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A4F6L2

- A4F6L2_SACEN

UniProt

A4F6L2 - A4F6L2_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 sitei317 – 3171Coenzyme AUniRule annotation
    Binding sitei341 – 3411Coenzyme AUniRule annotation
    Binding sitei393 – 3931Substrate; via nitrogen amideUniRule annotation
    Binding sitei508 – 5081SubstrateUniRule annotation
    Binding sitei523 – 5231SubstrateUniRule annotation
    Active sitei525 – 5251UniRule annotation
    Binding sitei531 – 5311Coenzyme AUniRule annotation
    Binding sitei534 – 5341SubstrateUniRule annotation
    Metal bindingi545 – 5451Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi547 – 5471Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi550 – 5501Magnesium; 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

    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_0337Imported
    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 residuei620 – 6201N6-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_0337.

    Structurei

    3D structure databases

    ProteinModelPortaliA4F6L2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni417 – 4226Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiGGCEAVT.
    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.

    A4F6L2-1 [UniParc]FASTAAdd to Basket

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    MSEPDGQSNT LDNLLTESRT FPPSGEFAAQ ANATSELYAQ ADADREAFWA    50
    DQARHLHWDT EWEQVLDWSG APFAKWFVGG KLNVAYNCVD RHVEAGNGDR 100
    VAIHWEGEPG DSRAITYAEL AREVSRTANA LASLGVGAGD RVAIYLPMLP 150
    EAVYSMLACA RLGALHSVVF GGFSSEALRT RINDAQAKVV ITADGQYRRG 200
    KAMPLKTNVD EAVAATPSVE HVLVVQRTKT DVEWNDGRDQ WWHDVVEGRP 250
    ASHTPEFFDS EHPLFILYTS GTTGRPKGIL HTSGGYLTQA AYTHRTVFDL 300
    KPETDVYWCT ADIGWVTGHT YIVYGPLANG ATQVIYEGTP NTPHEGRHWD 350
    IVQKYGVTLY YTAPTTIRTF MKWGAEIPAR YDLSTLRVLG SVGEPINPEA 400
    WMWYREHIGG NRAPIVDTWW QTETGAIMIS PLPGVTATKP GSAQVPLPGI 450
    AAKVVDESGE QVGHGGGGLL VLDQPWPAML RGIWGDDDRY RETYWSKFAD 500
    KGYYFAGDGA KYDDDGDIWL LGRVDDVMNV SGHRISTTEV ESALVSHPTV 550
    AEAAVVGASD PTTGQGIVAF VILRGGADDQ ASGEAAIKAL RDHVAHEIGP 600
    IAKPRQIMVV PELPKTRSGK IMRRLLRDVA ENREIGDVST LADSSVMDLI 650
    SAGLGKSTED 660
    Length:660
    Mass (Da):72,043
    Last modified:April 17, 2007 - v1
    Checksum:iF986E6A54DAD71C8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM420293 Genomic DNA. Translation: CAL99686.1.
    RefSeqiWP_011873025.1. NC_009142.1.
    YP_001102612.1. NC_009142.1.

    Genome annotation databases

    EnsemblBacteriaiCAL99686; CAL99686; SACE_0337.
    GeneIDi4940204.
    KEGGisen:SACE_0337.
    PATRICi23408036. VBISacEry28377_0340.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM420293 Genomic DNA. Translation: CAL99686.1 .
    RefSeqi WP_011873025.1. NC_009142.1.
    YP_001102612.1. NC_009142.1.

    3D structure databases

    ProteinModelPortali A4F6L2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405948.SACE_0337.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL99686 ; CAL99686 ; SACE_0337 .
    GeneIDi 4940204.
    KEGGi sen:SACE_0337.
    PATRICi 23408036. VBISacEry28377_0340.

    Phylogenomic databases

    eggNOGi COG0365.
    HOGENOMi HOG000229981.
    KOi K01895.
    OMAi GGCEAVT.
    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 nameiA4F6L2_SACEN
    AccessioniPrimary (citable) accession number: A4F6L2
    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