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Q9KV59

- ACSA_VIBCH

UniProt

Q9KV59 - ACSA_VIBCH

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (26 Sep 2003)
      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 sitei311 – 3111Coenzyme AUniRule annotation
    Binding sitei335 – 3351Coenzyme AUniRule annotation
    Binding sitei500 – 5001ATPUniRule annotation
    Binding sitei515 – 5151ATPUniRule annotation
    Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
    Binding sitei526 – 5261ATPUniRule 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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi387 – 3893ATPUniRule annotation
    Nucleotide bindingi411 – 4166ATPUniRule annotation

    GO - Molecular functioni

    1. acetate-CoA ligase activity Source: TIGR
    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: TIGR

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, 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:VC_0298
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000584: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 649649Acetyl-coenzyme A synthetasePRO_0000208392Add
    BLAST

    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

    Acetylation

    Interactioni

    Protein-protein interaction databases

    STRINGi243277.VC0298.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9KV59.
    SMRiQ9KV59. Positions 5-645.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni191 – 1944Coenzyme A bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    KOiK01895.
    OMAiAWIWYRD.
    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.

    Q9KV59-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEAHIYPVK QNIKAHTHAD NDTYLAMYQQ SIKDPEGFWS EHGKIVDWIK    50
    PFTKVKHTSF DPGHIDIRWF EDGTLNVSAN CIDRHLATRG DQVAIIWEGD 100
    DPTQDKTLTY KQLHQEVCRF ANALKEQGVR KGDVVCIYMP MVPEAAVAML 150
    ACTRIGAVHT IVFGGFSPEA LAGRIIDSNA KLVITADEGV RGGRAVPLKK 200
    NVDEALCNPE VKNISKVMVL KRTGGNVAWH EHRDIWWHEA TAKASDNCPP 250
    EEMKAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYATMTFK YVFDYQPNEV 300
    FWCTADVGWI TGHSYLVYGP LANGAKTILF EGVPNYPTTA RMSEVVDKHK 350
    VNILYTAPTA IRALMAKGDE AIKGTSRDSL RIMGSVGEPI NPEAWEWYYR 400
    TIGNEKSPIV DTWWQTETGG ILITPLPGAT ALKPGSATRP FFGVQPALVD 450
    NMGEIVEGAT EGNLVLLDSW PGQMRTVYGD HDRFEQTYFS TFKGMYFTGD 500
    GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESALVAFN KIAEAAVVGV 550
    PHDIKGQAIY AYITLNDGVY PSAELHKEVK DWVRKEIGAI ATPDVLHWTD 600
    ALPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVDR LIAEKAQLK 649
    Length:649
    Mass (Da):71,895
    Last modified:September 26, 2003 - v2
    Checksum:iA0C7282B14806B6E
    GO

    Sequence cautioni

    The sequence AAF93472.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003852 Genomic DNA. Translation: AAF93472.1. Different initiation.
    PIRiD82339.
    RefSeqiNP_229953.2. NC_002505.1.

    Genome annotation databases

    EnsemblBacteriaiAAF93472; AAF93472; VC_0298.
    GeneIDi2614968.
    KEGGivch:VC0298.
    PATRICi20079643. VBIVibCho83274_0280.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003852 Genomic DNA. Translation: AAF93472.1 . Different initiation.
    PIRi D82339.
    RefSeqi NP_229953.2. NC_002505.1.

    3D structure databases

    ProteinModelPortali Q9KV59.
    SMRi Q9KV59. Positions 5-645.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243277.VC0298.

    Protocols and materials databases

    DNASUi 2614968.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF93472 ; AAF93472 ; VC_0298 .
    GeneIDi 2614968.
    KEGGi vch:VC0298.
    PATRICi 20079643. VBIVibCho83274_0280.

    Phylogenomic databases

    eggNOGi COG0365.
    KOi K01895.
    OMAi AWIWYRD.
    OrthoDBi EOG68WR2H.

    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: ATCC 39315 / El Tor Inaba N16961.

    Entry informationi

    Entry nameiACSA_VIBCH
    AccessioniPrimary (citable) accession number: Q9KV59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: September 26, 2003
    Last modified: October 1, 2014
    This is version 77 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3