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P39979 (HPA3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-amino-acid N-acetyltransferase HPA3

Short name=DNT
EC=2.3.1.36
Alternative name(s):
Histone and other protein acetyltransferase 3
Gene names
Name:HPA3
Ordered Locus Names:YEL066W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.7

Catalytic activity

Acetyl-CoA + a D-amino acid = CoA + an N-acetyl-D-amino acid. Ref.6

Subcellular location

Cytoplasm. Nucleus Ref.4.

Post-translational modification

Autoacetylates. Ref.3

Miscellaneous

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

Sequence similarities

Belongs to the acetyltransferase family. GNAT subfamily.

Contains 1 N-acetyltransferase domain.

Biophysicochemical properties

Kinetic parameters:

KM=34 mM for D-Serine Ref.6

KM=54 mM for D-Alanine

Vmax=22 µmol/min/mg enzyme toward D-Serine

Vmax=18 µmol/min/mg enzyme toward D-Alanine

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 179179D-amino-acid N-acetyltransferase HPA3
PRO_0000074634

Regions

Domain32 – 179148N-acetyltransferase
Region116 – 12914Acetyl-CoA binding By similarity

Sites

Site1621Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P39979 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 53A18264798045DD

FASTA17920,699
        10         20         30         40         50         60 
MKKTPDPSPP FASTKNVGMS NEEPEKMVND RIVVKAIEPK DEEAWNKLWK EYQGFQKTVM 

        70         80         90        100        110        120 
PPEVATTTFA RFIDPTVKLW GALAFDTETG DAIGFAHYLN HLTSWHVEEV VYMNDLYVTE 

       130        140        150        160        170 
RARVKGVGRK LIEFVYSRAD ELGTPAVYWV TDHYNHRAQL LYTKVAYKTD KVLYKRNGY 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18795 Genomic DNA. Translation: AAB65021.1.
BK006939 Genomic DNA. Translation: DAA07588.1.
PIRS50523.
RefSeqNP_010848.1. NM_001178881.1.

3D structure databases

ProteinModelPortalP39979.
SMRP39979. Positions 30-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36663. 17 interactions.
DIPDIP-2063N.
IntActP39979. 3 interactions.
MINTMINT-492186.
STRING4932.YEL066W.

Proteomic databases

PaxDbP39979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL066W; YEL066W; YEL066W.
GeneID856642.
KEGGsce:YEL066W.

Organism-specific databases

CYGDYEL066w.
SGDS000000792. HPA3.

Phylogenomic databases

eggNOGCOG0454.
GeneTreeENSGT00390000015620.
HOGENOMHOG000078521.
OMAVHFLYHR.
OrthoDBEOG7X3R3Q.

Enzyme and pathway databases

BioCycYEAST:G3O-30181-MONOMER.

Gene expression databases

GenevestigatorP39979.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982604.

Entry information

Entry nameHPA3_YEAST
AccessionPrimary (citable) accession number: P39979
Secondary accession number(s): D3DLI4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 19, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families