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Protein

D-amino-acid N-acetyltransferase HPA3

Gene

HPA3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

N-acetyltransferase that acetylates histone H4 at 'Lys-8'. Also acetylates polyamines like putrescine, spermidine and spermine (PubMed:23775086). Acts on a wide range of D-amino acids. Catalyzes the N-acetylation 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 (PubMed:15375647). 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 (PubMed:10600387, PubMed:16362288).4 Publications

Catalytic activityi

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

Kineticsi

  1. KM=34 mM for D-Serine1 Publication
  2. KM=54 mM for D-Alanine1 Publication
  1. Vmax=22 µmol/min/mg enzyme toward D-Serine1 Publication
  2. Vmax=18 µmol/min/mg enzyme toward D-Alanine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei144 – 1441Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular detoxification of nitrogen compound Source: SGD
  • D-amino acid metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:G3O-30181-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
D-amino-acid N-acetyltransferase HPA31 Publication (EC:2.3.1.361 Publication, EC:2.3.1.481 Publication)
Short name:
DNT
Alternative name(s):
Histone and other protein acetyltransferase 31 Publication
Gene namesi
Name:HPA31 Publication
Ordered Locus Names:YEL066WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL066W.
SGDiS000000792. HPA3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 161160D-amino-acid N-acetyltransferase HPA3PRO_0000074634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Post-translational modificationi

Autoacetylates in an intermolecular reaction.1 Publication

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

BioGridi36663. 18 interactions.
DIPiDIP-2063N.
IntActiP39979. 3 interactions.
MINTiMINT-492186.

Structurei

3D structure databases

ProteinModelPortaliP39979.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 161148N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 11114Acetyl-CoA bindingBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000015620.
HOGENOMiHOG000078521.
InParanoidiP39979.
KOiK18852.
OMAiVHFLYHR.
OrthoDBiEOG7X3R3Q.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR032962. HPA2/HPA3.
[Graphical view]
PANTHERiPTHR10545:SF39. PTHR10545:SF39. 1 hit.
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39979-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNEEPEKMV NDRIVVKAIE PKDEEAWNKL WKEYQGFQKT VMPPEVATTT
60 70 80 90 100
FARFIDPTVK LWGALAFDTE TGDAIGFAHY LNHLTSWHVE EVVYMNDLYV
110 120 130 140 150
TERARVKGVG RKLIEFVYSR ADELGTPAVY WVTDHYNHRA QLLYTKVAYK
160
TDKVLYKRNG Y
Length:161
Mass (Da):18,814
Last modified:February 17, 2016 - v2
Checksum:i2A8DB00521975BDC
GO

Sequence cautioni

The sequence AAB65021.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence DAA07588.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18795 Genomic DNA. Translation: AAB65021.1. Different initiation.
BK006939 Genomic DNA. Translation: DAA07588.1. Different initiation.
PIRiS50523.
RefSeqiNP_010848.1. NM_001178881.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18795 Genomic DNA. Translation: AAB65021.1. Different initiation.
BK006939 Genomic DNA. Translation: DAA07588.1. Different initiation.
PIRiS50523.
RefSeqiNP_010848.1. NM_001178881.1.

3D structure databases

ProteinModelPortaliP39979.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36663. 18 interactions.
DIPiDIP-2063N.
IntActiP39979. 3 interactions.
MINTiMINT-492186.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YEL066W.
SGDiS000000792. HPA3.

Phylogenomic databases

GeneTreeiENSGT00390000015620.
HOGENOMiHOG000078521.
InParanoidiP39979.
KOiK18852.
OMAiVHFLYHR.
OrthoDBiEOG7X3R3Q.

Enzyme and pathway databases

BioCyciYEAST:G3O-30181-MONOMER.

Miscellaneous databases

PROiP39979.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR032962. HPA2/HPA3.
[Graphical view]
PANTHERiPTHR10545:SF39. PTHR10545:SF39. 1 hit.
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Biochemical characterization of Hpa2 and Hpa3, two small closely related acetyltransferases from Saccharomyces cerevisiae."
    Sampath V., Liu B., Tafrov S., Srinivasan M., Rieger R., Chen E.I., Sternglanz R.
    J. Biol. Chem. 288:21506-21513(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY, IDENTIFICATION OF PROBABLE INITIATION SITE.

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 17, 2016
Last modified: June 8, 2016
This is version 120 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.