Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8FXY7

- ACCD_BRUSU

UniProt

Q8FXY7 - ACCD_BRUSU

Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Brucella suis biovar 1 (strain 1330)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.UniRule annotation

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

    1. acetyl-CoA carboxylase activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-HAMAP
    2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway

    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

    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
    Ordered Locus Names:BR2107, BS1330_I2101
    OrganismiBrucella suis biovar 1 (strain 1330)
    Taxonomic identifieri204722 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000000824: Chromosome I, UP000007104: Chromosome I

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. acetyl-CoA carboxylase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 301301Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaPRO_0000389707Add
    BLAST

    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).UniRule annotation

    Protein-protein interaction databases

    STRINGi204722.BR2107.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8FXY7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AccD/PCCB family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0777.
    HOGENOMiHOG000021670.
    KOiK01963.
    OMAiYISVMTD.
    OrthoDBiEOG6HQSSF.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_01395. AcetylCoA_CT_beta.
    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.

    Q8FXY7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNWITNYVRP KINSMLGRRE MPENLWIKDP STGEMVFHKD LESNQFVIPS    50
    SGHHMRIKAK DRLRFFFDNG EYTTLEAPKV PLDPLKFRDE KKYIDRLKDY 100
    RSRTGMDDAI VNGLGTIEGL PIVATVQDFS FMGGSLGMGA GEAIIQGFEK 150
    AIELKRPLVL FASSGGARMQ EGILSLMQLP RTTVAVEMLK EAGLPYIVVL 200
    TNPTTGGVTA SYAMLGDIHI AEPGALIGFA GPRVIEQTIR EKLPEGFQSS 250
    EYLMEHGMVD MVVSRLELKA TIARLLKIMT KQPANSDAPA PQKPDADSKA 300
    A 301
    Length:301
    Mass (Da):33,270
    Last modified:March 1, 2003 - v1
    Checksum:iBCB69B33AEA8D566
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014291 Genomic DNA. Translation: AAN30997.1.
    CP002997 Genomic DNA. Translation: AEM19414.1.
    PIRiAF3504.
    RefSeqiNP_699082.1. NC_004310.3.
    YP_005616906.1. NC_017251.1.

    Genome annotation databases

    EnsemblBacteriaiAAN30997; AAN30997; BR2107.
    AEM19414; AEM19414; BS1330_I2101.
    GeneIDi1167810.
    12137890.
    KEGGibms:BR2107.
    bsi:BS1330_I2101.
    PATRICi17792647. VBIBruSui107850_2144.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014291 Genomic DNA. Translation: AAN30997.1 .
    CP002997 Genomic DNA. Translation: AEM19414.1 .
    PIRi AF3504.
    RefSeqi NP_699082.1. NC_004310.3.
    YP_005616906.1. NC_017251.1.

    3D structure databases

    ProteinModelPortali Q8FXY7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 204722.BR2107.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN30997 ; AAN30997 ; BR2107 .
    AEM19414 ; AEM19414 ; BS1330_I2101 .
    GeneIDi 1167810.
    12137890.
    KEGGi bms:BR2107.
    bsi:BS1330_I2101.
    PATRICi 17792647. VBIBruSui107850_2144.

    Phylogenomic databases

    eggNOGi COG0777.
    HOGENOMi HOG000021670.
    KOi K01963.
    OMAi YISVMTD.
    OrthoDBi EOG6HQSSF.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .

    Family and domain databases

    Gene3Di 3.90.226.10. 1 hit.
    HAMAPi MF_01395. AcetylCoA_CT_beta.
    InterProi IPR000438. Acetyl_CoA_COase_Trfase_b_su.
    IPR000022. Carboxyl_trans.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011762. COA_CT_N.
    [Graphical view ]
    Pfami PF01039. Carboxyl_trans. 1 hit.
    [Graphical view ]
    PRINTSi PR01070. ACCCTRFRASEB.
    SUPFAMi SSF52096. SSF52096. 1 hit.
    TIGRFAMsi TIGR00515. accD. 1 hit.
    PROSITEi PS50980. COA_CT_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1330.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1330.

    Entry informationi

    Entry nameiACCD_BRUSU
    AccessioniPrimary (citable) accession number: Q8FXY7
    Secondary accession number(s): G0K955
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 67 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

    Complete proteome

    Documents

    1. Brucella suis
      Brucella suis (strain 1330): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3