|
Name |
Accession |
Description |
Interval |
E-value |
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
13-332 |
7.49e-164 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 460.76 E-value: 7.49e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 13 GLTDEQVIEMYTYMLKARMFDERCFLLQRSGKIPFHVSGIGQETAQVAAAYALKKGtDYFLPYYRDYGFVLTVGMTLREL 92
Cdd:COG1071 16 DLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPG-DWIFPTYRDHGHALARGVDPKEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 93 LLSVFLKAEDPnSGGRQLPGHFGSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRKEFVSFVTFGDGSSNQGDFHEGCNFA 172
Cdd:COG1071 95 MAELFGKATGP-SKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 173 GVHKLPVIFMCENNQYAISVPLHKQTAG-SIAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGEGPTLIEAVMYRI 251
Cdd:COG1071 174 AVWKLPVVFVCENNGYAISTPVERQTAVeTIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 252 SPHSTSDNDLLYRTREEVETNRERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYAEQAPHPASEDTLLHVYG 331
Cdd:COG1071 254 GGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYA 333
|
.
gi 1102105150 332 D 332
Cdd:COG1071 334 E 334
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
22-314 |
1.48e-140 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 399.56 E-value: 1.48e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 22 MYTYMLKARMFDERCFLLQRSGKIP-FHVSGIGQETAQVAAAYALKKGtDYFLPYYRDYGFVLTVGMTLRELLLSVFLKA 100
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGgFYHLSIGQEAVAVGVAAALRPG-DWVFPTYRDHGHALARGVDLKEMLAELFGKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 101 EDPnSGGRQLPGHFGSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRKEFVSFVTFGDGSSNQGDFHEGCNFAGVHKLPVI 180
Cdd:cd02000 80 TGP-CKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 181 FMCENNQYAISVPLHKQTAG-SIAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGEGPTLIEAVMYRISPHSTSDN 259
Cdd:cd02000 159 FVCENNGYAISTPTSRQTAGtSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDD 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1102105150 260 DLLYRTREEVETNRERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYA 314
Cdd:cd02000 239 PSRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
14-332 |
6.40e-131 |
|
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 213783 [Multi-domain] Cd Length: 341 Bit Score: 376.87 E-value: 6.40e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 14 LTDEQVIEMYTYMLKARMFDERCFLLQRSGKIPFHVSGIGQETAQVAAAYALKKGtDYFLPYYRDYGFVLTVGMTLRELL 93
Cdd:TIGR03181 21 LSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKD-DWVFPSYRDHAAMLARGVPLVEIL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 94 LsvflkaedpNSGGRQLPGHFgSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRKEFVSFVTFGDGSSNQGDFHEGCNFAG 173
Cdd:TIGR03181 100 L---------YWRGDERGSWD-PEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGDFYEALNFAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 174 VHKLPVIFMCENNQYAISVPLHKQTAGS-IAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGEGPTLIEAVMYRIS 252
Cdd:TIGR03181 170 VFKAPVVFFVQNNQWAISVPRSKQTAAPtLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGPTLIEAVTYRLG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 253 PHSTSDNDLLYRTREEVETNRERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYAEQAPHPASEDTLLHVYGD 332
Cdd:TIGR03181 250 PHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPVDDIFDHVYAE 329
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
23-323 |
1.19e-105 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 311.18 E-value: 1.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 23 YTYMLKARMFDERCFLLQRSGKIPFHVSGIGQETAQVAAAYALKKGtDYFLPYYRDYGFVLTVGMTLRELLLSVFLKAED 102
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPG-DYIIPGYRDHGNLLARGLSLEEIFAELYGRVAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 103 PNSGGRQlpGHFGSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRKEFVSFVTFGDGSSNQGDFHEGCNFAGVHKLPVIFM 182
Cdd:pfam00676 80 GKGGSMH--GYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 183 CENNQYAISVPLHKQTAG-SIAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGEGPTLIEAVMYRISPHSTSDNDL 261
Cdd:pfam00676 158 CENNQYGISTPAERASAStTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1102105150 262 LYRTREEVETNR-ERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYAEQAPHPASE 323
Cdd:pfam00676 238 TYRTRDEYEEVRkKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
11-332 |
2.88e-52 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 175.82 E-value: 2.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 11 QLGLTDEQVIEMYTYMLKARMFDERCFLLQRSGKIPFHVSGI-GQETAQVAAAYALKKgTDYFLPYYRDYGFVLTVGMTL 89
Cdd:CHL00149 14 ENNINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGVIKLLAE-TDYVCSTYRDHVHALSKGVPP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 90 RELLLSVFLKaEDPNSGGRQLPGHFGSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRKEF-------VSFVTFGDGSSNQ 162
Cdd:CHL00149 93 KNVMAELFGK-ETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSIYRQQVLkevqplrVTACFFGDGTTNN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 163 GDFHEGCNFAGVHKLPVIFMCENNQYAISVPLHKQTA-GSIAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGEGP 241
Cdd:CHL00149 172 GQFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSiPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 242 TLIEAVMYRISPHSTSDNDLLyRTREEVETNRERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYAEQAPHPA 321
Cdd:CHL00149 252 TLIEALTYRFRGHSLADPDEL-RSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPN 330
|
330
....*....|.
