|
Name |
Accession |
Description |
Interval |
E-value |
| PDH_E1_alph_y |
TIGR03182 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
31-346 |
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: 274473 [Multi-domain] Cd Length: 315 Bit Score: 555.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 31 KEEEIDAYREMLLIRRFEEKAGQLYGMGLIGGFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGHMLAVGMSPRGVMAE 110
Cdd:TIGR03182 1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 111 LTGRQGGFSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLWK 190
Cdd:TIGR03182 81 LTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 191 LPVVYIIENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWTRSGKGPIILDMQTYRYRGHS 270
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270732723 271 MSDPAKYRSKEEVQKIKeEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQSDQEPDASELYTDILV 346
Cdd:TIGR03182 241 MSDPAKYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
17-346 |
7.27e-163 |
|
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: 458.45 E-value: 7.27e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 17 LSNTTKKAKIANFTKEEEIDAYREMLLIRRFEEKAGQLYGMGLIGgFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGH 96
Cdd:COG1071 5 LDPDGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIG-FYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 97 MLAVGMSPRGVMAELTGRQGGFSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQ 176
Cdd:COG1071 84 ALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 177 GQVYESFNMASLWKLPVVYIIENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWTRSGKGP 256
Cdd:COG1071 164 GDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 257 IILDMQTYRYRGHSMSD-PAKYRSKEEVQKIKeEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQSDQEP 335
Cdd:COG1071 244 TLIEAKTYRLGGHSTSDdPTRYRTKEEVEEWR-ERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEP 322
|
330
....*....|.
gi 1270732723 336 DASELYTDILV 346
Cdd:COG1071 323 DPEELFDDVYA 333
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
37-329 |
6.47e-146 |
|
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: 413.43 E-value: 6.47e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 37 AYREMLLIRRFEEKAGQLYGMGLIGGFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGHMLAVGMSPRGVMAELTGRQG 116
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 117 GFSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLWKLPVVYI 196
Cdd:cd02000 81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 197 IENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWTRSGKGPIILDMQTYRYRGHSMS-DPA 275
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDPS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1270732723 276 KYRSKEEVQKiKEEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFA 329
Cdd:cd02000 241 RYRTKEEVEE-WKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
30-346 |
4.30e-133 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 383.68 E-value: 4.30e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 30 TKEEEIDAYREMLLIRRFEEKAGQLYGMGLIGGFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGHMLAVGMSPRGVMA 109
Cdd:PLN02269 28 SKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLEVFA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 110 ELTGRQGGFSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLW 189
Cdd:PLN02269 108 ELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAALW 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 190 KLPVVYIIENNQYAMGTSVARASAETDFSRRGLSfeIPGIVVDGMDVRAVKGAADEAITWTRSgKGPIILDMQTYRYRGH 269
Cdd:PLN02269 188 DLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDY--VPGLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMDTYRYHGH 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270732723 270 SMSDP-AKYRSKEEVQKIKEEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQSDQEPDASELYTDILV 346
Cdd:PLN02269 265 SMSDPgSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVYV 342
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
39-338 |
2.32e-116 |
|
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: 338.92 E-value: 2.32e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 39 REMLLIRRFEEKAGQLYGMGLIGGFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGHMLAVGMSPRGVMAELTGRQGGF 118
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 119 SKGKggsMHMF--SKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLWKLPVVYI 196
Cdd:pfam00676 81 KGGS---MHGYygAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 197 IENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWTRSGKGPIILDMQTYRYRGHSMSDPA- 275
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPs 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270732723 276 KYRSKEEVQKIKEEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQSDQEPDAS 338
Cdd:pfam00676 238 TYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDH_E1_alph_y |
TIGR03182 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
31-346 |
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: 274473 [Multi-domain] Cd Length: 315 Bit Score: 555.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 31 KEEEIDAYREMLLIRRFEEKAGQLYGMGLIGGFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGHMLAVGMSPRGVMAE 110
Cdd:TIGR03182 1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 111 LTGRQGGFSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLWK 190
Cdd:TIGR03182 81 LTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 191 LPVVYIIENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWTRSGKGPIILDMQTYRYRGHS 270
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270732723 271 MSDPAKYRSKEEVQKIKeEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQSDQEPDASELYTDILV 346
Cdd:TIGR03182 241 MSDPAKYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
17-346 |
7.27e-163 |
|
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: 458.45 E-value: 7.27e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 17 LSNTTKKAKIANFTKEEEIDAYREMLLIRRFEEKAGQLYGMGLIGgFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGH 96
Cdd:COG1071 5 LDPDGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIG-FYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 97 MLAVGMSPRGVMAELTGRQGGFSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQ 176
Cdd:COG1071 84 ALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 177 GQVYESFNMASLWKLPVVYIIENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWTRSGKGP 256
Cdd:COG1071 164 GDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 257 IILDMQTYRYRGHSMSD-PAKYRSKEEVQKIKeEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQSDQEP 335
Cdd:COG1071 244 TLIEAKTYRLGGHSTSDdPTRYRTKEEVEEWR-ERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEP 322
|
330
....*....|.
