAT 320
Cdd:COG3961 239 PVATLPMGKGVIDESHPNYLGVYNGKLSEPEVREAVESADLILTIGVLLTDFNTGGFTYQYKPANIIEIHPDSVKIKDAV 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      321 FPGVQMKFVLQKLLTNIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTF 400
Cdd:COG3961 319 FTNLSMKDALQELAKKIDKRNLSAPPVAYPARTPPTPYPPANEPLTQEWLWNTVQNFLKPGDVIIAETGTSFFGALDIRL 398
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      401 PNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLI 480
Cdd:COG3961 399 PKGATFISQPLWGSIGYTLPAALGAALAA----PDRRVILFIGDGSLQLTVQEISTMIRWGLKPIIFVLNNDGYTIERAI 474
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PYD_A      481 HGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIMLPVFDAPQNLVKQAKLT 556
Cdd:COG3961 475 HGPTAPYNDIQSWDYTALPEAFGAKNGEAKFRATTGEELALALDVAFANNDRIRLIEVMLPVLDAPELLIDQAKAT 550
PLN02573 PLN02573
pyruvate decarboxylase
2-502 1.75e-105

pyruvate decarboxylase


Pssm-ID: 215311 [Multi-domain]  Cd Length: 578  Bit Score: 328.20  E-value: 1.75e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         2 SEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSA 81
Cdd:PLN02573  14 SDATLGRHLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTFTVGGLSV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        82 LNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQR 161
Cdd:PLN02573  94 LNAIAGAYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDFSQELRCFQTVTCYQAVINNLEDAHELIDTAISTALKESK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       162 PVYLGLPANLVDLNVPAkLLQTPIDMSLKP---NDAESEKEViDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLT 238
Cdd:PLN02573 174 PVYISVSCNLAAIPHPT-FSREPVPFFLTPrlsNKMSLEAAV-EAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADAS 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       239 QFPAFVTPMGKGSISEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRN 318
Cdd:PLN02573 252 GYPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGN 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       319 -ATFPGVQMK-FV--LQKLLTNIADAAKGYKPVAVPARTPANAAvpASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFG 394
Cdd:PLN02573 332 gPAFGCVLMKdFLeaLAKRVKKNTTAYENYKRIFVPEGEPLKSE--PGEPLRVNVLFKHIQKMLSGDTAVIAETGDSWFN 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       395 INQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY 474
Cdd:PLN02573 410 CQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAA----PDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGY 485
                        490       500
                 ....*....|....*....|....*....
1PYD_A       475 TIEKLIH-GPkaqYNEIQGWDHLSLLPTF 502
Cdd:PLN02573 486 TIEVEIHdGP---YNVIKNWNYTGLVDAI 511
TPP_PDC_IPDC cd02005
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ...
364-550 2.51e-94

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: 285.58  E-value: 2.51e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      364 PLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIG 443
Cdd:cd02005   1 PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALA----APDRRVILLVG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      444 DGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPKAQYNEIQGWDHLSLLPTFGAK-DYETHRVATTGEWDKLT 522
Cdd:cd02005  77 DGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPEASYNDIANWNYTKLPEVFGGGgGGLSFRVKTEGELDEAL 156
                       170       180
                ....*....|....*....|....*...
1PYD_A      523 QDKSFNdNSKIRMIEIMLPVFDAPQNLV 550
Cdd:cd02005 157 KDALFN-RDKLSLIEVILPKDDAPEALK 183
TPP_enzyme_N pfam02776
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
6-178 1.75e-31

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;


Pssm-ID: 426975 [Multi-domain]  Cd Length: 169  Bit Score: 119.65  E-value: 1.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A          6 LGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNG 84
Cdd:pfam02776   1 GAEALADVLKALGVDTVFGVPGGTILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGkPGVVLVTSGPGATNALTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         85 IAGSYAEhvgvlhvvGVP--SISSQAK-QLLLHHTLGNGDFTVfhRMSANISETTAMITDIATAPAEIDRCIRT-TYVTQ 160
Cdd:pfam02776  81 LANAYVD--------SVPliVISGQRPrSLVGRGALQQELDQL--ALFRPVTKWAVRVTSPDEIPEVLRRAFRAaMSGRP 150
                         170
                  ....*....|....*...
1PYD_A        161 RPVYLGLPANLVDLNVPA 178
Cdd:pfam02776 151 GPVYLEIPLDVLLEEVDE 168
 
Name Accession Description Interval E-value
PDC1 COG3961
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
1-556 0e+00

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: 933.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELS 80
Cdd:COG3961   1 SSPITVGDYLFDRLAQLGIKSIFGVPGDYNLSLLDKIYSVPGLRWVGNANELNAAYAADGYARLNGISALVTTFGVGELS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       81 ALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQ 160
Cdd:COG3961  81 ALNGIAGSYAEHVPVVHIVGVPTTSAQASGLLLHHTLGDGDFKVFHRMSKEITCAQAMLTDINTAPREIDRVIRTALKQR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      161 RPVYLGLPANLVDLNVPAKLlqTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQF 240
Cdd:COG3961 161 RPVYIGLPADVADLPIEAPL--TPLDLQLKTSDPEALSEVIDTIAELINKAKKPVILADALVSRFGLEKELKKLINATGF 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      241 PAFVTPMGKGSISEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNAT 320
Cdd:COG3961 239 PVATLPMGKGVIDESHPNYLGVYNGKLSEPEVREAVESADLILTIGVLLTDFNTGGFTYQYKPANIIEIHPDSVKIKDAV 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      321 FPGVQMKFVLQKLLTNIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTF 400
Cdd:COG3961 319 FTNLSMKDALQELAKKIDKRNLSAPPVAYPARTPPTPYPPANEPLTQEWLWNTVQNFLKPGDVIIAETGTSFFGALDIRL 398
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      401 PNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLI 480
Cdd:COG3961 399 PKGATFISQPLWGSIGYTLPAALGAALAA----PDRRVILFIGDGSLQLTVQEISTMIRWGLKPIIFVLNNDGYTIERAI 474
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PYD_A      481 HGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIMLPVFDAPQNLVKQAKLT 556
Cdd:COG3961 475 HGPTAPYNDIQSWDYTALPEAFGAKNGEAKFRATTGEELALALDVAFANNDRIRLIEVMLPVLDAPELLIDQAKAT 550
PLN02573 PLN02573
pyruvate decarboxylase
2-502 1.75e-105

pyruvate decarboxylase


Pssm-ID: 215311 [Multi-domain]  Cd Length: 578  Bit Score: 328.20  E-value: 1.75e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         2 SEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSA 81
Cdd:PLN02573  14 SDATLGRHLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTFTVGGLSV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        82 LNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQR 161
Cdd:PLN02573  94 LNAIAGAYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDFSQELRCFQTVTCYQAVINNLEDAHELIDTAISTALKESK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       162 PVYLGLPANLVDLNVPAkLLQTPIDMSLKP---NDAESEKEViDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLT 238
Cdd:PLN02573 174 PVYISVSCNLAAIPHPT-FSREPVPFFLTPrlsNKMSLEAAV-EAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADAS 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       239 QFPAFVTPMGKGSISEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRN 318
Cdd:PLN02573 252 GYPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGN 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       319 -ATFPGVQMK-FV--LQKLLTNIADAAKGYKPVAVPARTPANAAvpASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFG 394
Cdd:PLN02573 332 gPAFGCVLMKdFLeaLAKRVKKNTTAYENYKRIFVPEGEPLKSE--PGEPLRVNVLFKHIQKMLSGDTAVIAETGDSWFN 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       395 INQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY 474
Cdd:PLN02573 410 CQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAA----PDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGY 485
                        490       500
                 ....*....|....*....|....*....
1PYD_A       475 TIEKLIH-GPkaqYNEIQGWDHLSLLPTF 502
Cdd:PLN02573 486 TIEVEIHdGP---YNVIKNWNYTGLVDAI 511
TPP_PDC_IPDC cd02005
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ...
364-550 2.51e-94

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: 285.58  E-value: 2.51e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      364 PLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIG 443
Cdd:cd02005   1 PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALA----APDRRVILLVG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      444 DGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPKAQYNEIQGWDHLSLLPTFGAK-DYETHRVATTGEWDKLT 522
Cdd:cd02005  77 DGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPEASYNDIANWNYTKLPEVFGGGgGGLSFRVKTEGELDEAL 156
                       170       180
                ....*....|....*....|....*...
1PYD_A      523 QDKSFNdNSKIRMIEIMLPVFDAPQNLV 550
Cdd:cd02005 157 KDALFN-RDKLSLIEVILPKDDAPEALK 183
TPP_PYR_PDC_IPDC_like cd07038
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ...
9-169 6.79e-91

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: 275.91  E-value: 6.79e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        9 YLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGS 88
Cdd:cd07038   2 YLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVGELSALNGIAGA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       89 YAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLP 168
Cdd:cd07038  82 YAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGDFDVFLKMFEEITCAAARLTDPENAAEEIDRVLRTALRESRPVYIEIP 161

                .
1PYD_A      169 A 169
Cdd:cd07038 162 R 162
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
10-474 7.79e-59

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: 204.80  E-value: 7.79e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       10 LFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNGIAGS 88
Cdd:COG0028   8 LVEALEANGVDTVFGIPGGSILPLYDALYD-SGIRHILVRHEQGAAFAADGYARATGkPGVCLVTSGPGATNLLTGLADA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       89 YAEHVgvlhvvgvP--SISSQAKQLLLhhtlGNGDF--TVFHRMSANISETTAMITDIATAPAEIDRCIRTTyVTQR--P 162
Cdd:COG0028  87 YMDSV--------PllAITGQVPTSLI----GTDAFqeVDQVGLFRPITKYNFEVRSPEDIPEVVARAFRIA-LSGRpgP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      163 VYLGLPANLVDLNVPAKLLQTPIDMSLKPNDAESEKevIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPA 242
Cdd:COG0028 154 VVVDLPKDVLAAEAEEPGPEPAILPPYRPAPPPPEA--IRKAAELLAEAKRPVILAGGGVRRAGASEELRELAEKLGAPV 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      243 FVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKtKNIVEFHSDHMKIRNATFP 322
Cdd:COG0028 232 VTTLMGKGAVPEDHPLSLGM-LGMHGTKAANEALEEADLLLAVGARFDDRVTGYSGFAPP-AAIIHIDIDPAEIGKNYPV 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      323 GVQ----MKFVLQKLLTNIADA-AKGYKPVA--VPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTS---A 392
Cdd:COG0028 310 DVPivgdAKATLEALLEELKPErAAWLEELLeaRAAYRDLALEELADDGIKPQYVIKVLRELLPDDAIVVTDVGQHqmwA 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      393 FGINQTTFPNNTYgISqVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNND 472
Cdd:COG0028 390 ARYFDFYRPRRFL-TS-GGLGTMGFGLPAAIGAKLAA----PDRKVVAIAGDGGFMMNGQELETAVRYGLPVKIVVLNNG 463

                ..
1PYD_A      473 GY 474
Cdd:COG0028 464 GY 465
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
8-169 1.05e-51

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: 173.68  E-value: 1.05e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        8 KYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAG 87
Cdd:cd06586   1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       88 SYAEHVGVLHVVGVPSISSQAKQLllhhtlgnGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGL 167
Cdd:cd06586  81 AAAEHLPVVFLIGARGISAQAKQT--------FQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRL 152

                ..
1PYD_A      168 PA 169
Cdd:cd06586 153 PR 154
TPP_enzyme_N pfam02776
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
6-178 1.75e-31

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;


Pssm-ID: 426975 [Multi-domain]  Cd Length: 169  Bit Score: 119.65  E-value: 1.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A          6 LGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNG 84
Cdd:pfam02776   1 GAEALADVLKALGVDTVFGVPGGTILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGkPGVVLVTSGPGATNALTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         85 IAGSYAEhvgvlhvvGVP--SISSQAK-QLLLHHTLGNGDFTVfhRMSANISETTAMITDIATAPAEIDRCIRT-TYVTQ 160
Cdd:pfam02776  81 LANAYVD--------SVPliVISGQRPrSLVGRGALQQELDQL--ALFRPVTKWAVRVTSPDEIPEVLRRAFRAaMSGRP 150
                         170
                  ....*....|....*...
1PYD_A        161 RPVYLGLPANLVDLNVPA 178
Cdd:pfam02776 151 GPVYLEIPLDVLLEEVDE 168
TPP_enzyme_M pfam00205
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ...
201-333 2.29e-28

