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B4EEM3

- B4EEM3_BURCJ

UniProt

B4EEM3 - B4EEM3_BURCJ

Protein

Acetyl-coenzyme A synthetase

Gene

acoE

Organism
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315))
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 (23 Sep 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 sitei317 – 3171Coenzyme AUniRule annotation
    Binding sitei397 – 3971Substrate; via nitrogen amideUniRule annotation
    Binding sitei512 – 5121SubstrateUniRule annotation
    Binding sitei528 – 5281SubstrateUniRule annotation
    Active sitei530 – 5301UniRule annotation
    Binding sitei536 – 5361Coenzyme AUniRule annotation
    Binding sitei539 – 5391SubstrateUniRule annotation
    Metal bindingi550 – 5501Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi552 – 5521Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi555 – 5551Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei600 – 6001Coenzyme 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

    BioCyciBCEN216591:GJI4-2332-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:acoEImported
    Synonyms:acsAUniRule annotation
    ORF Names:BCAL2284Imported
    OrganismiBurkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315))Imported
    Taxonomic identifieri216591 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
    ProteomesiUP000001035: Chromosome 1

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei625 – 6251N6-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

    STRINGi216591.BCAL2284.

    Structurei

    3D structure databases

    ProteinModelPortaliB4EEM3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni421 – 4266Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiAWLWYHN.
    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.

    B4EEM3-1 [UniParc]FASTAAdd to Basket

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    MSAIESVLHE TRQFAPPAAL EKTAAISGMP AYRALVAEAE QDYEGFWARL    50
    AREGLTWHKP FTKVLDERNA PFYTWFDDGE LNASYNCLDR HVEAGHGERV 100
    AVIFEADDGT VTRVTYADLL ARVSRFANAL KKRGIGKGDR VVIYIPMSIE 150
    GIVAMQACAR IGATHSVVFG GFSAKSLNER LVDVGAVALI TADEQARGGK 200
    TLPLKSIADE AIALGGCEAV KSVIVYRRTG GKIDWHADRD LWMHELVDGE 250
    SDRCEPTWVG AEHPLFILYT SGSTGKPKGV QHSTGGYLLW AAQTMKWTFD 300
    WKPDDVFWCT ADIGWVTGHT YITYGPLACG GTQVVFEGVP TYPDAGRFWK 350
    MIGDHKVTVF YTAPTAIRSL IKAAEADDKV HPKSYDLSSL RIIGTVGEPI 400
    NPEAWMWYHK HVGHERCPIV DTWWQTETGG HMITPLPGAT PTVPGSCTLP 450
    LPGITAAVVD ETGQDVPNGQ GGILVVKRPW PAMIRTIWGD PERFKKSYYP 500
    EELGGTLYLA GDGTVRDKET GYFTIMGRID DVLNVSGHRL GTMEIESALV 550
    SHELVAEAAV VGRPDDTTGE AVVAFVVLKR SRPEGDEAAA LAKTLRDWVG 600
    KQIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEAI TQDTSTLENP 650
    AILEQLTEVR 660
    Length:660
    Mass (Da):72,326
    Last modified:September 23, 2008 - v1
    Checksum:i1D3EA6C06B20F342
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM747720 Genomic DNA. Translation: CAR52585.1.
    RefSeqiYP_002231409.1. NC_011000.1.

    Genome annotation databases

    EnsemblBacteriaiCAR52585; CAR52585; BCAL2284.
    GeneIDi6932391.
    KEGGibcj:BCAL2284.
    PATRICi19076480. VBIBurCen118154_2384.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM747720 Genomic DNA. Translation: CAR52585.1 .
    RefSeqi YP_002231409.1. NC_011000.1.

    3D structure databases

    ProteinModelPortali B4EEM3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 216591.BCAL2284.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAR52585 ; CAR52585 ; BCAL2284 .
    GeneIDi 6932391.
    KEGGi bcj:BCAL2284.
    PATRICi 19076480. VBIBurCen118154_2384.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BCEN216591:GJI4-2332-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 BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610Imported.

    Entry informationi

    Entry nameiB4EEM3_BURCJ
    AccessioniPrimary (citable) accession number: B4EEM3
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 23, 2008
    Last sequence update: September 23, 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 proteome, Reference proteomeImported

    External Data

    Dasty 3