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P39979

- HPA3_YEAST

UniProt

P39979 - HPA3_YEAST

Protein

D-amino-acid N-acetyltransferase HPA3

Gene

HPA3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    N-acetyltransferase which acts on a wide range of D-amino acids but shows extremely low activity toward histone. Catalyzes the N-acetylation of D-amino acids through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated. D-amino acids are toxic for the cell and their N-acetylation, preceding removal from cells, plays an important role in detoxification of D-amino acids.2 Publications

    Catalytic activityi

    Acetyl-CoA + a D-amino acid = CoA + an N-acetyl-D-amino acid.1 Publication

    Kineticsi

    1. KM=34 mM for D-Serine1 Publication
    2. KM=54 mM for D-Alanine1 Publication

    Vmax=22 µmol/min/mg enzyme toward D-Serine1 Publication

    Vmax=18 µmol/min/mg enzyme toward D-Alanine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei162 – 1621Important for catalytic activityBy similarity

    GO - Molecular functioni

    1. D-amino-acid N-acetyltransferase activity Source: SGD

    GO - Biological processi

    1. cellular detoxification of nitrogen compound Source: SGD
    2. D-amino acid metabolic process Source: SGD

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30181-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-amino-acid N-acetyltransferase HPA3 (EC:2.3.1.36)
    Short name:
    DNT
    Alternative name(s):
    Histone and other protein acetyltransferase 3
    Gene namesi
    Name:HPA3
    Ordered Locus Names:YEL066W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYEL066w.
    SGDiS000000792. HPA3.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 179179D-amino-acid N-acetyltransferase HPA3PRO_0000074634Add
    BLAST

    Post-translational modificationi

    Autoacetylates.

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP39979.
    PaxDbiP39979.

    Expressioni

    Gene expression databases

    GenevestigatoriP39979.

    Interactioni

    Protein-protein interaction databases

    BioGridi36663. 17 interactions.
    DIPiDIP-2063N.
    IntActiP39979. 3 interactions.
    MINTiMINT-492186.
    STRINGi4932.YEL066W.

    Structurei

    3D structure databases

    ProteinModelPortaliP39979.
    SMRiP39979. Positions 30-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 179148N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni116 – 12914Acetyl-CoA bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0454.
    GeneTreeiENSGT00390000015620.
    HOGENOMiHOG000078521.
    OMAiVHFLYHR.
    OrthoDBiEOG7X3R3Q.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view]
    PfamiPF00583. Acetyltransf_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39979-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKTPDPSPP FASTKNVGMS NEEPEKMVND RIVVKAIEPK DEEAWNKLWK    50
    EYQGFQKTVM PPEVATTTFA RFIDPTVKLW GALAFDTETG DAIGFAHYLN 100
    HLTSWHVEEV VYMNDLYVTE RARVKGVGRK LIEFVYSRAD ELGTPAVYWV 150
    TDHYNHRAQL LYTKVAYKTD KVLYKRNGY 179
    Length:179
    Mass (Da):20,699
    Last modified:February 1, 1995 - v1
    Checksum:i53A18264798045DD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18795 Genomic DNA. Translation: AAB65021.1.
    BK006939 Genomic DNA. Translation: DAA07588.1.
    PIRiS50523.
    RefSeqiNP_010848.1. NM_001178881.1.

    Genome annotation databases

    EnsemblFungiiYEL066W; YEL066W; YEL066W.
    GeneIDi856642.
    KEGGisce:YEL066W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18795 Genomic DNA. Translation: AAB65021.1 .
    BK006939 Genomic DNA. Translation: DAA07588.1 .
    PIRi S50523.
    RefSeqi NP_010848.1. NM_001178881.1.

    3D structure databases

    ProteinModelPortali P39979.
    SMRi P39979. Positions 30-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36663. 17 interactions.
    DIPi DIP-2063N.
    IntActi P39979. 3 interactions.
    MINTi MINT-492186.
    STRINGi 4932.YEL066W.

    Proteomic databases

    MaxQBi P39979.
    PaxDbi P39979.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YEL066W ; YEL066W ; YEL066W .
    GeneIDi 856642.
    KEGGi sce:YEL066W.

    Organism-specific databases

    CYGDi YEL066w.
    SGDi S000000792. HPA3.

    Phylogenomic databases

    eggNOGi COG0454.
    GeneTreei ENSGT00390000015620.
    HOGENOMi HOG000078521.
    OMAi VHFLYHR.
    OrthoDBi EOG7X3R3Q.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30181-MONOMER.

    Miscellaneous databases

    NextBioi 982604.

    Gene expression databases

    Genevestigatori P39979.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view ]
    Pfami PF00583. Acetyltransf_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    PROSITEi PS51186. GNAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily."
      Angus-Hill M.L., Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V.
      J. Mol. Biol. 294:1311-1325(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACETYLATION SUBSTRATE.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "D-amino acid N-acetyltransferase of Saccharomyces cerevisiae: a close homologue of histone acetyltransferase Hpa2p acting exclusively on free D-amino acids."
      Yow G.Y., Uo T., Yoshimura T., Esaki N.
      Arch. Microbiol. 182:396-403(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "Physiological role of D-amino acid-N-acetyltransferase of Saccharomyces cerevisiae: detoxification of D-amino acids."
      Yow G.Y., Uo T., Yoshimura T., Esaki N.
      Arch. Microbiol. 185:39-46(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHPA3_YEAST
    AccessioniPrimary (citable) accession number: P39979
    Secondary accession number(s): D3DLI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1200 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3