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P0AFG8

- ODP1_ECOLI

UniProt

P0AFG8 - ODP1_ECOLI

Protein

Pyruvate dehydrogenase E1 component

Gene

aceE

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 98 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.

    Catalytic activityi

    Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

    Cofactori

    Magnesium.
    Thiamine pyrophosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi231 – 2311Magnesium
    Metal bindingi261 – 2611Magnesium
    Metal bindingi263 – 2631Magnesium; via carbonyl oxygen

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
    5. pyruvate dehydrogenase activity Source: EcoliWiki

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Magnesium, Metal-binding, Pyruvate, Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:E1P-MONOMER.
    ECOL316407:JW0110-MONOMER.
    MetaCyc:E1P-MONOMER.
    SABIO-RKP0AFG8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component (EC:1.2.4.1)
    Short name:
    PDH E1 component
    Gene namesi
    Name:aceE
    Ordered Locus Names:b0114, JW0110
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10024. aceE.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 887886Pyruvate dehydrogenase E1 componentPRO_0000162243Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei716 – 7161N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0AFG8.
    PRIDEiP0AFG8.

    2D gel databases

    SWISS-2DPAGEP0AFG8.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AFG8.

    Interactioni

    Subunit structurei

    Homodimer. Part of the PDH complex, consisting of multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-542683,EBI-542683
    groLP0A6F52EBI-542683,EBI-543750
    nthP0AB832EBI-542683,EBI-555213
    ybhFP0A9U12EBI-542683,EBI-547696
    yciUP0A8L72EBI-542683,EBI-544511

    Protein-protein interaction databases

    BioGridi849234. 1 interaction.
    DIPiDIP-9039N.
    IntActiP0AFG8. 104 interactions.
    MINTiMINT-1261483.
    STRINGi511145.b0114.

    Structurei

    Secondary structure

    1
    887
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi66 – 683
    Helixi76 – 9924
    Helixi109 – 12416
    Beta strandi131 – 1333
    Beta strandi137 – 1393
    Helixi142 – 1443
    Helixi145 – 15410
    Helixi160 – 1634
    Turni181 – 1833
    Turni185 – 1873
    Helixi197 – 21418
    Beta strandi225 – 2306
    Helixi232 – 2354
    Helixi237 – 2404
    Helixi243 – 2486
    Beta strandi254 – 2607
    Beta strandi262 – 2643
    Beta strandi265 – 2695
    Helixi275 – 28511
    Beta strandi289 – 2935
    Helixi299 – 3057
    Helixi310 – 3178
    Helixi320 – 3267
    Helixi331 – 3377
    Beta strandi339 – 3424
    Helixi343 – 3464
    Turni347 – 3515
    Helixi354 – 3585
    Helixi363 – 3653
    Helixi367 – 37913
    Beta strandi385 – 3906
    Turni393 – 3964
    Turni398 – 4003
    Turni401 – 4033
    Helixi407 – 4093
    Helixi416 – 4249
    Helixi431 – 4344
    Helixi447 – 45812
    Helixi479 – 4824
    Helixi483 – 4864
    Helixi495 – 50612
    Turni510 – 5156
    Beta strandi516 – 5227
    Helixi525 – 5273
    Helixi530 – 5367
    Turni549 – 5524
    Beta strandi553 – 5553
    Beta strandi565 – 5673
    Helixi572 – 58312
    Helixi585 – 5884
    Beta strandi594 – 6007
    Helixi601 – 6033
    Helixi605 – 61713
    Beta strandi623 – 6286
    Turni631 – 6333
    Turni635 – 6373
    Turni639 – 6413
    Helixi646 – 6505
    Beta strandi656 – 6594
    Helixi664 – 67916
    Beta strandi687 – 6915
    Turni704 – 7063
    Helixi707 – 7126
    Beta strandi715 – 7206
    Beta strandi723 – 7319
    Helixi733 – 7353
    Helixi736 – 75015
    Beta strandi752 – 7587
    Helixi762 – 77817
    Helixi788 – 7925
    Beta strandi798 – 8014
    Helixi807 – 8104
    Helixi811 – 8155
    Beta strandi817 – 8193
    Beta strandi821 – 8244
    Helixi835 – 8417
    Helixi846 – 85914
    Beta strandi861 – 8633
    Helixi865 – 87410
    Turni884 – 8863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L8AX-ray1.85A/B2-887[»]
    1RP7X-ray2.09A/B2-887[»]
    2G25X-ray2.10A/B2-887[»]
    2G28X-ray1.85A/B2-887[»]
    2G67X-ray2.32A/B2-887[»]
    2IEAX-ray1.85A/B2-887[»]
    2QTAX-ray1.85A/B2-887[»]
    2QTCX-ray1.77A/B2-887[»]
    DisProtiDP00427.
    ProteinModelPortaliP0AFG8.
    SMRiP0AFG8. Positions 57-887.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AFG8.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG2609.
    HOGENOMiHOG000115215.
    KOiK00163.
    OMAiKGIYKLD.
    OrthoDBiEOG6BW4TW.
    PhylomeDBiP0AFG8.