gi 1270732723 336 DASELYTDILV 346
Cdd:COG1071 323 DPEELFDDVYA 333
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
37-329 |
6.47e-146 |
|
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: 413.43 E-value: 6.47e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 37 AYREMLLIRRFEEKAGQLYGMGLIGGFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGHMLAVGMSPRGVMAELTGRQG 116
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 117 GFSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLWKLPVVYI 196
Cdd:cd02000 81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 197 IENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWTRSGKGPIILDMQTYRYRGHSMS-DPA 275
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDPS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1270732723 276 KYRSKEEVQKiKEEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFA 329
Cdd:cd02000 241 RYRTKEEVEE-WKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
30-346 |
4.30e-133 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 383.68 E-value: 4.30e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 30 TKEEEIDAYREMLLIRRFEEKAGQLYGMGLIGGFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGHMLAVGMSPRGVMA 109
Cdd:PLN02269 28 SKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLEVFA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 110 ELTGRQGGFSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLW 189
Cdd:PLN02269 108 ELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAALW 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 190 KLPVVYIIENNQYAMGTSVARASAETDFSRRGLSfeIPGIVVDGMDVRAVKGAADEAITWTRSgKGPIILDMQTYRYRGH 269
Cdd:PLN02269 188 DLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDY--VPGLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMDTYRYHGH 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270732723 270 SMSDP-AKYRSKEEVQKIKEEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQSDQEPDASELYTDILV 346
Cdd:PLN02269 265 SMSDPgSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVYV 342
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
39-338 |
2.32e-116 |
|
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: 338.92 E-value: 2.32e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 39 REMLLIRRFEEKAGQLYGMGLIGGFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGHMLAVGMSPRGVMAELTGRQGGF 118
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 119 SKGKggsMHMF--SKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLWKLPVVYI 196
Cdd:pfam00676 81 KGGS---MHGYygAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 197 IENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWTRSGKGPIILDMQTYRYRGHSMSDPA- 275
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPs 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270732723 276 KYRSKEEVQKIKEEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQSDQEPDAS 338
Cdd:pfam00676 238 TYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
18-344 |
1.49e-102 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 308.41 E-value: 1.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 18 SNTTKKAKIANFTKEEEIDAYREMLLIRRFEEKAGQLYGMGLIGGFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGHM 97
Cdd:PLN02374 72 KNSKASASDLLVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 98 LAVGMSPRGVMAELTGRQGGFSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGSGLAFSNQY-------LGKDNVTLVYFG 170
Cdd:PLN02374 152 LSKGVPARAVMSELFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSKYrrevlkeESCDDVTLAFFG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 171 DGAANQGQVYESFNMASLWKLPVVYIIENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWT 250
Cdd:PLN02374 232 DGTCNNGQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 251 RSGKGPIILDMQTYRYRGHSMSDPAKYRSKEEVQKIKeEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQ 330
Cdd:PLN02374 312 RRGEGPTLVECETYRFRGHSLADPDELRDPAEKAHYA-ARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFAD 390
|
330
....*....|....