gi 1102105150 322 SEDTLLHVYGD 332
Cdd:CHL00149 331 ISDLKKYLFAD 341
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
13-332 |
7.49e-164 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 460.76 E-value: 7.49e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 13 GLTDEQVIEMYTYMLKARMFDERCFLLQRSGKIPFHVSGIGQETAQVAAAYALKKGtDYFLPYYRDYGFVLTVGMTLREL 92
Cdd:COG1071 16 DLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPG-DWIFPTYRDHGHALARGVDPKEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 93 LLSVFLKAEDPnSGGRQLPGHFGSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRKEFVSFVTFGDGSSNQGDFHEGCNFA 172
Cdd:COG1071 95 MAELFGKATGP-SKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 173 GVHKLPVIFMCENNQYAISVPLHKQTAG-SIAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGEGPTLIEAVMYRI 251
Cdd:COG1071 174 AVWKLPVVFVCENNGYAISTPVERQTAVeTIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 252 SPHSTSDNDLLYRTREEVETNRERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYAEQAPHPASEDTLLHVYG 331
Cdd:COG1071 254 GGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYA 333
|
.
gi 1102105150 332 D 332
Cdd:COG1071 334 E 334
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
22-314 |
1.48e-140 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 399.56 E-value: 1.48e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 22 MYTYMLKARMFDERCFLLQRSGKIP-FHVSGIGQETAQVAAAYALKKGtDYFLPYYRDYGFVLTVGMTLRELLLSVFLKA 100
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGgFYHLSIGQEAVAVGVAAALRPG-DWVFPTYRDHGHALARGVDLKEMLAELFGKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 101 EDPnSGGRQLPGHFGSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRKEFVSFVTFGDGSSNQGDFHEGCNFAGVHKLPVI 180
Cdd:cd02000 80 TGP-CKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 181 FMCENNQYAISVPLHKQTAG-SIAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGEGPTLIEAVMYRISPHSTSDN 259
Cdd:cd02000 159 FVCENNGYAISTPTSRQTAGtSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDD 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1102105150 260 DLLYRTREEVETNRERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYA 314
Cdd:cd02000 239 PSRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
14-332 |
6.40e-131 |
|
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 213783 [Multi-domain] Cd Length: 341 Bit Score: 376.87 E-value: 6.40e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 14 LTDEQVIEMYTYMLKARMFDERCFLLQRSGKIPFHVSGIGQETAQVAAAYALKKGtDYFLPYYRDYGFVLTVGMTLRELL 93
Cdd:TIGR03181 21 LSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKD-DWVFPSYRDHAAMLARGVPLVEIL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 94 LsvflkaedpNSGGRQLPGHFgSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRKEFVSFVTFGDGSSNQGDFHEGCNFAG 173
Cdd:TIGR03181 100 L---------YWRGDERGSWD-PEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGDFYEALNFAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 174 VHKLPVIFMCENNQYAISVPLHKQTAGS-IAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGEGPTLIEAVMYRIS 252
Cdd:TIGR03181 170 VFKAPVVFFVQNNQWAISVPRSKQTAAPtLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGPTLIEAVTYRLG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 253 PHSTSDNDLLYRTREEVETNRERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYAEQAPHPASEDTLLHVYGD 332
Cdd:TIGR03181 250 PHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPVDDIFDHVYAE 329
