|
Name |
Accession |
Description |
Interval |
E-value |
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
75-413 |
1.29e-150 |
|
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: 431.10 E-value: 1.29e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 75 KSQDPNFDEQTSLKMYKTMTQLNIMDRILYDSQRQGRISFYMTSFGEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYT 154
Cdd:COG1071 11 EAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 155 MENFMNQCYGNADDLGKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYAFKQQKDnNRIAVVYFGDGAASEGDAHAA 234
Cdd:COG1071 91 PKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGE-DEVAVAFFGDGATSEGDFHEA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 235 FNFAATLKCPIIFFCRNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARRVALT-NRPVLIEAM 313
Cdd:COG1071 170 LNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAgEGPTLIEAK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 314 TYRLGHHSTSDDSTAYRSSDEVQTWGDKDhPITRFKKYITERGWWNEEKEMEWQKEVKKRVLTEFAAAEKRKKAHYHDLF 393
Cdd:COG1071 250 TYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELF 328
|
330 340
....*....|....*....|
gi 86563357 394 EDVYDELPLRLRRQRDELDA 413
Cdd:COG1071 329 DDVYAEPPPHLAEQRAELAA 348
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
89-381 |
3.78e-150 |
|
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: 427.68 E-value: 3.78e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 89 MYKTMTQLNIMDRILYDSQRQGRIS-FYMTSFGEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYTMENFMNQCYGNAD 167
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGgFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 168 DLGKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYAFKQQKDNnRIAVVYFGDGAASEGDAHAAFNFAATLKCPIIF 247
Cdd:cd02000 81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGED-RVAVCFFGDGATNEGDFHEALNFAALWKLPVIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 248 FCRNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARRVAL-TNRPVLIEAMTYRLGHHSTSDDS 326
Cdd:cd02000 160 VCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARaGGGPTLIEAVTYRLGGHSTSDDP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 86563357 327 TAYRSSDEVQTWGDKDhPITRFKKYITERGWWNEEKEMEWQKEVKKRVLTEFAAA 381
Cdd:cd02000 240 SRYRTKEEVEEWKKRD-PILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
61-411 |
3.20e-120 |
|
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: 353.37 E-value: 3.20e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 61 PIYRVTNAVGDVIDKSQDPNFDEQTSLKMYKTMTQLNIMDRILYDSQRQGRISFYMTSFGEEGNHVGSAAALEPQDLIYG 140
Cdd:TIGR03181 1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 141 QYREAGVLLWRGYTMENFMNQCYGNAddlgKGRQMPmhfgtKERNFVTISSPLTTQLPQAVGSAYAFKQQKDNNrIAVVY 220
Cdd:TIGR03181 81 SYRDHAAMLARGVPLVEILLYWRGDE----RGSWDP-----EGVNILPPNIPIGTQYLHAAGVAYALKLRGEDN-VAVTY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 221 FGDGAASEGDAHAAFNFAATLKCPIIFFCRNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARR 300
Cdd:TIGR03181 151 FGDGGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 301 VALT-NRPVLIEAMTYRLGHHSTSDDSTAYRSSDEVQTWGDKDhPITRFKKYITERGWWNEEKEMEWQKEVKKRVLTEFA 379
Cdd:TIGR03181 231 RARSgGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKD-PILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVA 309
|
330 340 350
....*....|....*....|....*....|..
