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E4NDX1

- E4NDX1_KITSK

UniProt

E4NDX1 - E4NDX1_KITSK

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / KM-6054) (Streptomyces setae)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 22 (01 Oct 2014)
      Sequence version 1 (08 Feb 2011)
      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 sitei312 – 3121Coenzyme AUniRule annotation
    Binding sitei388 – 3881Substrate; via nitrogen amideUniRule annotation
    Binding sitei501 – 5011SubstrateUniRule annotation
    Binding sitei516 – 5161SubstrateUniRule annotation
    Active sitei518 – 5181UniRule annotation
    Binding sitei524 – 5241Coenzyme AUniRule annotation
    Binding sitei527 – 5271SubstrateUniRule 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

    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

    BioCyciKSET452652:GJFD-3594-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:KSE_35980Imported
    OrganismiKitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / KM-6054) (Streptomyces setae)Imported
    Taxonomic identifieri452652 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeKitasatospora
    ProteomesiUP000007076: Chromosome

    PTM / Processingi

    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

    AcetylationUniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliE4NDX1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni412 – 4176Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01895.
    OMAiAWIWYRD.

    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.

    E4NDX1-1 [UniParc]FASTAAdd to Basket

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    MSNESLANLL KEERRFAPPA ELAASANVTA DAYAQASEDR LAFWAEQARR    50
    LSWAVEPTET LDWSNPPFAK WFADGKLNVA YNCVDRHVEA GNGDRVAIHF 100
    EGEPGDSRAI TYAQLKDEVS KAANALESLG VAKGDRVAVY LPMIPEAVVA 150
    MLACARIGAA HSVVFGGFSA DAVASRIKDA DAKLVITADG GYRRGKPSAL 200
    KPAIDEALTK VDGVENVLVV RRTGEEVAWT EGRDVWWHEL VDGQSAEHTP 250
    EAHDAEQPLF ILYTSGTTGK PKGILHTSGG YLTQASFTHN AVFDLKPETD 300
    VYWCTADIGW VTGHSYIVYG PLSNGATQVI YEGTPDTPHQ GRMFEIVQKY 350
    GVTILYTAPT LIRTWMKWGD DIPAGFDLSS LRVLGSVGEP INPEAWVWYR 400
    EHIGAGKTPI VDTWWQTETG AIMISPLPGV TETKPGSAQR ALPGIAATVV 450
    DDEAREVPNG SGGYLVLTEP WPSMLRTIWG DDERYVDTYW SRFEGRYFAG 500
    DGAKKDEDGD IWLLGRVDDV MLVSGHNIST TEVESALVGH PAVAESAVVG 550
    AADATTGQAI VAFVILRGTA ADSEELIADL RNHVGKTLGP IAKPKQIKVV 600
    SELPKTRSGK IMRRLLRDIA EGREVGDTTT LADSSVMNLI QSQLPAAGAE 650
    G 651
    Length:651
    Mass (Da):70,350
    Last modified:February 8, 2011 - v1
    Checksum:i227EFC38369A670D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP010968 Genomic DNA. Translation: BAJ29402.1.
    RefSeqiYP_004905358.1. NC_016109.1.

    Genome annotation databases

    EnsemblBacteriaiBAJ29402; BAJ29402; KSE_35980.
    GeneIDi11348269.
    KEGGiksk:KSE_35980.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP010968 Genomic DNA. Translation: BAJ29402.1 .
    RefSeqi YP_004905358.1. NC_016109.1.

    3D structure databases

    ProteinModelPortali E4NDX1.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAJ29402 ; BAJ29402 ; KSE_35980 .
    GeneIDi 11348269.
    KEGGi ksk:KSE_35980.

    Phylogenomic databases

    KOi K01895.
    OMAi AWIWYRD.

    Enzyme and pathway databases

    BioCyci KSET452652:GJFD-3594-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 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / KM-6054Imported.

    Entry informationi

    Entry nameiE4NDX1_KITSK
    AccessioniPrimary (citable) accession number: E4NDX1
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 8, 2011
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 22 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