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D7A5Y5

- D7A5Y5_STAND

UniProt

D7A5Y5 - D7A5Y5_STAND

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 30 (01 Oct 2014)
      Sequence version 1 (10 Aug 2010)
      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 sitei310 – 3101Coenzyme AUniRule annotation
    Binding sitei334 – 3341Coenzyme AUniRule annotation
    Binding sitei386 – 3861Substrate; via nitrogen amideUniRule annotation
    Binding sitei499 – 4991SubstrateUniRule annotation
    Binding sitei514 – 5141SubstrateUniRule annotation
    Active sitei516 – 5161UniRule annotation
    Binding sitei522 – 5221Coenzyme AUniRule annotation
    Binding sitei525 – 5251SubstrateUniRule annotation
    Metal bindingi536 – 5361Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi541 – 5411Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei583 – 5831Coenzyme 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

    BioCyciSNOV639283:GCS4-2845-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:Snov_2812Imported
    OrganismiStarkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113)Imported
    Taxonomic identifieri639283 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeStarkeya
    ProteomesiUP000006633: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei608 – 6081N6-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

    ProteinModelPortaliD7A5Y5.
    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.
    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.

    D7A5Y5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDKIYDVPA EWAKRAFLNE HAYRAKYEAS VRDTEGFWAE EGKRIEWFEP    50
    YTIVKNTSYD PGHVSIKWFE DGVTNVAWNC IDRHLPRLAD QTAIIWEGDD 100
    PSQSRHITYQ ELHDEVCRFA NVLRNRNVEK GDRVTIYMPM IPEAAYAMLA 150
    CARLGAIHSV VFGGFSPDSL AGRIRDCGSK VIITADEGLR GGRKVPLKAN 200
    VDAAIAKVSD VEIDHVIVVK RTGGEVDMKP GRDVWYHQAA DLVTSECPAV 250
    PMNAEDPLFI LYTSGSTGLP KGVLHTTGGY LVYASMTHQY VFDYHDGDVY 300
    WCTADIGWVT GHSYIVYGPL ANGATTLMFE GVPNYPSNSR FWEVIDKHKV 350
    NIFYTAPTAI RALMQAGDEP VKKTSRASLR LLGSVGEPIN PEAWEWYHRV 400
    VGEDRCPIVD TWWQTETGGI LITPLPGATR LKPGSATQPF FGVIPQVVDA 450
    EGRVLEGACE GNLVIADSWP GQMRTVYGDH ERFMQTYFAT YPGKYFTGDG 500
    CRRDSDGYYW ITGRVDDVIN VSGHRMGTAE VESALVAHPK VSEAAVVGYP 550
    HDIKGQGIYA YVTLMAGAEP TEELRKELVA WVRREIGPIA SPDLIQFAPS 600
    LPKTRSGKIM RRILRKIAED EFGNLGDTST LADPTVVQDL ISQRQNKKHA 650
    AA 652
    Length:652
    Mass (Da):72,499
    Last modified:August 10, 2010 - v1
    Checksum:i1A1A1258EB1694A6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002026 Genomic DNA. Translation: ADH90100.1.
    RefSeqiWP_013167604.1. NC_014217.1.
    YP_003694719.1. NC_014217.1.

    Genome annotation databases

    EnsemblBacteriaiADH90100; ADH90100; Snov_2812.
    GeneIDi9333895.
    KEGGisno:Snov_2812.
    PATRICi38258209. VBIStaNov45716_2813.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002026 Genomic DNA. Translation: ADH90100.1 .
    RefSeqi WP_013167604.1. NC_014217.1.
    YP_003694719.1. NC_014217.1.

    3D structure databases

    ProteinModelPortali D7A5Y5.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADH90100 ; ADH90100 ; Snov_2812 .
    GeneIDi 9333895.
    KEGGi sno:Snov_2812.
    PATRICi 38258209. VBIStaNov45716_2813.

    Phylogenomic databases

    HOGENOMi HOG000229981.
    KOi K01895.
    OMAi AWIWYRD.

    Enzyme and pathway databases

    BioCyci SNOV639283:GCS4-2845-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 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113Imported.

    Entry informationi

    Entry nameiD7A5Y5_STAND
    AccessioniPrimary (citable) accession number: D7A5Y5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: August 10, 2010
    Last sequence update: August 10, 2010
    Last modified: October 1, 2014
    This is version 30 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