gi 86563357 380 AAEKRKKAHYHDLFEDVYDELPLRLRRQRDEL 411
Cdd:TIGR03181 310 EALALPPPPVDDIFDHVYAELPPELEEQRAEL 341
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
90-388 |
8.60e-119 |
|
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: 348.16 E-value: 8.60e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 90 YKTMTQLNIMDRILYDSQRQGRISFYMTSFGEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYTMENFMNQCYGNADDl 169
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 170 GKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYAFKQQKDNnRIAVVYFGDGAASEGDAHAAFNFAATLKCPIIFFC 249
Cdd:pfam00676 80 GKGGSMHGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKK-EVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 250 RNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARRVALT-NRPVLIEAMTYRLGHHSTSDDSTA 328
Cdd:pfam00676 159 ENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTgKGPFLIELVTYRYGGHSMSDDPST 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 329 YRSSDEVQTWGDKDHPITRFKKYITERGWWNEEKEMEWQKEVKKRVLTEFAAAEKRKKAH 388
Cdd:pfam00676 239 YRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPH 298
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
87-397 |
9.94e-48 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 167.20 E-value: 9.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 87 LKMYKTMTQLNIMDrILYDSQRQGRI--SFYMTSFGEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYTMENFMNQCYG 164
Cdd:PLN02269 33 VDFFRDMYLMRRME-IAADSLYKAKLirGFCHLYDGQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLEVFAELMG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 165 NADDLGKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYAFKQQKDNNrIAVVYFGDGAASEGDAHAAFNFAATLKCP 244
Cdd:PLN02269 112 RKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEEN-VAFALYGDGAANQGQLFEALNIAALWDLP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 245 IIFFCRNNGYAISTPTSEqyggdgiAGKGPAY---GLHT--IRVDGNDLLAVYNATKEARRVALTNRPVLIEAMTYRLGH 319
Cdd:PLN02269 191 VIFVCENNHYGMGTAEWR-------AAKSPAYykrGDYVpgLKVDGMDVLAVKQACKFAKEHALSNGPIVLEMDTYRYHG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 320 HSTSDDSTAYRSSDEVQTWGDKDHPITRFKKYITERGWWNEE--KEMEwqKEVKKRVLTEFAAAEKRKKAHYHDLFEDVY 397
Cdd:PLN02269 264 HSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAelKDIE--KEIRKEVDDAVAKAKESPMPDPSELFTNVY 341
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
75-413 |
1.29e-150 |
|
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: 431.10 E-value: 1.29e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 75 KSQDPNFDEQTSLKMYKTMTQLNIMDRILYDSQRQGRISFYMTSFGEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYT 154
Cdd:COG1071 11 EAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 155 MENFMNQCYGNADDLGKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYAFKQQKDnNRIAVVYFGDGAASEGDAHAA 234
Cdd:COG1071 91 PKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGE-DEVAVAFFGDGATSEGDFHEA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 235 FNFAATLKCPIIFFCRNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARRVALT-NRPVLIEAM 313
Cdd:COG1071 170 LNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAgEGPTLIEAK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 314 TYRLGHHSTSDDSTAYRSSDEVQTWGDKDhPITRFKKYITERGWWNEEKEMEWQKEVKKRVLTEFAAAEKRKKAHYHDLF 393
Cdd:COG1071 250 TYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELF 328
|
330 340
....*....|....*....|
gi 86563357 394 EDVYDELPLRLRRQRDELDA 413
Cdd:COG1071 329 DDVYAEPPPHLAEQRAELAA 348
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
89-381 |
3.78e-150 |
|
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: 427.68 E-value: 3.78e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 89 MYKTMTQLNIMDRILYDSQRQGRIS-FYMTSFGEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYTMENFMNQCYGNAD 167
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGgFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 168 DLGKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYAFKQQKDNnRIAVVYFGDGAASEGDAHAAFNFAATLKCPIIF 247
Cdd:cd02000 81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGED-RVAVCFFGDGATNEGDFHEALNFAALWKLPVIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 248 FCRNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARRVAL-TNRPVLIEAMTYRLGHHSTSDDS 326
Cdd:cd02000 160 VCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARaGGGPTLIEAVTYRLGGHSTSDDP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 86563357 327 TAYRSSDEVQTWGDKDhPITRFKKYITERGWWNEEKEMEWQKEVKKRVLTEFAAA 381
Cdd:cd02000 240 SRYRTKEEVEEWKKRD-PILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
61-411 |
3.20e-120 |
|
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: 353.37 E-value: 3.20e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 61 PIYRVTNAVGDVIDKSQDPNFDEQTSLKMYKTMTQLNIMDRILYDSQRQGRISFYMTSFGEEGNHVGSAAALEPQDLIYG 140
Cdd:TIGR03181 1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 141 QYREAGVLLWRGYTMENFMNQCYGNAddlgKGRQMPmhfgtKERNFVTISSPLTTQLPQAVGSAYAFKQQKDNNrIAVVY 220
Cdd:TIGR03181 81 SYRDHAAMLARGVPLVEILLYWRGDE----RGSWDP-----EGVNILPPNIPIGTQYLHAAGVAYALKLRGEDN-VAVTY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 221 FGDGAASEGDAHAAFNFAATLKCPIIFFCRNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARR 300
Cdd:TIGR03181 151 FGDGGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 301 VALT-NRPVLIEAMTYRLGHHSTSDDSTAYRSSDEVQTWGDKDhPITRFKKYITERGWWNEEKEMEWQKEVKKRVLTEFA 379
Cdd:TIGR03181 231 RARSgGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKD-PILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVA 309
|
330 340 350
....*....|....*....|....*....|..
