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Q2YLH5

- ACSA_BRUA2

UniProt

Q2YLH5 - ACSA_BRUA2

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Brucella abortus (strain 2308)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (07 Feb 2006)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.UniRule annotation

    Catalytic activityi

    ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

    Cofactori

    Magnesium.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei311 – 3111Coenzyme AUniRule annotation
    Binding sitei335 – 3351Coenzyme AUniRule annotation
    Binding sitei500 – 5001ATPUniRule annotation
    Binding sitei515 – 5151ATPUniRule annotation
    Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
    Binding sitei526 – 5261ATPUniRule annotation
    Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei586 – 5861Coenzyme A

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi387 – 3893ATPUniRule annotation
    Nucleotide bindingi411 – 4166ATPUniRule annotation

    GO - Molecular functioni

    1. acetate-CoA ligase activity Source: UniProtKB-HAMAP
    2. AMP binding Source: InterPro
    3. ATP binding Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from acetate Source: InterPro

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBABO359391:GKDV-1863-MONOMER.
    BMEL359391:GJOQ-1863-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
    Short name:
    AcCoA synthetaseUniRule annotation
    Short name:
    AcsUniRule annotation
    Alternative name(s):
    Acetate--CoA ligaseUniRule annotation
    Acyl-activating enzymeUniRule annotation
    Gene namesi
    Name:acsAUniRule annotation
    Ordered Locus Names:BAB1_1819
    OrganismiBrucella abortus (strain 2308)
    Taxonomic identifieri359391 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000002719: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 651651Acetyl-coenzyme A synthetasePRO_1000065274Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei611 – 6111N6-acetyllysineUniRule annotation

    Post-translational modificationi

    Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.UniRule annotation

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ2YLH5.

    Interactioni

    Protein-protein interaction databases

    STRINGi359391.BAB1_1819.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2YLH5.
    SMRiQ2YLH5. Positions 17-648.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni189 – 1924Coenzyme A bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiAWIWYRD.
    OrthoDBiEOG68WR2H.

    Family and domain databases

    HAMAPiMF_01123. Ac_CoA_synth.
    InterProiIPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2YLH5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEKLYPVLP EAKKNTLIDN ETYLEWYEES VSDPDGFWAK HGRRIDWFKP    50
    FTKVKNTDFN GDVTIKWYED GVTNVSYNCI DRHLKSRGDK VAIIWEGDNP 100
    YIDKKITYRE LYENVCRMAN VLKKHGVKKG DRVTIYLPMI PEAAYAMLAC 150
    ARIGAVHSVV FAGFSPEALA GRIVDCESTF VITADEGVRG GKPVALKENT 200
    DTAIDIAAKQ YVMVNKVLVV RRTGGKVSWG RGRDLWYHQE VASVEPHCEP 250
    EPMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHQ YVFDYHDGEI 300
    YWCTADVGWV TGHSYIVYGP LANGATTLMF EGVPNFPDQG RFWEVVDKHH 350
    VNIFYTAPTA LRALMGAGDE FVTRSSRSTL RLLGSVGEPI NPEAWEWYYN 400
    VVGDQKCPIV DTWWQTENGG ILITPLPGAT DLKPGSATRP FFGVKPVLVD 450
    NEGNVQEGVA DGNLCISDSW PGQMRTVYGD HKRFIETYFS TYKGMYFSGD 500
    GCRRDEDGYY WITGRVDDVL NISGHRLGTA EIESALVSHH SVSEAAVVGY 550
    PHPIKGQGIY CYVTLMTGAD AQDPDELRKE LVQHVRKEIG PIATPDKIQF 600
    APGLPKTRSG KIMRRILRKI AEDEFGALGD TSTLADPGVV DDLIENRQNK 650
    K 651
    Length:651
    Mass (Da):72,731
    Last modified:February 7, 2006 - v1
    Checksum:i7FB222A3EE6476CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM040264 Genomic DNA. Translation: CAJ11775.1.
    RefSeqiYP_415165.1. NC_007618.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ11775; CAJ11775; BAB1_1819.
    GeneIDi3788319.
    KEGGibmf:BAB1_1819.
    PATRICi17846672. VBIBruMel86222_1885.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM040264 Genomic DNA. Translation: CAJ11775.1 .
    RefSeqi YP_415165.1. NC_007618.1.

    3D structure databases

    ProteinModelPortali Q2YLH5.
    SMRi Q2YLH5. Positions 17-648.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 359391.BAB1_1819.

    Proteomic databases

    PRIDEi Q2YLH5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ11775 ; CAJ11775 ; BAB1_1819 .
    GeneIDi 3788319.
    KEGGi bmf:BAB1_1819.
    PATRICi 17846672. VBIBruMel86222_1885.

    Phylogenomic databases

    eggNOGi COG0365.
    HOGENOMi HOG000229981.
    KOi K01895.
    OMAi AWIWYRD.
    OrthoDBi EOG68WR2H.

    Enzyme and pathway databases

    BioCyci BABO359391:GKDV-1863-MONOMER.
    BMEL359391:GJOQ-1863-MONOMER.

    Family and domain databases

    HAMAPi MF_01123. Ac_CoA_synth.
    InterProi IPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 2308.

    Entry informationi

    Entry nameiACSA_BRUA2
    AccessioniPrimary (citable) accession number: Q2YLH5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 52 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, Reference proteome

    Documents

    1. Brucella abortus strain 2308
      Brucella abortus (strain 2308): entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3