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B1Z3L5

- B1Z3L5_BURA4

UniProt

B1Z3L5 - B1Z3L5_BURA4

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Burkholderia ambifaria (strain MC40-6)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (20 May 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 annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei321 – 3211Coenzyme AUniRule annotation
    Binding sitei401 – 4011Substrate; via nitrogen amideUniRule annotation
    Binding sitei516 – 5161SubstrateUniRule annotation
    Binding sitei532 – 5321SubstrateUniRule annotation
    Active sitei534 – 5341UniRule annotation
    Binding sitei540 – 5401Coenzyme AUniRule annotation
    Binding sitei543 – 5431SubstrateUniRule annotation
    Metal bindingi554 – 5541Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi556 – 5561Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi559 – 5591Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei604 – 6041Coenzyme 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

    BioCyciBAMB398577:GH38-5979-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:BamMC406_5891Imported
    OrganismiBurkholderia ambifaria (strain MC40-6)Imported
    Taxonomic identifieri398577 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
    ProteomesiUP000001680: Chromosome 3

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei629 – 6291N6-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

    STRINGi398577.BamMC406_5891.

    Structurei

    3D structure databases

    ProteinModelPortaliB1Z3L5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni425 – 4306Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiRRIFEPT.
    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.

    B1Z3L5-1 [UniParc]FASTAAdd to Basket

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    MENTLTAIVS ILQERRIFEP TADTRERATI SGMPAYQALA AEAERDYEGF    50
    WARLAREGLS WHKPFTKVLD ESDAPFYKWF DDGELNASYN CLDRHVEAGN 100
    GERVAVIFEA DDGTVTRVTY ADLLARVSRF ANALKKRGIA KGDRVVIYMP 150
    MSIEGIVAMQ ACARIGATHS VVFGGFSAKS LNERLVDVGA VALITADEQA 200
    RGGKTLPLKS IADEAIAMGG CEAVKSVIVY RRTGGKVDWH AGRDLWMHEL 250
    AHAESDTCAP EWVGAEHPLF ILYTSGSTGK PKGVQHSTGG YLLWAAQTMK 300
    WTFDWKPTDV FWCTADIGWV TGHTYITYGP LACGGTQVVF EGVPTYPDAG 350
    RFWKMIADHK VTVFYTAPTA IRSLIKAAEA DDKVHPKSYD LSSLRIIGTV 400
    GEPINPEAWM WYHKHVGQER CPIVDTWWQT ETGGHMITPL PGATPTVPGS 450
    CTLPLPGIMA AVVDETGQDV PNGQGGILVV KRPWPAMIRT IWGDPERFKK 500
    SYYPEELGGR LYLAGDGTVR DKDTGYFTIM GRIDDVLNVS GHRLGTMEIE 550
    SALVSHELVA EAAVVGRPDD TTGEAVVAFV VLKRSRPEGE EAAALAKTLR 600
    DWVGKQIGPI AKPKDIRFGD NLPKTRSGKI MRRLLRSLAK GEAITQDTST 650
    LENPAILDQL GQSL 664
    Length:664
    Mass (Da):72,777
    Last modified:May 20, 2008 - v1
    Checksum:i208A8B2F4243E6FD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001027 Genomic DNA. Translation: ACB68328.1.
    RefSeqiYP_001815881.1. NC_010557.1.

    Genome annotation databases

    EnsemblBacteriaiACB68328; ACB68328; BamMC406_5891.
    GeneIDi6182474.
    KEGGibac:BamMC406_5891.
    PATRICi19042153. VBIBurAmb82852_6352.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001027 Genomic DNA. Translation: ACB68328.1 .
    RefSeqi YP_001815881.1. NC_010557.1.

    3D structure databases

    ProteinModelPortali B1Z3L5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 398577.BamMC406_5891.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB68328 ; ACB68328 ; BamMC406_5891 .
    GeneIDi 6182474.
    KEGGi bac:BamMC406_5891.
    PATRICi 19042153. VBIBurAmb82852_6352.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BAMB398577:GH38-5979-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 sequence of chromosome 3 of Burkholderia ambifaria MC40-6."
      Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.
      , Ramette A., Konstantinidis K., Tiedje J., Richardson P.
      Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MC40-6Imported.

    Entry informationi

    Entry nameiB1Z3L5_BURA4
    AccessioniPrimary (citable) accession number: B1Z3L5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 42 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