|
Name |
Accession |
Description |
Interval |
E-value |
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
58-404 |
0e+00 |
|
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: 520.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 58 ELVQLLTPEGERVedaahaeYASYVADITPDELRGLYRDMVLTRRFDAEATALQRQGELGLWASLLGQEAAQIGSGRATR 137
Cdd:TIGR03181 1 ELVQVLDEDGNVV-------DPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 138 EDDYVFPTYREHGVAWCRGVDPTNLLGMFRGVNNGGWDPNSNNFHLYTIVIGSQALHATGYAMGVAKDGADSGVIAYFGD 217
Cdd:TIGR03181 74 KDDWVFPSYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 218 GASSQGDVSEAFNFAAVYNAPVVFFCQNNQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVTRWALDRAR 296
Cdd:TIGR03181 154 GGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPtLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERAR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 297 RGEGPALIEAYTYRMGAHTTSDDPSRYRHDDERAAWEAKDPILRLRRFLESANHADEGFFAELEAESETLGKRVREVVRA 376
Cdd:TIGR03181 234 SGGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALA 313
|
330 340
....*....|....*....|....*...
gi 490072943 377 MPDPDRFAIFENVYADGHALVDEERAQF 404
Cdd:TIGR03181 314 LPPPPVDDIFDHVYAELPPELEEQRAEL 341
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
59-406 |
6.32e-162 |
|
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: 459.22 E-value: 6.32e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 59 LVQLLTPEGERvedaahaeyaSYVADITPDELRGLYRDMVLTRRFDAEATALQRQGELGLWASLLGQEAAQIGSGRATRE 138
Cdd:COG1071 1 LVQVLDPDGTE----------AALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 139 DDYVFPTYREHGVAWCRGVDPTNLLGMFRG----VNNGGWDPN-----SNNFHLYTIVIGSQALHATGYAMGVAKDGADS 209
Cdd:COG1071 71 GDWIFPTYRDHGHALARGVDPKELMAELFGkatgPSKGRGGSMhffdkELNFLGGSGIVGGQLPHAVGAALAAKLRGEDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 210 GVIAYFGDGASSQGDVSEAFNFAAVYNAPVVFFCQNNQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVT 288
Cdd:COG1071 151 VAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVEtIADRAAGYGIPGVRVDGNDVLAVYAAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 289 RWALDRARRGEGPALIEAYTYRMGAHTTSDDPSRYRHDDERAAWEAKDPILRLRRFLESANHADEGFFAELEAESETLGK 368
Cdd:COG1071 231 KEAVERARAGEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVE 310
|
330 340 350
....*....|....*....|....*....|....*...
gi 490072943 369 RVREVVRAMPDPDRFAIFENVYADGHALVDEERAQFAA 406
Cdd:COG1071 311 EAVEFAEASPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
93-376 |
2.10e-120 |
|
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: 351.41 E-value: 2.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 93 LYRDMVLTRRFDAEATALQRQGEL-GLWASLLGQEAAQIGSGRATREDDYVFPTYREHGVAWCRGVDPTNLLGMF----R 167
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIgGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELfgkeT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 168 GVNNGG-----WDPNSNNFHLYTIVIGSQALHATGYAMGVAKDGADSGVIAYFGDGASSQGDVSEAFNFAAVYNAPVVFF 242
Cdd:cd02000 81 GPCKGRggsmhIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 243 CQNNQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVTRWALDRARRGEGPALIEAYTYRMGAHTTSDDPS 321
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTsIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490072943 322 RYRHDDERAAWEAKDPILRLRRFLESANHADEGFFAELEAESEtlgKRVREVVRA 376
Cdd:cd02000 241 RYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVK---AEVEEAVEF 292
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
94-379 |
4.89e-88 |
|
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: 269.19 E-value: 4.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 94 YRDMVLTRRFDAEATALQRQGELGLWASLLGQEAAQIGSGRATREDDYVFPTYREHGVAWCRGVDPTNLLGMFRG----- 168
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGrvakg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 169 ---VNNGGWDPNSNNFHLYTIVIGSQALHATGYAMGVAKDGADSGVIAYFGDGASSQGDVSEAFNFAAVYNAPVVFFCQN 245
