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Q66FM8

- ACSA_YERPS

UniProt

Q66FM8 - ACSA_YERPS

Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      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
    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 annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei311 – 3111Coenzyme AUniRule annotation
    Binding sitei335 – 3351Coenzyme AUniRule annotation
    Binding sitei500 – 5001ATPUniRule annotation
    Binding sitei515 – 5151ATPUniRule annotation
    Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
    Binding sitei526 – 5261ATPUniRule 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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi387 – 3893ATPUniRule annotation
    Nucleotide bindingi411 – 4166ATPUniRule 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

    Ligase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciYPSE273123:GI1M-338-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
    Ordered Locus Names:YPTB0308
    OrganismiYersinia pseudotuberculosis serotype I (strain IP32953)
    Taxonomic identifieri273123 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
    ProteomesiUP000001011: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 652652Acetyl-coenzyme A synthetasePRO_1000065337Add
    BLAST

    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

    Acetylation

    Interactioni

    Protein-protein interaction databases

    STRINGi273123.YPTB0308.

    Structurei

    3D structure databases

    ProteinModelPortaliQ66FM8.
    SMRiQ66FM8. Positions 5-647.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni191 – 1944Coenzyme A bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiDISWING.
    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.

    Q66FM8-1 [UniParc]FASTAAdd to Basket

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    MSQIHKHPIP AAIAEHALIT PEKYQHYYQQ SVQNPDEFWG EQGKIIDWIK    50
    PYKTVKNTSF DPGHVSIRWF EDGTLNLAAN CLDRHLAERG DQTAIIWEGD 100
    DPNQSKTVTY KQLHHDVCQF ANVLKSLGIK KGDVVAIYMP MVPEAAVAML 150
    ACARIGAVHS VIFGGFSPDA VAGRIIDSHS KLVITADEGI RAGRAIPLKK 200
    NVDEALKNPA ITSIKNVVVF QRTGNASYWE DGRDVWWHDL IKEASADCPP 250
    EEMNAEDPLF ILYTSGSTGK PKGVVHTTGG YLVYAALTFK YVFDYHPGDI 300
    YWCTADVGWV TGHSYLLYGP LACGAITLMF EGVPNYPGVN RLSQVVDKHK 350
    VNILYTAPTA IRALMAEGDK AIEGTKRDSL RIMGSVGEPI NPEAWEWYYN 400
    KIGNSKCPIV DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD 450
    NLGNPQEGVA EGNLVITDSW PGQARTLFGD HDRFEQTYFS TFKGMYFSGD 500
    GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGV 550
    PHNIKGQAIY AYITLNHGEE PTPELYTEVR NWVRKEIGPL ATPDILHWTD 600
    SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVEK LLEEKQSMQT 650
    PS 652
    Length:652
    Mass (Da):72,072
    Last modified:October 11, 2004 - v1
    Checksum:i92FA2E582F1F7B76
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX936398 Genomic DNA. Translation: CAH19548.1.
    RefSeqiYP_068854.1. NC_006155.1.

    Genome annotation databases

    EnsemblBacteriaiCAH19548; CAH19548; YPTB0308.
    GeneIDi2956405.
    KEGGiyps:YPTB0308.
    PATRICi18638765. VBIYerPse22266_0482.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX936398 Genomic DNA. Translation: CAH19548.1 .
    RefSeqi YP_068854.1. NC_006155.1.

    3D structure databases

    ProteinModelPortali Q66FM8.
    SMRi Q66FM8. Positions 5-647.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273123.YPTB0308.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH19548 ; CAH19548 ; YPTB0308 .
    GeneIDi 2956405.
    KEGGi yps:YPTB0308.
    PATRICi 18638765. VBIYerPse22266_0482.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci YPSE273123:GI1M-338-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: IP32953.

    Entry informationi

    Entry nameiACSA_YERPS
    AccessioniPrimary (citable) accession number: Q66FM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 61 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3