gi 86563357 380 AAEKRKKAHYHDLFEDVYDELPLRLRRQRDEL 411
Cdd:TIGR03181 310 EALALPPPPVDDIFDHVYAELPPELEEQRAEL 341
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
90-388 |
8.60e-119 |
|
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: 348.16 E-value: 8.60e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 90 YKTMTQLNIMDRILYDSQRQGRISFYMTSFGEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYTMENFMNQCYGNADDl 169
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 170 GKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYAFKQQKDNnRIAVVYFGDGAASEGDAHAAFNFAATLKCPIIFFC 249
Cdd:pfam00676 80 GKGGSMHGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKK-EVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 250 RNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARRVALT-NRPVLIEAMTYRLGHHSTSDDSTA 328
Cdd:pfam00676 159 ENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTgKGPFLIELVTYRYGGHSMSDDPST 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 329 YRSSDEVQTWGDKDHPITRFKKYITERGWWNEEKEMEWQKEVKKRVLTEFAAAEKRKKAH 388
Cdd:pfam00676 239 YRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPH 298
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
87-397 |
9.94e-48 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 167.20 E-value: 9.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 87 LKMYKTMTQLNIMDrILYDSQRQGRI--SFYMTSFGEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYTMENFMNQCYG 164
Cdd:PLN02269 33 VDFFRDMYLMRRME-IAADSLYKAKLirGFCHLYDGQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLEVFAELMG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 165 NADDLGKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYAFKQQKDNNrIAVVYFGDGAASEGDAHAAFNFAATLKCP 244
Cdd:PLN02269 112 RKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEEN-VAFALYGDGAANQGQLFEALNIAALWDLP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 245 IIFFCRNNGYAISTPTSEqyggdgiAGKGPAY---GLHT--IRVDGNDLLAVYNATKEARRVALTNRPVLIEAMTYRLGH 319
Cdd:PLN02269 191 VIFVCENNHYGMGTAEWR-------AAKSPAYykrGDYVpgLKVDGMDVLAVKQACKFAKEHALSNGPIVLEMDTYRYHG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 320 HSTSDDSTAYRSSDEVQTWGDKDHPITRFKKYITERGWWNEE--KEMEwqKEVKKRVLTEFAAAEKRKKAHYHDLFEDVY 397
Cdd:PLN02269 264 HSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAelKDIE--KEIRKEVDDAVAKAKESPMPDPSELFTNVY 341
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
80-371 |
5.35e-32 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 124.21 E-value: 5.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 80 NFDEQTSLKMYKTMtqlnIMDRILYDSQRQGRISFYMTSF-----GEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYT 154
Cdd:CHL00149 16 NINSMWLLVLYEDM----LLGRNFEDMCAQMYYRGKMFGFvhlynGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 155 MENFMNQCYGNADDLGKGRQMPMHFGTKERNFVTISSPLTTQLPQAVGSAYA--FKQQKDNN----RIAVVYFGDGAASE 228
Cdd:CHL00149 92 PKNVMAELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQsiYRQQVLKEvqplRVTACFFGDGTTNN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 229 GDAHAAFNFAATLKCPIIFFCRNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEA-RRVALTNRP 307