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: 109.96  E-value: 2.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        201 IDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGvYVGTLSKPEVKEAVESAD 280
Cdd:pfam00205   1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLG-MLGMHGTPAANEALEEAD 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
1PYD_A        281 LILSVGALLSDFNTGSFSYSY-KTKNIVEFHSDHMKIRNATFPGVQM----KFVLQKL 333
Cdd:pfam00205  80 LVLAVGARFDDIRTTGKLPEFaPDAKIIHIDIDPAEIGKNYPVDVPIvgdaKETLEAL 137
PRK06276 PRK06276
acetolactate synthase large subunit;
7-471 2.24e-26

acetolactate synthase large subunit;


Pssm-ID: 235766 [Multi-domain]  Cd Length: 586  Bit Score: 113.31  E-value: 2.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         7 GKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEgMRWAGNANELNAAYAADGYARIKGMS--CIITTfGVGELSALNG 84
Cdd:PRK06276   4 AEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSD-LIHILTRHEQAAAHAADGYARASGKVgvCVATS-GPGATNLVTG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        85 IAGSYAEHVGVLhvvgvpSISSQAKQlllhHTLGNGDFT------VFhrMSanISETTAMITDiataPAEIDRCIRTTY- 157
Cdd:PRK06276  82 IATAYADSSPVI------ALTGQVPT----KLIGNDAFQeidalgIF--MP--ITKHNFQIKK----PEEIPEIFRAAFe 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       158 --VTQRP--VYLGLPANLVDLNVPAKLLQTPIDMSL---KPNDAESEKEvIDTILALVKDAKNPVILADACCSRHDVKAE 230
Cdd:PRK06276 144 iaKTGRPgpVHIDLPKDVQEGELDLEKYPIPAKIDLpgyKPTTFGHPLQ-IKKAAELIAEAERPVILAGGGVIISGASEE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       231 TKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFH 310
Cdd:PRK06276 223 LIELSELVKIPVCTTLMGKGAFPEDHPLALGM-VGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHID 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       311 SDHMKI-RN--ATFPGV-QMKFVLQKLLTNI-ADAAKGYKPVAVPARTPANAAVPAST----PLKQEWMWNQLGNFLQEG 381
Cdd:PRK06276 302 IDPAEIgKNvrVDVPIVgDAKNVLRDLLAELmKKEIKNKSEWLERVKKLKKESIPRMDfddkPIKPQRVIKELMEVLREI 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       382 DVVIAETGTSAFGINQ--------TTFPNNTygISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQE 453
Cdd:PRK06276 382 DPSKNTIITTDVGQNQmwmahffkTSAPRSF--ISSGGLGTMGFGFPAAIGAKVAK----PDANVIAITGDGGFLMNSQE 455
                        490
                 ....*....|....*...
1PYD_A       454 ISTMIRWGLKPYLFVLNN 471
Cdd:PRK06276 456 LATIAEYDIPVVICIFDN 473
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
371-539 2.66e-26

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: 105.03  E-value: 2.66e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      371 WNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYG-ISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQL 449
Cdd:cd00568   3 LAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRfLTSTGFGAMGYGLPAAIGAALAA----PDRPVVCIAGDGGFMM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      450 TVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGP----KAQYNEIQGWDHLSLLPTFGAKdyeTHRVATTGEWDKLTQDk 525
Cdd:cd00568  79 TGQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAfyggRVSGTDLSNPDFAALAEAYGAK---GVRVEDPEDLEAALAE- 154
                       170
                ....*....|....
1PYD_A      526 sFNDNSKIRMIEIM 539
Cdd:cd00568 155 -ALAAGGPALIEVK 167
PRK07282 PRK07282
acetolactate synthase large subunit;
1-471 3.17e-25

acetolactate synthase large subunit;


Pssm-ID: 180919 [Multi-domain]  Cd Length: 566  Bit Score: 109.53  E-value: 3.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         1 MSEITL-----GKYL-FERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITT 73
Cdd:PRK07282   1 MEKISLespksGSDLvLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGkLGVAVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        74 FGVGELSALNGIAGSYAEHV---GVLHVVGVPSISSQAKQLLlhHTLGngdftvfhrMSANISETTAMITDIatapAEID 150
Cdd:PRK07282  81 SGPGATNAITGIADAMSDSVpllVFTGQVARAGIGKDAFQEA--DIVG---------ITMPITKYNYQIRET----ADIP 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       151 RCIRTTY---VTQR--PVYLGLPANLVDLNVpAKLLQTPIDM-----SLKPNDAESEKevidtILALVKDAKNPVILADA 220
Cdd:PRK07282 146 RIITEAVhiaTTGRpgPVVIDLPKDVSALET-DFIYDPEVNLpsyqpTLEPNDMQIKK-----ILKQLSKAKKPVILAGG 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       221 CCSRHDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTG---SF 297
Cdd:PRK07282 220 GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLFLGM-GGMHGSYAANIAMTEADFMINIGSRFDDRLTGnpkTF 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       298 SysyktKNIVEFHSD-----HMKIRNATFPGV-QMKFVLQKLL------TNIADAAKgyKPVAVPARTPANAavPASTPL 365
Cdd:PRK07282 299 A-----KNAKVAHIDidpaeIGKIIKTDIPVVgDAKKALQMLLaeptvhNNTEKWIE--KVTKDKNRVRSYD--KKERVV 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       366 KQEWMWNQLGNFLQEGDVVIAETGTSAFGINQ-TTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIGD 444
Cdd:PRK07282 370 QPQAVIERIGELTNGDAIVVTDVGQHQMWAAQyYPYQNERQLVTSGGLGTMGFGIPAAIGAKIA----NPDKEVILFVGD 445
                        490       500
                 ....*....|....*....|....*..
1PYD_A       445 GSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK07282 446 GGFQMTNQELAILNIYKVPIKVVMLNN 472
PRK06048 PRK06048
acetolactate synthase large subunit;
1-474 3.96e-24

acetolactate synthase large subunit;


Pssm-ID: 180368 [Multi-domain]  Cd Length: 561  Bit Score: 106.01  E-value: 3.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKGMSCI-ITTFGVGEL 79
Cdd:PRK06048   5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARATGKVGVcVATSGPGAT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        80 SALNGIAGSYAEHVGVLhvvgvpSISSQAKQLLLhhtlGNGDFtvfhrMSANISETTAMITD---IATAPAEIDRCIRTT 156
Cdd:PRK06048  84 NLVTGIATAYMDSVPIV------ALTGQVPRSMI----GNDAF-----QEADITGITMPITKhnyLVQDAKDLPRIIKEA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       157 Y---VTQR--PVYLGLPANL----VDLNVPAKLLQTPIDMSLKPNDAESEKEVidtilALVKDAKNPVILADACCSRHDV 227
Cdd:PRK06048 149 FhiaSTGRpgPVLIDLPKDVttaeIDFDYPDKVELRGYKPTYKGNPQQIKRAA-----ELIMKAERPIIYAGGGVISSNA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       228 KAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGvYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIV 307
Cdd:PRK06048 224 SEELVELAETIPAPVTTTLMGIGAIPTEHPLSLG-MLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKII 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       308 EFHSDHMKIR---NATFPGV-QMKFVLQKLLTNIA--DAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEG 381
Cdd:PRK06048 303 HIDIDPAEISknvKVDVPIVgDAKQVLKSLIKYVQycDRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCPDA 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       382 dVVIAETGTSAFGINQttFPNNTYGISQVLWGSIGfTTGATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWG 461
Cdd:PRK06048 383 -IIVTEVGQHQMWAAQ--YFKYKYPRTFITSGGLG-TMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQND 458
                        490
                 ....*....|...
1PYD_A       462 LKPYLFVLNNdGY 474
Cdd:PRK06048 459 IPVIVAILNN-GY 470
PRK08527 PRK08527
acetolactate synthase large subunit;
2-471 5.30e-23

acetolactate synthase large subunit;


Pssm-ID: 181458 [Multi-domain]  Cd Length: 563  Bit Score: 102.87  E-value: 5.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         2 SEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELS 80
Cdd:PRK08527   1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGkVGVAIVTSGPGFTN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        81 ALNGIAGSYAEHVGVLHvvgvpsISSQAKQlllhhTLGNGDftVFHRMSA-NISETTAMITDIATAPAEIDRCIRTTYVT 159
Cdd:PRK08527  81 AVTGLATAYMDSIPLVL------ISGQVPN-----SLIGTD--AFQEIDAvGISRPCVKHNYLVKSIEELPRILKEAFYI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       160 QR-----PVYLGLP----ANLVDLNVPAKllqtpIDM-SLKPNDAESEKEvIDTILALVKDAKNPVILADACCSRHDVKA 229
Cdd:PRK08527 148 ARsgrpgPVHIDIPkdvtATLGEFEYPKE-----ISLkTYKPTYKGNSRQ-IKKAAEAIKEAKKPLFYLGGGAILSNASE 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       230 ETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEF 309
Cdd:PRK08527 222 EIRELVKKTGIPAVETLMARGVLRSDDPLLLGM-LGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHV 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       310 HSDHM---KIRNATFPGV-QMKFVLQKLLTNIAD-AAKGYKP-VAVPARTpaNAAVPAS-----TPLKQEWMWNQLGNFL 378
Cdd:PRK08527 301 DIDPSsisKIVNADYPIVgDLKNVLKEMLEELKEeNPTTYKEwREILKRY--NELHPLSyedsdEVLKPQWVIERVGELL 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       379 QEGDVVIAETGTSAFGINQT---TFP---NNTYGIsqvlwGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQ 452
Cdd:PRK08527 379 GDDAIISTDVGQHQMWVAQFypfNYPrqlATSGGL-----GTMGYGLPAALGAKLAV----PDKVVINFTGDGSILMNIQ 449
                        490
                 ....*....|....*....
1PYD_A       453 EISTMIRWGLKPYLFVLNN 471
Cdd:PRK08527 450 ELMTAVEYKIPVINIILNN 468
PRK08322 PRK08322
acetolactate synthase large subunit;
14-474 1.29e-22

acetolactate synthase large subunit;


Pssm-ID: 236239 [Multi-domain]  Cd Length: 547  Bit Score: 101.44  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        14 LKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKGMS--CIiTTFGVGELSALNGIAgsYAe 91
Cdd:PRK08322  11 LENEGVEYIFGIPGEENLDLLEALRD-SSIKLILTRHEQGAAFMAATYGRLTGKAgvCL-STLGPGATNLVTGVA--YA- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        92 hvgvlHVVGVP--SISSQAKQLLLHHtlgnGDFTVFH--RMSANISETTAMITDIATAPAEIDRCIRTTyVTQRP--VYL 165
Cdd:PRK08322  86 -----QLGGMPmvAITGQKPIKRSKQ----GSFQIVDvvAMMAPLTKWTRQIVSPDNIPEVVREAFRLA-EEERPgaVHL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       166 GLPANLVDLNVPAKLLqtPIDMSLKPNdaeSEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVT 245
Cdd:PRK08322 156 ELPEDIAAEETDGKPL--PRSYSRRPY---ASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTT 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       246 PMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFnTGSFSYSYKTKNIVEFHSDHMKIRNATFPgvQ 325
Cdd:PRK08322 231 QMGKGVIPETHPLSLGT-AGLSQGDYVHCAIEHADLIINVGHDVIEK-PPFFMNPNGDKKVIHINFLPAEVDPVYFP--Q 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       326 MKFV------LQKLLTNIADAAKGYKPVAVPARTP-----ANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGtsAFG 394
Cdd:PRK08322 307 VEVVgdiansLWQLKERLADQPHWDFPRFLKIREAieahlEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNG--AYK 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       395 I----NQTTFPNNTYGISQvlwgsiGFTT-GATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVL 469
Cdd:PRK08322 385 IwfarNYRAYEPNTCLLDN------ALATmGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLIL 458

                 ....*
1PYD_A       470 NNDGY 474
Cdd:PRK08322 459 NDNAY 463
TPP_PYR_POX_like cd07035
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ...
9-169 3.00e-22

