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G7UST0

- G7UST0_PSEUP

UniProt

G7UST0 - G7UST0_PSEUP

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pseudoxanthomonas spadix (strain BD-a59)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 16 (01 Oct 2014)
      Sequence version 1 (25 Jan 2012)
      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 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 annotation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciPSPA1045855:GH5V-3138-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:DSC_00690Imported
    OrganismiPseudoxanthomonas spadix (strain BD-a59)Imported
    Taxonomic identifieri1045855 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaePseudoxanthomonas
    ProteomesiUP000005870: 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

    Structurei

    3D structure databases

    ProteinModelPortaliG7UST0.
    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

    KOiK01895.

    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.

    G7UST0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDLYPVDPA FARQARVDAA TYARDYKASI EQPEAFWKQV AQRLDWIKAP    50
    TRIKDVSFDV DDFHIQWFAD GELNASVNCL DRQLEARGDK IALLFEPDSP 100
    DSESYGVTYR QLHARVCRLA NALRSLGVAK GDRVTIYLPM IPDAAVAMLA 150
    CARIGAVHSV VFGGFAPNSI ADRVADCASK LIITADEGLR GSRKIPLKAN 200
    VDAALKLPGT SSVETVLVVR HTGGPVDMQA PRDRWFHDVV DSQPDTCEPE 250
    RMNAEDPLFI LYTSGSTGKP KGVLHTTGGY LLWAAYTHEL VFDLKEDDIY 300
    WCTADVGWVT GHSYIVYGPL ANGATSLVFE GVPSYPDNSR FWQVVDKHRV 350
    SLFYTAPTAI RALMREGDGP VRKTSRKTLR VLGTVGEPIN PEAWRWYYEV 400
    VGDSRCPIVD TWWQTETGGH MITPLPGATA LKPGSATVPF FGVQPAVVDA 450
    NGVELEGQAE GNLVIKDSWP GQMRTVYGDH QRFIDTYFRT YPGTYFTGDG 500
    CRRDADGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK VAEAAVVGFP 550
    HDLKGQGIYA YVTLVAGEQP TEELRKELIA HVRKEIGPIA SPDHLQWAPG 600
    LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVDSL VSERKVR 647
    Length:647
    Mass (Da):71,329
    Last modified:January 25, 2012 - v1
    Checksum:i07780B2B3F86F15E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003093 Genomic DNA. Translation: AER54791.1.
    RefSeqiWP_014162112.1. NC_016147.2.
    YP_004928832.1. NC_016147.2.

    Genome annotation databases

    EnsemblBacteriaiAER54791; AER54791; DSC_00690.
    GeneIDi11374541.
    KEGGipsd:DSC_00690.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003093 Genomic DNA. Translation: AER54791.1 .
    RefSeqi WP_014162112.1. NC_016147.2.
    YP_004928832.1. NC_016147.2.

    3D structure databases

    ProteinModelPortali G7UST0.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AER54791 ; AER54791 ; DSC_00690 .
    GeneIDi 11374541.
    KEGGi psd:DSC_00690.

    Phylogenomic databases

    KOi K01895.

    Enzyme and pathway databases

    BioCyci PSPA1045855:GH5V-3138-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. "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas spadix BD-a59."
      Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.
      J. Bacteriol. 194:544-544(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: BD-a59Imported.

    Entry informationi

    Entry nameiG7UST0_PSEUP
    AccessioniPrimary (citable) accession number: G7UST0
    Entry historyi
    Integrated into UniProtKB/TrEMBL: January 25, 2012
    Last sequence update: January 25, 2012
    Last modified: October 1, 2014
    This is version 16 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