Cdd:pfam00676 81 kggSMHGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 246 NQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVTRWALDRARRGEGPALIEAYTYRMGAHTTSDDPSRYR 324
Cdd:pfam00676 161 NQYGISTPAERASASTtYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSTYR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490072943 325 HDDE-RAAWEAKDPILRLRRFLESANHADEgffAELEAESETLGKRVREVVRAMPD 379
Cdd:pfam00676 241 TRDEyEEVRKKKDPIQRFKEHLVSKGVWSE---EELKAIEKEVRKEVEEAFKKAES 293
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
85-392 |
4.49e-55 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 188.23 E-value: 4.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 85 ITPDELRGLYRDMVLTRRFDAEATALQRQGELGLWASLL-GQEAAQIGSGRATREDDYVFPTYREHGVAWCRGVDPTNLL 163
Cdd:PLN02374 83 VTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVM 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 164 GMFRGVNNGGWDPNSNNFHLYT---------------IVIGSQALHATGYAMGVAKD-GADSGVIAYFGDGASSQGDVSE 227
Cdd:PLN02374 163 SELFGKATGCCRGQGGSMHMFSkehnllggfafigegIPVATGAAFSSKYRREVLKEeSCDDVTLAFFGDGTCNNGQFFE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 228 AFNFAAVYNAPVVFFCQNNQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVTRWALDRARRGEGPALIEA 306
Cdd:PLN02374 243 CLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPeIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVEC 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 307 YTYRMGAHTTSdDPSRYRHDDERAAWEAKDPILRLRRFLESANHADEgffAELEAESETLGKRVREVVR---AMPDPDRF 383
Cdd:PLN02374 323 ETYRFRGHSLA-DPDELRDPAEKAHYAARDPIAALKKYLIENGLATE---AELKAIEKKIDEVVEDAVEfadASPLPPRS 398
|
....*....
gi 490072943 384 AIFENVYAD 392
Cdd:PLN02374 399 QLLENVFAD 407
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
58-404 |
0e+00 |
|
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: 520.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 58 ELVQLLTPEGERVedaahaeYASYVADITPDELRGLYRDMVLTRRFDAEATALQRQGELGLWASLLGQEAAQIGSGRATR 137
Cdd:TIGR03181 1 ELVQVLDEDGNVV-------DPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 138 EDDYVFPTYREHGVAWCRGVDPTNLLGMFRGVNNGGWDPNSNNFHLYTIVIGSQALHATGYAMGVAKDGADSGVIAYFGD 217
Cdd:TIGR03181 74 KDDWVFPSYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 218 GASSQGDVSEAFNFAAVYNAPVVFFCQNNQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVTRWALDRAR 296
Cdd:TIGR03181 154 GGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPtLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERAR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 297 RGEGPALIEAYTYRMGAHTTSDDPSRYRHDDERAAWEAKDPILRLRRFLESANHADEGFFAELEAESETLGKRVREVVRA 376
Cdd:TIGR03181 234 SGGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALA 313
|
330 340
....*....|....*....|....*...
gi 490072943 377 MPDPDRFAIFENVYADGHALVDEERAQF 404
Cdd:TIGR03181 314 LPPPPVDDIFDHVYAELPPELEEQRAEL 341
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
59-406 |
6.32e-162 |
|
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: 459.22 E-value: 6.32e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 59 LVQLLTPEGERvedaahaeyaSYVADITPDELRGLYRDMVLTRRFDAEATALQRQGELGLWASLLGQEAAQIGSGRATRE 138
Cdd:COG1071 1 LVQVLDPDGTE----------AALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 139 DDYVFPTYREHGVAWCRGVDPTNLLGMFRG----VNNGGWDPN-----SNNFHLYTIVIGSQALHATGYAMGVAKDGADS 209
Cdd:COG1071 71 GDWIFPTYRDHGHALARGVDPKELMAELFGkatgPSKGRGGSMhffdkELNFLGGSGIVGGQLPHAVGAALAAKLRGEDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 210 GVIAYFGDGASSQGDVSEAFNFAAVYNAPVVFFCQNNQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVT 288
Cdd:COG1071 151 VAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVEtIADRAAGYGIPGVRVDGNDVLAVYAAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 289 RWALDRARRGEGPALIEAYTYRMGAHTTSDDPSRYRHDDERAAWEAKDPILRLRRFLESANHADEGFFAELEAESETLGK 368
Cdd:COG1071 231 KEAVERARAGEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVE 310
|
330 340 350
....*....|....*....|....*....|....*...
