Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

Gene

accA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.UniRule annotation1 Publication

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.UniRule annotation1 Publication

Enzyme regulationi

Competitively inhibited by pyrrolidine dione antibiotic moiramide B (CPD1).1 Publication

Kineticsi

  1. KM=100 µM for malonyl-CoA1 Publication
  2. KM=10 mM for biocytin1 Publication

    Pathwayi: malonyl-CoA biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA), Biotin carboxylase (accC), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD)
    This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

    GO - Molecular functioni

    • acetyl-CoA carboxylase activity Source: UniProtKB-HAMAP
    • ATP binding Source: UniProtKB-KW
    • identical protein binding Source: IntAct

    GO - Biological processi

    • fatty acid biosynthetic process Source: EcoCyc
    • long-chain fatty acid biosynthetic process Source: EcoliWiki
    • malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:CARBOXYL-TRANSFERASE-ALPHA-MONOMER.
    ECOL316407:JW0180-MONOMER.
    MetaCyc:CARBOXYL-TRANSFERASE-ALPHA-MONOMER.
    SABIO-RKP0ABD5.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaUniRule annotation (EC:6.4.1.2UniRule annotation)
    Short name:
    ACCase subunit alphaUniRule annotation
    Short name:
    Acetyl-CoA carboxylase carboxyltransferase subunit alphaUniRule annotation
    Gene namesi
    Name:accAUniRule annotation
    Ordered Locus Names:b0185, JW0180
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11647. accA.

    Subcellular locationi

    GO - Cellular componenti

    • acetate CoA-transferase complex Source: EcoCyc
    • cytoplasm Source: EcoliWiki
    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 319318Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaPRO_0000146774Add
    BLAST

    Proteomic databases

    EPDiP0ABD5.
    PaxDbiP0ABD5.
    PRIDEiP0ABD5.

    Interactioni

    Subunit structurei

    Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-542031,EBI-542031
    accDP0A9Q514EBI-542031,EBI-542064

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi4259753. 211 interactions.
    DIPiDIP-35897N.
    IntActiP0ABD5. 31 interactions.
    MINTiMINT-1228651.
    STRINGi511145.b0185.

    Structurei

    Secondary structure

    1
    319
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 145Combined sources
    Turni15 – 206Combined sources
    Helixi39 – 435Combined sources
    Helixi44 – 485Combined sources
    Turni49 – 524Combined sources
    Helixi53 – 564Combined sources
    Helixi60 – 678Combined sources
    Helixi75 – 828Combined sources
    Beta strandi84 – 885Combined sources
    Beta strandi93 – 953Combined sources
    Beta strandi101 – 1088Combined sources
    Beta strandi111 – 1188Combined sources
    Helixi126 – 1294Combined sources
    Helixi131 – 1333Combined sources
    Helixi137 – 15216Combined sources
    Beta strandi157 – 1648Combined sources
    Helixi170 – 1745Combined sources
    Helixi177 – 18913Combined sources
    Beta strandi195 – 20410Combined sources
    Helixi205 – 2095Combined sources
    Beta strandi215 – 2195Combined sources
    Beta strandi224 – 2285Combined sources
    Helixi230 – 2378Combined sources
    Helixi244 – 2518Combined sources
    Helixi255 – 2595Combined sources
    Turni260 – 2623Combined sources
    Helixi275 – 2773Combined sources
    Helixi279 – 29315Combined sources
    Turni294 – 2996Combined sources
    Helixi302 – 31514Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F9YX-ray3.20A1-319[»]
    ProteinModelPortaliP0ABD5.
    SMRiP0ABD5. Positions 4-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ABD5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AccA family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4107QM9. Bacteria.
    COG0825. LUCA.
    HOGENOMiHOG000273832.
    InParanoidiP0ABD5.
    KOiK01962.
    OMAiHSVYTVA.
    OrthoDBiEOG6HQSSF.
    PhylomeDBiP0ABD5.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00823. AcetylCoA_CT_alpha.
    InterProiIPR001095. Acetyl_CoA_COase_a_su.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    [Graphical view]
    PfamiPF03255. ACCA. 1 hit.
    [Graphical view]
    PRINTSiPR01069. ACCCTRFRASEA.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00513. accA. 1 hit.
    PROSITEiPS50989. COA_CT_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0ABD5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSLNFLDFEQ PIAELEAKID SLTAVSRQDE KLDINIDEEV HRLREKSVEL
    60 70 80 90 100
    TRKIFADLGA WQIAQLARHP QRPYTLDYVR LAFDEFDELA GDRAYADDKA
    110 120 130 140 150
    IVGGIARLDG RPVMIIGHQK GRETKEKIRR NFGMPAPEGY RKALRLMQMA
    160 170 180 190 200
    ERFKMPIITF IDTPGAYPGV GAEERGQSEA IARNLREMSR LGVPVVCTVI
    210 220 230 240 250
    GEGGSGGALA IGVGDKVNML QYSTYSVISP EGCASILWKS ADKAPLAAEA
    260 270 280 290 300
    MGIIAPRLKE LKLIDSIIPE PLGGAHRNPE AMAASLKAQL LADLADLDVL
    310
    STEDLKNRRY QRLMSYGYA
    Length:319
    Mass (Da):35,242
    Last modified:January 23, 2007 - v2
    Checksum:iA810DE891CEA2B4F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M96394 Genomic DNA. Translation: AAA70370.1.
    D49445 Genomic DNA. Translation: BAA08425.1.
    U70214 Genomic DNA. Translation: AAB08614.1.
    U00096 Genomic DNA. Translation: AAC73296.1.
    AP009048 Genomic DNA. Translation: BAA77860.2.
    D87518 Genomic DNA. Translation: BAA21655.1.
    M19334 Genomic DNA. No translation available.
    PIRiA43452.
    RefSeqiNP_414727.1. NC_000913.3.
    WP_000055741.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73296; AAC73296; b0185.
    BAA77860; BAA77860; BAA77860.
    GeneIDi944895.
    KEGGiecj:JW0180.
    eco:b0185.
    PATRICi32115481. VBIEscCol129921_0192.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M96394 Genomic DNA. Translation: AAA70370.1.
    D49445 Genomic DNA. Translation: BAA08425.1.
    U70214 Genomic DNA. Translation: AAB08614.1.
    U00096 Genomic DNA. Translation: AAC73296.1.
    AP009048 Genomic DNA. Translation: BAA77860.2.
    D87518 Genomic DNA. Translation: BAA21655.1.
    M19334 Genomic DNA. No translation available.
    PIRiA43452.
    RefSeqiNP_414727.1. NC_000913.3.
    WP_000055741.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F9YX-ray3.20A1-319[»]
    ProteinModelPortaliP0ABD5.
    SMRiP0ABD5. Positions 4-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259753. 211 interactions.
    DIPiDIP-35897N.
    IntActiP0ABD5. 31 interactions.
    MINTiMINT-1228651.
    STRINGi511145.b0185.