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: 93.37  E-value: 3.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        9 YLFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNGIAG 87
Cdd:cd07035   2 ALVEALKAEGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGkPGVVLVTSGPGLTNAVTGLAN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       88 SYAEhvgvlhvvgvpS-----ISSQAKQlllhHTLGNGDFTVF--HRMSANISETTAMITDIATAPAEIDRCIRTTYVT- 159
Cdd:cd07035  81 AYLD-----------SipllvITGQRPT----AGEGRGAFQEIdqVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGr 145
                       170
                ....*....|
1PYD_A      160 QRPVYLGLPA 169
Cdd:cd07035 146 PGPVALDLPK 155
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
2-513 1.25e-20

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 95.44  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         2 SEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGels 80
Cdd:PRK07064   1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGgLGVALTSTGTG--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        81 ALNgIAGSYAEHVGvlhvvgvpsissqAKQLLLHHT-------LGNgDFTVFHR------MSANISETTAMITDIATAPA 147
Cdd:PRK07064  78 AGN-AAGALVEALT-------------AGTPLLHITgqietpyLDQ-DLGYIHEapdqltMLRAVSKAAFRVRSAETALA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       148 EIDRCIRTTyvtqrpvyLGLPANLVDLNVPAKLLQTPIDMS-----LKPNDAESEKEVIDTILALVKDAKNPVILADAcC 222
Cdd:PRK07064 143 TIREAVRVA--------LTAPTGPVSVEIPIDIQAAEIELPddlapVHVAVPEPDAAAVAELAERLAAARRPLLWLGG-G 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       223 SRHDVKaETKKLIDLTqFPAFVTPMGKGSISEQHPRYGGVYVGTlskPEVKEAVESADLILSVGALLSDFNTGSFSysyk 302
Cdd:PRK07064 214 ARHAGA-EVKRLVDLG-FGVVTSTQGRGVVPEDHPASLGAFNNS---AAVEALYKTCDLLLVVGSRLRGNETLKYS---- 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       303 tkniVEFHSDHMKI-----------RNATFPGVQMKFVLQKLLTNIADAAKGYKPVAVPARTPANAAVPAstplkqewMW 371
Cdd:PRK07064 285 ----LALPRPLIRVdadaaadgrgyPNDLFVHGDAARVLARLADRLEGRLSVDPAFAADLRAAREAAVAD--------LR 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       372 NQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQV-----------LWGSIGFTTGATLGAAFAaeeiDPKKRVIL 440
Cdd:PRK07064 353 KGLGPYAKLVDALRAALPRDGNWVRDVTISNSTWGNRLLpifepranvhaLGGGIGQGLAMAIGAALA----GPGRKTVG 428
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1PYD_A       441 FIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY----TIEKLIHGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVA 513
Cdd:PRK07064 429 LVGDGGLMLNLGELATAVQENANMVIVLMNDGGYgvirNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSAD 505
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
2-471 1.68e-18

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 88.66  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         2 SEITLGKYLFERLKQVNVNTVFG--LPGDFNLSLldkiyEVEGMRWAGNANELNAAYAADGYARIKGMSCIITtfgvgel 79
Cdd:PRK06112  12 LNGTVAHAIARALKRHGVEQIFGqsLPSALFLAA-----EAIGIRQIAYRTENAGGAMADGYARVSGKVAVVT------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        80 sALNGIAGS-----YAEHVGVLHvvgvPSIS-----------SQAKQLLLHHTLGNGDFTVFHRMSanISETTAMITDIA 143
Cdd:PRK06112  80 -AQNGPAATllvapLAEALKASV----PIVAlvqdvnrdqtdRNAFQELDHIALFQSCTKWVRRVT--VAERIDDYVDQA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       144 TAPAEIDRcirttyvtQRPVYLGLPANLVDLNVPAKLLQTPIDMSLKPND-AESEKEVIDTILALVKDAKNPVILADACC 222
Cdd:PRK06112 153 FTAATSGR--------PGPVVLLLPADLLTAAAAAPAAPRSNSLGHFPLDrTVPAPQRLAEAASLLAQAQRPVVVAGGGV 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       223 SRHDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPE-----VKEAVESADLILSVGALLSDFNTGSF 297
Cdd:PRK06112 225 HISGASAALAALQSLAGLPVATTNMGKGAVDETHPLSLGV-VGSLMGPRspgrhLRDLVREADVVLLVGTRTNQNGTDSW 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       298 SYSYKTKNIVEFHSDHMKI-RNATfpgvQMKFVLQKLLTnIADAAKGYKPVAVPARTPANAAVPA--------------- 361
Cdd:PRK06112 304 SLYPEQAQYIHIDVDGEEVgRNYE----ALRLVGDARLT-LAALTDALRGRDLAARAGRRAALEPaiaagreahredsap 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       362 -----STPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGI-NQTTFPN------NTYGISQVLWGsIGFTTGATLGAafaa 429
Cdd:PRK06112 379 valsdASPIRPERIMAELQAVLTGDTIVVADASYSSIWVaNFLTARRagmrflTPRGLAGLGWG-VPMAIGAKVAR---- 453
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
1PYD_A       430 eeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06112 454 ----PGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNN 491
PRK08266 PRK08266
hypothetical protein; Provisional
1-474 8.46e-18

hypothetical protein; Provisional


Pssm-ID: 181337 [Multi-domain]  Cd Length: 542  Bit Score: 86.60  E-value: 8.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEG-MRWAGNANELNAAYAADGYARIKGMSCIITTF-GVGE 78
Cdd:PRK08266   1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVpGPGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        79 LSALNGIAGSYAehvgvlhvvgvpsisSQAKQLLL-----HHTLGNGdFTVFHRMSANiSETTAMIT---DIATAPAEID 150
Cdd:PRK08266  81 LNAGAALLTAYG---------------CNSPVLCLtgqipSALIGKG-RGHLHEMPDQ-LATLRSFTkwaERIEHPSEAP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       151 RCIRTTYVT-----QRPVYLGLPANLVDLNVP-AKLLQTPIDMSLKPNDaesekEVIDTILALVKDAKNPVILADAccSR 224
Cdd:PRK08266 144 ALVAEAFQQmlsgrPRPVALEMPWDVFGQRAPvAAAPPLRPAPPPAPDP-----DAIAAAAALIAAAKNPMIFVGG--GA 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       225 HDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYggvyvgtLSKPEVKEAVESADLILSVGallSDFNTGSFSYSYKTK 304
Cdd:PRK08266 217 AGAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLG-------LNFAAAYELWPQTDVVIGIG---SRLELPTFRWPWRPD 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       305 N--IVEFHSDHMKIRNATfPGVQMKFVLQKLLTNIADAAKGYKPVAvPARTPANAAVPASTPLKQEWMWNQLGnFLQegd 382
Cdd:PRK08266 287 GlkVIRIDIDPTEMRRLK-PDVAIVADAKAGTAALLDALSKAGSKR-PSRRAELRELKAAARQRIQAVQPQAS-YLR--- 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       383 VVIAETGTSAFGINQttfpnntygISQV-LWGSIGF---------TTG--ATLGAAFA----AEEIDPKKRVILFIGDGS 446
Cdd:PRK08266 361 AIREALPDDGIFVDE---------LSQVgFASWFAFpvyaprtfvTCGyqGTLGYGFPtalgAKVANPDRPVVSITGDGG 431
                        490       500
                 ....*....|....*....|....*...
1PYD_A       447 LQLTVQEISTMIRWGLKPYLFVLNNDGY 474
Cdd:PRK08266 432 FMFGVQELATAVQHNIGVVTVVFNNNAY 459
PRK08611 PRK08611
pyruvate oxidase; Provisional
1-471 9.59e-18

pyruvate oxidase; Provisional


Pssm-ID: 181502 [Multi-domain]  Cd Length: 576  Bit Score: 86.59  E-value: 9.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKI-YEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGE 78
Cdd:PRK08611   1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrKEQDKIKFIQVRHEEVAALAAAAYAKLTGkIGVCLSIGGPGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        79 LSALNGIAGSYAEhvgvlhvvgvpsissQAKQLLLhhtLGNGDFTVFHRMSANISETTAMITDIA----------TAPAE 148
Cdd:PRK08611  81 IHLLNGLYDAKMD---------------HVPVLAL---AGQVTSDLLGTDFFQEVNLEKMFEDVAvynhqimsaeNLPEI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       149 IDRCIRTTYVTQRPVYLGLPANLVDLNVPAKlLQTPIDmSLKPNDAESEKEVIDTILALVKDAKNPVILADAccSRHDVK 228
Cdd:PRK08611 143 VNQAIRTAYEKKGVAVLTIPDDLPAQKIKDT-TNKTVD-TFRPTVPSPKPKDIKKAAKLINKAKKPVILAGL--GAKHAK 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       229 AETKKLIDLTQFPAFVTPMGKGSISEQHPRY-GGV-YVGTlsKPEVkEAVESADLILSVGAllsdfntgsfSYSY----- 301
Cdd:PRK08611 219 EELLAFAEKAKIPIIHTLPAKGIIPDDHPYSlGNLgKIGT--KPAY-EAMQEADLLIMVGT----------NYPYvdylp 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       302 -KTKNIvEFHSDHMKI--RNATFPGVQ--MKFVLQKLLTNIAdaakgykpvAVPAR-----TPANAAV----------PA 361
Cdd:PRK08611 286 kKAKAI-QIDTDPANIgkRYPVNVGLVgdAKKALHQLTENIK---------HVEDRrfleaCQENMAKwwkwmeedenNA 355
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       362 STPLKQEWMWNQLGNFLQEGDVVIAETGTS----AFGINQTtfPNNTYGISQVLWgsigfTTGATLGAAFAAEEIDPKKR 437
Cdd:PRK08611 356 STPIKPERVMAAIQKIADDDAVLSVDVGTVtvwsARYLNLG--TNQKFIISSWLG-----TMGCGLPGAIAAKIAFPDRQ 428
                        490       500       510
                 ....*....|....*....|....*....|....
1PYD_A       438 VILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK08611 429 AIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNN 462
PRK06882 PRK06882
acetolactate synthase 3 large subunit;
1-471 8.26e-17

acetolactate synthase 3 large subunit;


Pssm-ID: 168717 [Multi-domain]  Cd Length: 574  Bit Score: 83.42  E-value: 8.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGEL 79
Cdd:PRK06882   1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGkVGCVLVTSGPGAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        80 SALNGIAGSYAEHVGVLHvvgvpsISSQAKQLLlhhtLGNGDFTVFHRMSanISETTAMITDIATAPAEIDRCIRTTYV- 158
Cdd:PRK06882  81 NAITGIATAYTDSVPLVI------LSGQVPSNL----IGTDAFQECDMLG--ISRPVVKHSFIVKNAEDIPSTIKKAFYi 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       159 --TQR--PVYLGLPANLVDlnvPAKLL--QTPIDMSLK---PNdAESEKEVIDTILALVKDAKNPVILADACCsrhdVKA 229
Cdd:PRK06882 149 asTGRpgPVVIDIPKDMVN---PANKFtyEYPEEVSLRsynPT-VQGHKGQIKKALKALLVAKKPVLFVGGGV----ITA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       230 E-TKKLIDLTQ---FPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKN 305
Cdd:PRK06882 221 EcSEQLTQFAQklnLPVTSSLMGLGAYPSTDKQFLGM-LGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAK 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       306 IVEFHSDHMKIRN---ATFPGV-QMKFVLQKLLTNIADA--AKGykpvavpartpaNAAVPASTPLKQEWMWNQLGNF-- 377
Cdd:PRK06882 300 VIHIDIDPTSISKnvpAYIPIVgSAKNVLEEFLSLLEEEnlAKS------------QTDLTAWWQQINEWKAKKCLEFdr 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       378 ----------------LQEGDVVIA-ETGT-SAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVI 439
Cdd:PRK06882 368 tsdvikpqqvveaiyrLTNGDAYVAsDVGQhQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFA----HPEATVV 443
                        490       500       510
                 ....*....|....*....|....*....|..
1PYD_A       440 LFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06882 444 CVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
PRK06725 PRK06725
acetolactate synthase large subunit;
3-471 5.01e-16

acetolactate synthase large subunit;