gi 490072943 369 RVREVVRAMPDPDRFAIFENVYADGHALVDEERAQFAA 406
Cdd:COG1071 311 EAVEFAEASPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
93-376 |
2.10e-120 |
|
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: 351.41 E-value: 2.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 93 LYRDMVLTRRFDAEATALQRQGEL-GLWASLLGQEAAQIGSGRATREDDYVFPTYREHGVAWCRGVDPTNLLGMF----R 167
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIgGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELfgkeT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 168 GVNNGG-----WDPNSNNFHLYTIVIGSQALHATGYAMGVAKDGADSGVIAYFGDGASSQGDVSEAFNFAAVYNAPVVFF 242
Cdd:cd02000 81 GPCKGRggsmhIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 243 CQNNQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVTRWALDRARRGEGPALIEAYTYRMGAHTTSDDPS 321
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTsIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490072943 322 RYRHDDERAAWEAKDPILRLRRFLESANHADEGFFAELEAESEtlgKRVREVVRA 376
Cdd:cd02000 241 RYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVK---AEVEEAVEF 292
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
94-379 |
4.89e-88 |
|
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: 269.19 E-value: 4.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 94 YRDMVLTRRFDAEATALQRQGELGLWASLLGQEAAQIGSGRATREDDYVFPTYREHGVAWCRGVDPTNLLGMFRG----- 168
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGrvakg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 169 ---VNNGGWDPNSNNFHLYTIVIGSQALHATGYAMGVAKDGADSGVIAYFGDGASSQGDVSEAFNFAAVYNAPVVFFCQN 245
Cdd:pfam00676 81 kggSMHGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 246 NQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVTRWALDRARRGEGPALIEAYTYRMGAHTTSDDPSRYR 324
Cdd:pfam00676 161 NQYGISTPAERASASTtYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSTYR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490072943 325 HDDE-RAAWEAKDPILRLRRFLESANHADEgffAELEAESETLGKRVREVVRAMPD 379
Cdd:pfam00676 241 TRDEyEEVRKKKDPIQRFKEHLVSKGVWSE---EELKAIEKEVRKEVEEAFKKAES 293
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
85-392 |
4.49e-55 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 188.23 E-value: 4.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 85 ITPDELRGLYRDMVLTRRFDAEATALQRQGELGLWASLL-GQEAAQIGSGRATREDDYVFPTYREHGVAWCRGVDPTNLL 163
Cdd:PLN02374 83 VTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVM 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 164 GMFRGVNNGGWDPNSNNFHLYT---------------IVIGSQALHATGYAMGVAKD-GADSGVIAYFGDGASSQGDVSE 227
Cdd:PLN02374 163 SELFGKATGCCRGQGGSMHMFSkehnllggfafigegIPVATGAAFSSKYRREVLKEeSCDDVTLAFFGDGTCNNGQFFE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 228 AFNFAAVYNAPVVFFCQNNQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVTRWALDRARRGEGPALIEA 306
Cdd:PLN02374 243 CLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPeIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVEC 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 307 YTYRMGAHTTSdDPSRYRHDDERAAWEAKDPILRLRRFLESANHADEgffAELEAESETLGKRVREVVR---AMPDPDRF 383
Cdd:PLN02374 323 ETYRFRGHSLA-DPDELRDPAEKAHYAARDPIAALKKYLIENGLATE---AELKAIEKKIDEVVEDAVEfadASPLPPRS 398
|
....*....
