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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

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. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Controls translation of mRNA for both itself and the alpha-subunit (accA) by binding to a probable hairpin in the 5' of the mRNA. Binding to mRNA inhibits translation; this is partially relieved by acetyl-CoA. Increasing amounts of mRNA also inhibit enzyme activity.

Catalytic activityi

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

Cofactori

Zn2+UniRule annotation1 PublicationNote: Binds 1 zinc ion per subunit. The zinc is involved in both translation regulation via mRNA-binding and catalysis.UniRule annotation1 Publication

Enzyme regulationi

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

Kineticsi

  1. KM=40.0 µM for malonyl-CoA2 Publications
  2. KM=11.4 mM for biocytin2 Publications

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi27 – 271Zinc
    Metal bindingi30 – 301Zinc
    Metal bindingi46 – 461Zinc
    Metal bindingi49 – 491Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri27 – 4923C4-typeCuratedAdd
    BLAST

    GO - Molecular functioni

    • acetyl-CoA carboxylase activity Source: EcoliWiki
    • ATP binding Source: UniProtKB-KW
    • DNA binding Source: EcoCyc
    • mRNA binding Source: EcoCyc
    • zinc ion binding Source: EcoCyc

    GO - Biological processi

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

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Translation regulation

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:CARBOXYL-TRANSFERASE-BETA-MONOMER.
    ECOL316407:JW2313-MONOMER.
    MetaCyc:CARBOXYL-TRANSFERASE-BETA-MONOMER.
    SABIO-RKP0A9Q5.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaUniRule annotation (EC:6.4.1.2UniRule annotation)
    Short name:
    ACCase subunit betaUniRule annotation
    Short name:
    Acetyl-CoA carboxylase carboxyltransferase subunit betaUniRule annotation
    Gene namesi
    Name:accDUniRule annotation
    Synonyms:dedB, usg
    Ordered Locus Names:b2316, JW2313
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10217. accD.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi27 – 271C → A: Vmax decreases 9-fold. 1 Publication
    Mutagenesisi30 – 301C → A: Vmax decreases 140-fold. Loss of nucleic acid-binding. 1 Publication
    Mutagenesisi46 – 461C → A: Vmax decreases 11-fold. 1 Publication
    Mutagenesisi49 – 491C → A: Vmax decreases 8-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 304304Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaPRO_0000199770Add
    BLAST

    Proteomic databases

    EPDiP0A9Q5.
    PaxDbiP0A9Q5.
    PRIDEiP0A9Q5.

    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
    accAP0ABD514EBI-542064,EBI-542031

    Protein-protein interaction databases

    BioGridi4261361. 233 interactions.
    DIPiDIP-35878N.
    IntActiP0A9Q5. 28 interactions.
    MINTiMINT-1234646.
    STRINGi511145.b2316.

    Structurei

    Secondary structure

    1
    304
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni28 – 303Combined sources
    Turni36 – 449Combined sources
    Turni47 – 493Combined sources
    Helixi57 – 648Combined sources
    Helixi88 – 903Combined sources
    Beta strandi105 – 1128Combined sources
    Beta strandi121 – 1255Combined sources
    Turni130 – 1323Combined sources
    Helixi137 – 15216Combined sources
    Beta strandi156 – 16510Combined sources
    Helixi167 – 1704Combined sources
    Helixi171 – 18919Combined sources
    Beta strandi194 – 20310Combined sources
    Helixi204 – 2074Combined sources
    Helixi210 – 2123Combined sources
    Beta strandi215 – 2195Combined sources
    Beta strandi224 – 2285Combined sources
    Helixi230 – 2378Combined sources
    Turni243 – 2464Combined sources
    Helixi248 – 2514Combined sources
    Helixi252 – 2543Combined sources
    Beta strandi258 – 2603Combined sources
    Helixi263 – 27715Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F9YX-ray3.20B1-304[»]
    ProteinModelPortaliP0A9Q5.
    SMRiP0A9Q5. Positions 23-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9Q5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AccD/PCCB family.UniRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri27 – 4923C4-typeCuratedAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiENOG4108IDZ. Bacteria.
    COG0777. LUCA.
    HOGENOMiHOG000021670.
    InParanoidiP0A9Q5.
    KOiK01963.
    OMAiPEGLWIK.
    PhylomeDBiP0A9Q5.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_01395. AcetylCoA_CT_beta. 1 hit.
    InterProiIPR000438. Acetyl_CoA_COase_Trfase_b_su.
    IPR000022. Carboxyl_trans.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011762. COA_CT_N.
    [Graphical view]
    PfamiPF01039. Carboxyl_trans. 1 hit.
    [Graphical view]
    PRINTSiPR01070. ACCCTRFRASEB.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00515. accD. 1 hit.
    PROSITEiPS50980. COA_CT_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A9Q5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSWIERIKSN ITPTRKASIP EGVWTKCDSC GQVLYRAELE RNLEVCPKCD
    60 70 80 90 100
    HHMRMTARNR LHSLLDEGSL VELGSELEPK DVLKFRDSKK YKDRLASAQK
    110 120 130 140 150
    ETGEKDALVV MKGTLYGMPV VAAAFEFAFM GGSMGSVVGA RFVRAVEQAL
    160 170 180 190 200
    EDNCPLICFS ASGGARMQEA LMSLMQMAKT SAALAKMQER GLPYISVLTD
    210 220 230 240 250
    PTMGGVSASF AMLGDLNIAE PKALIGFAGP RVIEQTVREK LPPGFQRSEF
    260 270 280 290 300
    LIEKGAIDMI VRRPEMRLKL ASILAKLMNL PAPNPEAPRE GVVVPPVPDQ

