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Q2NXE2

- ACSA_XANOM

UniProt

Q2NXE2 - ACSA_XANOM

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (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 sitei310 – 3101Coenzyme AUniRule annotation
    Binding sitei334 – 3341Coenzyme AUniRule annotation
    Binding sitei499 – 4991ATPUniRule annotation
    Binding sitei514 – 5141ATPUniRule annotation
    Binding sitei522 – 5221Coenzyme A; via carbonyl oxygenUniRule annotation
    Binding sitei525 – 5251ATPUniRule annotation
    Metal bindingi536 – 5361Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi541 – 5411Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei583 – 5831Coenzyme AUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi386 – 3883ATPUniRule annotation
    Nucleotide bindingi410 – 4156ATPUniRule 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

    BioCyciXORY342109:GIX9-4339-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:XOO4280
    OrganismiXanthomonas oryzae pv. oryzae (strain MAFF 311018)
    Taxonomic identifieri342109 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    ProteomesiUP000001957: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 647647Acetyl-coenzyme A synthetasePRO_1000085008Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei608 – 6081N6-acetyllysineUniRule annotation

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation

    Interactioni

    Protein-protein interaction databases

    STRINGi342109.XOO_4280.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2NXE2.
    SMRiQ2NXE2. Positions 9-644.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni190 – 1934Coenzyme A bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000128470.
    KOiK01895.
    OMAiRRIFEPT.
    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.

    Q2NXE2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADVYPVDPA FAADARVTRE QYAALYRESI EHPEQFWGKA AQRLEWFKQP    50
    TQVKDVSYAL DDFHIRWFGD GELNASVNCL DRQLATRGDK TALLFEPDSP 100
    DAASYPVTYR QLYERVCKLG NALRNLGVKK GDRVTIYLPM IVDAAVAMLA 150
    CARIGAVHSV VFGGFAANSI ADRVIDCQSK LIITADEGLR GGKKIPLKAN 200
    VDAALKIPGT NTIETVLVVR HTGGAVEMQA PRDRWFHDVV DGQPAECEPE 250
    RMNAEDPLFI LYTSGSTGKP KGVLHTTAGY LLFASYTHEV VFDLREDDIY 300
    WCTADVGWVT GHSYIVYGPL ANGATAVMFE GVPNYPNVSR FWEVIDKHQV 350
    TIFYTAPTAI RALMRDGAEP VKKTSRKSLR LLGSVGEPIN PEAWRWYYDV 400
    VGDSRCPIVD TWWQTETGGI LISPLAGAVD LKPGSATLPF FGVQPALVDA 450
    EGKILEGATE GNLVLLDSWP GQMRSVYGDH QRFIDTYFRT YPGSYFTGDG 500
    CRRDADGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK VAEAAVVGFP 550
    HDVKGQGIYA YVTLIAGETP SDELHKELVS WVRKEIGPIA SPDHLQWAPG 600
    LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVDSL VNERLTR 647
    Length:647
    Mass (Da):71,366
    Last modified:February 7, 2006 - v1
    Checksum:i33558E37802A2523
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008229 Genomic DNA. Translation: BAE71035.1.
    RefSeqiYP_453309.1. NC_007705.1.

    Genome annotation databases

    EnsemblBacteriaiBAE71035; BAE71035; BAE71035.
    GeneIDi3859446.
    KEGGixom:XOO_4280.
    PATRICi24119017. VBIXanOry49434_4911.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008229 Genomic DNA. Translation: BAE71035.1 .
    RefSeqi YP_453309.1. NC_007705.1.

    3D structure databases

    ProteinModelPortali Q2NXE2.
    SMRi Q2NXE2. Positions 9-644.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 342109.XOO_4280.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAE71035 ; BAE71035 ; BAE71035 .
    GeneIDi 3859446.
    KEGGi xom:XOO_4280.
    PATRICi 24119017. VBIXanOry49434_4911.

    Phylogenomic databases

    eggNOGi COG0365.
    HOGENOMi HOG000128470.
    KOi K01895.
    OMAi RRIFEPT.
    OrthoDBi EOG68WR2H.

    Enzyme and pathway databases

    BioCyci XORY342109:GIX9-4339-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. "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity."
      Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.
      Jpn. Agric. Res. Q. 39:275-287(2005)
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MAFF 311018.

    Entry informationi

    Entry nameiACSA_XANOM
    AccessioniPrimary (citable) accession number: Q2NXE2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 58 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3