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E3DHF3

- E3DHF3_ERWSE

UniProt

E3DHF3 - E3DHF3_ERWSE

Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Erwinia sp. (strain Ejp617)
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. Acs undergoes a two-step reaction. In the first half reaction, Acs 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
    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
    Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.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 sitei335 – 3351Coenzyme 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: UniProtKB-HAMAP
    2. chemotaxis Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    LigaseUniRule annotation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciESP215689:GLCY-773-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:acsUniRule annotationImported
    Ordered Locus Names:EJP617_07610Imported
    OrganismiErwinia sp. (strain Ejp617)Imported
    Taxonomic identifieri215689 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeErwinia
    ProteomesiUP000006865: 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

    ProteinModelPortaliE3DHF3.
    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.

    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.

    E3DHF3-1 [UniParc]FASTAAdd to Basket

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    MSHAHIYPIP ANIAQNTLIN PRQYHSMYQQ SVQDPEAFWG EQGKIVDWIK    50
    PYATVKNTSF APGNISIRWY EDGTLNLAAN CLDRHLAARG DHPAMIWEGD 100
    DASESKTITY RELHHDVCRF SNALKALGIH KGDVVAIYMP MVPEAAVAML 150
    ACARIGAVHS VIFGGFSPEA VAGRIIDSHA RLVITADEGV RAGRTIPLKK 200
    NVDDALNNPG VTSVDNVIVL RRTGKEISWH HGRDLWWHEQ VNSASEQHQP 250
    EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPEDI 300
    YWCTADVGWI TGHSYLLYGP LACGATTLMF EGVPNWPKPS RMAEVVDKHR 350
    VTILYTAPTA VRALMAEGDK AIAGTHRSSL RILGSVGEPI NPEAWEWFHQ 400
    KIGNGHCPIS DTWWQTETGG FMIAPLPGAT ALKPGSATHP FFGVQPALVD 450
    NEGHLQEGAS EGNLVIVDSW PGQARTLFGD HQRFEQTYFS TFKNRYFSGD 500
    GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVSHP KIAEAAVVGI 550
    PHALKGQAIY AYITLNRGEE PSPQLYSEVR AWVRKEIGPI ATPDVLHWTE 600
    SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPGVVDK LLEEKLSINM 650
    P 651
    Length:651
    Mass (Da):71,837
    Last modified:January 11, 2011 - v1
    Checksum:iC60FB21842232F2D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002124 Genomic DNA. Translation: ADP10442.1.
    RefSeqiWP_014542524.1. NC_017445.1.
    YP_005817329.1. NC_017445.1.

    Genome annotation databases

    EnsemblBacteriaiADP10442; ADP10442; EJP617_07610.
    GeneIDi12428730.
    KEGGierj:EJP617_07610.
    PATRICi42938204. VBIErwSp41759_0819.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002124 Genomic DNA. Translation: ADP10442.1 .
    RefSeqi WP_014542524.1. NC_017445.1.
    YP_005817329.1. NC_017445.1.

    3D structure databases

    ProteinModelPortali E3DHF3.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADP10442 ; ADP10442 ; EJP617_07610 .
    GeneIDi 12428730.
    KEGGi erj:EJP617_07610.
    PATRICi 42938204. VBIErwSp41759_0819.

    Phylogenomic databases

    KOi K01895.

    Enzyme and pathway databases

    BioCyci ESP215689:GLCY-773-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 Japanese Erwinia strain Ejp617, a bacterial shoot blight pathogen of pear."
      Park D.H., Thapa S.P., Choi B.S., Kim W.S., Hur J.H., Cho J.M., Lim J.S., Choi I.Y., Lim C.K.
      J. Bacteriol. 193:586-587(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ejp617Imported.

    Entry informationi

    Entry nameiE3DHF3_ERWSE
    AccessioniPrimary (citable) accession number: E3DHF3
    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