HPA3_YEAST
ID HPA3_YEAST Reviewed; 161 AA.
AC P39979; D3DLI4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=D-amino-acid N-acetyltransferase HPA3 {ECO:0000303|PubMed:15375647};
DE Short=DNT;
DE EC=2.3.1.36 {ECO:0000269|PubMed:15375647};
DE EC=2.3.1.48 {ECO:0000269|PubMed:23775086};
DE AltName: Full=Histone and other protein acetyltransferase 3 {ECO:0000303|PubMed:10600387};
GN Name=HPA3 {ECO:0000303|PubMed:10600387};
GN OrderedLocusNames=YEL066W {ECO:0000312|SGD:S000000792};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND ACETYLATION SUBSTRATE.
RX PubMed=10600387; DOI=10.1006/jmbi.1999.3338;
RA Angus-Hill M.L., Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V.;
RT "Crystal structure of the histone acetyltransferase Hpa2: a tetrameric
RT member of the Gcn5-related N-acetyltransferase superfamily.";
RL J. Mol. Biol. 294:1311-1325(1999).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15375647; DOI=10.1007/s00203-004-0724-y;
RA Yow G.Y., Uo T., Yoshimura T., Esaki N.;
RT "D-amino acid N-acetyltransferase of Saccharomyces cerevisiae: a close
RT homologue of histone acetyltransferase Hpa2p acting exclusively on free D-
RT amino acids.";
RL Arch. Microbiol. 182:396-403(2004).
RN [7]
RP FUNCTION.
RX PubMed=16362288; DOI=10.1007/s00203-005-0060-x;
RA Yow G.Y., Uo T., Yoshimura T., Esaki N.;
RT "Physiological role of D-amino acid-N-acetyltransferase of Saccharomyces
RT cerevisiae: detoxification of D-amino acids.";
RL Arch. Microbiol. 185:39-46(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND IDENTIFICATION OF PROBABLE INITIATION
RP SITE.
RX PubMed=23775086; DOI=10.1074/jbc.m113.486274;
RA Sampath V., Liu B., Tafrov S., Srinivasan M., Rieger R., Chen E.I.,
RA Sternglanz R.;
RT "Biochemical characterization of Hpa2 and Hpa3, two small closely related
RT acetyltransferases from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 288:21506-21513(2013).
CC -!- FUNCTION: N-acetyltransferase that acetylates histone H4 at 'Lys-8'.
CC Also acetylates polyamines like putrescine, spermidine and spermine
CC (PubMed:23775086). Acts on a wide range of D-amino acids. Catalyzes the
CC N-acetylation through an ordered bi-bi mechanism, in which acetyl-CoA
CC is the first substrate to be bound and CoA is the last product to be
CC liberated (PubMed:15375647). D-amino acids are toxic for the cell and
CC their N-acetylation, preceding removal from cells, plays an important
CC role in detoxification of D-amino acids (PubMed:10600387,
CC PubMed:16362288). {ECO:0000269|PubMed:10600387,
CC ECO:0000269|PubMed:15375647, ECO:0000269|PubMed:16362288,
CC ECO:0000269|PubMed:23775086}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-alpha-amino acid + acetyl-CoA = an N-acetyl-D-amino acid +
CC CoA + H(+); Xref=Rhea:RHEA:20704, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58496,
CC ChEBI:CHEBI:59871; EC=2.3.1.36;
CC Evidence={ECO:0000269|PubMed:15375647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:23775086};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 mM for D-Serine {ECO:0000269|PubMed:15375647};
CC KM=54 mM for D-Alanine {ECO:0000269|PubMed:15375647};
CC Vmax=22 umol/min/mg enzyme toward D-Serine
CC {ECO:0000269|PubMed:15375647};
CC Vmax=18 umol/min/mg enzyme toward D-Alanine
CC {ECO:0000269|PubMed:15375647};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Autoacetylates in an intermolecular reaction.
CC {ECO:0000305|PubMed:10600387}.
CC -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB65021.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA07588.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18795; AAB65021.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006939; DAA07588.1; ALT_INIT; Genomic_DNA.
DR PIR; S50523; S50523.
DR RefSeq; NP_010848.1; NM_001178881.1.
DR AlphaFoldDB; P39979; -.
DR SMR; P39979; -.
DR BioGRID; 36663; 51.
DR DIP; DIP-2063N; -.
DR IntAct; P39979; 1.
DR STRING; 4932.YEL066W; -.
DR iPTMnet; P39979; -.
DR PaxDb; P39979; -.
DR PRIDE; P39979; -.
DR GeneID; 856642; -.
DR KEGG; sce:YEL066W; -.
DR SGD; S000000792; HPA3.
DR eggNOG; KOG3216; Eukaryota.
DR HOGENOM; CLU_013985_32_0_1; -.
DR InParanoid; P39979; -.
DR BioCyc; YEAST:G3O-30181-MON; -.
DR BRENDA; 2.3.1.48; 984.
DR Reactome; R-SCE-351200; Interconversion of polyamines.
DR SABIO-RK; P39979; -.
DR PRO; PR:P39979; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39979; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0047812; F:D-amino-acid N-acetyltransferase activity; IDA:SGD.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:SGD.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; IMP:SGD.
DR GO; GO:0046416; P:D-amino acid metabolic process; IMP:SGD.
DR GO; GO:0006473; P:protein acetylation; IDA:SGD.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032962; HPA2/HPA3.
DR PANTHER; PTHR10545:SF42; PTHR10545:SF42; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cytoplasm; Nucleus; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..161
FT /note="D-amino-acid N-acetyltransferase HPA3"
FT /id="PRO_0000074634"
FT DOMAIN 14..161
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 98..111
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q06592"
FT SITE 144
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q06592"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 161 AA; 18814 MW; 2A8DB00521975BDC CRC64;
MSNEEPEKMV NDRIVVKAIE PKDEEAWNKL WKEYQGFQKT VMPPEVATTT FARFIDPTVK
LWGALAFDTE TGDAIGFAHY LNHLTSWHVE EVVYMNDLYV TERARVKGVG RKLIEFVYSR
ADELGTPAVY WVTDHYNHRA QLLYTKVAYK TDKVLYKRNG Y
