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P31638

- ACSA_CUPNH

UniProt

P31638 - ACSA_CUPNH

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      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. Although acetate is the preferred substrate of AcsA, propionate is also used, but at a diminished rate compared with that of acetate. Fatty acids with more than three carbon atoms are usually not accepted as substrates by AcsA.1 PublicationUniRule annotation

    Catalytic activityi

    ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

    Cofactori

    Magnesium.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei317 – 3171Coenzyme AUniRule annotation
    Binding sitei512 – 5121ATPUniRule annotation
    Binding sitei528 – 5281ATPUniRule annotation
    Binding sitei536 – 5361Coenzyme A; via carbonyl oxygenUniRule annotation
    Binding sitei539 – 5391ATPUniRule annotation
    Metal bindingi550 – 5501Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi555 – 5551Magnesium; via carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi397 – 3993ATPUniRule annotation
    Nucleotide bindingi421 – 4266ATPUniRule 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. acetoin catabolic process Source: UniProtKB-UniPathway
    2. acetyl-CoA biosynthetic process from acetate Source: InterPro

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciCNEC381666:GJUJ-2492-MONOMER.
    MetaCyc:MONOMER-13637.
    UniPathwayiUPA00040.

    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
    Synonyms:acoE
    Ordered Locus Names:H16_A2525
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000008210: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 660660Acetyl-coenzyme A synthetasePRO_0000208353Add
    BLAST

    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

    Acetylation

    Interactioni

    Protein-protein interaction databases

    STRINGi381666.H16_A2525.

    Structurei

    3D structure databases

    ProteinModelPortaliP31638.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni197 – 2004Coenzyme A bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiAHERYEN.
    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.

    P31638-1 [UniParc]FASTAAdd to Basket

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    MSAIESVMQE HRVFNPPEGF ASQAAIPSME AYQALCDEAE RDYEGFWARH    50
    ARELLHWTKP FTKVLDQSNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV 100
    AIVFEADDGS VTRVTYRELH GKVCRFANGL KALGIRKGDR VVIYMPMSVE 150
    GVVAMQACAR LGATHSVVFG GFSAKSLQER LVDVGAVALI TADEQMRGGK 200
    ALPLKAIADD ALALGGCEAV RNVIVYRRTG GKVAWTEGRD RWMEDVSAGQ 250
    PDTCEAEPVS AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWTFD 300
    IKPDDLFWCT ADIGWVTGHT YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD 350
    MIARHKVSIF YTAPTAIRSL IKAAEADEKI 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):72,602
    Last modified:July 1, 1993 - v1
    Checksum:iEA03022F82C5C502
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97217 Genomic DNA. Translation: AAA21945.1.
    AM260479 Genomic DNA. Translation: CAJ93612.1.
    PIRiA45736.
    RefSeqiWP_011615709.1. NC_008313.1.
    YP_726980.1. NC_008313.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ93612; CAJ93612; H16_A2525.
    GeneIDi4247141.
    KEGGireh:H16_A2525.
    PATRICi35234555. VBIRalEut6770_2916.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97217 Genomic DNA. Translation: AAA21945.1 .
    AM260479 Genomic DNA. Translation: CAJ93612.1 .
    PIRi A45736.
    RefSeqi WP_011615709.1. NC_008313.1.
    YP_726980.1. NC_008313.1.

    3D structure databases

    ProteinModelPortali P31638.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 381666.H16_A2525.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ93612 ; CAJ93612 ; H16_A2525 .
    GeneIDi 4247141.
    KEGGi reh:H16_A2525.
    PATRICi 35234555. VBIRalEut6770_2916.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00040 .
    BioCyci CNEC381666:GJUJ-2492-MONOMER.
    MetaCyc:MONOMER-13637.

    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. "Identification and molecular characterization of the acetyl coenzyme A synthetase gene (acoE) of Alcaligenes eutrophus."
      Priefert H., Steinbuechel A.
      J. Bacteriol. 174:6590-6599(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

    Entry informationi

    Entry nameiACSA_CUPNH
    AccessioniPrimary (citable) accession number: P31638
    Secondary accession number(s): Q0K8Q9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3