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Q01NE9

- Q01NE9_SOLUE

UniProt

Q01NE9 - Q01NE9_SOLUE

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Solibacter usitatus (strain Ellin6076)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (14 Nov 2006)
      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 sitei307 – 3071Coenzyme AUniRule annotation
    Binding sitei383 – 3831Substrate; via nitrogen amideUniRule annotation
    Binding sitei496 – 4961SubstrateUniRule annotation
    Binding sitei511 – 5111SubstrateUniRule annotation
    Active sitei513 – 5131UniRule annotation
    Binding sitei519 – 5191Coenzyme AUniRule annotation
    Binding sitei522 – 5221SubstrateUniRule annotation
    Metal bindingi533 – 5331Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi535 – 5351Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei580 – 5801Coenzyme 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

    BioCyciSUSI234267:GHSK-7980-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:Acid_7927Imported
    OrganismiSolibacter usitatus (strain Ellin6076)Imported
    Taxonomic identifieri234267 [NCBI]
    Taxonomic lineageiBacteriaAcidobacteriaSolibacteresSolibacteralesSolibacteraceaeCandidatus Solibacter
    ProteomesiUP000000671: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei605 – 6051N6-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

    STRINGi234267.Acid_7927.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01NE9.
    SMRiQ01NE9. Positions 10-617.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni407 – 4126Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiAWIWYRD.
    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.

    Q01NE9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADANVYPPS AEFVSTANVK GMAGYRALYQ RAAEKPEEFW GELADQELHW    50
    FRKWTHVFEW DPPFAKWFAG GKINASYNCI DRHLSTPRKN KVAILWEGEP 100
    GDQRMITYQE LHRLVCRFAN VLKARGLKAG DRAIIYMGMV PELPVAVLAC 150
    ARLGIIHSVV FGGFSAEALK ARIQDLEAQV VITCDGAWRR GKEVRLKDAV 200
    DESLAGCDTV KDVIVYRRTG GSIPMQEGRD HWWHDLDTEA SEVCPAEELD 250
    SEHPLYVLYT SGTTGKPKGI VHTTGGYLLQ AHMTMKWVFD LHEEDTYWCT 300
    ADIGWVTGHS YIVYGPLSAG ATSVMYEGAP DFPQPDRFWR LIEKYKVNIF 350
    YTSPTAIRSF VRQGDQWPNA HDMSSLRLLG SVGEPINPAA WEWYYKVIGK 400
    ERCPIVDTWW QTETGAIMIA PMPGAVPLKP GSGTLPLPGV IADIVDLQGN 450
    PVEANREGFL IVRRPWPSIA RTLWREPDRY KQAYWERVPG VYLAGDAARR 500
    DEDGYFWILG RVDDVMNVSG HRLSTMELES ALVRHPAVAE AAVVGKPHEI 550
    TGQAVACFVT LKKGTWDHTA LAEELRKWVA HEIGSFAKPE QIRFTDSLPK 600
    TRSGKIMRRL LREIVTSNSV TGDVTTLEDL SVVTRLSAQH DED 643
    Length:643
    Mass (Da):72,281
    Last modified:November 14, 2006 - v1
    Checksum:i207212BA2B0D0D0E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000473 Genomic DNA. Translation: ABJ88821.1.
    RefSeqiYP_829106.1. NC_008536.1.

    Genome annotation databases

    EnsemblBacteriaiABJ88821; ABJ88821; Acid_7927.
    GeneIDi4424186.
    KEGGisus:Acid_7927.
    PATRICi32018658. VBICanSol30224_8273.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000473 Genomic DNA. Translation: ABJ88821.1 .
    RefSeqi YP_829106.1. NC_008536.1.

    3D structure databases

    ProteinModelPortali Q01NE9.
    SMRi Q01NE9. Positions 10-617.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 234267.Acid_7927.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABJ88821 ; ABJ88821 ; Acid_7927 .
    GeneIDi 4424186.
    KEGGi sus:Acid_7927.
    PATRICi 32018658. VBICanSol30224_8273.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SUSI234267:GHSK-7980-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: Ellin6076Imported.

    Entry informationi

    Entry nameiQ01NE9_SOLUE
    AccessioniPrimary (citable) accession number: Q01NE9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 14, 2006
    Last sequence update: November 14, 2006
    Last modified: October 1, 2014
    This is version 52 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