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E3IPI9

- E3IPI9_DESVR

UniProt

E3IPI9 - E3IPI9_DESVR

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Desulfovibrio vulgaris (strain RCH1)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 25 (01 Oct 2014)
      Sequence version 1 (11 Jan 2011)
      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 sitei321 – 3211Coenzyme AUniRule annotation
    Binding sitei397 – 3971Substrate; via nitrogen amideUniRule annotation
    Binding sitei510 – 5101SubstrateUniRule annotation
    Binding sitei525 – 5251SubstrateUniRule annotation
    Active sitei527 – 5271UniRule annotation
    Binding sitei533 – 5331Coenzyme AUniRule annotation
    Binding sitei536 – 5361SubstrateUniRule annotation
    Metal bindingi547 – 5471Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi549 – 5491Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi552 – 5521Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei594 – 5941Coenzyme 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

    BioCyciDVUL573059:GLCM-2818-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:Deval_2742Imported
    OrganismiDesulfovibrio vulgaris (strain RCH1)Imported
    Taxonomic identifieri573059 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
    ProteomesiUP000001496: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei619 – 6191N6-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

    ProteinModelPortaliE3IPI9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni201 – 2044Coenzyme AUniRule annotation
    Regioni421 – 4266Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01895.
    OMAiRRIFEPT.

    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.

    E3IPI9-1 [UniParc]FASTAAdd to Basket

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    MSQERIESMM DEKRHFAPPA DSRGRAHVSG EAAREALVRR AAEDPEGFWG    50
    ERAAQLIDWF KPWDTVLDAD MNEPRIEWFK GGRLNVAHNC LDRHVAGNRR 100
    NKAAIIWQGE PEEDVRVLTY QMLYDEVRRF AAVLRKMGVH KGDRVSLYMP 150
    MIPELAVAML ACARIGAVHS IVFAGFSAVS LQNRIHDCEA KVVVTADAVL 200
    RAGRRIPLKV NVDEAVRQCP SVEKVVVVNR GSLEVTMEEG RDLWWHEVMA 250
    DRTLDVDRPC EEMDAEDMLF ILYTSGSTGK PKGVVHTTGG YLTYAAHTTQ 300
    WVFDVQDDDV YWCTADIGWI TGHSYIVYGP LALGATSLMF EGVPSWPSPD 350
    RFWRIVEKFR VNIFYTAPTV VRALMREGTD WTERHDLSSL RVLGSVGEPI 400
    NPEAWMWYHT HIGKGRLPIV DTWWQTETGG IMISGLPYAT TLKPGSATQP 450
    LPGVDAAIVR PDGSPAGPNE GGHLVIRKPW PGMLRGIFGS PERYRSTYFE 500
    RFPGMYESGD GARTDTDGYF WIMGRLDDVI NVSGHRMGTA EVESALVAHP 550
    SVAEAAVVGM PHAVKGEAIY AYVTLGADAE ETEELRAELR AWVRKEIGPI 600
    ATPDVLQFAE GLPKTRSGKI MRRILRKIAA GATSEFGDTS TLADPGVVSD 650
    LIEGRLQLTG R 661
    Length:661
    Mass (Da):73,499
    Last modified:January 11, 2011 - v1
    Checksum:iD33CE2558CB40921
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002297 Genomic DNA. Translation: ADP87884.1.
    RefSeqiWP_010940228.1. NC_017310.1.
    YP_005703522.1. NC_017310.1.

    Genome annotation databases

    EnsemblBacteriaiADP87884; ADP87884; Deval_2742.
    GeneIDi12868602.
    KEGGidvg:Deval_2742.
    PATRICi42913287. VBIDesVul75230_2905.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002297 Genomic DNA. Translation: ADP87884.1 .
    RefSeqi WP_010940228.1. NC_017310.1.
    YP_005703522.1. NC_017310.1.

    3D structure databases

    ProteinModelPortali E3IPI9.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADP87884 ; ADP87884 ; Deval_2742 .
    GeneIDi 12868602.
    KEGGi dvg:Deval_2742.
    PATRICi 42913287. VBIDesVul75230_2905.

    Phylogenomic databases

    KOi K01895.
    OMAi RRIFEPT.

    Enzyme and pathway databases

    BioCyci DVUL573059:GLCM-2818-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: RCH1Imported.

    Entry informationi

    Entry nameiE3IPI9_DESVR
    AccessioniPrimary (citable) accession number: E3IPI9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: January 11, 2011
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 25 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