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P06959 (ODP2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:aceF
Ordered Locus Names:b0115, JW0111
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 630629Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162278

Regions

Domain2 – 7473Lipoyl-binding 1
Domain106 – 17772Lipoyl-binding 2
Domain207 – 27872Lipoyl-binding 3
Region317 – 630314Subunit binding, catalytic
Region373 – 38917Hydrophobic
Region542 – 56726Hydrophobic

Sites

Active site5471 Potential
Active site6031
Active site6071 Potential

Amino acid modifications

Modified residue411N6-lipoyllysine
Modified residue1441N6-lipoyllysine
Modified residue2451N6-lipoyllysine
Modified residue3961N6-acetyllysine Ref.9

Experimental info

Mutagenesis6031H → C: Abolishes catalytic activity. Ref.6

Secondary structure

................. 630
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06959 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 802A513A1E88F5DA

FASTA63066,096
        10         20         30         40         50         60 
MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS 

        70         80         90        100        110        120 
VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP AAAAAKDVNV PDIGSDEVEV 

       130        140        150        160        170        180 
TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KVNVGDKVST GSLIMVFEVA 

       190        200        210        220        230        240 
GEAGAAAPAA KQEAAPAAAP APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT 

       250        260        270        280        290        300 
VEGDKASMEV PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA 

       310        320        330        340        350        360 
AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT GRKGRILRED 

       370        380        390        400        410        420 
VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW 

       430        440        450        460        470        480 
VMIPHVTHFD KTDITELEAF RKQQNEEAAK RKLDVKITPV VFIMKAVAAA LEQMPRFNSS 

       490        500        510        520        530        540 
LSEDGQRLTL KKYINIGVAV DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA 

       550        560        570        580        590        600 
GEMQGGCFTI SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS 

       610        620        630 
FDHRVIDGAD GARFITIINN TLSDIRRLVM 

« Hide

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] [Europe PMC] [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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: LIPOYLATED DOMAINS STUDIES.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+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.
PIRXXECDP. A30278.
RefSeqNP_414657.1. NC_000913.3.
YP_488418.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QJONMR-A206-284[»]
2K7VNMR-A/B206-293[»]
ProteinModelPortalP06959.
SMRP06959. Positions 1-183, 206-284, 328-365, 388-630.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9040N.
IntActP06959. 84 interactions.
MINTMINT-1311573.
STRING511145.b0115.

2D gel databases

SWISS-2DPAGEP06959.

Proteomic databases

PaxDbP06959.
PRIDEP06959.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73226; AAC73226; b0115.
BAB96685; BAB96685; BAB96685.
GeneID12932377.
944794.
KEGGecj:Y75_p0112.
eco:b0115.
PATRIC32115331. VBIEscCol129921_0117.

Organism-specific databases

EchoBASEEB0024.
EcoGeneEG10025. aceF.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281562.
KOK00627.
OMATEIMVAV.
OrthoDBEOG610413.
PhylomeDBP06959.
ProtClustDBPRK11854.

Enzyme and pathway databases

BioCycEcoCyc:E2P-MONOMER.
ECOL316407:JW0111-MONOMER.
MetaCyc:E2P-MONOMER.

Gene expression databases

GenevestigatorP06959.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsTIGR01348. PDHac_trf_long. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06959.
PROP06959.

Entry information

Entry nameODP2_ECOLI
AccessionPrimary (citable) accession number: P06959
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene