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B2FNG6

- B2FNG6_STRMK

UniProt

B2FNG6 - B2FNG6_STRMK

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Stenotrophomonas maltophilia (strain K279a)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (10 Jun 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 sitei310 – 3101Coenzyme AUniRule annotation
    Binding sitei334 – 3341Coenzyme AUniRule annotation
    Binding sitei386 – 3861Substrate; via nitrogen amideUniRule annotation
    Binding sitei499 – 4991SubstrateUniRule annotation
    Binding sitei514 – 5141SubstrateUniRule annotation
    Active sitei516 – 5161UniRule annotation
    Binding sitei522 – 5221Coenzyme AUniRule annotation
    Binding sitei525 – 5251SubstrateUniRule annotation
    Metal bindingi536 – 5361Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi541 – 5411Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei583 – 5831Coenzyme 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

    BioCyciSMAL522373:GJE8-4460-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 annotationImported
    Ordered Locus Names:Smlt4623Imported
    OrganismiStenotrophomonas maltophilia (strain K279a)Imported
    Taxonomic identifieri522373 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
    ProteomesiUP000008840: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei608 – 6081N6-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

    STRINGi522373.Smlt4623.

    Structurei

    3D structure databases

    ProteinModelPortaliB2FNG6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni410 – 4156Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiHPPQKML.
    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.

    B2FNG6-1 [UniParc]FASTAAdd to Basket

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    MADIYPVDPQ FAAKARIDKT SYEQQYQASV TDPDGFWGKA AERLQWMRKP    50
    TRIKNVSYDL SDFHIKWFED GELNASVNCL DRQLETRGDK TALLFEPDGP 100
    DAPAQHVTYR ELYERTCRLG NALRNLGVKK GDRVTIYLPM IVDAAVAMLA 150
    CARIGAIHSV VFGGFAPNSI ADRVSDCQSK LIITADEGLR GGRRIPLKAN 200
    VDAALKLPGT NTVETVLVVR HTGGAVDMQA PRDRWFHDVV DSQPATCEPE 250
    RMNAEDPLFI LYTSGSTGKP KGVLHTTGGY LLYAAYTHEA VFDLREDDIY 300
    WCTADVGWVT GHSYIVYGPL ANGATSLMFE GVPNYPDTSR FWNVIDKHKV 350
    TIFYTAPTAI RALMREGEEP VKKTSRASLR LLGSVGEPIN PEAWRWYYEV 400
    VGDSRCPIVD TWWQTETGGI LISPLAGAMD LKPGSATLPF FGVQPALVNA 450
    DGEIQDGPTE GNLIIRDSWP GQMRTVYGDH QRFIDTYFRT YPGSYFTGDG 500
    CRRDEDGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK VAEAAVVGFP 550
    HDVKGQGIYA YVTLVAEEAP SDELHKELIA WVRKEIGPIA TPDHLQWAPG 600
    LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVASL VDERKVR 647
    Length:647
    Mass (Da):71,696
    Last modified:June 10, 2008 - v1
    Checksum:i309006DBC8BA7090
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM743169 Genomic DNA. Translation: CAQ47977.1.
    RefSeqiYP_001974253.1. NC_010943.1.

    Genome annotation databases

    EnsemblBacteriaiCAQ47977; CAQ47977; Smlt4623.
    GeneIDi6392775.
    KEGGisml:Smlt4623.
    PATRICi23704627. VBISteMal45202_4358.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM743169 Genomic DNA. Translation: CAQ47977.1 .
    RefSeqi YP_001974253.1. NC_010943.1.

    3D structure databases

    ProteinModelPortali B2FNG6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 522373.Smlt4623.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAQ47977 ; CAQ47977 ; Smlt4623 .
    GeneIDi 6392775.
    KEGGi sml:Smlt4623.
    PATRICi 23704627. VBISteMal45202_4358.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SMAL522373:GJE8-4460-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. "The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
      Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A.
      , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
      Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K279aImported.

    Entry informationi

    Entry nameiB2FNG6_STRMK
    AccessioniPrimary (citable) accession number: B2FNG6
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 44 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3