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D7BFC2

- D7BFC2_MEISD

UniProt

D7BFC2 - D7BFC2_MEISD

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus silvanus)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 26 (01 Oct 2014)
      Sequence version 1 (10 Aug 2010)
      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 sitei316 – 3161Coenzyme AUniRule annotation
    Binding sitei340 – 3401Coenzyme AUniRule annotation
    Binding sitei392 – 3921Substrate; via nitrogen amideUniRule annotation
    Binding sitei506 – 5061SubstrateUniRule annotation
    Binding sitei521 – 5211SubstrateUniRule annotation
    Active sitei523 – 5231UniRule annotation
    Binding sitei529 – 5291Coenzyme AUniRule annotation
    Binding sitei532 – 5321SubstrateUniRule annotation
    Metal bindingi543 – 5431Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi545 – 5451Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi548 – 5481Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei590 – 5901Coenzyme 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

    BioCyciMSIL526227:GJ9Q-1617-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:Mesil_1588Imported
    OrganismiMeiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus silvanus)Imported
    Taxonomic identifieri526227 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeMeiothermus
    ProteomesiUP000001916: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei615 – 6151N6-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

    ProteinModelPortaliD7BFC2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni416 – 4216Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiAWIWYRD.

    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.

    D7BFC2-1 [UniParc]FASTAAdd to Basket

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    MDQSADRIEA VLKEERVFYP SEDFKRSALL AKPEEYQALY EESLRDPEGF    50
    WGRFAGEFHW FEPWKKVLEW NVPYAKWFVG GKTNLTYNAL DRHLASRRNK 100
    AAIVFEGEPG DSRVLTYHDL HREVSKFANV LKGLGVNKGD RVTIYLPMIP 150
    EAAIAMLACA RIGAIHSVVF GGFSASALAE RINDAQSAVL VTADGGWRRG 200
    SVVPLKANAD EALASTESVR HVVVVRRVGQ EVPMLPGRDH WYHELMASAS 250
    DRCEAEPLDS EHPLFILYTS GSTGKPKGVM HTTAGYMAYV ALTARYVFDL 300
    KETDTYFCTA DVGWVTGHSY VVYGLLLNGA TTLMYEGAPN WPDEGRIWNI 350
    IDKYGVSILY TAPTAIRAFM KWGEQWPLKY RLSSLRLLGS VGEPINPEAW 400
    LWYYHVIGKG RCPIVDTWWQ TETGGIMITT LPGVHPMKPG HAGKPFFGVE 450
    PDIVDTSGKT ITGADEGGHL IIKRPWPSML RTVWGDPERY ERQYWSQYPG 500
    NYFTGDGARR DSDGYYLIMG RVDDVLNVSG HRLGTMEVES ALVSHPAVAE 550
    AAVVGRPDPI KGEGIVAFVT LKAGYTPSDA LSAELKAHVV KAIGAIARPD 600
    EIRFTEAMPK TRSGKIMRRL LRQIAAGESE IKGDTSTLED RSVVERLKAA 650
    Q 651
    Length:651
    Mass (Da):72,374
    Last modified:August 10, 2010 - v1
    Checksum:iD8E7C2C5D25B4AF0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002042 Genomic DNA. Translation: ADH63475.1.
    RefSeqiWP_013158039.1. NC_014212.1.
    YP_003684983.1. NC_014212.1.

    Genome annotation databases

    EnsemblBacteriaiADH63475; ADH63475; Mesil_1588.
    GeneIDi9251092.
    KEGGimsv:Mesil_1588.
    PATRICi38191955. VBIMeiSil18825_1623.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002042 Genomic DNA. Translation: ADH63475.1 .
    RefSeqi WP_013158039.1. NC_014212.1.
    YP_003684983.1. NC_014212.1.

    3D structure databases

    ProteinModelPortali D7BFC2.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADH63475 ; ADH63475 ; Mesil_1588 .
    GeneIDi 9251092.
    KEGGi msv:Mesil_1588.
    PATRICi 38191955. VBIMeiSil18825_1623.

    Phylogenomic databases

    HOGENOMi HOG000229981.
    KOi K01895.
    OMAi AWIWYRD.

    Enzyme and pathway databases

    BioCyci MSIL526227:GJ9Q-1617-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: ATCC 700542 / DSM 9946 / VI-R2Imported.

    Entry informationi

    Entry nameiD7BFC2_MEISD
    AccessioniPrimary (citable) accession number: D7BFC2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: August 10, 2010
    Last sequence update: August 10, 2010
    Last modified: October 1, 2014
    This is version 26 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