    Family and domain databases

    Gene3Di3.40.50.920. 1 hit.
    3.40.50.970. 2 hits.
    InterProiIPR004660. 2-oxoA_DH_E1.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005474. Transketolase_N.
    [Graphical view]
    PfamiPF00456. Transketolase_N. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000156. Pyruvate_dh_E1. 1 hit.
    SUPFAMiSSF52518. SSF52518. 2 hits.
    SSF52922. SSF52922. 1 hit.
    TIGRFAMsiTIGR00759. aceE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P0AFG8-1 [UniParc]FASTAAdd to Basket

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    MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN    50
    VAAGTGISNY INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK 100
    DLELGGHMAS FQSSATIYDV CFNHFFRARN EQDGGDLVYF QGHISPGVYA 150
    RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH PKLMPEFWQF PTVSMGLGPI 200
    GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK GAITIATREK 250
    LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD 300
    ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA 350
    DWTDEQIWAL NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA 400
    AEGKNIAHQV KKMNMDGVRH IRDRFNVPVS DADIEKLPYI TFPEGSEEHT 450
    YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ DFGALLEEQS KEISTTIAFV 500
    RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS PNGQQYTPQD 550
    REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY 600
    SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS 650
    LTIPNCISYD PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP 700
    AMPEGAEEGI RKGIYKLETI EGSKGKVQLL GSGSILRHVR EAAEILAKDY 750
    GVGSDVYSVT SFTELARDGQ DCERWNMLHP LETPRVPYIA QVMNDAPAVA 800
    STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH HFEVDASYVV 850
    VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA 887
    Length:887
    Mass (Da):99,668
    Last modified:January 23, 2007 - v2
    Checksum:i7FB3811DE11BDD02
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti146 – 1461P → R in CAA24740. (PubMed:6343085)Curated
    Sequence conflicti276 – 2761Missing in CAA24740. (PubMed:6343085)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01498 Genomic DNA. Translation: CAA24740.1.
    U00096 Genomic DNA. Translation: AAC73225.1.
    AP009048 Genomic DNA. Translation: BAB96684.2.
    S67363 Genomic DNA. Translation: AAB29357.1.
    PIRiB64734. DEECPV.
    RefSeqiNP_414656.1. NC_000913.3.
    YP_488417.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73225; AAC73225; b0114.
    BAB96684; BAB96684; BAB96684.
    GeneIDi12932309.
    944834.
    KEGGiecj:Y75_p0111.
    eco:b0114.
    PATRICi32115329. VBIEscCol129921_0116.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01498 Genomic DNA. Translation: CAA24740.1 .
    U00096 Genomic DNA. Translation: AAC73225.1 .
    AP009048 Genomic DNA. Translation: BAB96684.2 .
    S67363 Genomic DNA. Translation: AAB29357.1 .
    PIRi B64734. DEECPV.
    RefSeqi NP_414656.1. NC_000913.3.
    YP_488417.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L8A X-ray 1.85 A/B 2-887 [» ]
    1RP7 X-ray 2.09 A/B 2-887 [» ]
    2G25 X-ray 2.10 A/B 2-887 [» ]
    2G28 X-ray 1.85 A/B 2-887 [» ]
    2G67 X-ray 2.32 A/B 2-887 [» ]
    2IEA X-ray 1.85 A/B 2-887 [» ]
    2QTA X-ray 1.85 A/B 2-887 [» ]
    2QTC X-ray 1.77 A/B 2-887 [» ]
    DisProti DP00427.
    ProteinModelPortali P0AFG8.
    SMRi P0AFG8. Positions 57-887.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 849234. 1 interaction.
    DIPi DIP-9039N.
    IntActi P0AFG8. 104 interactions.
    MINTi MINT-1261483.
    STRINGi 511145.b0114.

