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P06959

- ODP2_ECOLI

UniProt

P06959 - ODP2_ECOLI

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

    Cofactori

    Binds 3 lipoyl cofactors covalently.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei547 – 5471Sequence Analysis
    Active sitei603 – 6031
    Active sitei607 – 6071Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: EcoliWiki
    2. lipoic acid binding Source: EcoliWiki
    3. protein binding Source: IntAct

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: EcoliWiki
    2. glycolytic process Source: UniProtKB-KW
    3. oxidation-reduction process Source: GOC
    4. pyruvate metabolic process Source: EcoliWiki

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Glycolysis

    Enzyme and pathway databases

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

    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
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10025. aceF.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. pyruvate dehydrogenase complex Source: EcoliWiki

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi603 – 6031H → C: Abolishes catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 630629Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162278Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411N6-lipoyllysine2 Publications
    Modified residuei144 – 1441N6-lipoyllysine2 Publications
    Modified residuei245 – 2451N6-lipoyllysine1 Publication
    Modified residuei396 – 3961N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP06959.
    PRIDEiP06959.

    2D gel databases

    SWISS-2DPAGEP06959.

    Expressioni

    Gene expression databases

    GenevestigatoriP06959.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dcmP0AED92EBI-542707,EBI-548525
    intAP320532EBI-542707,EBI-552967
    lpdAP0A9P03EBI-542707,EBI-542856
    pinRP0ADI02EBI-542707,EBI-544672

    Protein-protein interaction databases

    DIPiDIP-9040N.
    IntActiP06959. 84 interactions.
    MINTiMINT-1311573.
    STRINGi511145.b0115.

    Structurei

    Secondary structure

    1
    630
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi206 – 2094
    Beta strandi215 – 2173
    Beta strandi219 – 2235
    Beta strandi227 – 2293
    Beta strandi236 – 24611
    Beta strandi248 – 2547
    Beta strandi256 – 2605
    Beta strandi276 – 2805

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QJONMR-A206-284[»]
    2K7VNMR-A/B206-293[»]
    ProteinModelPortaliP06959.
    SMRiP06959. Positions 1-183, 206-284, 328-365, 388-630.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06959.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7473Lipoyl-binding 1Add
    BLAST
    Domaini106 – 17772Lipoyl-binding 2Add
    BLAST
    Domaini207 – 27872Lipoyl-binding 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni317 – 630314Subunit binding, catalyticAdd
    BLAST
    Regioni373 – 38917HydrophobicAdd
    BLAST
    Regioni542 – 56726HydrophobicAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 3 lipoyl-binding domains.Curated

    Keywords - Domaini

    Lipoyl, Repeat

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281562.
    KOiK00627.
    OMAiTEIMVAV.
    OrthoDBiEOG610413.
    PhylomeDBiP06959.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR003016. 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]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 3 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 3 hits.
    TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
    PS00189. LIPOYL. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P06959-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ    50
    AGIVKEIKVS VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP 100
    AAAAAKDVNV PDIGSDEVEV TEILVKVGDK VEAEQSLITV EGDKASMEVP 150
    APFAGTVKEI KVNVGDKVST GSLIMVFEVA GEAGAAAPAA KQEAAPAAAP 200
    APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT VEGDKASMEV 250
    PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA 300
    AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT 350
    GRKGRILRED VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI 400
    EEVELGRIQK ISGANLSRNW VMIPHVTHFD KTDITELEAF RKQQNEEAAK 450
    RKLDVKITPV VFIMKAVAAA LEQMPRFNSS LSEDGQRLTL KKYINIGVAV 500
    DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA GEMQGGCFTI 550
    SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS 600
    FDHRVIDGAD GARFITIINN TLSDIRRLVM 630
    Length:630
    Mass (Da):66,096
    Last modified:January 23, 2007 - v3
    Checksum:i802A513A1E88F5DA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01498 Genomic DNA. Translation: CAA24741.1.
    U00096 Genomic DNA. Translation: AAC73226.1.
    AP009048 Genomic DNA. Translation: BAB96685.1.
    PIRiA30278. XXECDP.
    RefSeqiNP_414657.1. NC_000913.3.
    YP_488418.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73226; AAC73226; b0115.
    BAB96685; BAB96685; BAB96685.
    GeneIDi12932377.
    944794.
    KEGGiecj:Y75_p0112.
    eco:b0115.
    PATRICi32115331. VBIEscCol129921_0117.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488418.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QJO NMR - A 206-284 [» ]
    2K7V NMR - A/B 206-293 [» ]
    ProteinModelPortali P06959.
    SMRi P06959. Positions 1-183, 206-284, 328-365, 388-630.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9040N.
    IntActi P06959. 84 interactions.
    MINTi MINT-1311573.
    STRINGi 511145.b0115.

    2D gel databases

    SWISS-2DPAGE P06959.

    Proteomic databases

    PaxDbi P06959.
    PRIDEi P06959.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73226 ; AAC73226 ; b0115 .
    BAB96685 ; BAB96685 ; BAB96685 .
    GeneIDi 12932377.
    944794.
    KEGGi ecj:Y75_p0112.
    eco:b0115.
    PATRICi 32115331. VBIEscCol129921_0117.

    Organism-specific databases

    EchoBASEi EB0024.
    EcoGenei EG10025. aceF.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281562.
    KOi K00627.
    OMAi TEIMVAV.
    OrthoDBi EOG610413.
    PhylomeDBi P06959.

    Enzyme and pathway databases

    BioCyci EcoCyc:E2P-MONOMER.
    ECOL316407:JW0111-MONOMER.
    MetaCyc:E2P-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P06959.
    PROi P06959.

    Gene expression databases

    Genevestigatori P06959.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 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 ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 3 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 3 hits.
    TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 3 hits.
    PS00189. LIPOYL. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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], LIPOYLATION AT LYS-41; LYS-144 AND LYS-245.
      Strain: K12.
    2. 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, LIPOYLATION AT LYS-41.
    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, LIPOYLATION AT LYS-144.
    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.

    Entry informationi

    Entry nameiODP2_ECOLI
    AccessioniPrimary (citable) accession number: P06959
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 157 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3