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B2SU07

- B2SU07_XANOP

UniProt

B2SU07 - B2SU07_XANOP

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Xanthomonas oryzae pv. oryzae (strain PXO99A)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (01 Jul 2008)
      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 annotationSAAS annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei310 – 3101Coenzyme AUniRule annotation
    Binding sitei334 – 3341Coenzyme AUniRule annotation
    Binding sitei386 – 3861Substrate; via nitrogen amideUniRule annotation
    Binding sitei499 – 4991SubstrateUniRule annotation
    Binding sitei514 – 5141SubstrateUniRule annotation
    Active sitei516 – 5161UniRule annotation
    Binding sitei522 – 5221Coenzyme AUniRule annotation
    Binding sitei525 – 5251SubstrateUniRule 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

    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

    LigaseUniRule annotationImported

    Keywords - Ligandi

    ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciXORY360094:GI45-5032-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 annotationImported
    Ordered Locus Names:PXO_03257Imported
    OrganismiXanthomonas oryzae pv. oryzae (strain PXO99A)Imported
    Taxonomic identifieri360094 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    ProteomesiUP000001740: Chromosome

    PTM / Processingi

    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

    AcetylationUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi360094.PXO_03257.

    Structurei

    3D structure databases

    ProteinModelPortaliB2SU07.
    SMRiB2SU07. Positions 9-644.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni410 – 4156Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiTGSEVPW.
    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.

    B2SU07-1 [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:July 1, 2008 - v1
    Checksum:i33558E37802A2523
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000967 Genomic DNA. Translation: ACD61559.1.
    RefSeqiYP_001916091.1. NC_010717.1.

    Genome annotation databases

    EnsemblBacteriaiACD61559; ACD61559; PXO_03257.
    GeneIDi6308552.
    KEGGixop:PXO_03257.
    PATRICi24129651. VBIXanOry73153_5152.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000967 Genomic DNA. Translation: ACD61559.1 .
    RefSeqi YP_001916091.1. NC_010717.1.

    3D structure databases

    ProteinModelPortali B2SU07.
    SMRi B2SU07. Positions 9-644.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 360094.PXO_03257.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACD61559 ; ACD61559 ; PXO_03257 .
    GeneIDi 6308552.
    KEGGi xop:PXO_03257.
    PATRICi 24129651. VBIXanOry73153_5152.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci XORY360094:GI45-5032-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: PXO99AImported.

    Entry informationi

    Entry nameiB2SU07_XANOP
    AccessioniPrimary (citable) accession number: B2SU07
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 1, 2008
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 47 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3