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
23-323 |
1.19e-105 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 311.18 E-value: 1.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 23 YTYMLKARMFDERCFLLQRSGKIPFHVSGIGQETAQVAAAYALKKGtDYFLPYYRDYGFVLTVGMTLRELLLSVFLKAED 102
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPG-DYIIPGYRDHGNLLARGLSLEEIFAELYGRVAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 103 PNSGGRQlpGHFGSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRKEFVSFVTFGDGSSNQGDFHEGCNFAGVHKLPVIFM 182
Cdd:pfam00676 80 GKGGSMH--GYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 183 CENNQYAISVPLHKQTAG-SIAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGEGPTLIEAVMYRISPHSTSDNDL 261
Cdd:pfam00676 158 CENNQYGISTPAERASAStTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1102105150 262 LYRTREEVETNR-ERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYAEQAPHPASE 323
Cdd:pfam00676 238 TYRTRDEYEEVRkKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
11-332 |
2.88e-52 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 175.82 E-value: 2.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 11 QLGLTDEQVIEMYTYMLKARMFDERCFLLQRSGKIPFHVSGI-GQETAQVAAAYALKKgTDYFLPYYRDYGFVLTVGMTL 89
Cdd:CHL00149 14 ENNINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGVIKLLAE-TDYVCSTYRDHVHALSKGVPP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 90 RELLLSVFLKaEDPNSGGRQLPGHFGSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRKEF-------VSFVTFGDGSSNQ 162
Cdd:CHL00149 93 KNVMAELFGK-ETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSIYRQQVLkevqplrVTACFFGDGTTNN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 163 GDFHEGCNFAGVHKLPVIFMCENNQYAISVPLHKQTA-GSIAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGEGP 241
Cdd:CHL00149 172 GQFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSiPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 242 TLIEAVMYRISPHSTSDNDLLyRTREEVETNRERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYAEQAPHPA 321
Cdd:CHL00149 252 TLIEALTYRFRGHSLADPDEL-RSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPN 330
|
330
....*....|.
gi 1102105150 322 SEDTLLHVYGD 332
Cdd:CHL00149 331 ISDLKKYLFAD 341
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
11-335 |
1.77e-51 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 176.29 E-value: 1.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 11 QLGLTDEQVIEMYTYMLKARMFDERCFLLQRSGKIPFHVSGI-GQETAQVAAAYALKKGtDYFLPYYRDYGFVLTVGMTL 89
Cdd:PLN02374 80 DLLVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGFIKLLKKD-DSVVSTYRDHVHALSKGVPA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 90 RELLLSVFLKAED--PNSGGRQlpgHFGSKKLNIVTGSSPVTTQVPHAVGFALGAKLQRK-------EFVSFVTFGDGSS 160
Cdd:PLN02374 159 RAVMSELFGKATGccRGQGGSM---HMFSKEHNLLGGFAFIGEGIPVATGAAFSSKYRREvlkeescDDVTLAFFGDGTC 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 161 NQGDFHEGCNFAGVHKLPVIFMCENNQYAISVPLHKQTAG-SIAERALGYGFPGVKVDGRDALEVYRVVKEARERALRGE 239
Cdd:PLN02374 236 NNGQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDpEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 240 GPTLIEAVMYRISPHSTSDNDLLyRTREEVETNRERDGIPRLRNYMISCGIWSEDREAELAAQIKQELTEATDYAEQAPH 319
Cdd:PLN02374 316 GPTLVECETYRFRGHSLADPDEL-RDPAEKAHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPL 394
|
330
....*....|....*.
