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UniProtKB - P06959 (ODP2_ECOLI)
Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Gene
aceF
Organism
Escherichia coli (strain K12)
Status
Functioni
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic activityi
- (R)-N6-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N6-(S8-acetyldihydrolipoyl)-L-lysyl-[protein] + CoAEC:2.3.1.12
Cofactori
(R)-lipoateNote: Binds 3 lipoyl cofactors covalently.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 547 | Sequence analysis | 1 | |
Active sitei | 603 | 1 | ||
Active sitei | 607 | Sequence analysis | 1 |
GO - Molecular functioni
- acetyltransferase activity Source: GO_Central
- dihydrolipoyllysine-residue acetyltransferase activity Source: EcoliWiki
- lipoic acid binding Source: EcoliWiki
GO - Biological processi
- acetyl-CoA biosynthetic process from pyruvate Source: EcoliWiki
- glycolytic process Source: UniProtKB-KW
- pyruvate metabolic process Source: EcoliWiki
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Glycolysis |
Enzyme and pathway databases
BioCyci | EcoCyc:E2P-MONOMER |
BRENDAi | 2.3.1.12, 2026 |
SABIO-RKi | P06959 |
Names & Taxonomyi
Protein namesi | Recommended name: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC:2.3.1.12)Alternative name(s): Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex E2 |
Gene namesi | Name:aceF Ordered Locus Names:b0115, JW0111 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Other locations
- cytoplasm Source: EcoliWiki
- pyruvate dehydrogenase complex Source: EcoCyc
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 603 | H → C: Abolishes catalytic activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000162278 | 2 – 630 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST | 629 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 41 | N6-lipoyllysinePROSITE-ProRule annotation2 Publications | 1 | |
Modified residuei | 144 | N6-lipoyllysinePROSITE-ProRule annotation2 Publications | 1 | |
Modified residuei | 245 | N6-lipoyllysinePROSITE-ProRule annotation1 Publication | 1 | |
Modified residuei | 396 | N6-acetyllysine1 Publication | 1 |
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P06959 |
PaxDbi | P06959 |
PRIDEi | P06959 |
2D gel databases
SWISS-2DPAGEi | P06959 |
PTM databases
iPTMneti | P06959 |
Interactioni
Subunit structurei
Forms a 24-polypeptide structural core with octahedral symmetry.
Binary interactionsi
P06959
Protein-protein interaction databases
BioGRIDi | 4261371, 5 interactors 849195, 1 interactor |
ComplexPortali | CPX-3943, Pyruvate dehydrogenase complex |
DIPi | DIP-9040N |
IntActi | P06959, 86 interactors |
STRINGi | 511145.b0115 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P06959 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P06959 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2 – 75 | Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST | 74 | |
Domaini | 105 – 178 | Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST | 74 | |
Domaini | 206 – 279 | Lipoyl-binding 3PROSITE-ProRule annotationAdd BLAST | 74 | |
Domaini | 328 – 365 | Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST | 38 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 373 – 389 | HydrophobicAdd BLAST | 17 | |
Regioni | 542 – 567 | HydrophobicAdd BLAST | 26 |
Sequence similaritiesi
Belongs to the 2-oxoacid dehydrogenase family.Curated
Keywords - Domaini
Lipoyl, RepeatPhylogenomic databases
eggNOGi | COG0508, Bacteria |
HOGENOMi | CLU_016733_10_0_6 |
InParanoidi | P06959 |
PhylomeDBi | P06959 |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit 4.10.320.10, 1 hit |
InterProi | View protein in InterPro IPR003016, 2-oxoA_DH_lipoyl-BS IPR001078, 2-oxoacid_DH_actylTfrase IPR006256, AcTrfase_Pyrv_DH_cplx IPR000089, Biotin_lipoyl IPR023213, CAT-like_dom_sf IPR036625, E3-bd_dom_sf IPR004167, PSBD IPR011053, Single_hybrid_motif |
PANTHERi | PTHR43178:SF2, PTHR43178:SF2, 4 hits |
Pfami | View protein in Pfam PF00198, 2-oxoacid_dh, 1 hit PF00364, Biotin_lipoyl, 3 hits PF02817, E3_binding, 1 hit |
SUPFAMi | SSF47005, SSF47005, 1 hit SSF51230, SSF51230, 3 hits |