Cdd:CHL00149 172 GQFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAvERARQGDGP 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86563357 308 VLIEAMTYRLGHHSTSDDStAYRSSDEVQTWGDKDhPITRFKKYITERGWWNEEKEMEWQKEVK 371
Cdd:CHL00149 252 TLIEALTYRFRGHSLADPD-ELRSKQEKEAWVARD-PIKKLKSYIIDNELASQKELNKIQREVK 313
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
120-381 |
3.69e-29 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 118.12 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 120 GEEGNHVGSAAALEPQDLIYGQYREAGVLLWRGYTMENFMNQCYGNADDLGKGRQMPMHFGTKERNFVTISSPLTTQLPQ 199
Cdd:PLN02374 123 GQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVMSELFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 200 AVGSAYAFK------QQKDNNRIAVVYFGDGAASEGDAHAAFNFAATLKCPIIFFCRNNGYAISTPTSEQYGGDGIAGKG 273
Cdd:PLN02374 203 ATGAAFSSKyrrevlKEESCDDVTLAFFGDGTCNNGQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 274 PAYGLHTIRVDGNDLLAVYNATKEA-RRVALTNRPVLIEAMTYRLGHHSTSDDStAYRSSDEVQTWGDKDhPITRFKKYI 352
Cdd:PLN02374 283 PAFGMPGVHVDGMDVLKVREVAKEAiERARRGEGPTLVECETYRFRGHSLADPD-ELRDPAEKAHYAARD-PIAALKKYL 360
|
250 260 270
....*....|....*....|....*....|.
gi 86563357 353 TERGWWNEEKEMEWQKEVKKRV--LTEFAAA 381
Cdd:PLN02374 361 IENGLATEAELKAIEKKIDEVVedAVEFADA 391
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
163-314 |
2.64e-17 |
|
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: 81.01 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 163 YGNADDLGKGRQ----MPMHFGTKERNFVTISS-PLTTQLPQAVGSAYAFKQQKDNNRIaVVYFGDGAASEGDAHAAFNF 237
Cdd:cd02012 72 YLPEEDLKTFRQlgsrLPGHPEYGLTPGVEVTTgSLGQGLSVAVGMALAEKLLGFDYRV-YVLLGDGELQEGSVWEAASF 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86563357 238 AATLKC-PIIFFCRNNGYAISTPTSEQYGGDGIAGKGPAYGLHTIRVDGNDLLAVYNATKEARRValTNRPVLIEAMT 314
Cdd:cd02012 151 AGHYKLdNLIAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKS--KGKPTLIIAKT 226
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
176-314 |
4.95e-13 |
|
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: 66.90 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 176 PMHFGTkernfVTISSPLTTQLPQAVGSAYAFKqqkdnNRIAVVYFGDGAASEGdaHAAFNFAATLKCPIIFFCRNNGYA 255
Cdd:cd00568 36 GRRFLT-----STGFGAMGYGLPAAIGAALAAP-----DRPVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNNGGY 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 256 ISTPTSE--QYGGDGIAGK---------GPAYGLHTIRVDgnDLLAVYNATKEARRvalTNRPVLIEAMT 314
Cdd:cd00568 104 GTIRMHQeaFYGGRVSGTDlsnpdfaalAEAYGAKGVRVE--DPEDLEAALAEALA---AGGPALIEVKT 168
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
197-314 |
7.41e-12 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 67.08 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 197 LPQAVGSAYAFK-QQKDNNRIAVVYF--------GDGAASEGDAHAAFNFAATLKC-PIIFFCRNNGYAISTPTSEQYGG 266
Cdd:PRK05899 124 LANAVGMALAEKyLAALFNRPGLDIVdhytyvlcGDGDLMEGISHEACSLAGHLKLgNLIVIYDDNRISIDGPTEGWFTE 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 86563357 267 DgIAGKGPAYGLHTIRVDGNDLLAVYNATKEARRValtNRPVLIEAMT 314