    EPEA
    Length:304
    Mass (Da):33,322
    Last modified:July 19, 2005 - v1
    Checksum:i401FEC94D728F3CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 772EL → SV in AAA23965 (PubMed:3040734).Curated
    Sequence conflicti225 – 23915IGFAG…QTVRE → MALPVRVLSNRPFAK in AAA23807 (PubMed:3040739).CuratedAdd
    BLAST
    Sequence conflicti225 – 23915IGFAG…QTVRE → MALPVRVLSNRPFAK in AAA23801 (PubMed:3040739).CuratedAdd
    BLAST
    Sequence conflicti226 – 23510GFAGPRVIEQ → ALPVRVLSNR in AAA23965 (PubMed:3040734).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M32445 Genomic DNA. Translation: AAA23807.1.
    J02808 Genomic DNA. Translation: AAA23801.1.
    M68934 Genomic DNA. Translation: AAA23965.1.
    U00096 Genomic DNA. Translation: AAC75376.1.
    AP009048 Genomic DNA. Translation: BAA16173.1.
    S53037 mRNA. Translation: AAB24894.2.
    PIRiB65004. XMECBD.
    RefSeqiNP_416819.1. NC_000913.3.
    WP_000118404.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75376; AAC75376; b2316.
    BAA16173; BAA16173; BAA16173.
    GeneIDi946796.
    KEGGiecj:JW2313.
    eco:b2316.
    PATRICi32120003. VBIEscCol129921_2411.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M32445 Genomic DNA. Translation: AAA23807.1.
    J02808 Genomic DNA. Translation: AAA23801.1.
    M68934 Genomic DNA. Translation: AAA23965.1.
    U00096 Genomic DNA. Translation: AAC75376.1.
    AP009048 Genomic DNA. Translation: BAA16173.1.
    S53037 mRNA. Translation: AAB24894.2.
    PIRiB65004. XMECBD.
    RefSeqiNP_416819.1. NC_000913.3.
    WP_000118404.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F9YX-ray3.20B1-304[»]
    ProteinModelPortaliP0A9Q5.
    SMRiP0A9Q5. Positions 23-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261361. 233 interactions.
    DIPiDIP-35878N.
    IntActiP0A9Q5. 28 interactions.
    MINTiMINT-1234646.
    STRINGi511145.b2316.

    Proteomic databases

    EPDiP0A9Q5.
    PaxDbiP0A9Q5.
    PRIDEiP0A9Q5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75376; AAC75376; b2316.
    BAA16173; BAA16173; BAA16173.
    GeneIDi946796.
    KEGGiecj:JW2313.
    eco:b2316.
    PATRICi32120003. VBIEscCol129921_2411.

    Organism-specific databases

    EchoBASEiEB0213.
    EcoGeneiEG10217. accD.

    Phylogenomic databases

    eggNOGiENOG4108IDZ. Bacteria.
    COG0777. LUCA.
    HOGENOMiHOG000021670.
    InParanoidiP0A9Q5.
    KOiK01963.
    OMAiPEGLWIK.
    PhylomeDBiP0A9Q5.

    Enzyme and pathway databases

    UniPathwayiUPA00655; UER00711.
    BioCyciEcoCyc:CARBOXYL-TRANSFERASE-BETA-MONOMER.
    ECOL316407:JW2313-MONOMER.
    MetaCyc:CARBOXYL-TRANSFERASE-BETA-MONOMER.
    SABIO-RKP0A9Q5.

    Miscellaneous databases

    EvolutionaryTraceiP0A9Q5.
    PROiP0A9Q5.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_01395. AcetylCoA_CT_beta. 1 hit.
    InterProiIPR000438. Acetyl_CoA_COase_Trfase_b_su.
    IPR000022. Carboxyl_trans.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011762. COA_CT_N.
    [Graphical view]
    PfamiPF01039. Carboxyl_trans. 1 hit.
    [Graphical view]
    PRINTSiPR01070. ACCCTRFRASEB.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00515. accD. 1 hit.
    PROSITEiPS50980. COA_CT_NTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiACCD_ECOLI
    AccessioniPrimary (citable) accession number: P0A9Q5
    Secondary accession number(s): P08193, P76937, P78251
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 19, 2005
    Last modified: September 7, 2016
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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.