gi 1270732723 331 SDQEPDASELYTDI 344
Cdd:PLN02374 391 ASPLPPRSQLLENV 404
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
28-341 |
7.80e-96 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 288.30 E-value: 7.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 28 NFTKEEEIDAYREMLLIRRFEEKAGQLYGMGLIGGFCHLYIGQEAVVIGTLKAAKEGDQVITSYRDHGHMLAVGMSPRGV 107
Cdd:CHL00149 16 NINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 108 MAELTGRQGGFSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGSGLAFSNQY-------LGKDNVTLVYFGDGAANQGQVY 180
Cdd:CHL00149 96 MAELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSIYrqqvlkeVQPLRVTACFFGDGTTNNGQFF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 181 ESFNMASLWKLPVVYIIENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWTRSGKGPIILD 260
Cdd:CHL00149 176 ECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 261 MQTYRYRGHSMSDPAKYRSKEEvQKIKEEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQSDQEPDASEL 340
Cdd:CHL00149 256 ALTYRFRGHSLADPDELRSKQE-KEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDL 334
|
.
gi 1270732723 341 Y 341
Cdd:CHL00149 335 K 335
|
|
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
30-341 |
6.39e-82 |
|
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: 252.45 E-value: 6.39e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 30 TKEEEIDAYREMLLIRRFEEKAGQLYGMGLIGGFCHLYiGQEAVVIGTLKAAKEGDQVITSYRDHGHMLAVGMSPRGVMA 109
Cdd:TIGR03181 22 SDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNL-GQEAAQVGSALALRKDDWVFPSYRDHAAMLARGVPLVEILL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 110 ELTGRQGGFSkgkggsmhmFSKEKNFYGGHGIVGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLW 189
Cdd:TIGR03181 101 YWRGDERGSW---------DPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGDFYEALNFAGVF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 190 KLPVVYIIENNQYAMGTSVARASAETDFSRRGLSFEIPGIVVDGMDVRAVKGAADEAITWTRSGKGPIILDMQTYRYRGH 269
Cdd:TIGR03181 172 KAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGPTLIEAVTYRLGPH 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270732723 270 SMSD-PAKYRSKEEVQKiKEEQDPIDQVRNRILQQGFASEDDLKSIDKEVRAIVADAVDFAQSDQEPDASELY 341
Cdd:TIGR03181 252 TTADdPTRYRTKEEEEE-WRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPVDDIF 323
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
138-287 |
1.22e-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: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 138 GHGIvgaqvPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLWKL-PVVYIIENNQYAMGTSVARASAETD 216
Cdd:cd02012 108 GQGL-----SVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNRIQIDGPTDDILFTED 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 217 FSRRGLSFeipG---IVVDGMDVRAVKGAADEAitwtRSGKG-PIILDMQTYRYRG-HSMSDPAKYR----SKEEVQKIK 287
Cdd:cd02012 183 LAKKFEAF---GwnvIEVDGHDVEEILAALEEA----KKSKGkPTLIIAKTIKGKGvPFMENTAKWHgkplGEEEVELAK 255
|
|
| TPP_E1_OGDC_like |
cd02016 |
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ... |
170-273 |
7.86e-09 |
|
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDC). OGDC catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA and carbon dioxide, a key reaction of the tricarboxylic acid cycle.
