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K0CWU1

- K0CWU1_ALTME

UniProt

K0CWU1 - K0CWU1_ALTME

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Alteromonas macleodii (strain English Channel 673)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 11 (01 Oct 2014)
      Sequence version 1 (28 Nov 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 sitei311 – 3111Coenzyme AUniRule annotation
    Binding sitei387 – 3871Substrate; via nitrogen amideUniRule annotation
    Binding sitei500 – 5001SubstrateUniRule annotation
    Binding sitei515 – 5151SubstrateUniRule annotation
    Active sitei517 – 5171UniRule annotation
    Binding sitei523 – 5231Coenzyme AUniRule annotation
    Binding sitei526 – 5261SubstrateUniRule annotation
    Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei584 – 5841Coenzyme 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

    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:AMEC673_16675Imported
    OrganismiAlteromonas macleodii (strain English Channel 673)Imported
    Taxonomic identifieri1004788 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas
    ProteomesiUP000006296: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei609 – 6091N6-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

    ProteinModelPortaliK0CWU1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni191 – 1944Coenzyme AUniRule annotation
    Regioni411 – 4166Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01895.
    OMAiDISWING.

    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.

    K0CWU1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTASKTYPVP ENILQSTHLT ASQYDEMYKQ SVEQPEAFWA EHASMLEWYQ    50
    KPTKIKNTMF GENDVSIKWF EDGELNASYN CIDRHLADNA TKVAFHWEGD 100
    SPEDSQDITY QQVHYEVCKL ANALKEMGVA KGDRVAIYMP MVPEAAYAML 150
    ACARIGAVHS VIFGGFSPNA IADRINDSNA KVVITADEGR RAGRSIPLKA 200
    NVDKALAGDA CPSITHVLVH KLTGGDVDWN AKHDVWWHDA VDGVSAQCEP 250
    EVMNAEDPLF ILYTSGSTGT PKGVVHTTGG YLLYSAMTFK YAFDYKEDDV 300
    YWCTADVGWI TGHSYMVYGP MVNAASQVFF EGVPTYPDVK RIAQVVEKYK 350
    VNSLYTAPTA IRALMAHGDV PTEGCDVSSL RLLGTVGEPI NPEAWEWYHR 400
    VIGMSRCPII DTWWQTETGG HMILPLPGAT ELKPGSATRP FFGIQPALFD 450
    ADGNELEGAA EGNLVIKDSW PSQARTVYGD HQRFINTYFS AYKGVYFTGD 500
    GARCDEDGFY WITGRVDDVL NVSGHRLGTA EIESALVAHP KVAEAAVVGF 550
    PHDIKGQGIY VYVTPNEGVE ANEALTKELK AWVRQELSPI ATPDMIQWSR 600
    GLPKTRSGKI MRRILRKIAA NEHEQLGDTS TLADPSVVDT LIEERLNK 648
    Length:648
    Mass (Da):71,668
    Last modified:November 28, 2012 - v1
    Checksum:iB044EA01F57280B0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003844 Genomic DNA. Translation: AFT76017.1.
    RefSeqiYP_006800394.1. NC_018678.1.

    Genome annotation databases

    EnsemblBacteriaiAFT76017; AFT76017; AMEC673_16675.
    GeneIDi13741805.
    KEGGiamg:AMEC673_16675.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003844 Genomic DNA. Translation: AFT76017.1 .
    RefSeqi YP_006800394.1. NC_018678.1.

    3D structure databases

    ProteinModelPortali K0CWU1.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AFT76017 ; AFT76017 ; AMEC673_16675 .
    GeneIDi 13741805.
    KEGGi amg:AMEC673_16675.

    Phylogenomic databases

    KOi K01895.
    OMAi DISWING.

    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. "Genomes of surface isolates of Alteromonas macleodii: the life of a widespread marine opportunistic copiotroph."
      Lopez-Perez M., Gonzaga A., Martin-Cuadrado A.B., Onyshchenko O., Ghavidel A., Ghai R., Rodriguez-Valera F.
      Sci. Rep. 2:696-696(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: English Channel 673Imported.

    Entry informationi

    Entry nameiK0CWU1_ALTME
    AccessioniPrimary (citable) accession number: K0CWU1
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 28, 2012
    Last sequence update: November 28, 2012
    Last modified: October 1, 2014
    This is version 11 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