gi 1102105150 320 PASEDTLLHVYGDGGG 335
Cdd:PLN02374 395 PPRSQLLENVFADPKG 410
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
53-337 |
3.53e-46 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 160.26 E-value: 3.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 53 GQETAQVAAAYALKKgTDYFLPYYRDYGFVLTVGMTLRELLLSVFLKaEDPNSGGRQLPGHFGSKKLNIVTGSSPVTTQV 132
Cdd:PLN02269 67 GQEAVAVGMEAAITK-EDAIITAYRDHCTHLGRGGTVLEVFAELMGR-KDGCSRGKGGSMHFYKKDANFYGGHGIVGAQV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 133 PHAVGFALGAKLQRKEFVSFVTFGDGSSNQGDFHEGCNFAGVHKLPVIFMCENNQYAISVPLHKqTAGSIAERALGYGFP 212
Cdd:PLN02269 145 PLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWR-AAKSPAYYKRGDYVP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 213 GVKVDGRDALEVYRVVKEARERALRgEGPTLIEAVMYRISPHSTSDNDLLYRTREEVETNR-ERDGIPRLRNYMISCGIW 291
Cdd:PLN02269 224 GLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRqERDPIERVRKLLLAHELA 302
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1102105150 292 SEDREAELAAQIKQELTEATDYAEQAPHPASEDTLLHVYGDGGGLQ 337
Cdd:PLN02269 303 TEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVYVKGLGVE 348
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
134-248 |
6.14e-11 |
|
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: 60.35 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 134 HAVGFALGAKLQRKEFVSFVTFGDGSsnqgdFHEGCN---FAGVHKLPVIFMCENNQYAISVPLHKQTAGSI-------- 202
Cdd:cd00568 50 YGLPAAIGAALAAPDRPVVCIAGDGG-----FMMTGQelaTAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGrvsgtdls 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1102105150 203 ----AERALGYGFPGVKVDGRDALEvyrvvkEARERALRGEGPTLIEAVM 248
Cdd:cd00568 125 npdfAALAEAYGAKGVRVEDPEDLE------AALAEALAAGGPALIEVKT 168
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
77-246 |
1.28e-10 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 60.98 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 77 RDYgFVLTVG---MTLRELL-LSVFLKAEDPNS----GGRqLPGHFGSKKLNIVTgsspVTT----Q-VPHAVGFALGAK 143
Cdd:cd02012 49 RDR-FVLSKGhasPALYAVLaLAGYLPEEDLKTfrqlGSR-LPGHPEYGLTPGVE----VTTgslgQgLSVAVGMALAEK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 144 LQRKEFVSFVTFGDGSSNQGDFHEGCNFAGVHKL-PVIFMCENNQYAISVPLHKQTA-GSIAERALGYGFPGVKVDGRDA 221
Cdd:cd02012 123 LLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNRIQIDGPTDDILFtEDLAKKFEAFGWNVIEVDGHDV 202
|
170 180
....*....|....*....|....*
gi 1102105150 222 LEVYRVVKEARERALRgegPTLIEA 246
Cdd:cd02012 203 EEILAALEEAKKSKGK---PTLIIA 224
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
135-246 |
3.66e-09 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 57.84 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 135 AVGFALGAKLQRKEFVS----------FVTFGDGSSNQGDFHEGCNFAGVHKL-PVIFMCENNQYAISVPLHKQTAGSIA 203
Cdd:PRK05899 127 AVGMALAEKYLAALFNRpgldivdhytYVLCGDGDLMEGISHEACSLAGHLKLgNLIVIYDDNRISIDGPTEGWFTEDVK 206
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1102105150 204 ERALGYGFPGVKVDGRDALEVYRVVKEAREralrGEGPTLIEA 246
Cdd:PRK05899 207 KRFEAYGWHVIEVDGHDVEAIDAAIEEAKA----STKPTLIIA 245
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
130-244 |
