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G0F1A2

- G0F1A2_CUPNN

UniProt

G0F1A2 - G0F1A2_CUPNN

Protein

Acetyl-coenzyme A synthetase

Gene

acsA3

Organism
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / N-1) (Ralstonia eutropha)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 20 (01 Oct 2014)
      Sequence version 1 (19 Oct 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 sitei317 – 3171Coenzyme AUniRule annotation
    Binding sitei397 – 3971Substrate; via nitrogen amideUniRule annotation
    Binding sitei512 – 5121SubstrateUniRule annotation
    Binding sitei528 – 5281SubstrateUniRule annotation
    Active sitei530 – 5301UniRule annotation
    Binding sitei536 – 5361Coenzyme AUniRule annotation
    Binding sitei539 – 5391SubstrateUniRule annotation
    Metal bindingi550 – 5501Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi555 – 5551Magnesium; 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

    BioCyciCNEC1042878:GH0Z-2410-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:acsA3Imported
    Synonyms:acsAUniRule annotation
    Ordered Locus Names:CNE_1c24100Imported
    OrganismiCupriavidus necator (strain ATCC 43291 / DSM 13513 / N-1) (Ralstonia eutropha)Imported
    Taxonomic identifieri1042878 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000006798: Chromosome 1

    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

    Structurei

    3D structure databases

    ProteinModelPortaliG0F1A2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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.

    G0F1A2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAIESVMQE HRVFNPPEGF ASQAAIPSME AYRALCDEAE RDYEGFWARH    50
    ARELLHWNKP FTKVLDESNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV 100
    AIVFEADDGT VTRVTYRELH GKVCRFANGL KALGIKKGDR VVIYMPMSVE 150
    GVVAMQACAR LGATHSVVFG GFSAKSLQER LVDVGAVALI TADEQMRGGK 200
    ALPLKAIADD ALALGGCEAV RNVIVYRRTG GKVAWTEGRD RWMEDVSAGQ 250
    PDICEAEPVS AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWSFD 300
    IKPDDLFWCT ADIGWVTGHT YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD 350
    MIARHKVSIF YTAPTAIRSL IKAAEADDKI HPKQYDLSSL RLLGTVGEPI 400
    NPEAWMWYYK NIGNERCPIV DTFWQTETGG HMITPLPGAT PLVPGSCTLP 450
    LPGIMAAIVD ETGHDVPNGN GGILVVKRPW PAMIRTIWGD PERFRKSYFP 500
    EELGGKLYLA GDGSIRDKDT GYFTIMGRID DVLNVSGHRM GTMEIESALV 550
    SNPLVAEAAV VGRPDDMTGE AICAFVVLKR SRPTGEEAVK IATELRNWVG 600
    KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEEI TQDTSTLENP 650
    AILEQLKQAQ 660
    Length:660
    Mass (Da):72,614
    Last modified:October 19, 2011 - v1
    Checksum:i3381FFD2F26F1B3B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002877 Genomic DNA. Translation: AEI77733.1.
    RefSeqiYP_004686214.1. NC_015726.1.

    Genome annotation databases

    EnsemblBacteriaiAEI77733; AEI77733; CNE_1c24100.
    GeneIDi10918801.
    KEGGicnc:CNE_1c24100.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002877 Genomic DNA. Translation: AEI77733.1 .
    RefSeqi YP_004686214.1. NC_015726.1.

    3D structure databases

    ProteinModelPortali G0F1A2.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEI77733 ; AEI77733 ; CNE_1c24100 .
    GeneIDi 10918801.
    KEGGi cnc:CNE_1c24100.

    Phylogenomic databases

    KOi K01895.

    Enzyme and pathway databases

    BioCyci CNEC1042878:GH0Z-2410-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 the type strain Cupriavidus necator N-1."
      Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.
      J. Bacteriol. 193:5017-5017(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43291 / DSM 13513 / N-1Imported.

    Entry informationi

    Entry nameiG0F1A2_CUPNN
    AccessioniPrimary (citable) accession number: G0F1A2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: October 19, 2011
    Last sequence update: October 19, 2011
    Last modified: October 1, 2014
    This is version 20 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