Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q12X88

- Q12X88_METBU

UniProt

Q12X88 - Q12X88_METBU

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (22 Aug 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei309 – 3091Coenzyme AUniRule annotation
    Binding sitei385 – 3851Substrate; 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 sitei584 – 5841Coenzyme 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 annotation, Metal-bindingUniRule annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMBUR259564:GHBZ-1022-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:Mbur_0999Imported
    OrganismiMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)Imported
    Taxonomic identifieri259564 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides
    ProteomesiUP000001979: 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

    Interactioni

    Protein-protein interaction databases

    STRINGi259564.Mbur_0999.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12X88.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni409 – 4146Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiQTAILFE.

    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.

    Q12X88-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTETIESLLK EQQEFHPSAD FVKQANMNDP HIYEKAEADI EGFWEGLAGN    50
    IDWFKKWDTV LDWQPPHAKW FSGGKLNASY NCLDRHVQKH GDKPALIWEG 100
    EMENSETYTY KELRDATARF AAGLKELGVK KGDVVTIYLP MVPEAVISML 150
    ACSRIGAPHS VVFAGFSSEA LAQRVEDAHS RFVITCNGYF HKGNLIQQKE 200
    RADKGLENAP AVEKVIVVDH AANIIPMKEE RDIWWNDLIH NVDSECEPEH 250
    MDSEDTLFIM YTSGTTGRPK GVVHTTGGYM VGTNVTSNWI FDLKDDDIFW 300
    CTADVGWITG HSYLVYGPLS NGATIVMHEG APDYPDKGRF WDIVEKYGVT 350
    IFYTAPTAIR TFMKWGDEIP AKYDLSSLRL LGSVGEPINP KAWLWYYETI 400
    GKSKCPIVDT WWQTETGMIM ISPLPGITTM RPGTATRPFP GIKANILDDE 450
    GNEVPMGSGG YLALQNPWPS MIRTINGDEQ RFIDTYWSKW GADTYLTGDG 500
    ARKDEDGNFW ILGRLDDVIK VSGHRLGTME IESALVSHPS VAEAAVDGKV 550
    DEIKGEVICA YVILESSCDD QCSILEDELK QHVVDEIGPI ARPKMIIFTE 600
    ELPKTRSGKI MRRVLKAITN GTEIGDISTL QDPAVVEDLK RKVNEIGEQ 649
    Length:649
    Mass (Da):72,668
    Last modified:August 22, 2006 - v1
    Checksum:i4C72352FF0A22D0B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000300 Genomic DNA. Translation: ABE51938.1.
    RefSeqiWP_011499087.1. NC_007955.1.
    YP_565688.1. NC_007955.1.

    Genome annotation databases

    EnsemblBacteriaiABE51938; ABE51938; Mbur_0999.
    GeneIDi3998104.
    KEGGimbu:Mbur_0999.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000300 Genomic DNA. Translation: ABE51938.1 .
    RefSeqi WP_011499087.1. NC_007955.1.
    YP_565688.1. NC_007955.1.

    3D structure databases

    ProteinModelPortali Q12X88.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 259564.Mbur_0999.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE51938 ; ABE51938 ; Mbur_0999 .
    GeneIDi 3998104.
    KEGGi mbu:Mbur_0999.

    Phylogenomic databases

    eggNOGi COG0365.
    HOGENOMi HOG000229981.
    KOi K01895.
    OMAi QTAILFE.

    Enzyme and pathway databases

    BioCyci MBUR259564:GHBZ-1022-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: DSM 6242 / NBRC 107633 / OCM 468 / ACE-MImported.

    Entry informationi

    Entry nameiQ12X88_METBU
    AccessioniPrimary (citable) accession number: Q12X88
    Entry historyi
    Integrated into UniProtKB/TrEMBL: August 22, 2006
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 56 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