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I4ERQ3

- I4ERQ3_MODMB

UniProt

I4ERQ3 - I4ERQ3_MODMB

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Modestobacter marinus (strain BC501)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 12 (01 Oct 2014)
      Sequence version 1 (05 Sep 2012)
      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 sitei313 – 3131Coenzyme AUniRule annotation
    Binding sitei389 – 3891Substrate; via nitrogen amideUniRule annotation
    Binding sitei503 – 5031SubstrateUniRule annotation
    Binding sitei518 – 5181SubstrateUniRule annotation
    Active sitei520 – 5201UniRule annotation
    Binding sitei526 – 5261Coenzyme AUniRule annotation
    Binding sitei529 – 5291SubstrateUniRule annotation
    Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi545 – 5451Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei588 – 5881Coenzyme 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

    BioCyciMMAR477641:GLGK-607-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 annotationImported
    Ordered Locus Names:MODMU_0609Imported
    OrganismiModestobacter marinus (strain BC501)Imported
    Taxonomic identifieri1144889 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeGeodermatophilaceaeModestobacter
    ProteomesiUP000006461: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei613 – 6131N6-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

    ProteinModelPortaliI4ERQ3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni413 – 4186Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01895.

    Family and domain databases

    HAMAPiMF_01123. Ac_CoA_synth.
    InterProiIPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    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.

    Sequencei

    Sequence statusi: Complete.

    I4ERQ3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSETTEAHGL TNPEGGFPPP EALAAAANVG PDVYDRAAAD RVGFWEEAAR    50
    RLDWAQPWDQ ALDWSNPPFA KWFVGGKLNV AVNCVDRHVD AGHGDQVAYH 100
    WIGEPGDTRT LTYAQLKDEV CKAANALVEL GVQAGDRVAI YLPMIPEAVV 150
    AMLACARIGA VHMVVFGGFS PDALASRITD ADAKVVITAD GGYRRGAPSA 200
    LKPNVDEALT KTEGVRSVLV VRRTETDVEW TEGRDVWWHE LVDRQPAEHE 250
    AEAFDAEHPL YIMYTSGTTA KPKGILHTTG GYLTQVSYSH WAVFDIKPDT 300
    DVFWTAADVG WVTGHSYIVY GPLSNRTTSV MYEGTPETPH RGRWWEIVQE 350
    YGVTVLYTAP TTIRTFMKWG EDVPAGFDLS SLRLLGSVGE PINPEAWLWY 400
    HTHIGGGRCP IVDTWWQTET GAHMITPLPA VTTLKPGSAQ RPLPGIAASV 450
    VDEEGKPIEP GATGYLVLTE PWPAMLRTIW GDDDRYVDTY WSRYGQGVYF 500
    AGDGAKLDED GDIWLLGRVD DVMNVSGHRI STTEVESALV SHPTVAEAAV 550
    VGATDPTTGQ GIVAFVILRG DAVDSGEDLV KTLRQHVRKE IGPIASPRQI 600
    MVVAELPKTR SGKIMRRLLR DVAENRELGD VTTLTDSSVM ELISSKLPSS 650
    ASED 654
    Length:654
    Mass (Da):71,418
    Last modified:September 5, 2012 - v1
    Checksum:i51ECCF44189295FF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FO203431 Genomic DNA. Translation: CCH86066.1.
    RefSeqiYP_006364565.1. NC_017955.1.

    Genome annotation databases

    EnsemblBacteriaiCCH86066; CCH86066; MODMU_0609.
    GeneIDi13007694.
    KEGGimmar:MODMU_0609.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FO203431 Genomic DNA. Translation: CCH86066.1 .
    RefSeqi YP_006364565.1. NC_017955.1.

    3D structure databases

    ProteinModelPortali I4ERQ3.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCH86066 ; CCH86066 ; MODMU_0609 .
    GeneIDi 13007694.
    KEGGi mmar:MODMU_0609.

    Phylogenomic databases

    KOi K01895.

    Enzyme and pathway databases

    BioCyci MMAR477641:GLGK-607-MONOMER.

    Family and domain databases

    HAMAPi MF_01123. Ac_CoA_synth.
    InterProi IPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of radiation-resistant Modestobacter marinus strain BC501, a representative Actinobacterium that thrives on calcareous stone surfaces."
      Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L., Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A., Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.
      J. Bacteriol. 194:4773-4774(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: BC501Imported.

    Entry informationi

    Entry nameiI4ERQ3_MODMB
    AccessioniPrimary (citable) accession number: I4ERQ3
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 5, 2012
    Last sequence update: September 5, 2012
    Last modified: October 1, 2014
    This is version 12 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