    Proteomic databases

    EPDiP0ABD5.
    PaxDbiP0ABD5.
    PRIDEiP0ABD5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73296; AAC73296; b0185.
    BAA77860; BAA77860; BAA77860.
    GeneIDi944895.
    KEGGiecj:JW0180.
    eco:b0185.
    PATRICi32115481. VBIEscCol129921_0192.

    Organism-specific databases

    EchoBASEiEB1600.
    EcoGeneiEG11647. accA.

    Phylogenomic databases

    eggNOGiENOG4107QM9. Bacteria.
    COG0825. LUCA.
    HOGENOMiHOG000273832.
    InParanoidiP0ABD5.
    KOiK01962.
    OMAiHSVYTVA.
    OrthoDBiEOG6HQSSF.
    PhylomeDBiP0ABD5.

    Enzyme and pathway databases

    UniPathwayiUPA00655; UER00711.
    BioCyciEcoCyc:CARBOXYL-TRANSFERASE-ALPHA-MONOMER.
    ECOL316407:JW0180-MONOMER.
    MetaCyc:CARBOXYL-TRANSFERASE-ALPHA-MONOMER.
    SABIO-RKP0ABD5.

    Miscellaneous databases

    EvolutionaryTraceiP0ABD5.
    PROiP0ABD5.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00823. AcetylCoA_CT_alpha.
    InterProiIPR001095. Acetyl_CoA_COase_a_su.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    [Graphical view]
    PfamiPF03255. ACCA. 1 hit.
    [Graphical view]
    PRINTSiPR01069. ACCCTRFRASEA.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00513. accA. 1 hit.
    PROSITEiPS50989. COA_CT_CTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase."
      Li S.-J., Cronan J.E. Jr.
      J. Biol. Chem. 267:16841-16847(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. "The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme."
      Yamamoto Y., Miwa Y., Miyoshi K., Furuyama J., Ohmori H.
      Genes Genet. Syst. 72:167-172(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
      Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "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 24.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Characterization of a second lysine decarboxylase isolated from Escherichia coli."
      Kikuchi Y., Kojima H., Tanaka T., Takatsuka Y., Kamio Y.
      J. Bacteriol. 179:4486-4492(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-319.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Sequence analysis of the Escherichia coli dnaE gene."
      Tomasiewicz H.G., McHenry C.S.
      J. Bacteriol. 169:5735-5744(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
    9. "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.
    10. "Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity."
      Freiberg C., Brunner N.A., Schiffer G., Lampe T., Pohlmann J., Brands M., Raabe M., Haebich D., Ziegelbauer K.
      J. Biol. Chem. 279:26066-26073(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    11. "The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme."
      Bilder P., Lightle S., Bainbridge G., Ohren J., Finzel B., Sun F., Holley S., Al-Kassim L., Spessard C., Melnick M., Newcomer M., Waldrop G.L.
      Biochemistry 45:1712-1722(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).

    Entry informationi

    Entry nameiACCA_ECOLI
    AccessioniPrimary (citable) accession number: P0ABD5
    Secondary accession number(s): P30867
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: January 23, 2007
    Last modified: March 16, 2016
    This is version 101 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.