    2D gel databases

    SWISS-2DPAGE P0AFG8.

    Proteomic databases

    PaxDbi P0AFG8.
    PRIDEi P0AFG8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73225 ; AAC73225 ; b0114 .
    BAB96684 ; BAB96684 ; BAB96684 .
    GeneIDi 12932309.
    944834.
    KEGGi ecj:Y75_p0111.
    eco:b0114.
    PATRICi 32115329. VBIEscCol129921_0116.

    Organism-specific databases

    EchoBASEi EB0023.
    EcoGenei EG10024. aceE.

    Phylogenomic databases

    eggNOGi COG2609.
    HOGENOMi HOG000115215.
    KOi K00163.
    OMAi KGIYKLD.
    OrthoDBi EOG6BW4TW.
    PhylomeDBi P0AFG8.

    Enzyme and pathway databases

    BioCyci EcoCyc:E1P-MONOMER.
    ECOL316407:JW0110-MONOMER.
    MetaCyc:E1P-MONOMER.
    SABIO-RK P0AFG8.

    Miscellaneous databases

    EvolutionaryTracei P0AFG8.
    PROi P0AFG8.

    Gene expression databases

    Genevestigatori P0AFG8.

    Family and domain databases

    Gene3Di 3.40.50.920. 1 hit.
    3.40.50.970. 2 hits.
    InterProi IPR004660. 2-oxoA_DH_E1.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005474. Transketolase_N.
    [Graphical view ]
    Pfami PF00456. Transketolase_N. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000156. Pyruvate_dh_E1. 1 hit.
    SUPFAMi SSF52518. SSF52518. 2 hits.
    SSF52922. SSF52922. 1 hit.
    TIGRFAMsi TIGR00759. aceE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the pyruvate dehydrogenase component."
      Stephens P.E., Darlison M.G., Lewis H.M., Guest J.R.
      Eur. J. Biochem. 133:155-162(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
      Fujita N., Mori H., Yura T., Ishihama A.
      Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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], SEQUENCE REVISION TO 145 AND 275.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within the pdhR gene."
      Haydon D.J., Quail M.A., Guest J.R.
      FEBS Lett. 336:43-47(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
      Strain: K12.
    6. "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.
    7. "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.
    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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-716, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    9. "Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution."
      Arjunan P., Nemeria N., Brunskill A., Chandrasekhar K., Sax M., Yan Y., Jordan F., Guest J.R., Furey W.
      Biochemistry 41:5213-5221(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

    Entry informationi

    Entry nameiODP1_ECOLI
    AccessioniPrimary (citable) accession number: P0AFG8
    Secondary accession number(s): P06958, P78049, Q53382
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 98 of the entry and version 2 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

    External Data

    Dasty 3