TIGRFAMsi | TIGR01348, PDHac_trf_long, 1 hit |
PROSITEi | View protein in PROSITE PS50968, BIOTINYL_LIPOYL, 3 hits PS00189, LIPOYL, 3 hits PS51826, PSBD, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P06959-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ
60 70 80 90 100
AGIVKEIKVS VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP
110 120 130 140 150
AAAAAKDVNV PDIGSDEVEV TEILVKVGDK VEAEQSLITV EGDKASMEVP
160 170 180 190 200
APFAGTVKEI KVNVGDKVST GSLIMVFEVA GEAGAAAPAA KQEAAPAAAP
210 220 230 240 250
APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT VEGDKASMEV
260 270 280 290 300
PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA
310 320 330 340 350
AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT
360 370 380 390 400
GRKGRILRED VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI
410 420 430 440 450
EEVELGRIQK ISGANLSRNW VMIPHVTHFD KTDITELEAF RKQQNEEAAK
460 470 480 490 500
RKLDVKITPV VFIMKAVAAA LEQMPRFNSS LSEDGQRLTL KKYINIGVAV
510 520 530 540 550
DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA GEMQGGCFTI
560 570 580 590 600
SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS
610 620 630
FDHRVIDGAD GARFITIINN TLSDIRRLVM
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01498 Genomic DNA Translation: CAA24741.1 U00096 Genomic DNA Translation: AAC73226.1 AP009048 Genomic DNA Translation: BAB96685.1 |
PIRi | A30278, XXECDP |
RefSeqi | NP_414657.1, NC_000913.3 WP_000963518.1, NZ_STEB01000010.1 |
Genome annotation databases
EnsemblBacteriai | AAC73226; AAC73226; b0115 BAB96685; BAB96685; BAB96685 |
GeneIDi | 66671597 944794 |
KEGGi | ecj:JW0111 eco:b0115 |
PATRICi | fig|1411691.4.peg.2167 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01498 Genomic DNA Translation: CAA24741.1 U00096 Genomic DNA Translation: AAC73226.1 AP009048 Genomic DNA Translation: BAB96685.1 |
PIRi | A30278, XXECDP |
RefSeqi | NP_414657.1, NC_000913.3 WP_000963518.1, NZ_STEB01000010.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1QJO | NMR | - | A | 206-284 | [»] | |
2K7V | NMR | - | A/B | 206-293 | [»] | |
7B9K | electron microscopy | 3.16 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X | 1-630 | [»] | |
SMRi | P06959 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261371, 5 interactors 849195, 1 interactor |
ComplexPortali | CPX-3943, Pyruvate dehydrogenase complex |
DIPi | DIP-9040N |
IntActi | P06959, 86 interactors |
STRINGi | 511145.b0115 |
PTM databases
iPTMneti | P06959 |
2D gel databases
SWISS-2DPAGEi | P06959 |
Proteomic databases
jPOSTi | P06959 |
PaxDbi | P06959 |
PRIDEi | P06959 |
Genome annotation databases
EnsemblBacteriai | AAC73226; AAC73226; b0115 BAB96685; BAB96685; BAB96685 |
GeneIDi | 66671597 944794 |
KEGGi | ecj:JW0111 eco:b0115 |
PATRICi | fig|1411691.4.peg.2167 |
Organism-specific databases
EchoBASEi | EB0024 |
Phylogenomic databases
eggNOGi | COG0508, Bacteria |
HOGENOMi | CLU_016733_10_0_6 |
InParanoidi | P06959 |
PhylomeDBi | P06959 |
Enzyme and pathway databases
BioCyci | EcoCyc:E2P-MONOMER |
BRENDAi | 2.3.1.12, 2026 |
SABIO-RKi | P06959 |
Miscellaneous databases
EvolutionaryTracei | P06959 |
PROi | PR:P06959 |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit 4.10.320.10, 1 hit |
InterProi | View protein in InterPro IPR003016, 2-oxoA_DH_lipoyl-BS IPR001078, 2-oxoacid_DH_actylTfrase IPR006256, AcTrfase_Pyrv_DH_cplx IPR000089, Biotin_lipoyl IPR023213, CAT-like_dom_sf IPR036625, E3-bd_dom_sf IPR004167, PSBD IPR011053, Single_hybrid_motif |
PANTHERi | PTHR43178:SF2, PTHR43178:SF2, 4 hits |
Pfami | View protein in Pfam PF00198, 2-oxoacid_dh, 1 hit PF00364, Biotin_lipoyl, 3 hits PF02817, E3_binding, 1 hit |
SUPFAMi | SSF47005, SSF47005, 1 hit SSF51230, SSF51230, 3 hits |
TIGRFAMsi | TIGR01348, PDHac_trf_long, 1 hit |
PROSITEi | View protein in PROSITE PS50968, BIOTINYL_LIPOYL, 3 hits PS00189, LIPOYL, 3 hits PS51826, PSBD, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ODP2_ECOLI | |
Accessioni | P06959Primary (citable) accession number: P06959 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1988 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 206 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families