Pssm-ID: 180672 [Multi-domain]  Cd Length: 570  Bit Score: 81.17  E-value: 5.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         3 EITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSA 81
Cdd:PRK06725  14 EVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARASGkVGVVFATSGPGATNL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        82 LNGIAGSYAEHVGVLHvvgvpsISSQ-AKQLLLHHTLGNGDFTvfhRMSANISETTAMITDIAtapaEIDRCIRTTYVTQ 160
Cdd:PRK06725  93 VTGLADAYMDSIPLVV------ITGQvATPLIGKDGFQEADVV---GITVPVTKHNYQVRDVN----QLSRIVQEAFYIA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       161 R-----PVYLGLPANLVDLNVPA-----------KLLQTPIDMSLKpndaesekEVIDTIlalvKDAKNPVILADACCSR 224
Cdd:PRK06725 160 EsgrpgPVLIDIPKDVQNEKVTSfynevveipgyKPEPRPDSMKLR--------EVAKAI----SKAKRPLLYIGGGVIH 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       225 HDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGS---FSYSY 301
Cdd:PRK06725 228 SGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLFLGM-LGMHGTYAANMAVTECDLLLALGVRFDDRVTGKlelFSPHS 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       302 KTKNI----VEFHS----------DHMKIRNATFP---GVQMKFVLQKLLTNIADAAKGYKPvavpartpanaavpASTP 364
Cdd:PRK06725 307 KKVHIdidpSEFHKnvaveypvvgDVKKALHMLLHmsiHTQTDEWLQKVKTWKEEYPLSYKQ--------------KESE 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       365 LKQEWMWNQLGNFLQEGDVVIAETGT-SAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAEEidpkKRVILFIG 443
Cdd:PRK06725 373 LKPQHVINLVSELTNGEAIVTTEVGQhQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEE----ELVICIAG 448
                        490       500
                 ....*....|....*....|....*...
1PYD_A       444 DGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06725 449 DASFQMNIQELQTIAENNIPVKVFIINN 476
PRK07524 PRK07524
5-guanidino-2-oxopentanoate decarboxylase;
4-474 7.15e-16

5-guanidino-2-oxopentanoate decarboxylase;


Pssm-ID: 236041 [Multi-domain]  Cd Length: 535  Bit Score: 80.40  E-value: 7.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         4 ITLGKYLFERLKQVNVNTVFGLPGdfnlslldkIYEVE--------GMRWAGNANELNAAYAADGYARIKGMS--CIITT 73
Cdd:PRK07524   2 TTCGEALVRLLEAYGVETVFGIPG---------VHTVElyrglagsGIRHVTPRHEQGAGFMADGYARVSGKPgvCFIIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        74 fGVGELSALNGIAGSYAEhvgvlhvvGVPS--ISS-QAKQLLLHhtlGNGdftVFHR------MSANISETTAMITDIAT 144
Cdd:PRK07524  73 -GPGMTNIATAMGQAYAD--------SIPMlvISSvNRRASLGK---GRG---KLHElpdqraMVAGVAAFSHTLMSAED 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       145 APAEIDR------CIRTtyvtqRPVYLGLPANLVDLNVPAKLLQTPidmsLKPNDAESEKEVIDTILALVKDAKNPVILA 218
Cdd:PRK07524 138 LPEVLARafavfdSARP-----RPVHIEIPLDVLAAPADHLLPAPP----TRPARPGPAPAALAQAAERLAAARRPLILA 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       219 DACCSrhDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGvyvGTLSKPEVKEAVESADLILSVGALLSD-----FN 293
Cdd:PRK07524 209 GGGAL--AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLG---ASQSLPAVRALIAEADVVLAVGTELGEtdydvYF 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       294 TGSFSYSyktKNIVEFHSDHMKI-RNATfPGVQM----KFVLQKLLTNIADAAKgykpvavPARTPANAAVPASTPLKQE 368
Cdd:PRK07524 284 DGGFPLP---GELIRIDIDPDQLaRNYP-PALALvgdaRAALEALLARLPGQAA-------AADWGAARVAALRQALRAE 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       369 WMWNQLG--NFLQegdvVIAETGTSAFGINQTTFP----NNTYGISQVL-W-------GSIGFTTGATLGAAFAAeeidP 434
Cdd:PRK07524 353 WDPLTAAqvALLD----TILAALPDAIFVGDSTQPvyagNLYFDADAPRrWfnastgyGTLGYGLPAAIGAALGA----P 424
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
1PYD_A       435 KKRVILFIGDGSLQLTVQEISTMIRWGLkPYLFVL-NNDGY 474
Cdd:PRK07524 425 ERPVVCLVGDGGLQFTLPELASAVEADL-PLIVLLwNNDGY 464
PRK08199 PRK08199
thiamine pyrophosphate protein; Validated
1-476 2.43e-15

thiamine pyrophosphate protein; Validated


Pssm-ID: 181285 [Multi-domain]  Cd Length: 557  Bit Score: 78.76  E-value: 2.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCI-ITTFGVGEL 79
Cdd:PRK08199   5 PRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGIcFVTRGPGAT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        80 SALNGIagsyaehvgvlhvvgvpsisSQAKQ----LLL------HHTLGNGDFTV--FHRMSANISETTAMITDIATAPA 147
Cdd:PRK08199  85 NASIGV--------------------HTAFQdstpMILfvgqvaRDFREREAFQEidYRRMFGPMAKWVAEIDDAARIPE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       148 EIDRCIRTTyVTQR--PVYLGLPAN-LVDLNVPAKLLQTPIDMSlKPNDAEsekevIDTILALVKDAKNPVILADAccSR 224
Cdd:PRK08199 145 LVSRAFHVA-TSGRpgPVVLALPEDvLSETAEVPDAPPYRRVAA-APGAAD-----LARLAELLARAERPLVILGG--SG 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       225 HDVKAEtkklIDLTQFP-AFVTPMG-----KGSISEQHPRYGGvYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFS 298
Cdd:PRK08199 216 WTEAAV----ADLRAFAeRWGLPVAcafrrQDLFDNRHPNYAG-DLGLGINPALAARIREADLVLAVGTRLGEVTTQGYT 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       299 ---YSYKTKNIVEFHSDHMKIrNATFPGVQMkfvLQKLLTNIADAAKGYKPVAVPARTPANAAVPA-----STPLKQEWM 370
Cdd:PRK08199 291 lldIPVPRQTLVHVHPDAEEL-GRVYRPDLA---IVADPAAFAAALAALEPPASPAWAEWTAAAHAdylawSAPLPGPGA 366
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       371 wNQLG---NFLQE---GDVVIAeTGTSAF-GINQTTFPNNTYGisqvlwGSIGFTTGAT---LGAAFAAEEIDPKKRVIL 440
Cdd:PRK08199 367 -VQLGevmAWLRErlpADAIIT-NGAGNYaTWLHRFFRFRRYR------TQLAPTSGSMgygLPAAIAAKLLFPERTVVA 438
                        490       500       510
                 ....*....|....*....|....*....|....*..
1PYD_A       441 FIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY-TI 476
Cdd:PRK08199 439 FAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYgTI 475
PRK06456 PRK06456
acetolactate synthase large subunit;
4-458 3.62e-15

acetolactate synthase large subunit;


Pssm-ID: 180569 [Multi-domain]  Cd Length: 572  Bit Score: 78.34  E-value: 3.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         4 ITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYE-VEG--MRWAGNANELNAAYAADGYARIKGMSCIIT-TFGVGEL 79
Cdd:PRK06456   2 PTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFVEdLANgeLRHVLMRHEQAAAHAADGYARASGVPGVCTaTSGPGTT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        80 SALNGIAGSYAEHV---GVLHVVGVPSISSQAKQllLHHTLGngdftVFhrmsANISETTAMITDIATAPAEIDRCIrtt 156
Cdd:PRK06456  82 NLVTGLITAYWDSSpviAITGQVPRSVMGKMAFQ--EADAMG-----VF----ENVTKYVIGIKRIDEIPQWIKNAF--- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       157 YV--TQR--PVYLGLPANLVDLNVP-AKLLQTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAET 231
Cdd:PRK06456 148 YIatTGRpgPVVIDIPRDIFYEKMEeIKWPEKPLVKGYRDFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEV 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       232 KKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKT-KNIVEFH 310
Cdd:PRK06456 228 LELAELLHIPIVSTFPGKTAIPHDHPLYFGP-MGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVN 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       311 SDHMKIRNATFPGVQM----KFVLQKLLTNIADAAKGYKPVAVPART--------------------------------P 354
Cdd:PRK06456 307 IDPTDGEKAIKVDVGIygnaKIILRELIKAITELGQKRDRSAWLKRVkeykeyysqfyyteengklkpwkimktirqalP 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       355 ANAAVpaSTPLKQEWMWNQLGNFLQEGDVVIAETGTsafginqttfpnntygisqvlwGSIGFTTGATLGAAFAAeeidP 434
Cdd:PRK06456 387 RDAIV--TTGVGQHQMWAEVFWEVLEPRTFLTSSGM----------------------GTMGFGLPAAMGAKLAR----P 438
                        490       500
                 ....*....|....*....|....
1PYD_A       435 KKRVILFIGDGSLQLTVQEISTMI 458
Cdd:PRK06456 439 DKVVVDLDGDGSFLMTGTNLATAV 462
PRK07525 PRK07525
sulfoacetaldehyde acetyltransferase; Validated
12-478 2.58e-14

sulfoacetaldehyde acetyltransferase; Validated


Pssm-ID: 236042 [Multi-domain]  Cd Length: 588  Bit Score: 75.80  E-value: 2.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        12 ERLKQVNVNTVFGLPGDFNLSLLDkIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNGIAGSYA 90
Cdd:PRK07525  14 ETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGrMGMVIGQNGPGITNFVTAVATAYW 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        91 EHVGVLHvvgvpsISSQAKQLllhhTLGNGDF------TVFHRMSANISEttamITDIATAPAEIDRCIRTTYVTQRPVY 164
Cdd:PRK07525  93 AHTPVVL------VTPQAGTK----TIGQGGFqeaeqmPMFEDMTKYQEE----VRDPSRMAEVLNRVFDKAKRESGPAQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       165 LGLPANL----VDLNVPAkllqtPIDMSLKPNDAESekevIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQF 240
Cdd:PRK07525 159 INIPRDYfygvIDVEIPQ-----PVRLERGAGGEQS----LAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       241 PAFVTPMGKGSISEQHPryggVYVGTLSKPEVKEAVES---ADLILSVGALLSDFNT---GSFSYSYKTKNI--VEFHSD 312
Cdd:PRK07525 230 PVACGYLHNDAFPGSHP----LWVGPLGYNGSKAAMELiakADVVLALGTRLNPFGTlpqYGIDYWPKDAKIiqVDINPD 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       313 HMKIRNATFPGVQ--MKFVLQKLLTNIADAAKG------------------YKPVA------VPARTPANAAVPASTPlk 366
Cdd:PRK07525 306 RIGLTKKVSVGICgdAKAVARELLARLAERLAGdagreerkaliaaeksawEQELSswdhedDDPGTDWNEEARARKP-- 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       367 qEWM-----WNQLGNFLQEGDVVIAETG-TSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVIL 440
Cdd:PRK07525 384 -DYMhprqaLREIQKALPEDAIVSTDIGnNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIAC----PDRPVVG 458
                        490       500       510
                 ....*....|....*....|....*....|....*...
1PYD_A       441 FIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEK 478
Cdd:PRK07525 459 FAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEK 496
IolD COG3962
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ...
201-510 7.21e-14

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: 74.35  E-value: 7.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      201 IDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSISEQHP-RYGGVYV-GTLSkpeVKEAVES 278
Cdd:COG3962 219 LADAAALIKSAKKPLIVAGGGVLYSGAREALRAFAETHGIPVVETQAGKSALAWDHPlNLGGVGVtGTLA---ANRAAEE 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      279 ADLILSVGALLSDFNTGSfsysyktknivefhsdhmkirNATFPGVQMKFvlqkLLTNIA--DAAK-GYKPVAVPARTPA 355
Cdd:COG3962 296 ADLVIGIGTRLQDFTTGS---------------------KALFKNPGVKF----LNLNVQpfDAYKhDALPLVADARAGL 350
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      356 NAAVPASTPLKQEWMW-----NQLGNFLQEGDVVIAETG--------TSAFG-INQTTFPNNTY--------GISQVLWG 413
Cdd:COG3962 351 EALSEALGGYRTAAGWtdereRLKAAWDAEADAPTAKNHflntlptqTQVIGaVQRTISDDSVVvcaagslpGDLHKLWR 430
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      414 S--------------IGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY-TIEK 478
Cdd:COG3962 431 AgvpgtyhleygfscMGYEIAGGLGAKAA----EPDREVYVMVGDGSYMMLNSELATSVMLGKKIIVVLLDNRGYgCINR 506
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
1PYD_A      479 L--IHGPKAQYNEIQGWDHLSLLP---------TFGAKDYETH 510
Cdd:COG3962 507 LqmATGGASFNNLLRDTDHEEEILqvdfaahaeSYGAKAYKVG 549
PRK07710 PRK07710
acetolactate synthase large subunit;
10-471 1.44e-13

acetolactate synthase large subunit;


