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A8G3Y5

- A8G3Y5_PROM2

UniProt

A8G3Y5 - A8G3Y5_PROM2

Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Prochlorococcus marinus (strain MIT 9215)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (13 Nov 2007)
      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 sitei322 – 3221Coenzyme AUniRule annotation
    Binding sitei398 – 3981Substrate; via nitrogen amideUniRule annotation
    Binding sitei516 – 5161SubstrateUniRule annotation
    Binding sitei531 – 5311SubstrateUniRule annotation
    Active sitei533 – 5331UniRule annotation
    Binding sitei539 – 5391Coenzyme AUniRule annotation
    Binding sitei542 – 5421SubstrateUniRule annotation
    Metal bindingi553 – 5531Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi555 – 5551Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi558 – 5581Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei600 – 6001Coenzyme 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 annotation, Metal-bindingUniRule annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciPMAR93060:GI08-725-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:P9215_07011Imported
    OrganismiProchlorococcus marinus (strain MIT 9215)Imported
    Taxonomic identifieri93060 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000002014: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei625 – 6251N6-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

    STRINGi93060.P9215_07011.

    Structurei

    3D structure databases

    ProteinModelPortaliA8G3Y5.
    SMRiA8G3Y5. Positions 21-658.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni422 – 4276Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiAGCAVFV.
    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.

    A8G3Y5-1 [UniParc]FASTAAdd to Basket

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    MSLDKKNSIN NILEEKRIFP PSKKFAENSN ISTQEELLSL KKQASDNPIQ    50
    FWESFAKSEL DWFKPFQTVL DKENAPFFKW FKEGKLNITY NCLDRHIKRG 100
    LGGKTALIWE GEPGDSKKYT YEELLKEVCK AANALKAIGV KKGDLVCIYM 150
    PMIPEAMFAM LACARIGAPH SVVFGGFSSE ALKDRLIDGN ARFVITADGG 200
    FRKDKVIELK KAVDAAIESG ADKVVEKVVV VQRSQKNISM VDDRDFWWHE 250
    LLKDQKDHCE PEIMNSEDRL FILYTSGSTG KPKGVVHTTG GYNLWTHLTF 300
    KWIFDLKDDD IYWCTADVGW ITGHSYIVYG PLSNGATTLM YEGVPRPSNL 350
    GAFWEIVQKY KVSIFYTAPT AIRAFMKSGR EIPDKYNLES LRLLGTVGEP 400
    INPEAWMWYK DVIGKDKCPI VDTWWQTETG GVMISPLPGV VATKPGSATF 450
    PLPGIEVEIV DKNGDKVKEN EGGYLIIKKP WPGMMRTIHG NSERYLESYW 500
    EYISFKGEQN VYFAGDGARI DEDGYIWIMG RVDDVISVSG HRLGTMEIES 550
    ALVSHKSVAE SAVVGKKDDL KGEVIVAFVS LEKDVNGSSE LVENLKKHVV 600
    NEIGIIAKPE KIIISDFLPK TRSGKIMRRI LRSLAAGEKI SGDISTLEDS 650
    SVLEKLKELS 660
    Length:660
    Mass (Da):74,061
    Last modified:November 13, 2007 - v1
    Checksum:i00F0F96C4E7DDEEB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000825 Genomic DNA. Translation: ABV50316.1.
    RefSeqiYP_001483902.1. NC_009840.1.

    Genome annotation databases

    EnsemblBacteriaiABV50316; ABV50316; P9215_07011.
    GeneIDi5615997.
    KEGGipmh:P9215_07011.
    PATRICi22990866. VBIProMar119824_0708.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000825 Genomic DNA. Translation: ABV50316.1 .
    RefSeqi YP_001483902.1. NC_009840.1.

    3D structure databases

    ProteinModelPortali A8G3Y5.
    SMRi A8G3Y5. Positions 21-658.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 93060.P9215_07011.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV50316 ; ABV50316 ; P9215_07011 .
    GeneIDi 5615997.
    KEGGi pmh:P9215_07011.
    PATRICi 22990866. VBIProMar119824_0708.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PMAR93060:GI08-725-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: MIT 9215Imported.

    Entry informationi

    Entry nameiA8G3Y5_PROM2
    AccessioniPrimary (citable) accession number: A8G3Y5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 13, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 48 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