Pssm-ID: 238974 [Multi-domain] Cd Length: 265 Bit Score: 55.61 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 170 GDGA-ANQGQVYESFNMaslWKLP------VVYIIENNQYAMGTS--VARASAE-TDFSRrglSFEIPGIVVDGMDVRAV 239
Cdd:cd02016 148 GDAAfAGQGVVYETLNL---SNLPgyttggTIHIVVNNQIGFTTDprDSRSSPYcTDVAK---MIGAPIFHVNGDDPEAV 221
|
90 100 110
....*....|....*....|....*....|....
gi 1270732723 240 KGAADEAITWTRSGKGPIILDMQTYRYRGHSMSD 273
Cdd:cd02016 222 VRATRLALEYRQKFKKDVVIDLVCYRRHGHNELD 255
|
|
| sucA |
PRK09404 |
2-oxoglutarate dehydrogenase E1 component; Reviewed |
170-320 |
3.79e-06 |
|
2-oxoglutarate dehydrogenase E1 component; Reviewed
Pssm-ID: 236499 [Multi-domain] Cd Length: 924 Bit Score: 48.57 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 170 GDGA-ANQGQVYESFNMAslwKLP------VVYIIENNQYAMGTSVARA-SAE--TDFSRrglSFEIPGIVVDGMDVRAV 239
Cdd:PRK09404 350 GDAAfAGQGVVAETLNLS---QLRgyrtggTIHIVINNQIGFTTSPPDDrSTPycTDVAK---MVQAPIFHVNGDDPEAV 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 240 KGAADEAITWTRSGKGPIILDMQTYRYRGHSMSD------PAKYrskeevQKIKEEQDPIDQVRNRILQQGFASEDDLKS 313
Cdd:PRK09404 424 VFATRLALEYRQKFKKDVVIDLVCYRRHGHNEGDepsftqPLMY------KKIKKHPTTRELYADKLVAEGVITEEEADE 497
|
....*..
gi 1270732723 314 IDKEVRA 320
Cdd:PRK09404 498 MVNEYRD 504
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
170-290 |
6.45e-06 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 47.96 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 170 GDGA-ANQGQVYESFNMASLWKLPV---VYIIENNQYAMGTS--VARASA-ETDFSRrglSFEIPGIVVDGMDVRAVKGA 242
Cdd:PRK12270 655 GDAAfAGQGVVAETLNLSQLRGYRTggtIHIVVNNQVGFTTApeSSRSSEyATDVAK---MIQAPIFHVNGDDPEAVVRV 731
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1270732723 243 ADEAITWTRSGKGPIILDMQTYRYRGH------SMSDPAKY---RSKEEVQKIKEEQ 290
Cdd:PRK12270 732 ARLAFEYRQRFHKDVVIDLVCYRRRGHnegddpSMTQPLMYdliDAKRSVRKLYTEA 788
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
135-268 |
7.57e-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: 46.00 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 135 FYGGHGivGAQVPIGSGLAFSNQYLGKDNVTLVYFGDGAANQGQVYESFNMASLWKLPVVYIIENNQYAMGTSVARASae 214
Cdd:cd02007 72 FGTGHS--STSISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVGTPG-- 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1270732723 215 TDFSRRGLSFEIPgivVDGMDVRAVKGAADEAitwtRSGKGPIILDMQTYRYRG 268
Cdd:cd02007 148 NLFEELGFRYIGP---VDGHNIEALIKVLKEV----KDLKGPVLLHVVTKKGKG 194
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
134-260 |
9.92e-03 |
|
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: 36.46 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732723 134 NFYGGHGIVGAQVPIGSGLAFSNqylgKDNVTLVYFGDGAAN-QGQVYESfnmASLWKLPVVYIIENNQ-YAMGtsvaRA 211
Cdd:cd00568 40 LTSTGFGAMGYGLPAAIGAALAA----PDRPVVCIAGDGGFMmTGQELAT---AVRYGLPVIVVVFNNGgYGTI----RM 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1270732723 212 SAETDFSRRGLSFEIPGI----VVDGMDVRAVK----GAADEAITWTRSGKGPIILD 260
Cdd:cd00568 109 HQEAFYGGRVSGTDLSNPdfaaLAEAYGAKGVRvedpEDLEAALAEALAAGGPALIE 165
|
|
| |