Pssm-ID: 236076 [Multi-domain]  Cd Length: 571  Bit Score: 73.26  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        10 LFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKGM-SCIITTFGVGELSALNGIAGS 88
Cdd:PRK07710  22 LIEALEKEGVEVIFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARISGKpGVVIATSGPGATNVVTGLADA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        89 YAEH---VGVLHVVGVPSISSQAKQlllhhtlgngdftvfhrmSANISETTAMITD---IATAPAEIDRCIRTTY---VT 159
Cdd:PRK07710 101 MIDSlplVVFTGQVATSVIGSDAFQ------------------EADIMGITMPVTKhnyQVRKASDLPRIIKEAFhiaTT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       160 QR--PVYLGLPANLVdlnVPAKLLQTPIDMSL---KPNdAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKL 234
Cdd:PRK07710 163 GRpgPVLIDIPKDMV---VEEGEFCYDVQMDLpgyQPN-YEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       235 IDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHM 314
Cdd:PRK07710 239 AEQQEIPVVHTLLGLGGFPADHPLFLGM-AGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       315 KI-RN--ATFPGV-QMKFVLQKLLT---NIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAE 387
Cdd:PRK07710 318 EIgKNvpTEIPIVaDAKQALQVLLQqegKKENHHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTD 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       388 TGTSAFGINQ-TTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYL 466
Cdd:PRK07710 398 VGQHQMWAAQyYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLA----KPDETVVAIVGDGGFQMTLQELSVIKELSLPVKV 473

                 ....*
1PYD_A       467 FVLNN 471
Cdd:PRK07710 474 VILNN 478
PRK07092 PRK07092
benzoylformate decarboxylase; Reviewed
11-474 2.07e-13

benzoylformate decarboxylase; Reviewed


Pssm-ID: 235931 [Multi-domain]  Cd Length: 530  Bit Score: 72.68  E-value: 2.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        11 FERLKQVNVNTVFGLPGDFNLSLL----DKIYEVEGMRwagnanELNAAYAADGYARIKGMSCII---TTFGVGelSALN 83
Cdd:PRK07092  19 IDLLRRFGITTVFGNPGSTELPFLrdfpDDFRYVLGLQ------EAVVVGMADGYAQATGNAAFVnlhSAAGVG--NAMG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        84 GIAGSYAehvgvlhvVGVPSI---SSQAKQLL-LHHTLGNGDFTVFHRMSANISETTAMITDIataPAEIDRCIRTTYVT 159
Cdd:PRK07092  91 NLFTAFK--------NHTPLVitaGQQARSILpFEPFLAAVQAAELPKPYVKWSIEPARAEDV---PAAIARAYHIAMQP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       160 QR-PVYLGLPANlvDLNVPAKLLqTPIDMSlkpNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLT 238
Cdd:PRK07092 160 PRgPVFVSIPYD--DWDQPAEPL-PARTVS---SAVRPDPAALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERH 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       239 QFPAFVTPM-GKGSISEQHPRYGGVYvgTLSKPEVKEAVESADLILSVGALLsdfntgsFSYSyktkniVEFHSDHMKIR 317
Cdd:PRK07092 234 RAPVWVAPMsGRCSFPEDHPLFAGFL--PASREKISALLDGHDLVLVIGAPV-------FTYH------VEGPGPHLPEG 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       318 NATF-----PGV------------QMKFVLQKLLTNIADAAKgykpVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQE 380
Cdd:PRK07092 299 AELVqltddPGEaawapmgdaivgDIRLALRDLLALLPPSAR----PAPPARPMPPPAPAPGEPLSVAFVLQTLAALRPA 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       381 GDVVIAETgTSAFGINQTTFP---NNTY--GISqvlwGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEIS 455
Cdd:PRK07092 375 DAIVVEEA-PSTRPAMQEHLPmrrQGSFytMAS----GGLGYGLPAAVGVALA----QPGRRVIGLIGDGSAMYSIQALW 445
                        490       500
                 ....*....|....*....|
1PYD_A       456 TMIRWGLkPYLFV-LNNDGY 474
Cdd:PRK07092 446 SAAQLKL-PVTFViLNNGRY 464
PRK07979 PRK07979
acetolactate synthase 3 large subunit;
19-471 2.33e-13

acetolactate synthase 3 large subunit;


Pssm-ID: 181185 [Multi-domain]  Cd Length: 574  Bit Score: 72.58  E-value: 2.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        19 VNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNGIAGSYAEHVGVLH 97
Cdd:PRK07979  19 VKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDSIPLVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        98 vvgvpsISSQ-AKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIataPAEIDRCIRTTyVTQRP--VYLGLPANLVDl 174
Cdd:PRK07979  99 ------LSGQvATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDI---PQVLKKAFWLA-ASGRPgpVVVDLPKDILN- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       175 nvPAKLLQT--PIDMSLKPND--AESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKG 250
Cdd:PRK07979 168 --PANKLPYvwPESVSMRSYNptTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSSLMGLG 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       251 SISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIR---NATFPGV-QM 326
Cdd:PRK07979 246 AFPATHRQSLGM-LGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISktvTADIPIVgDA 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       327 KFVLQKLLTNIADAAKGYKPVAVP----------ARTPANAAVPASTPLKQ---EWMWNqlgnfLQEGDVVIaetgTSAF 393
Cdd:PRK07979 325 RQVLEQMLELLSQESAHQPLDEIRdwwqqieqwrARQCLKYDTHSEKIKPQaviETLWR-----LTKGDAYV----TSDV 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       394 GINQT------TFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLF 467
Cdd:PRK07979 396 GQHQMfaalyyPFDKPRRWINSGGLGTMGFGLPAALGVKMAL----PEETVVCVTGDGSIQMNIQELSTALQYELPVLVL 471

                 ....
1PYD_A       468 VLNN 471
Cdd:PRK07979 472 NLNN 475
PRK07418 PRK07418
acetolactate synthase large subunit;
10-471 5.25e-12

acetolactate synthase large subunit;


Pssm-ID: 236014 [Multi-domain]  Cd Length: 616  Bit Score: 68.54  E-value: 5.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        10 LFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGN---ANELNAAYAADGYARIKGM--SCIITTfGVGELSALNG 84
Cdd:PRK07418  25 LMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAEGWLKHilvRHEQGAAHAADGYARATGKvgVCFGTS-GPGATNLVTG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        85 IAGSYAEH---VGVLHVVGVPSISSQAKQlllhhtlgngdftvfhrmSANISETTAMITD---IATAPAEIDRCIRTTY- 157
Cdd:PRK07418 104 IATAQMDSvpmVVITGQVPRPAIGTDAFQ------------------ETDIFGITLPIVKhsyVVRDPSDMARIVAEAFh 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       158 --VTQR--PVYLGLPANlVDLN----VPAKllqtPIDMSL-------KPNDAEsekevIDTILALVKDAKNP-------V 215
Cdd:PRK07418 166 iaSSGRpgPVLIDIPKD-VGQEefdyVPVE----PGSVKPpgyrptvKGNPRQ-----INAALKLIEEAERPllyvgggA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       216 ILADAccsrHDvkaETKKLIDLTQFPAFVTPMGKGSISEQHPryggVYVGTL---SKPEVKEAVESADLILSVGALLSDF 292
Cdd:PRK07418 236 ISAGA----HA---ELKELAERFQIPVTTTLMGKGAFDEHHP----LSVGMLgmhGTAYANFAVTECDLLIAVGARFDDR 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       293 NTGSF-SYSYKTKNIvefhsdHMKI--------RNATFPGV-QMKFVLQKLLtniadaaKGYKPVAVPARTpanaavpas 362
Cdd:PRK07418 305 VTGKLdEFASRAKVI------HIDIdpaevgknRRPDVPIVgDVRKVLVKLL-------ERSLEPTTPPRT--------- 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       363 tplkQEWM-----WNQLGNFL---QEGDV----VIAETG--------TSAFGINQ---TTFPNNtyG----ISQVLWGSI 415
Cdd:PRK07418 363 ----QAWLerinrWKQDYPLVvppYEGEIypqeVLLAVRdlapdayyTTDVGQHQmwaAQFLRN--GprrwISSAGLGTM 436
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
1PYD_A       416 GFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK07418 437 GFGMPAAMGVKVAL----PDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN 488
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
387-474 7.21e-12

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 426974 [Multi-domain]  Cd Length: 151  Bit Score: 63.37  E-value: 7.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        387 ETGTSAFGINQ--TTFPNNTYgISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLKP 464
Cdd:pfam02775   1 DIGCHQMWAAQyyRFRPPRRY-LTSGGLGTMGYGLPAAIGAKLA----RPDRPVVAIAGDGGFQMNLQELATAVRYNLPI 75
                          90
                  ....*....|
1PYD_A        465 YLFVLNNDGY 474
Cdd:pfam02775  76 TVVVLNNGGY 85
PLN02470 PLN02470
acetolactate synthase
10-471 8.02e-12

acetolactate synthase


Pssm-ID: 215261 [Multi-domain]  Cd Length: 585  Bit Score: 67.84  E-value: 8.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        10 LFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCI-ITTFGVGELSALNGIAGS 88
Cdd:PLN02470  19 LVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVcIATSGPGATNLVTGLADA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        89 YAEHVGVLhvvgvpSISSQAKQLLLhhtlGNGDF--TVFHRMSANISETTAMITDIAtapaEIDRCIRTTYVTQR----- 161
Cdd:PLN02470  99 LLDSVPLV------AITGQVPRRMI----GTDAFqeTPIVEVTRSITKHNYLVMDVE----DIPRVIREAFFLASsgrpg 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       162 PVYLGLPANLV------DLNVPAKLlqtPIDMSLKPndAESEKEVIDTILALVKDAKNPVILADACCSrhDVKAETKKLI 235
Cdd:PLN02470 165 PVLVDIPKDIQqqlavpNWNQPMKL---PGYLSRLP--KPPEKSQLEQIVRLISESKRPVVYVGGGCL--NSSEELREFV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       236 DLTQFPAFVTPMGKGSISEQHPRY-------GGVYVGTlskpevkeAVESADLILSVGALLSDFNTGSFSYSYKTKNIVE 308
Cdd:PLN02470 238 ELTGIPVASTLMGLGAFPASDELSlqmlgmhGTVYANY--------AVDSADLLLAFGVRFDDRVTGKLEAFASRASIVH 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       309 FHSDHMKIRNATFPGVQM----KFVLQKLLTNI-ADAAKGYKPVAVPARTPAN-AAVPASTPLKQEWMWNQ----LGNFL 378
Cdd:PLN02470 310 IDIDPAEIGKNKQPHVSVcadvKLALQGLNKLLeERKAKRPDFSAWRAELDEQkEKFPLSYPTFGDAIPPQyaiqVLDEL 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       379 QEGDVVIAeTGTsafGINQT------TFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQ 452
Cdd:PLN02470 390 TDGNAIIS-TGV---GQHQMwaaqwyKYKEPRRWLTSGGLGAMGFGLPAAIGAAAA----NPDAIVVDIDGDGSFIMNIQ 461
                        490
                 ....*....|....*....
1PYD_A       453 EISTMIRWGLKPYLFVLNN 471
Cdd:PLN02470 462 ELATIHVENLPVKIMVLNN 480
PRK08978 PRK08978
acetolactate synthase 2 catalytic subunit; Reviewed
14-471 8.50e-12

