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A4FCA0

- A4FCA0_SACEN

UniProt

A4FCA0 - A4FCA0_SACEN

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Saccharopolyspora erythraea (strain NRRL 23338)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (17 Apr 2007)
      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 sitei325 – 3251Coenzyme AUniRule annotation
    Binding sitei349 – 3491Coenzyme AUniRule annotation
    Binding sitei401 – 4011Substrate; via nitrogen amideUniRule annotation
    Binding sitei516 – 5161SubstrateUniRule annotation
    Binding sitei531 – 5311SubstrateUniRule annotation
    Active sitei533 – 5331UniRule annotation
    Binding sitei539 – 5391Coenzyme AUniRule annotation
    Binding sitei542 – 5421SubstrateUniRule annotation
    Metal bindingi553 – 5531Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi555 – 5551Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi558 – 5581Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei603 – 6031Coenzyme 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

    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:SACE_2375Imported
    OrganismiSaccharopolyspora erythraea (strain NRRL 23338)Imported
    Taxonomic identifieri405948 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora
    ProteomesiUP000006728: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei628 – 6281N6-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

    STRINGi405948.SACE_2375.

    Structurei

    3D structure databases

    ProteinModelPortaliA4FCA0.
    SMRiA4FCA0. Positions 29-641.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni425 – 4306Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiKMEHLRI.
    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.

    A4FCA0-1 [UniParc]FASTAAdd to Basket

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    MSSKRVERLE VGKHSQNTLD NLLHEERIHA PSGEFAAQAN ATSELYAQAD    50
    ADREAFWADQ ARHLHWDTEW EQVLDWSGAP FAKWFVGGKL NVAYNCVDRH 100
    VEAGNGDRVA IHWEGEPGDS RAITYAELAR EVSRTANALA SLGVGAGDRV 150
    AIYLPMLPEA VYSMLACARL GALHSVVFGG FSSEALRTRI NDAQAKVVIT 200
    ADGQYRRGKA MPLKTNVDEA VAATPSVEHV LVVQRTKTDV EWNDGRDQWW 250
    HDVVEGRPAS HTPEFFDSEH PLFILYTSGT TGRPKGILHT SGGYLTQAAY 300
    THRTVFDLKP ETDVYWCTAD IGWVTGHTYI VYGPLANGAT QVIYEGTPNT 350
    PHEGRHWDIV QKYGVTLYYT APTTIRTFMK WGAEIPARYD LSTLRVLGSV 400
    GEPINPEAWM WYREHIGGNR APIVDTWWQT ETGAIMISPL PGVTATKPGS 450
    AQVPLPGIAA KVVDESGEQV GHGGGGLLVL DQPWPAMLRG IWGDDDRYRE 500
    TYWSKFADKG YYFAGDGAKY DDDGDIWLLG RVDDVMNVSG HRISTTEVES 550
    ALVSHPTVAE AAVVGASDPT TGQGIVAFVI LRGGADDQAS GEAAIKALRD 600
    HVAHEIGPIA KPRQIMVVPE LPKTRSGKIM RRLLRDVAEN REIGDVSTLA 650
    DSSVMNLISA GFATSSDD 668
    Length:668
    Mass (Da):73,110
    Last modified:April 17, 2007 - v1
    Checksum:iC7663AB223D18862
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM420293 Genomic DNA. Translation: CAM01675.1.
    RefSeqiWP_011873661.1. NC_009142.1.
    YP_001104600.1. NC_009142.1.

    Genome annotation databases

    EnsemblBacteriaiCAM01675; CAM01675; SACE_2375.
    GeneIDi4942224.
    KEGGisen:SACE_2375.
    PATRICi23412162. VBISacEry28377_2375.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM420293 Genomic DNA. Translation: CAM01675.1 .
    RefSeqi WP_011873661.1. NC_009142.1.
    YP_001104600.1. NC_009142.1.

    3D structure databases

    ProteinModelPortali A4FCA0.
    SMRi A4FCA0. Positions 29-641.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405948.SACE_2375.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAM01675 ; CAM01675 ; SACE_2375 .
    GeneIDi 4942224.
    KEGGi sen:SACE_2375.
    PATRICi 23412162. VBISacEry28377_2375.

    Phylogenomic databases

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

    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. "Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
      Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
      Nat. Biotechnol. 25:447-453(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NRRL 23338Imported.

    Entry informationi

    Entry nameiA4FCA0_SACEN
    AccessioniPrimary (citable) accession number: A4FCA0
    Entry historyi
    Integrated into UniProtKB/TrEMBL: April 17, 2007
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 51 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