Cdd:PRK05899 204 D-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAS---TKPTLIIAKT 247
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
195-314 |
9.75e-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: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 195 TQLPQAVGSAYAFKQQKDNNR-IAVVyfGDGAASEGDAHAAFNFAATLKCPIIFFCRNNGYAISTPTseqyggdgiaGKG 273
Cdd:cd02007 79 TSISAALGMAVARDLKGKKRKvIAVI--GDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNV----------GTP 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 86563357 274 PAY----GLHTIR-VDGNDLLAVYNATKEARRvalTNRPVLIEAMT 314
Cdd:cd02007 147 GNLfeelGFRYIGpVDGHNIEALIKVLKEVKD---LKGPVLLHVVT 189
|
|
| PLN02790 |
PLN02790 |
transketolase |
185-401 |
2.26e-07 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 53.10 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 185 NFVT-----ISSPLTTQLPQAVGSAYAFKQ-----QKDNNRI----AVVYFGDGAASEGDAHAAFNFAATLKC-PIIFFC 249
Cdd:PLN02790 94 NFETpgievTTGPLGQGIANAVGLALAEKHlaarfNKPDHKIvdhyTYCILGDGCQMEGISNEAASLAGHWGLgKLIVLY 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 250 RNNGYAISTPTSEQYGGDgIAGKGPAYGLHTIRVDG--NDLLAVYNATKEARrvALTNRPVLIEAMT---YRLGHHSTSD 324
Cdd:PLN02790 174 DDNHISIDGDTEIAFTED-VDKRYEALGWHTIWVKNgnTDYDEIRAAIKEAK--AVTDKPTLIKVTTtigYGSPNKANSY 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 325 DS-TAYRSSDEV----QTWGDKDHPI-------TRFKKYITErgwwNEEKEMEWQKevkkrvltEFAAAEKRKKAHYHDL 392
Cdd:PLN02790 251 SVhGAALGEKEVdatrKNLGWPYEPFhvpedvkSHWSKHTKE----GAALEAEWNA--------KFAEYKKKYPEEAAEL 318
|
....*....
gi 86563357 393 FEDVYDELP 401
Cdd:PLN02790 319 KSLISGELP 327
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
219-372 |
2.84e-07 |
|
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: 52.00 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 219 VYFGDGAASEGDAHAAFNFAATLKC-PIIFFCRNNGYAISTPTSEQYGGDgIAGKGPAYGLHTIRV-DGNDLLAVYNATK 296
Cdd:pfam00456 149 VFLGDGCLMEGVSSEASSLAGHLGLgNLIVFYDDNQISIDGETKISFTED-TAARFEAYGWHVIEVeDGHDVEAIAAAIE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 297 EARRValTNRPVLIEAMTYrLGHHS-----TSDDSTAYRSSDEV----QTWGDKDHP--------ITRFKKYITErgwwN 359
Cdd:pfam00456 228 EAKAE--KDKPTLIKCRTV-IGYGSpnkqgTHDVHGAPLGADEVaalkQKLGWDPYKpfeipaevYDAWKEKVAE----G 300
|
170
....*....|...
gi 86563357 360 EEKEMEWQKEVKK 372
Cdd:pfam00456 301 AKAEAEWNELFAA 313
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
194-310 |
3.76e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 42.69 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86563357 194 TTQLPQAVGSAYAFKQQKDN-NRIAVVyfGDGAASEGDAHAAFNFAATLKCPIIFFCRNNGYAIstptSEQYGG------ 266
Cdd:PRK12315 116 STSIALATGLAKARDLKGEKgNIIAVI--GDGSLSGGLALEGLNNAAELKSNLIIIVNDNQMSI----AENHGGlyknlk 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 86563357 267 -----DGIAGKGP--AYGLHTIRV-DGNDLLAVYNATKEarrVALTNRPVLI 310
Cdd:PRK12315 190 elrdtNGQSENNLfkAMGLDYRYVeDGNDIESLIEAFKE---VKDIDHPIVL 238
|
|
| |