acetolactate synthase 2 catalytic subunit; Reviewed


Pssm-ID: 181601 [Multi-domain]  Cd Length: 548  Bit Score: 67.60  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        14 LKQVNVNTVFGLPGDFNLSLLDKIY--EVEGM--RwagnaNELNAAYAADGYARIKGMS--CIITTfGVGELSALNGIAG 87
Cdd:PRK08978  11 LRAQGVDTVFGYPGGAIMPVYDALYdgGVEHLlcR-----HEQGAAMAAIGYARATGKVgvCIATS-GPGATNLITGLAD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        88 SYAEhvgvlhvvGVP--SISSQAKQLLlhhtLGNGDFT---VFHrMSANISETTAMITDIATAPAEIDRCIRttyVTQR- 161
Cdd:PRK08978  85 ALLD--------SVPvvAITGQVSSPL----IGTDAFQeidVLG-LSLACTKHSFLVQSLEELPEIMAEAFE---IASSg 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       162 ---PVylglpanLVDLNVPAKLLQTPIDMSLKPNDAESE--KEVIDTILALVKDAKNPVI-------LADAccsrhdVKA 229
Cdd:PRK08978 149 rpgPV-------LVDIPKDIQLAEGELEPHLTTVENEPAfpAAELEQARALLAQAKKPVLyvgggvgMAGA------VPA 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       230 eTKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSF-SYSYKTKNIve 308
Cdd:PRK08978 216 -LREFLAATGMPAVATLKGLGAVEADHPYYLGM-LGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLnTFAPHAKVI-- 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       309 fhsdHM--------KIR----------NATFPGVQMKFVLQKLLTNIADAAKGYK--------PVAVPA-------RTPA 355
Cdd:PRK08978 292 ----HLdidpaeinKLRqahvalqgdlNALLPALQQPLNIDAWRQHCAQLRAEHAwrydhpgeAIYAPAllkqlsdRKPA 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       356 NAAVpaSTPLKQEWMW-------NQLGNFLqegdvviaetgTSAfGInqttfpnntygisqvlwGSIGFTTGATLGAAFA 428
Cdd:PRK08978 368 DTVV--TTDVGQHQMWvaqhmrfTRPENFI-----------TSS-GL-----------------GTMGFGLPAAIGAQVA 416
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
1PYD_A       429 aeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK08978 417 ----RPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDN 455
TPP_PYR_POX cd07039
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ...
5-171 1.26e-11

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: 62.95  E-value: 1.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        5 TLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALN 83
Cdd:cd07039   1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGkLGVCLGSSGPGAIHLLN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       84 GIAGSYAEhvgvlhvvGVP--SISSQakqllLHHTLGNGDF---TVFHRMSANISETTAMITDIATAPAEIDRCIRTTYV 158
Cdd:cd07039  81 GLYDAKRD--------RAPvlAIAGQ-----VPTDELGTDYfqeVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIA 147
                       170
                ....*....|...
1PYD_A      159 TQRPVYLGLPANL 171
Cdd:cd07039 148 KRGVAVLILPGDV 160
Gcl COG3960
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];
14-474 1.43e-11

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


Pssm-ID: 226469 [Multi-domain]  Cd Length: 592  Bit Score: 66.83  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       14 LKQVNVNTVFGLPGdfnlSLLDKIYEveGMRWAGNANEL------NAAYAADGYARIK--GMSCIITTFGVGELSALNGI 85
Cdd:COG3960  14 LEKEGITTAFGVPG----AAINPFYS--ALRKHGGIRHIlarhveGASHMAEGYTRATagNIGVCIGTSGPAGTDMITGL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       86 AGSYAEHVGVLhvvgvpSISSQAKQLLLHHTlgngDFtvfhrMSANISETTAMITDIATA---PAEIDRCIRTTYVTQRP 162
Cdd:COG3960  88 YSASADSIPIL------CITGQAPRARLHKE----DF-----QAVDIEAIAKPVSKWAVTvrePALVPRVLQQAFHLMRS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      163 vylGLPAN-LVDLNVPAKLLQTPIDMS----LKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDL 237
Cdd:COG3960 153 ---GRPGPvLIDLPFDVQVAEIEFDPDmyepLPVYKPAATRVQAEKALAMLIQAERPLIVAGGGVINADAAALLQEFAEL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      238 TQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEA-VESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKI 316
Cdd:COG3960 230 TGVPVIPTLMGWGCIPDDHPLMAGM-VGLQTSHRYGNAtLLASDMVFGIGNRWANRHTGSVEVYTEGRKFIHVDIEPTQI 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      317 RNATFPGVQMKFVLQKLLTNIADAAKGYKPVA-VPARTPANAAVPA------------STPLKQEWMWNQLGNFLQEGDV 383
Cdd:COG3960 309 GRVFCPDLGIVSDAKAALTLLLDVAQEWKKAGkLPCRKAWVADCQQrkrtllrkthfdNVPVKPQRVYEEMNKAFGRDVC 388
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      384 VIAETGTSAFGINQTTF---PNNTYGISQVlwGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRW 460
Cdd:COG3960 389 YVTTIGLSQIAAAQFLHvfkPRHWINCGQA--GPLGWTIPAALGVCAA----DPKRNVVAISGDYDFQFLIEELAVGAQF 462
                       490
                ....*....|....
1PYD_A      461 GLkPYLFVLNNDGY 474
Cdd:COG3960 463 KI-PYIHVLVNNAY 475
PRK08979 PRK08979
acetolactate synthase 3 large subunit;
18-471 4.92e-11

acetolactate synthase 3 large subunit;


Pssm-ID: 181602 [Multi-domain]  Cd Length: 572  Bit Score: 65.23  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        18 NVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNGIAGSYAEHVGVL 96
Cdd:PRK08979  18 GVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGkVGVVLVTSGPGATNTITGIATAYMDSIPMV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        97 HvvgvpsISSQAKQLLlhhtLGNGDFTVFHR--MSANISETTAMITDIATAPAEIDRCIrttYV--TQR--PVYLGLPAN 170
Cdd:PRK08979  98 V------LSGQVPSNL----IGNDAFQECDMigISRPVVKHSFLVKDAEDIPEIIKKAF---YIasTGRpgPVVIDLPKD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       171 LVDlnvPAKLL--QTPIDMSLK---PNDAESEKEVIDTILALVKdAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVT 245
Cdd:PRK08979 165 CLN---PAILHpyEYPESIKMRsynPTTSGHKGQIKRGLQALLA-AKKPVLYVGGGAIISGADKQILQLAEKLNLPVVST 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       246 PMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRN---ATFP 322
Cdd:PRK08979 241 LMGLGAFPGTHKNSLGM-LGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKtvrVDIP 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       323 GV-QMKFVLQKLLTNIADAAKGYKPVAVPA--------RTPANAAVPASTP-LKQEWMWNQLGNfLQEGDVVIAetgtSA 392
Cdd:PRK08979 320 IVgSADKVLDSMLALLDESGETNDEAAIASwwneievwRSRNCLAYDKSSErIKPQQVIETLYK-LTNGDAYVA----SD 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       393 FGINQT------TFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYL 466
Cdd:PRK08979 395 VGQHQMfaalyyPFDKPRRWINSGGLGTMGFGLPAAMGVKFAM----PDETVVCVTGDGSIQMNIQELSTALQYDIPVKI 470

                 ....*
1PYD_A       467 FVLNN 471
Cdd:PRK08979 471 INLNN 475
PRK09259 PRK09259
putative oxalyl-CoA decarboxylase; Validated
9-473 6.12e-11

putative oxalyl-CoA decarboxylase; Validated


Pssm-ID: 236433 [Multi-domain]  Cd Length: 569  Bit Score: 65.01  E-value: 6.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         9 YLFERLKQVNVNTVFGLPGdFNLSLLDKIYEVEGMRWAGNANELNAAYAA--DGYARIKGMSCIiTTFGVGELSALNGIA 86
Cdd:PRK09259  15 LVIDALKLNGIDTIYGVVG-IPITDLARLAQAEGIRYIGFRHEQSAGNAAaaAGFLTQKPGVCL-TVSAPGFLNGLTALA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        87 GSyaehvgvlHVVGVPSI----SSQAKQLLLHHtlgnGDFTVFHRMSANISETTAM-----ITDIATAPAeidRCIRTTy 157
Cdd:PRK09259  93 NA--------TTNCFPMImisgSSEREIVDLQQ----GDYEELDQLNAAKPFCKAAfrvnrAEDIGIGVA---RAIRTA- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       158 VTQRP--VYLGLPANLV----DLNVPAKLLQTPIDMSLK--PNDaesekEVIDTILALVKDAKNPVIL--ADACCSRHDv 227
Cdd:PRK09259 157 VSGRPggVYLDLPAKVLaqtmDADEALTSLVKVVDPAPAqlPAP-----EAVDRALDLLKKAKRPLIIlgKGAAYAQAD- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       228 kAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVYVGTlskpevkeAVESADLILSVGA----LLSDFNTGSFSYSYKT 303
Cdd:PRK09259 231 -EQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSL--------ALANADVVLLVGArlnwLLSHGKGKTWGADKKF 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       304 KNI----VEFHSDhMKIrNATFPGvQMKFVLQKLLTNIadAAKGYKPVA-----VPARTPANAAVPAST------PLKqe 368
Cdd:PRK09259 302 IQIdiepQEIDSN-RPI-AAPVVG-DIGSVMQALLAGL--KQNTFKAPAewldaLAERKEKNAAKMAEKlstdtqPMN-- 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       369 wMWNQLG---NFLQEG-DV-VIAEtgtsafGINQTTFPNNTYGISQV-------LWGSIGFTTGATLGAAfaaeeIDPKK 436
Cdd:PRK09259 375 -FYNALGairDVLKENpDIyLVNE------GANTLDLARNIIDMYKPrhrldcgTWGVMGIGMGYAIAAA-----VETGK 442
                        490       500       510
                 ....*....|....*....|....*....|....*..
1PYD_A       437 RVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDG 473
Cdd:PRK09259 443 PVVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGG 479
PRK07586 PRK07586
acetolactate synthase large subunit;
334-476 1.67e-10

acetolactate synthase large subunit;


Pssm-ID: 236063 [Multi-domain]  Cd Length: 514  Bit Score: 63.32  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       334 LTNIADA--AKGYKPVAVPARTPAnaavPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTT-------FPNNT 404
Cdd:PRK07586 308 LEALADAlgAKPAAPPLAAPARPP----LPTGALTPEAIAQVIAALLPENAIVVDESITSGRGFFPATagaaphdWLTLT 383
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1PYD_A       405 yGisqvlwGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTI 476
Cdd:PRK07586 384 -G------GAIGQGLPLATGAAVAC----PDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAI 444
PRK06965 PRK06965
acetolactate synthase 3 catalytic subunit; Validated
2-471 1.74e-10

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 180780 [Multi-domain]  Cd Length: 587  Bit Score: 63.67  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         2 SEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELS 80
Cdd:PRK06965  19 ADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGkVGVALVTSGPGVTN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        81 ALNGIAGSYAEHVGVLHvvgvpsISSQAKQlllhHTLGNGDF----TVfhRMSANISETTAMITDiataPAEIDRCIRTT 156
Cdd:PRK06965  99 AVTGIATAYMDSIPMVV------ISGQVPT----AAIGQDAFqecdTV--GITRPIVKHNFLVKD----VRDLAETVKKA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       157 YVTQRPvylGLPANLVdlnvpaklLQTPIDMSLKPNDAESEKEV---------------IDTILALVKDAKNP------- 214
Cdd:PRK06965 163 FYIART---GRPGPVV--------VDIPKDVSKTPCEYEYPKSVemrsynpvtkghsgqIRKAVSLLLSAKRPyiytggg 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       215 VILADACcsrhdvkAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNT 294
Cdd:PRK06965 232 VILANAS-------RELRQLADLLGYPVTNTLMGLGAYPASDKKFLGM-LGMHGTYEANMAMQHCDVLIAIGARFDDRVI 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       295 GSFS-YSYKTKNIVEFHSDHMKIR---NATFPGV-QMKFVLQKLLTNIADAAKGYKPVAVPARTPANAAVPASTPLKQ-- 367
Cdd:PRK06965 304 GNPAhFASRPRKIIHIDIDPSSISkrvKVDIPIVgDVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGWRSRDCLKYdr 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       368 -----------EWMWNqlgnfLQEGDVVIaetgTSAFGINQtTFPNNTYGISQV-LW---GSIGfTTGATLGAAFAAEEI 432
Cdd:PRK06965 384 eseiikpqyvvEKLWE-----LTDGDAFV----CSDVGQHQ-MWAAQFYRFNEPrRWinsGGLG-TMGVGLPYAMGIKMA 452
                        490       500       510
                 ....*....|....*....|....*....|....*....
1PYD_A       433 DPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06965 453 HPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNN 491
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
373-478 5.59e-10

