Reviewed,
UniProtKB/Swiss-Prot P06959 (ODP2_ECOLI)
Last modified
February 9, 2010.
Version 120.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex EC=2.3.1.12 Alternative name(s): E2 Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 630 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | 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 activity | Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. |
| Cofactor | Binds 3 lipoyl cofactors covalently. |
| Subunit structure | Forms a 24-polypeptide structural core with octahedral symmetry. |
| Sequence similarities | Belongs to the 2-oxoacid dehydrogenase family. Contains 3 lipoyl-binding domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Domain | Lipoyl Repeat |
| Molecular function | Acyltransferase Transferase |
| PTM | Acetylation |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | acetyl-CoA biosynthetic process from pyruvate Inferred from mutant phenotype. Source: UniProtKB glycolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | pyruvate dehydrogenase complex Inferred from direct assay. Source: UniProtKB |
| Molecular function | dihydrolipoyllysine-residue acetyltransferase activity Inferred from direct assay. Source: UniProtKB lipoic acid bindingInferred from direct assay. Source: UniProtKB protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| alkA | P04395 | 1 | EBI-542707,EBI-544077 | |
| dcm | P0AED9 | 1 | EBI-542707,EBI-548525 | |
| intA | P32053 | 1 | EBI-542707,EBI-552967 | |
| pinR | P0ADI0 | 1 | EBI-542707,EBI-544672 | |
| recG | P24230 | 1 | EBI-542707,EBI-556882 | |
| rnt | P30014 | 1 | EBI-542707,EBI-557418 | |
| tyrR | P07604 | 1 | EBI-542707,EBI-559274 | |
| yraL | P67087 | 1 | EBI-542707,EBI-561394 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||
Molecule processing | |||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.4 | ||||||||||||||||||||
| Chain | 2 – 630 | 629 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex | PRO_0000162278 | |||||||||||||||||||
Regions | |||||||||||||||||||||||
| Domain | 2 – 74 | 73 | Lipoyl-binding 1 | ||||||||||||||||||||
| Domain | 106 – 177 | 72 | Lipoyl-binding 2 | ||||||||||||||||||||
| Domain | 207 – 278 | 72 | Lipoyl-binding 3 | ||||||||||||||||||||
| Region | 317 – 630 | 314 | Subunit binding, catalytic | ||||||||||||||||||||
| Region | 373 – 389 | 17 | Hydrophobic | ||||||||||||||||||||
| Region | 542 – 567 | 26 | Hydrophobic | ||||||||||||||||||||
Sites | |||||||||||||||||||||||
| Active site | 547 | 1 | Potential | ||||||||||||||||||||
| Active site | 603 | 1 | |||||||||||||||||||||
| Active site | 607 | 1 | Potential | ||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||
| Modified residue | 41 | 1 | N6-lipoyllysine | ||||||||||||||||||||
| Modified residue | 144 | 1 | N6-lipoyllysine | ||||||||||||||||||||
| Modified residue | 245 | 1 | N6-lipoyllysine | ||||||||||||||||||||
| Modified residue | 396 | 1 | N6-acetyllysine Ref.8 | ||||||||||||||||||||
Experimental info | |||||||||||||||||||||||
| Mutagenesis | 603 | 1 | H → C: Abolishes catalytic activity. Ref.6 | ||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||
| Beta strand | 206 – 209 | 4 | |||||||||||||||||||||
| Beta strand | 215 – 217 | 3 | |||||||||||||||||||||
| Beta strand | 219 – 223 | 5 | |||||||||||||||||||||
| Beta strand | 236 – 246 | 11 | |||||||||||||||||||||
| Beta strand | 248 – 254 | 7 | |||||||||||||||||||||
| Beta strand | 256 – 260 | 5 | |||||||||||||||||||||
| Beta strand | 276 – 280 | 5 | |||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component." Stephens P.E., Darlison M.G., Lewis H.M., Guest J.R. Eur. J. Biochem. 133:481-489(1983) [PubMed: 6345153] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2. |
| [5] | "Amino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli." Hale G., Perham R.N. Biochem. J. 187:905-908(1980) [PubMed: 6821375] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-47. |
| [6] | "Overexpression of restructured pyruvate dehydrogenase complexes and site-directed mutagenesis of a potential active-site histidine residue." Russel G.C., Guest J.R. Biochem. J. 269:443-450(1990) [PubMed: 2201286] [Abstract] Cited for: MUTAGENESIS OF HIS-603. |
| [7] | "Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli." Ali S.T., Guest J.R. Biochem. J. 271:139-145(1990) [PubMed: 2121129] [Abstract] Cited for: LIPOYLATED DOMAINS STUDIES. |
| [8] | "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | V01498 Genomic DNA. Translation: CAA24741.1. U00096 Genomic DNA. Translation: AAC73226.1. AP009048 Genomic DNA. Translation: BAB96685.1. | ||||||||||||||||||
| PIR | XXECDP. A30278. | ||||||||||||||||||
| RefSeq | AP_000776.1. NP_414657.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| SMR | P06959. Positions 1-81, 106-183, 326-370, 388-630. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-9040N. | ||||||||||||||||||
| IntAct | P06959. 83 interactions. | ||||||||||||||||||
| STRING | P06959. | ||||||||||||||||||
2-D gel databases | |||||||||||||||||||
| SWISS-2DPAGE | P06959. | ||||||||||||||||||
| ECO2DBASE | C062.7. 6TH EDITION. C070.0. 6TH EDITION. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | P06959. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 944794. | ||||||||||||||||||
| GenomeReviews | Gene locus JW0111 in contig AP009048_GR. Gene locus b0115 in contig U00096_GR. | ||||||||||||||||||
| KEGG | ecj:JW0111. eco:b0115. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| EchoBASE | EB0024. | ||||||||||||||||||
| EcoGene | EG10025. aceF. | ||||||||||||||||||
| CMR | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG0508. | ||||||||||||||||||
| HOGENOM | HBG630916. | ||||||||||||||||||
| OMA | MEIPAPK. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | EcoCyc:E2P-MONOMER. ECOL168927:B0115-MONOMER. MetaCyc:E2P-MONOMER. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| Genevestigator | P06959. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR006256. AcTrfase_Pyrv_DH_cplx. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. IPR011053. Single_hybrid_motif. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:4.10.320.10. E3_bd. 1 hit. | ||||||||||||||||||
| Pfam | PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 3 hits. PF02817. E3_binding. 1 hit. [Graphical view] | ||||||||||||||||||
| TIGRFAMs | TIGR01348. PDHac_trf_long. 1 hit. | ||||||||||||||||||
| PROSITE | PS50968. BIOTINYL_LIPOYL. 3 hits. PS00189. LIPOYL. 3 hits. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | ODP2_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P06959 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