gi 490072943 384 AIFENVYAD 392
Cdd:PLN02374 399 QLLENVFAD 407
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
93-392 |
2.30e-51 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 175.82 E-value: 2.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 93 LYRDMVLTRRFDAEATALQRQGELGLWASLL-GQEAAQIGSGRATREDDYVFPTYREHGVAWCRGVDPTNLLGMFRGVNN 171
Cdd:CHL00149 25 LYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVMAELFGKET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 172 GGWDPNSNNFHLYT---------------IVIGSQALHATGYAMGVAKDGADSGVIA-YFGDGASSQGDVSEAFNFAAVY 235
Cdd:CHL00149 105 GCSRGRGGSMHIFSaphnflggfafigegIPIALGAAFQSIYRQQVLKEVQPLRVTAcFFGDGTTNNGQFFECLNMAVLW 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 236 NAPVVFFCQNNQWAISESNEKQTRVP-LYQRAQGFGFPGVRVDGNDVLASLAVTRWALDRARRGEGPALIEAYTYRMGAH 314
Cdd:CHL00149 185 KLPIIFVVENNQWAIGMAHHRSTSIPeIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEALTYRFRGH 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490072943 315 TTSdDPSRYRHDDERAAWEAKDPILRLRRFLESANHADEGFFAELEAESETLGKRVREVVRAMPDPDRFAIFENVYAD 392
Cdd:CHL00149 265 SLA-DPDELRSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDLKKYLFAD 341
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
86-393 |
1.49e-38 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 142.16 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 86 TPDELRGLYRDMVLTRRFDAEATALQR----QGELGLWAsllGQEAAQIGSGRATREDDYVFPTYREHGVAWCRGVDPTN 161
Cdd:PLN02269 28 SKQELVDFFRDMYLMRRMEIAADSLYKakliRGFCHLYD---GQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 162 LLGMFRGVNNGGWDPNSNNFHLYT----------IViGSQALHATGYAMGVAKDGADSGVIAYFGDGASSQGDVSEAFNF 231
Cdd:PLN02269 105 VFAELMGRKDGCSRGKGGSMHFYKkdanfygghgIV-GAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 232 AAVYNAPVVFFCQNNQWAISESNEKQTRVPLYQRaQGFGFPGVRVDGNDVLASLAVTRWALDRARRgEGPALIEAYTYRM 311
Cdd:PLN02269 184 AALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYK-RGDYVPGLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMDTYRY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 312 GAHTTSDDPSRYRHDDERAAW-EAKDPILRLRRFLESANHADEgffAELEAESETLGKRVREVV---RAMPDPDRFAIFE 387
Cdd:PLN02269 262 HGHSMSDPGSTYRTRDEISGVrQERDPIERVRKLLLAHELATE---AELKDIEKEIRKEVDDAVakaKESPMPDPSELFT 338
|
....*.
gi 490072943 388 NVYADG 393
Cdd:PLN02269 339 NVYVKG 344
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
195-308 |
5.65e-09 |
|
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: 56.36 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 195 ATGYAMGVAKDGADSGVIAYFGDGASSQGDVSEAFNFAAVYN-APVVFFCQNNQWAISESNEKQTRV-PLYQRAQGFGFP 272
Cdd:cd02012 114 AVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKlDNLIAIVDSNRIQIDGPTDDILFTeDLAKKFEAFGWN 193
|
90 100 110
....*....|....*....|....*....|....*..
gi 490072943 273 GVRVDGNDVLASLAvtrwALDRARRGEG-PALIEAYT 308
Cdd:cd02012 194 VIEVDGHDVEEILA----ALEEAKKSKGkPTLIIAKT 226
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
189-308 |
8.53e-09 |
|
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: 54.57 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 189 GSQAL-HATGYAMGVAKDGADSGVIAYFGDGasSQGDVSEAFNFAAVYNAPVVFFCQNNQ-----WAISESNEKQTRVPL 262
Cdd:cd00568 44 GFGAMgYGLPAAIGAALAAPDRPVVCIAGDG--GFMMTGQELATAVRYGLPVIVVVFNNGgygtiRMHQEAFYGGRVSGT 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 490072943 263 YQR-------AQGFGFPGVRVDGNDVLASlavtrwALDRARRGEGPALIEAYT 308
Cdd:cd00568 122 DLSnpdfaalAEAYGAKGVRVEDPEDLEA------ALAEALAAGGPALIEVKT 168
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
195-308 |
7.98e-08 |
|
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: 52.16 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 195 ATGYAMGVAKDGADSGVIAYFGDGASSQGDVSEAFNFAAVYNAPVVFFCQNNQWAISESNEKQTrvPLYQrAQGFGFPGV 274
Cdd:cd02007 84 ALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVGTPG--NLFE-ELGFRYIGP 160
|
90 100 110
....*....|....*....|....*....|....
