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B0KHW7

- B0KHW7_PSEPG

UniProt

B0KHW7 - B0KHW7_PSEPG

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pseudomonas putida (strain GB-1)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (18 Mar 2008)
      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 annotationSAAS annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei307 – 3071Coenzyme AUniRule annotation
    Binding sitei331 – 3311Coenzyme AUniRule annotation
    Binding sitei383 – 3831Substrate; via nitrogen amideUniRule annotation
    Binding sitei496 – 4961SubstrateUniRule annotation
    Binding sitei511 – 5111SubstrateUniRule annotation
    Active sitei513 – 5131UniRule annotation
    Binding sitei519 – 5191Coenzyme AUniRule annotation
    Binding sitei522 – 5221SubstrateUniRule annotation
    Metal bindingi533 – 5331Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi535 – 5351Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei580 – 5801Coenzyme 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 annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciPPUT76869:GIXB-4782-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:PputGB1_4701Imported
    OrganismiPseudomonas putida (strain GB-1)Imported
    Taxonomic identifieri76869 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002157: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei605 – 6051N6-acetyllysineUniRule annotation

    Post-translational modificationi

    Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.UniRule annotation

    Keywords - PTMi

    AcetylationUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi76869.PputGB1_4701.

    Structurei

    3D structure databases

    ProteinModelPortaliB0KHW7.
    SMRiB0KHW7. Positions 21-641.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni407 – 4126Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiRRIFEPT.
    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.

    B0KHW7-1 [UniParc]FASTAAdd to Basket

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    MFDIRNYPQA LAVSQSATPT PDEYHRLYRQ SVDDPDTFWA EQAKRLDWIK    50
    PWSSVQQCDL NTGKARWFDG AQLNVSYNCI DRHLAQRGEQ TALLWEGDDP 100
    KDSKAITYRE LHRQVCRLAN AMKARGVKKG DRVCIYMPMI PEAAFAMLAC 150
    TRIGAIHSVV FGGFSPDALR DRILDADCRT VITADEGVRG GKRVPLKQNV 200
    DKALASCPAV SSVLVVRRTG GDVAWAEGRD LWYHEVTEKA GDDCPPEPMA 250
    AEDPLFILYT SGSTGKPKGV LHTTGGYLLQ ATMTFKVVFD YRDGEVFWCT 300
    ADVGWVTGHS YIVYGPLANG AISLMFEGVP NYPDTSRFWQ VVDKHQVNIF 350
    YTAPTALRAL MREGSAPLQG TSRKSLRLLG SVGEPINPEA WEWYFEAVGQ 400
    KRCPIVDTWW QTETGGIMLT PLPGSQALKP GCATQPMFGV QPALLDEKGK 450
    LIEGPGAGLL VIKASWPGQI RSVYGDHQRM VDTYFKPMPG YYFTGDGARR 500
    DADGDYWITG RIDDVINVSG HRIGTAEVES ALVLHDSVAE AAVVGYPHDL 550
    KGQGVYAFVT TMNGVTPDDT LKAELLALVS KEIGSFAKPE LIQWAPALPK 600
    TRSGKIMRRI LRKIACNELD NLGDTSTLAD PSVVQGLIDK RLNQ 644
    Length:644
    Mass (Da):71,051
    Last modified:March 18, 2008 - v1
    Checksum:i6DA55322F09A7A93
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000926 Genomic DNA. Translation: ABZ00588.1.
    RefSeqiYP_001670923.1. NC_010322.1.

    Genome annotation databases

    EnsemblBacteriaiABZ00588; ABZ00588; PputGB1_4701.
    GeneIDi5872512.
    KEGGippg:PputGB1_4701.
    PATRICi19936495. VBIPsePut76638_4709.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000926 Genomic DNA. Translation: ABZ00588.1 .
    RefSeqi YP_001670923.1. NC_010322.1.

    3D structure databases

    ProteinModelPortali B0KHW7.
    SMRi B0KHW7. Positions 21-641.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 76869.PputGB1_4701.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABZ00588 ; ABZ00588 ; PputGB1_4701 .
    GeneIDi 5872512.
    KEGGi ppg:PputGB1_4701.
    PATRICi 19936495. VBIPsePut76638_4709.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PPUT76869:GIXB-4782-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: GB-1Imported.

    Entry informationi

    Entry nameiB0KHW7_PSEPG
    AccessioniPrimary (citable) accession number: B0KHW7
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 18, 2008
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 43 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