4.19e-06 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 46.77 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 130 TQVPHAVGFALGAKLQRKEFVSFVTFGDGSSNQGDFHEGCNFAGVHKLPVIFMCENNQYAISVPLHKQtaGSIAErALGY 209
Cdd:cd02007 79 TSISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVGTP--GNLFE-ELGF 155
|
90 100 110
....*....|....*....|....*....|....*
gi 1102105150 210 GFPGVkVDGRDALEVYRVVKEARERAlrgeGPTLI 244
Cdd:cd02007 156 RYIGP-VDGHNIEALIKVLKEVKDLK----GPVLL 185
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
135-246 |
8.01e-06 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 45.27 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 135 AVGFALGAKLQR--KEFVSFVtfGDGSSnqgdFHEGCNFAGV--HKLPVIFMCENNQY---------------AISVPLH 195
Cdd:pfam02775 33 GLPAAIGAKLARpdRPVVAIA--GDGGF----QMNLQELATAvrYNLPITVVVLNNGGygmtrgqqtpfgggrYSGPSGK 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1102105150 196 KQTAGSIAERALGYGFPGVKVDGRDALEvyrvvkEARERALRGEGPTLIEA 246
Cdd:pfam02775 107 ILPPVDFAKLAEAYGAKGARVESPEELE------EALKEALEHDGPALIDV 151
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
135-248 |
2.54e-04 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 42.84 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 135 AVGFALGAKLQRKEFVSFVTFGDGSsnqgdfhegcnF---------AGVHKLPVIFMCENNQY--AISvplHKQTA---- 199
Cdd:COG0028 417 GLPAAIGAKLARPDRPVVAITGDGG-----------FqmnlqelatAVRYGLPVKVVVLNNGGlgMVR---QWQELfygg 482
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1102105150 200 ---GS---------IAEralGYGFPGVKVDGRDALEvyrvvkEARERALRGEGPTLIEAVM 248
Cdd:COG0028 483 rysGTdlpnpdfakLAE---AFGAKGERVETPEELE------AALEEALASDGPALIDVRV 534
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
77-245 |
8.37e-04 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 40.83 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 77 RDYgFVLTVG---MTLRELL-LSVF-LKAEDPNSGgRQL----PGH---FGSKKLNIVTGssPVTTQVPHAVGFA----- 139
Cdd:pfam00456 55 RDR-FVLSNGhgsMLLYSLLhLTGYdLSMEDLKSF-RQLgsktPGHpefGHTAGVEVTTG--PLGQGIANAVGMAiaern 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 140 LGAKLQRKEF-----VSFVTFGDGSSNQGDFHEGCNFAGVHKL-PVIFMCENNQYAISVPLHKQTAGSIAERALGYGFPG 213
Cdd:pfam00456 131 LAATYNRPGFdivdhYTYVFLGDGCLMEGVSSEASSLAGHLGLgNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHV 210
|
170 180 190
....*....|....*....|....*....|...
gi 1102105150 214 VKV-DGRDALEVYRVVKEARERALRgegPTLIE 245
Cdd:pfam00456 211 IEVeDGHDVEAIAAAIEEAKAEKDK---PTLIK 240
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
60-217 |
2.04e-03 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 40.04 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 60 AAAYALKKgtdYFLPYY--------RDYgFVLTVG---MTLRELL-LSVF-LKAEDPNSGgRQL----PGH---FGSKKL 119
Cdd:PTZ00089 37 PIAHILWS---EVMKYNpkdprwinRDR-FVLSNGhasALLYSMLhLTGYdLSMEDLKNF-RQLgsrtPGHperHITPGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102105150 120 NIVTGssPVTTQVPHAVGFA-----LGAKLQRKEF-----VSFVTFGDGSSNQGDFHEGCNFAG---VHKLPVIFmcENN 186
Cdd:PTZ00089 112 EVTTG--PLGQGIANAVGLAiaekhLAAKFNRPGHpifdnYVYVICGDGCLQEGVSQEALSLAGhlgLEKLIVLY--DDN 187
|
170 180 190
....*....|....*....|....*....|.
gi 1102105150 187 QYAISVPLHKQTAGSIAERALGYGFPGVKVD 217
Cdd:PTZ00089 188 KITIDGNTDLSFTEDVEKKYEAYGWHVIEVD 218
|
|
| |
