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Q5GU25

- Q5GU25_XANOR

UniProt

Q5GU25 - Q5GU25_XANOR

Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (01 Mar 2005)
      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 sitei359 – 3591Coenzyme AUniRule annotation
    Binding sitei383 – 3831Coenzyme AUniRule annotation
    Binding sitei435 – 4351Substrate; via nitrogen amideUniRule annotation
    Binding sitei548 – 5481SubstrateUniRule annotation
    Binding sitei563 – 5631SubstrateUniRule annotation
    Active sitei565 – 5651UniRule annotation
    Binding sitei571 – 5711Coenzyme AUniRule annotation
    Binding sitei574 – 5741SubstrateUniRule annotation
    Metal bindingi585 – 5851Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi587 – 5871Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi590 – 5901Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei632 – 6321Coenzyme 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 annotation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciXORY291331:GJBV-4197-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:acsImported
    Synonyms:acsAUniRule annotation
    Ordered Locus Names:XOO4544Imported
    OrganismiXanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)Imported
    Taxonomic identifieri291331 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    ProteomesiUP000006735: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei657 – 6571N6-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

    STRINGi291331.XOO4544.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5GU25.
    SMRiQ5GU25. Positions 58-693.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni459 – 4646Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiHPPQKML.
    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.

    Q5GU25-1 [UniParc]FASTAAdd to Basket

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    MCAGALPGGL RPRSKAPLAV GTEWMRHTDC LPREAVTPSS DKFIASEGAM    50
    ADVYPVDPAF AADARVTREQ YAALYRESIE HPEQFWGKAA QRLEWFKQPT 100
    QVKDVSYALD DFHIRWFGDG ELNASVNCLD RQLATRGDKT ALLFEPDSPD 150
    AASYPVTYRQ LYERVCKLGN ALRNLGVKKG DRVTIYLPMI VDAAVAMLAC 200
    ARIGAVHSVV FGGFAANSIA DRVIDCQSKL IITADEGLRG GKKIPLKANV 250
    DAALKIPGTN TIETVLVVRH TGGAVEMQAP RDRWFQDVVD GQPAECEPER 300
    MNAEDPLFIL YTSGSTGKPK GVLHTTAGYL LFASYTHEVV FDLREDDIYW 350
    CTADVGWVTG HSYIVYGPLA NGATAVMFEG VPNYPNVSRF WEVIDKHQVT 400
    IFYTAPTAIR ALMRDGAEPV KKTSRKSLRL LGSVGEPINP EAWRWYYDVV 450
    GDSRCPIVDT WWQTETGGIL ISPLAGAVDL KPGSATLPFF GVQPALVDAE 500
    GKILEGATEG NLVLLDSWPG QMRSVYGDHQ RFIDTYFRTY PGSYFTGDGC 550
    RRDADGYYWI TGRVDDVINV SGHRIGTAEV ESALVSHPKV AEAAVVGFPH 600
    DVKGQGIYAY VTLIAGETPS DELHKELVSW VRKEIGPIAS PDHLQWAPGL 650
    PKTRSGKIMR RILRKIAENA PDQLGDTSTL ADPSVVDSLV NERLTR 696
    Length:696
    Mass (Da):76,479
    Last modified:March 1, 2005 - v1
    Checksum:i79025F1A1D84B06A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013598 Genomic DNA. Translation: AAW77798.1.
    RefSeqiWP_011260815.1. NC_006834.1.
    YP_203183.1. NC_006834.1.

    Genome annotation databases

    EnsemblBacteriaiAAW77798; AAW77798; XOO4544.
    GeneIDi3262868.
    KEGGixoo:XOO4544.
    PATRICi24108869. VBIXanOry111333_5045.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013598 Genomic DNA. Translation: AAW77798.1 .
    RefSeqi WP_011260815.1. NC_006834.1.
    YP_203183.1. NC_006834.1.

    3D structure databases

    ProteinModelPortali Q5GU25.
    SMRi Q5GU25. Positions 58-693.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 291331.XOO4544.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW77798 ; AAW77798 ; XOO4544 .
    GeneIDi 3262868.
    KEGGi xoo:XOO4544.
    PATRICi 24108869. VBIXanOry111333_5045.

    Phylogenomic databases

    HOGENOMi HOG000229981.
    KOi K01895.
    OMAi HPPQKML.
    OrthoDBi EOG68WR2H.

    Enzyme and pathway databases

    BioCyci XORY291331:GJBV-4197-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: KACC10331 / KXO85Imported.

    Entry informationi

    Entry nameiQ5GU25_XANOR
    AccessioniPrimary (citable) accession number: Q5GU25
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 1, 2005
    Last sequence update: March 1, 2005
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3