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: 58.38  E-value: 5.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      373 QLGNFLQEGDVVIAETGTSAFGINQ---TTFPNNTYGISQvlwGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQL 449
Cdd:cd02002   9 ALAAALPEDAIIVDEAVTNGLPLRDqlpLTRPGSYFTLRG---GGLGWGLPAAVGAALA----NPDRKVVAIIGDGSFMY 81
                        90       100       110
                ....*....|....*....|....*....|
1PYD_A      450 TVQEISTMIRWGLkPYLFV-LNNDGYTIEK 478
Cdd:cd02002  82 TIQALWTAARYGL-PVTVViLNNRGYGALR 110
PRK07789 PRK07789
acetolactate synthase 1 catalytic subunit; Validated
14-456 7.39e-10

acetolactate synthase 1 catalytic subunit; Validated


Pssm-ID: 236098 [Multi-domain]  Cd Length: 612  Bit Score: 61.54  E-value: 7.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        14 LKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMS--CIITTfGVGELSALNGIAGSYAE 91
Cdd:PRK07789  41 LEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVgvCMATS-GPGATNLVTPIADANMD 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        92 hvgvlhvvGVP--SISSQAKQLLlhhtLGNGDFtvfhrMSANISETTAMITD---IATAPAEIDRCIRTTY---VTQRPv 163
Cdd:PRK07789 120 --------SVPvvAITGQVGRGL----IGTDAF-----QEADIVGITMPITKhnfLVTDADDIPRVIAEAFhiaSTGRP- 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       164 ylGlpANLVDlnVPAKLLQT------PIDMSL---KPNDAESEKeVIDTILALVKDAKNPVILADACCSRHDVKAETKKL 234
Cdd:PRK07789 182 --G--PVLVD--IPKDALQAqttfswPPRMDLpgyRPVTKPHGK-QIREAAKLIAAARRPVLYVGGGVIRAEASAELREL 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       235 IDLTQFPAFVTPMGKGSISEQHPRYGGV--YVGTLskPEVKeAVESADLILSVGALLSDFNTG---SFSYSYKtknIVef 309
Cdd:PRK07789 255 AELTGIPVVTTLMARGAFPDSHPQHLGMpgMHGTV--AAVA-ALQRSDLLIALGARFDDRVTGkldSFAPDAK---VI-- 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       310 HSD-----HMKIRNATFPGV-QMKFVLQKLLTNI-ADAAKGYKPV---------AVPARTPANAAVPASTPLKQEWMWNQ 373
Cdd:PRK07789 327 HADidpaeIGKNRHADVPIVgDVKEVIAELIAALrAEHAAGGKPDltawwayldGWRETYPLGYDEPSDGSLAPQYVIER 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       374 LGnflqegdvviAETGTSAF---GINQ-----TTF-----PN---NTYGIsqvlwGSIGFTTGATLGAAFAAeeidPKKR 437
Cdd:PRK07789 407 LG----------EIAGPDAIyvaGVGQhqmwaAQFidyekPRtwlNSGGL-----GTMGYAVPAAMGAKVGR----PDKE 467
                        490
                 ....*....|....*....
1PYD_A       438 VILFIGDGSLQLTVQEIST 456
Cdd:PRK07789 468 VWAIDGDGCFQMTNQELAT 486
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
413-471 3.78e-09

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: 56.35  E-value: 3.78e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
1PYD_A      413 GSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:cd02015  50 GTMGFGLPAAIGAKVAR----PDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNN 104
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
376-507 6.12e-09

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: 55.23  E-value: 6.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      376 NFLQEGDVVIAEtGTSAFGINQTTFPNN---TYGISQVlWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQ 452
Cdd:cd02004  10 EALPDDAIIVSD-GGNTMDWARYILRPRkprHRLDAGT-FGTLGVGLGYAIAAALAR----PDKRVVLVEGDGAFGFSGM 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1PYD_A      453 EISTMIRWGLKPYLFVLNNDGYTIEKliHGPKAQYNEIQgwDHLSLLPT---------FGAKDY 507
Cdd:cd02004  84 ELETAVRYNLPIVVVVGNNGGWYQGL--DGQQLSYGLGL--PVTTLLPDtrydlvaeaFGGKGE 143
PRK06457 PRK06457
pyruvate dehydrogenase; Provisional
5-471 6.54e-09

pyruvate dehydrogenase; Provisional


Pssm-ID: 180570 [Multi-domain]  Cd Length: 549  Bit Score: 58.30  E-value: 6.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         5 TLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALN 83
Cdd:PRK06457   3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRK-SKVKYVQVRHEEGAALAASVEAKITGkPSACMGTSGPGSIHLLN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        84 GIAGSYAEHVGVLhvvgvpSISSQAKQLLLHHtlgngDFtvFH-----RMSANISETTAMITDIATAPAEIDRCIRTTyV 158
Cdd:PRK06457  82 GLYDAKMDHAPVI------ALTGQVESDMIGH-----DY--FQevnltKLFDDVAVFNQILINPENAEYIIRRAIREA-I 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       159 TQRPV-YLGLPANLVDLNVPAKLLQ-TPIDMSLKPNDAESEKEVIDtilalvkDAKNPVILADAccSRHDVKAETKKLID 236
Cdd:PRK06457 148 SKRGVaHINLPVDILRKSSEYKGSKnTEVGKVKYSIDFSRAKELIK-------ESEKPVLLIGG--GTRGLGKEINRFAE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       237 LTQFPAFVTPMGKGSISEQHPR-YGGV-YVGTlsKPEVkEAVESADLILSVGAllsdfntgSFSYS----YKTKNI-VEF 309
Cdd:PRK06457 219 KIGAPIIYTLNGKGILPDLDPKvMGGIgLLGT--KPSI-EAMDKADLLIMLGT--------SFPYVnflnKSAKVIqVDI 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       310 HSDHMKIR----------NATFPGVQMKFVLQKLLTNIADAAKGYKpvavpaRTPANAAVPASTPLKQEWMWNQLGNFLQ 379
Cdd:PRK06457 288 DNSNIGKRldvdlsypipVAEFLNIDIEEKSDKFYEELKGKKEDWL------DSISKQENSLDKPMKPQRVAYIVSQKCK 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       380 EGDVVIAETGTSAFGINQ--TTFPNNTYGISQVLwGSIGFTTGATLGAAFAAeeiDPKKRVILFIGDGSLQLTVQEISTM 457
Cdd:PRK06457 362 KDAVIVTDTGNVTMWTARhfRASGEQTFIFSAWL-GSMGIGVPGSVGASFAV---ENKRQVISFVGDGGFTMTMMELITA 437
                        490
                 ....*....|....
1PYD_A       458 IRWGLKPYLFVLNN 471
Cdd:PRK06457 438 KKYDLPVKIIIYNN 451
PRK06466 PRK06466
acetolactate synthase 3 large subunit;
1-471 1.08e-08

acetolactate synthase 3 large subunit;


Pssm-ID: 180578 [Multi-domain]  Cd Length: 574  Bit Score: 57.83  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMS-CIITTFGVGEL 79
Cdd:PRK06466   1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTgVVLVTSGPGAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        80 SALNGIAGSYAEHVGVLHvvgvpsISSQAKQlllhHTLGNGDF--TVFHRMSANISETTAMITDiataPAEIDRCIRTT- 156
Cdd:PRK06466  81 NAITGIATAYMDSIPMVV------LSGQVPS----TLIGEDAFqeTDMVGISRPIVKHSFMVKH----ASEIPEIIKKAf 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       157 YVTQR----PVYLGLPANLVDLNV------PAKLLQTPIDMSLKPNDAESEKEViDTILAlvkdAKNPVILADACCSRHD 226
Cdd:PRK06466 147 YIAQSgrpgPVVVDIPKDMTNPAEkfeyeyPKKVKLRSYSPAVRGHSGQIRKAV-EMLLA----AKRPVIYSGGGVVLGN 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       227 VKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNI 306
Cdd:PRK06466 222 ASALLTELAHLLNLPVTNTLMGLGGFPGTDRQFLGM-LGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKI 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       307 VEFHSDHMKIRN---ATFPGV-QMKFVLQKLLTNIADAAKgykpvavparTPANAAVPAstplkqeWmWNQLGNFLQEGD 382
Cdd:PRK06466 301 IHIDIDPASISKtikADIPIVgPVESVLTEMLAILKEIGE----------KPDKEALAA-------W-WKQIDEWRGRHG 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       383 VVIAETGTSAFGINQTTFP-------NNTYGISQV-----------------LW---GSIGfTTGATLGAAFAAEEIDPK 435
Cdd:PRK06466 363 LFPYDKGDGGIIKPQQVVEtlyevtnGDAYVTSDVgqhqmfaaqyykfnkpnRWinsGGLG-TMGFGLPAAMGVKLAFPD 441
                        490       500       510
                 ....*....|....*....|....*....|....*.
1PYD_A       436 KRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06466 442 QDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNN 477
ilvB CHL00099
acetohydroxyacid synthase large subunit
10-471 1.11e-08

acetohydroxyacid synthase large subunit


Pssm-ID: 214363 [Multi-domain]  Cd Length: 585  Bit Score: 57.79  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        10 LFERLKQVNVNTVFGLPGDFNLSLLDKIY--EVEGM------RwagnaNELNAAYAADGYARIKGMS--CIITTfGVGEL 79
Cdd:CHL00099  16 LIDSLVRHGVKHIFGYPGGAILPIYDELYawEKKGLikhilvR-----HEQGAAHAADGYARSTGKVgvCFATS-GPGAT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        80 SALNGIAGSYAEHVGVLHvvgvpsISSQAKQLLLhhtlGNGDFT-----------VFHrmSANISETTAMITDIATApae 148
Cdd:CHL00099  90 NLVTGIATAQMDSVPLLV------ITGQVGRAFI----GTDAFQevdifgitlpiVKH--SYVVRDARDISRIVAEA--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       149 idrcirtTYVTQR----PVYLGLPANL----------VDLNVPAKLLQTPIDMSLKPNDaesekevIDTILALVKDAKNP 214
Cdd:CHL00099 155 -------FYIAKHgrpgPVLIDIPKDVglekfdyyppEPGNTIIKILGCRPIYKPTIKR-------IEQAAKLILQSSQP 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       215 -------VILADAccsrhdvKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGA 287
Cdd:CHL00099 221 llyvgggAIISDA-------HQEITELAELYKIPVTTTLMGKGIFDEDHPLCLGM-LGMHGTAYANFAVSECDLLIALGA 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       288 LLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNATFPGV----QMKFVLQKLLTNIADAAKGYKPVAVPA-RTPANA---AV 359
Cdd:CHL00099 293 RFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVaivgDVKKVLQELLELLKNSPNLLESEQTQAwRERINRwrkEY 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       360 PASTPLKQEWMWNQlgnflqegdVVIAETGTSAfginQTTFPNNTYGISQvLW------------------GSIGFTTGA 421
Cdd:CHL00099 373 PLLIPKPSTSLSPQ---------EVINEISQLA----PDAYFTTDVGQHQ-MWaaqflkckprkwlssaglGTMGYGLPA 438
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
1PYD_A       422 TLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:CHL00099 439 AIGAQIA----HPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINN 484
PRK08155 PRK08155
acetolactate synthase large subunit;
14-472 5.64e-07

acetolactate synthase large subunit;


