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Q98ET8

- ACSA_RHILO

UniProt

Q98ET8 - ACSA_RHILO

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Oct 2001)
      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 sitei312 – 3121Coenzyme AUniRule annotation
    Binding sitei336 – 3361Coenzyme AUniRule annotation
    Binding sitei501 – 5011ATPUniRule annotation
    Binding sitei516 – 5161ATPUniRule annotation
    Binding sitei524 – 5241Coenzyme A; via carbonyl oxygenUniRule annotation
    Binding sitei527 – 5271ATPUniRule annotation
    Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi543 – 5431Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei585 – 5851Coenzyme AUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi388 – 3903ATPUniRule annotation
    Nucleotide bindingi412 – 4176ATPUniRule 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

    Ligase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMLOT266835:GJ9L-3186-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:mlr4089
    OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
    Taxonomic identifieri266835 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
    ProteomesiUP000000552: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 651651Acetyl-coenzyme A synthetasePRO_0000208380Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei610 – 6101N6-acetyllysineUniRule annotation

    Post-translational modificationi

    Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.UniRule annotation

    Keywords - PTMi

    Acetylation

    Interactioni

    Protein-protein interaction databases

    STRINGi266835.mlr4089.

    Structurei

    3D structure databases

    ProteinModelPortaliQ98ET8.
    SMRiQ98ET8. Positions 5-647.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni190 – 1934Coenzyme A bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiQTAILFE.
    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.

    Q98ET8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEVHVHRVQ PAWKKNALID NDTYLKWYAD SIKNPDKFWG KHGKRIDWFK    50
    PFSKVKNTSF DGKVSIKWFE DGLTNVSYNC IDRHLKKRGD QTAIIWEGDN 100
    PYDDKKITYN ELYERVCRLA NVMKKHGVKK GDRVTIYMPM IPEAAYAMLA 150
    CTRIGAIHSI VFGGFSPDAL AGRIVDCEST FVITADEGLR GGKSIPLKEN 200
    TDKAIDIAAK NFVMVKNVLV VRRTGGKVGW APGRDLWYHD EVATVKAECK 250
    PEKMKAEDPL FILYTSGSTG KPKGVLHTTA GYLVYASMTH QYVFDYHDGD 300
    IYWCTADVGW VTGHSYIVYG PLANGATTLM FEGVPNYPSQ SRFWEVIDKH 350
    KVNIFYTAPT ALRALMGAGN DPVKKTSRKS LRVLGSVGEP INPEAWEWYF 400
    NVVGNGKVPI VDTWWQTETG GILITPLPGA TDLKAGSATR PFFGVKPQLV 450
    DGEGKVLEGA ADGNLCITDS WPGQMRTVYG DHDRFVQTYF STYKGKYFTG 500
    DGCRRDADGY YWITGRVDDV INVSGHRMGT AEVESALVSH DKVSEAAVVG 550
    YPHDIKGQGI YSYVTLMKGE EPTEDLRKEL IAHVRKEIGA IASPDKIQFA 600
    PGLPKTRSGK IMRRILRKIA EDDFSTLGDT STLADPAVVD DLIANRQNKK 650
    G 651
    Length:651
    Mass (Da):72,530
    Last modified:October 1, 2001 - v1
    Checksum:iC7A0AC5011C4D43F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000012 Genomic DNA. Translation: BAB50829.1.
    RefSeqiNP_105043.1. NC_002678.2.

    Genome annotation databases

    EnsemblBacteriaiBAB50829; BAB50829; BAB50829.
    GeneIDi1227704.
    KEGGimlo:mlr4089.
    PATRICi22480693. VBIMesLot2464_3234.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000012 Genomic DNA. Translation: BAB50829.1 .
    RefSeqi NP_105043.1. NC_002678.2.

    3D structure databases

    ProteinModelPortali Q98ET8.
    SMRi Q98ET8. Positions 5-647.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266835.mlr4089.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB50829 ; BAB50829 ; BAB50829 .
    GeneIDi 1227704.
    KEGGi mlo:mlr4089.
    PATRICi 22480693. VBIMesLot2464_3234.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci MLOT266835:GJ9L-3186-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: MAFF303099.

    Entry informationi

    Entry nameiACSA_RHILO
    AccessioniPrimary (citable) accession number: Q98ET8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3