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

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    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)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001467742 – 319Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaAdd BLAST318

    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

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1319
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi10 – 14Combined sources5
    Turni15 – 20Combined sources6
    Helixi39 – 43Combined sources5
    Helixi44 – 48Combined sources5
    Turni49 – 52Combined sources4
    Helixi53 – 56Combined sources4
    Helixi60 – 67Combined sources8
    Helixi75 – 82Combined sources8
    Beta strandi84 – 88Combined sources5
    Beta strandi93 – 95Combined sources3
    Beta strandi101 – 108Combined sources8
    Beta strandi111 – 118Combined sources8
    Helixi126 – 129Combined sources4
    Helixi131 – 133Combined sources3
    Helixi137 – 152Combined sources16
    Beta strandi157 – 164Combined sources8
    Helixi170 – 174Combined sources5
    Helixi177 – 189Combined sources13
    Beta strandi195 – 204Combined sources10
    Helixi205 – 209Combined sources5
    Beta strandi215 – 219Combined sources5
    Beta strandi224 – 228Combined sources5
    Helixi230 – 237Combined sources8
    Helixi244 – 251Combined sources8
    Helixi255 – 259Combined sources5
    Turni260 – 262Combined sources3
    Helixi275 – 277Combined sources3
    Helixi279 – 293Combined sources15
    Turni294 – 299Combined sources6
    Helixi302 – 315Combined sources14

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP0ABD5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini35 – 296CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST262

    Sequence similaritiesi

    Belongs to the AccA family.UniRule annotation
    Contains 1 CoA carboxyltransferase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

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

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00823. AcetylCoA_CT_alpha. 1 hit.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2F9YX-ray3.20A1-319[»]
    ProteinModelPortaliP0ABD5.
    SMRiP0ABD5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259753. 211 interactors.
    DIPiDIP-35897N.
    IntActiP0ABD5. 31 interactors.
    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.
    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. 1 hit.
    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...

    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: November 2, 2016
    This is version 104 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.