Pssm-ID: 181257 [Multi-domain]  Cd Length: 564  Bit Score: 52.40  E-value: 5.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        14 LKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMS--CIITTfGVGELSALNGIAGSYAE 91
Cdd:PRK08155  23 LERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPavCMACS-GPGATNLVTAIADARLD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        92 HV-GVLHVVGVPS--ISSQAKQLLlhHTLGngdftvfhrMSANISETTAMITDIATAPAEIDRCIRttyVTQR----PVY 164
Cdd:PRK08155 102 SIpLVCITGQVPAsmIGTDAFQEV--DTYG---------ISIPITKHNYLVRDIEELPQVISDAFR---IAQSgrpgPVW 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       165 LGLPAN----LVDLnvpAKLLQTPIDMSLKPNDAESekevIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQF 240
Cdd:PRK08155 168 IDIPKDvqtaVIEL---EALPAPAEKDAAPAFDEES----IRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       241 PAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTG---SFSYSYKTKNIVEFHSDHMKIR 317
Cdd:PRK08155 241 PTTMTLMALGMLPKAHPLSLGM-LGMHGARSTNYILQEADLLIVLGARFDDRAIGkteQFCPNAKIIHVDIDRAELGKIK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       318 NATFpGVQ--MKFVLQKLLTNIADAAKG--YKPVA-----VPARTPAnaavpASTPLKQEWMWNQLGNFLQEGDVVIAET 388
Cdd:PRK08155 320 QPHV-AIQadVDDVLAQLLPLVEAQPRAewHQLVAdlqreFPCPIPK-----ADDPLSHYGLINAVAACVDDNAIITTDV 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       389 GTSAFGINQTtFPNNtyGISQVL----WGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKP 464
Cdd:PRK08155 394 GQHQMWTAQA-YPLN--RPRQWLtsggLGTMGFGLPAAIGAALAN----PERKVLCFSGDGSLMMNIQEMATAAENQLDV 466

                 ....*...
1PYD_A       465 YLFVLNND 472
Cdd:PRK08155 467 KIILMNNE 474
PRK11269 PRK11269
glyoxylate carboligase; Provisional
14-474 6.76e-07

glyoxylate carboligase; Provisional


Pssm-ID: 183066 [Multi-domain]  Cd Length: 591  Bit Score: 51.90  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        14 LKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIK----GMsCIITTFGVGElsalNGIAGSY 89
Cdd:PRK11269  14 LEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATagniGV-CIGTSGPAGT----DMITGLY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        90 AehvgvLHVVGVP--SISSQAKQLLLHHTlgngDFtvfhrMSANISETTAMITDIATA---PAEIDRCIRTTYVTQR--- 161
Cdd:PRK11269  89 S-----ASADSIPilCITGQAPRARLHKE----DF-----QAVDIESIAKPVTKWAVTvrePALVPRVFQQAFHLMRsgr 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       162 --PVYLGLPanlvdLNVPAKLLQTPIDM--SLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDL 237
Cdd:PRK11269 155 pgPVLIDLP-----FDVQVAEIEFDPDTyePLPVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAEL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       238 TQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEA--VESaDLILSVGALLSDFNTGSFSYSYKTKNIVE------- 308
Cdd:PRK11269 230 TGVPVIPTLMGWGAIPDDHPLMAGM-VGLQTSHRYGNAtlLAS-DFVLGIGNRWANRHTGSVEVYTKGRKFVHvdieptq 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       309 ----FHSDHMKIRNAtfpgvqmKFVLQKLLtniaDAAKGYKPV-AVPARTPANAAVPA------------STPLKQEWMW 371
Cdd:PRK11269 308 igrvFGPDLGIVSDA-------KAALELLV----EVAREWKAAgRLPDRSAWVADCQErkrtllrkthfdNVPIKPQRVY 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       372 NQLgnflqegdvviaetgTSAFGiNQTTFPnNTYGISQVL------------W------GSIGFTTGATLGAAFAaeeiD 433
Cdd:PRK11269 377 EEM---------------NKAFG-RDTCYV-STIGLSQIAaaqflhvykprhWincgqaGPLGWTIPAALGVRAA----D 435
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
1PYD_A       434 PKKRVILFIGDGSLQLTVQEISTMIRWGLkPYLFVLNNDGY 474
Cdd:PRK11269 436 PDRNVVALSGDYDFQFLIEELAVGAQFNL-PYIHVLVNNAY 475
PRK09107 PRK09107
acetolactate synthase 3 catalytic subunit; Validated
3-471 9.25e-07

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 236380 [Multi-domain]  Cd Length: 595  Bit Score: 51.63  E-value: 9.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         3 EITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSA 81
Cdd:PRK09107  10 QMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGkPGVVLVTSGPGATNA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        82 LNGIAGSYAEHVGVLhvvgvpSISSQAKQlllhHTLGNGDF----TVfhRMSANISETTAMITDIATAPAEIDRCIRTTy 157
Cdd:PRK09107  90 VTPLQDALMDSIPLV------CITGQVPT----HLIGSDAFqecdTV--GITRPCTKHNWLVKDVNDLARVIHEAFHVA- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       158 VTQRP--VYLGLPANLV----DLNVPAKLLQTPIDMSLKPNDAESekevIDTILALVKDAKNPVILADACCSRHDVKAET 231
Cdd:PRK09107 157 TSGRPgpVVVDIPKDVQfatgTYTPPQKAPVHVSYQPKVKGDAEA----ITEAVELLANAKRPVIYSGGGVINSGPEASR 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       232 --KKLIDLTQFPAFVTPMGKGSiseqHPRYGGVYVGTLSKP---EVKEAVESADLILSVGALLSDFNTG---SFSYSYKT 303
Cdd:PRK09107 233 llRELVELTGFPITSTLMGLGA----YPASGKNWLGMLGMHgtyEANMAMHDCDVMLCVGARFDDRITGrldAFSPNSKK 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       304 KNIVEFHSDHMKIRNATFPgvqmkfVLQKLLTNIADAAKGYKpvaVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDV 383
Cdd:PRK09107 309 IHIDIDPSSINKNVRVDVP------IIGDVGHVLEDMLRLWK---ARGKKPDKEALADWWGQIARWRARNSLAYTPSDDV 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       384 VIAEtgtsaFGINQ---TTFPNNTYGISQV----LWGS--IGF-------------TTGATLGAAFAAEEIDPKKRVILF 441
Cdd:PRK09107 380 IMPQ-----YAIQRlyeLTKGRDTYITTEVgqhqMWAAqfFGFeepnrwmtsgglgTMGYGLPAALGVQIAHPDALVIDI 454
                        490       500       510
                 ....*....|....*....|....*....|
1PYD_A       442 IGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK09107 455 AGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
PRK08617 PRK08617
acetolactate synthase AlsS;
14-286 9.71e-07

acetolactate synthase AlsS;


Pssm-ID: 236312 [Multi-domain]  Cd Length: 552  Bit Score: 51.39  E-value: 9.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        14 LKQVNVNTVFGLPG---D--FNlSLLDKIYEVEGMRwagnaNELNAAYAADGYARIKGMS-CIITTFGVGELSALNGIAG 87
Cdd:PRK08617  15 LINQGVKYVFGIPGakiDrvFD-ALEDSGPELIVTR-----HEQNAAFMAAAIGRLTGKPgVVLVTSGPGVSNLATGLVT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A        88 SYAEHVgvlhvvgvP--SISSQAK---QL-LLHHTLGNGDftvfhrMSANISETTAMITDIATAPAEIDRCIRTTyVTQR 161
Cdd:PRK08617  89 ATAEGD--------PvvAIGGQVKradRLkRTHQSMDNVA------LFRPITKYSAEVQDPDNLSEVLANAFRAA-ESGR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       162 P--VYLGLPANLVDLNVPAKLLQTPIDMSLKPNDAEsekeVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQ 239
Cdd:PRK08617 154 PgaAFVSLPQDVVDAPVTSKAIAPLSKPKLGPASPE----DINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTN 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
1PYD_A       240 FPAFVTPMGKGSISEQH-PRYGGvYVGTLSKPEVKEAVESADLILSVG 286
Cdd:PRK08617 230 LPVVETFQAAGVISRELeDHFFG-RVGLFRNQPGDELLKKADLVITIG 276
PRK08327 PRK08327
thiamine pyrophosphate-requiring protein;
351-474 1.41e-06

thiamine pyrophosphate-requiring protein;


Pssm-ID: 236243 [Multi-domain]  Cd Length: 569  Bit Score: 51.15  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       351 ARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFpnNTYgISQVLWGSIGFTTGATLGAAFAae 430
Cdd:PRK08327 371 AKRAEIERLKDRGPITPAYLSYCLGEVADEYDAIVTEYPFVPRQARLNKP--GSY-FGDGSAGGLGWALGAALGAKLA-- 445
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
1PYD_A       431 eiDPKKRVILFIGDGSLQLTVQEISTMI--RWGLKPYLFVLNNDGY 474
Cdd:PRK08327 446 --TPDRLVIATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
TPP_POX cd02014
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...
364-471 5.86e-06

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: 46.75  E-value: 5.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      364 PLKQEWMWNQLGNFLQEGDVVIAETGTSA-FGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFI 442
Cdd:cd02014   1 PIHPERVAAELNKRAPDDAIFTIDVGNVTvWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLA----YPDRQVIALS 76
                        90       100
                ....*....|....*....|....*....
1PYD_A      443 GDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:cd02014  77 GDGGFAMLMGDLITAVKYNLPVIVVVFNN 105
PRK12474 PRK12474
hypothetical protein; Provisional
334-476 4.70e-05

hypothetical protein; Provisional


Pssm-ID: 139002 [Multi-domain]  Cd Length: 518  Bit Score: 46.02  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A       334 LTNIADAAKGykPVAVPARTPANAAVPASTPLKQEwMWNQL-GNFLQEGDVVIAETGTS--AFGINQTTFPNNTYgiSQV 410
Cdd:PRK12474 312 LQDLADAVDA--PAEPAARTPLALPALPKGALNSL-GVAQLiAHRTPDQAIYADEALTSglFFDMSYDRARPHTH--LPL 386
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PYD_A       411 LWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTI 476
Cdd:PRK12474 387 TGGSIGQGLPLAAGAAVAA----PDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAI 448
TPP_ALS cd02010
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ...
418-508 5.21e-05

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: 44.20  E-value: 5.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      418 TTGATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTI----EKLIHGPKAqYNEIQGW 493
Cdd:cd02010  49 TMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQELETAVRLKIPLVVLIWNDNGYGLikwkQEKEYGRDS-GVDFGNP 127
                        90
                ....*....|....*
1PYD_A      494 DHLSLLPTFGAKDYE 508
Cdd:cd02010 128 DFVKYAESFGAKGYR 142
TPP_Xsc_like cd02013
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ...
364-478 3.32e-04

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: 42.11  E-value: 3.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      364 PLKQEWMWNQLGNFLQEGDVVIAETG-TSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFI 442
Cdd:cd02013   3 PMHPRQVLRELEKAMPEDAIVSTDIGnICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAA----PDRPVVAIA 78
                        90       100       110
                ....*....|....*....|....*....|....*.
1PYD_A      443 GDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEK 478
Cdd:cd02013  79 GDGAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEK 114
PRK09124 PRK09124
ubiquinone-dependent pyruvate dehydrogenase;
5-85 8.76e-04

ubiquinone-dependent pyruvate dehydrogenase;


Pssm-ID: 181661 [Multi-domain]  Cd Length: 574  Bit Score: 41.90  E-value: 8.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         5 TLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGM------SCiittfGVGE 78
Cdd:PRK09124   4 TVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGElavcagSC-----GPGN 78

                 ....*..
1PYD_A        79 LSALNGI 85
Cdd:PRK09124  79 LHLINGL 85
TPP_IolD cd02003
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ...
405-474 1.14e-03

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


Pssm-ID: 238961 [Multi-domain]  Cd Length: 205  Bit Score: 40.37  E-value: 1.14e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A      405 YGISqvlwgSIGFTTGATLGAAFAAEEIDpkkrVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY 474
Cdd:cd02003  45 YGYS-----CMGYEIAAGLGAKLAKPDRE----VYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGF 105
PRK08273 PRK08273
thiamine pyrophosphate protein; Provisional
1-84 2.66e-03

thiamine pyrophosphate protein; Provisional


Pssm-ID: 181344 [Multi-domain]  Cd Length: 597  Bit Score: 40.66  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A         1 MSEiTLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEG-MRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGE 78
Cdd:PRK08273   1 MSQ-TVADFILERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAHAKFTGeVGVCLATSGPGA 79

                 ....*.
1PYD_A        79 LSALNG 84
Cdd:PRK08273  80 IHLLNG 85
TPP_Gcl cd02006
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ...
413-474 3.90e-03

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: 38.80  E-value: 3.90e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1PYD_A      413 GSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLkPYLFVLNNDGY 474
Cdd:cd02006  57 GPLGWTVPAALGVAAA----DPDRQVVALSGDYDFQFMIEELAVGAQHRI-PYIHVLVNNAY 113
 
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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