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E8S8F1

- E8S8F1_MICSL

UniProt

E8S8F1 - E8S8F1_MICSL

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Micromonospora sp. (strain L5)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 24 (01 Oct 2014)
      Sequence version 1 (05 Apr 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 annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei310 – 3101Coenzyme AUniRule annotation
    Binding sitei386 – 3861Substrate; via nitrogen amideUniRule annotation
    Binding sitei507 – 5071SubstrateUniRule annotation
    Binding sitei522 – 5221SubstrateUniRule annotation
    Active sitei524 – 5241UniRule annotation
    Binding sitei530 – 5301Coenzyme AUniRule annotation
    Binding sitei533 – 5331SubstrateUniRule annotation
    Metal bindingi544 – 5441Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi546 – 5461Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi549 – 5491Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei595 – 5951Coenzyme 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

    BioCyciMSP648999:GHVN-411-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:ML5_0403Imported
    OrganismiMicromonospora sp. (strain L5)Imported
    Taxonomic identifieri648999 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeMicromonospora
    ProteomesiUP000008685: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei620 – 6201N6-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

    ProteinModelPortaliE8S8F1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni410 – 4156Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiAWIWYRD.

    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.

    E8S8F1-1 [UniParc]FASTAAdd to Basket

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    MSEALANLLN ETRQFPPPAE LAANANVTAE AYEEAAGDRL AFWERQAGRL    50
    AWAQPWEQVL DWSNAPFAKW FTGGRLNVAY NCLDRHVEAG LGDKVAIHWE 100
    GEPGDTRTVT YADLHKLTCQ AANALTELGV TAGDRVAIYL PMIPEAAVAM 150
    LACARIGATH SVVFGGFSAD ALTNRIQDAS AKVVITADGG FRRGKPSALK 200
    PTVDEAVANC PSVEHVLVVR RTGEEVAWSA KDHWWHETVE TASPEHEAQA 250
    FDAEHPLFIL YTSGTTARPK GILHTTGGYL TQTSYTTHAV FDLKPETDVY 300
    WCTADIGWVT GHSYIVYGPL SNGATQVMYE GTPDTPHKGR FWEVVDKYKV 350
    TILYTAPTLI RTMMKWGEDI PAGYDLSSLR LLGSVGEPIN PEAWIWYRQH 400
    VGRGELPVVD TWWQTETGAI MISPLPGVTE AKPGSAMSPL PGIVADVVDD 450
    QGQSVPNGGG GYLVLKEPWP SMLRTIWGDD NRFLETYWSR FGAGANTGDE 500
    WVYFAGDGAK KDDDGHIWLL GRVDDVMLVS GHNISTTEVE SALVSHPSVA 550
    EAAVVGATDP TTGQAIVAFA IPRGSAEISG DAGEQLIAEL RNHVAKTLGP 600
    IAKPRQIMLV PELPKTRSGK IMRRLLRDVA ENRSLGDVTT LQDSSVMELI 650
    SSGMSGGKSD ED 662
    Length:662
    Mass (Da):71,800
    Last modified:April 5, 2011 - v1
    Checksum:i31D50DC26ECEAAFB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002399 Genomic DNA. Translation: ADU05955.1.
    RefSeqiWP_013473573.1. NC_014815.1.
    YP_004080106.1. NC_014815.1.

    Genome annotation databases

    EnsemblBacteriaiADU05955; ADU05955; ML5_0403.
    GeneIDi10055885.
    KEGGimil:ML5_0403.
    PATRICi45268612. VBIMicSp154089_0413.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002399 Genomic DNA. Translation: ADU05955.1 .
    RefSeqi WP_013473573.1. NC_014815.1.
    YP_004080106.1. NC_014815.1.

    3D structure databases

    ProteinModelPortali E8S8F1.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADU05955 ; ADU05955 ; ML5_0403 .
    GeneIDi 10055885.
    KEGGi mil:ML5_0403.
    PATRICi 45268612. VBIMicSp154089_0413.

    Phylogenomic databases

    HOGENOMi HOG000229981.
    KOi K01895.
    OMAi AWIWYRD.

    Enzyme and pathway databases

    BioCyci MSP648999:GHVN-411-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: L5Imported.

    Entry informationi

    Entry nameiE8S8F1_MICSL
    AccessioniPrimary (citable) accession number: E8S8F1
    Entry historyi
    Integrated into UniProtKB/TrEMBL: April 5, 2011
    Last sequence update: April 5, 2011
    Last modified: October 1, 2014
    This is version 24 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