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G0GUJ0

- G0GUJ0_KLEPN

UniProt

G0GUJ0 - G0GUJ0_KLEPN

Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Klebsiella pneumoniae KCTC 2242
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. 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. 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 annotationImported

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciKPNE1049565:GLF0-90-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 annotation
    ORF Names:KPN2242_00445Imported
    OrganismiKlebsiella pneumoniae KCTC 2242Imported
    Taxonomic identifieri1049565 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella
    ProteomesiUP000008890: 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

    ProteinModelPortaliG0GUJ0.
    SMRiG0GUJ0. Positions 5-647.
    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.

    G0GUJ0-1 [UniParc]FASTAAdd to Basket

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    MSQIHKHPIP ANIAERCLIN PDQYKAQYQQ SITDPDTFWG EQGKILDWMR    50
    PYTRVKNTSF APGNISIKWY EDGTLNLAAN CLDRHLAERG DQTAIIWEGD 100
    DASQSKHITY RELHADVCRF ANVLLDLGIK KGDVVAIYMP MVPEAAVAML 150
    ACARIGAIHS VIFGGFSPEA VAGRIIDSSS RLVITADEGL RAGRAIPLKK 200
    NVDDALKNPN VKSIEHVVVL KRTGGNIDWQ EGRDLWWSDL IANASAEHRP 250
    VEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPGDI 300
    YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMCQVVDKHK 350
    VSILYTAPTA IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK 400
    KIGNEKCPVM DTWWQTETGG FMITPLPGAI ELKAGSATRP FFGVQPVLVD 450
    NEGLPLDGAT EGNLAIADSW PGQARTLFGD HERFEQTYFS TFKNMYFSGD 500
    GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVSHP KIAEAAVVGI 550
    PHNIKGQAIY AYVTLNHGEE PTPELYAEVR NWVRKEIGPL ATPDVLHWTD 600
    SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAITM 650
    PS 652
    Length:652
    Mass (Da):71,997
    Last modified:October 19, 2011 - v1
    Checksum:i43CDD4E14C66ECEA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002910 Genomic DNA. Translation: AEJ96016.1.
    RefSeqiYP_005952581.1. NC_017540.1.

    Genome annotation databases

    EnsemblBacteriaiAEJ96016; AEJ96016; KPN2242_00445.
    GeneIDi12543437.
    KEGGikpo:KPN2242_00445.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002910 Genomic DNA. Translation: AEJ96016.1 .
    RefSeqi YP_005952581.1. NC_017540.1.

    3D structure databases

    ProteinModelPortali G0GUJ0.
    SMRi G0GUJ0. Positions 5-647.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEJ96016 ; AEJ96016 ; KPN2242_00445 .
    GeneIDi 12543437.
    KEGGi kpo:KPN2242_00445.

    Phylogenomic databases

    KOi K01895.

    Enzyme and pathway databases

    BioCyci KPNE1049565:GLF0-90-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 2,3-Butanediol-Producing Klebsiella pneumoniae Strain KCTC 2242."
      Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J., Yang K.S.
      J. Bacteriol. 194:2736-2737(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: KCTC 2242Imported.

    Entry informationi

    Entry nameiG0GUJ0_KLEPN
    AccessioniPrimary (citable) accession number: G0GUJ0
    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