gi 490072943 275 rVDGNDVLASLAVtrwaLDRARRGEGPALIEAYT 308
Cdd:cd02007 161 -VDGHNIEALIKV----LKEVKDLKGPVLLHVVT 189
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
197-308 |
1.78e-06 |
|
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: 47.98 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 197 GYAM----GVAKDGADSGVIAYFGDGassqgdvseAFNF-------AAVYNAPVVFFCQNNQ-WAISESNEKQ------- 257
Cdd:cd02002 52 GWGLpaavGAALANPDRKVVAIIGDG---------SFMYtiqalwtAARYGLPVTVVILNNRgYGALRSFLKRvgpegpg 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490072943 258 TRVPLYQR-----------AQGFGFPGVRVDGNDVLASlavtrwALDRARRGEGPALIEAYT 308
Cdd:cd02002 123 ENAPDGLDlldpgidfaaiAKAFGVEAERVETPEELDE------ALREALAEGGPALIEVVV 178
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
197-306 |
2.24e-05 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 44.11 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 197 GYAMGVAKDGADSGVIAYFGDGASsqGDVSEAFNFAAVYNAPVVFFCQNNQ-WAisesNEKQTRVPLYQR---------- 265
Cdd:pfam02775 35 PAAIGAKLARPDRPVVAIAGDGGF--QMNLQELATAVRYNLPITVVVLNNGgYG----MTRGQQTPFGGGrysgpsgkil 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 490072943 266 --------AQGFGFPGVRVDGNDVLASlavtrwALDRARRGEGPALIEA 306
Cdd:pfam02775 109 ppvdfaklAEAYGAKGARVESPEELEE------ALKEALEHDGPALIDV 151
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
199-306 |
2.90e-04 |
|
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: 41.33 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 199 AMGVAKDGADSGVIAYFGDGaSSQGDVSEaFNFAAVYNAPVVFFCQNN-------QWA-------ISESNEKqtRVPLYQ 264
Cdd:cd02015 59 AIGAKVARPDKTVICIDGDG-SFQMNIQE-LATAAQYNLPVKIVILNNgslgmvrQWQelfyegrYSHTTLD--SNPDFV 134
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490072943 265 R-AQGFGFPGVRVDGNDVLASlavtrwALDRARRGEGPALIEA 306
Cdd:cd02015 135 KlAEAYGIKGLRVEKPEELEA------ALKEALASDGPVLLDV 171
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
195-308 |
6.25e-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: 42.07 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 195 ATGYAMGVAKDGADSGVIAYFGDGAssqgdvseaFNF-------AAVYNAPVVFFCQNN-------QWAISESNEKQTRV 260
Cdd:COG0028 417 GLPAAIGAKLARPDRPVVAITGDGG---------FQMnlqelatAVRYGLPVKVVVLNNgglgmvrQWQELFYGGRYSGT 487
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 490072943 261 PLYQR-----AQGFGFPGVRVDGNDVLASlavtrwALDRARRGEGPALIEAYT 308
Cdd:COG0028 488 DLPNPdfaklAEAFGAKGERVETPEELEA------ALEEALASDGPALIDVRV 534
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
188-308 |
2.38e-03 |
|
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: 38.67 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490072943 188 IGSqALHATgyaMGVAKDGA--------DSGVIAYFGDGASSQgdVSEAFNFAAVYNAPVVFFCQNNQ------------ 247
Cdd:cd02014 45 ILS-GLLAT---MGNGLPGAiaaklaypDRQVIALSGDGGFAM--LMGDLITAVKYNLPVIVVVFNNSdlgfikweqevm 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490072943 248 ----WAISESNekqtrvPLYQR-AQGFGFPGVRVDGNDVLASlavtrwALDRARRGEGPALIEAYT 308
Cdd:cd02014 119 gqpeFGVDLPN------PDFAKiAEAMGIKGIRVEDPDELEA------ALDEALAADGPVVIDVVT 172
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
195-254 |
2.69e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 39.99 E-value: 2.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490072943 195 ATGYAmgVAKD--GADSGVIAYFGDGASSQGDVSEAFNFAAVYNAPVVFFCQNNQWAISESN 254
Cdd:PRK12315 122 ATGLA--KARDlkGEKGNIIAVIGDGSLSGGLALEGLNNAAELKSNLIIIVNDNQMSIAENH 181
|
|
| |
