NAT5_YEAST
ID NAT5_YEAST Reviewed; 176 AA.
AC Q08689; D6W2V4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=N-alpha-acetyltransferase NAT5 {ECO:0000305};
DE Short=NatA complex subunit NAT5;
DE EC=2.3.1.258 {ECO:0000269|PubMed:25886145};
GN Name=NAT5 {ECO:0000303|PubMed:25886145, ECO:0000312|SGD:S000005779};
GN OrderedLocusNames=YOR253W;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND IDENTIFICATION IN THE NATA COMPLEX.
RX PubMed=14517307; DOI=10.1128/mcb.23.20.7403-7414.2003;
RA Gautschi M., Just S., Mun A., Ross S., Rucknagel P., Dubaquie Y.,
RA Ehrenhofer-Murray A., Rospert S.;
RT "The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to
RT the ribosome and interacts with nascent polypeptides.";
RL Mol. Cell. Biol. 23:7403-7414(2003).
RN [5]
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 [6]
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 [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25886145; DOI=10.1002/pmic.201400575;
RA Van Damme P., Hole K., Gevaert K., Arnesen T.;
RT "N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and
RT suggests a kinetic competition between N-terminal acetyltransferases and
RT methionine aminopeptidases.";
RL Proteomics 15:2436-2446(2015).
CC -!- FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of
CC proteins that retain their initiating methionine (PubMed:25886145). Has
CC a broad substrate specificity: able to acetylate the initiator
CC methionine of most peptides (PubMed:25886145). Non-essential component
CC of the NatA N-terminal acetyltransferase (PubMed:14517307).
CC {ECO:0000269|PubMed:14517307, ECO:0000269|PubMed:25886145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein];
CC Xref=Rhea:RHEA:50564, Rhea:RHEA-COMP:12726, Rhea:RHEA-COMP:12727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133398, ChEBI:CHEBI:133399; EC=2.3.1.258;
CC Evidence={ECO:0000269|PubMed:25886145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein];
CC Xref=Rhea:RHEA:50568, Rhea:RHEA-COMP:12728, Rhea:RHEA-COMP:12729,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133400, ChEBI:CHEBI:133401; EC=2.3.1.258;
CC Evidence={ECO:0000269|PubMed:25886145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein];
CC Xref=Rhea:RHEA:50572, Rhea:RHEA-COMP:12730, Rhea:RHEA-COMP:12731,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133402, ChEBI:CHEBI:133403; EC=2.3.1.258;
CC Evidence={ECO:0000269|PubMed:25886145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein];
CC Xref=Rhea:RHEA:50576, Rhea:RHEA-COMP:12732, Rhea:RHEA-COMP:12733,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133404, ChEBI:CHEBI:133405; EC=2.3.1.258;
CC Evidence={ECO:0000269|PubMed:25886145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein];
CC Xref=Rhea:RHEA:50580, Rhea:RHEA-COMP:12734, Rhea:RHEA-COMP:12735,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133406, ChEBI:CHEBI:133407; EC=2.3.1.258;
CC Evidence={ECO:0000269|PubMed:25886145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.258;
CC Evidence={ECO:0000269|PubMed:25886145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.258;
CC Evidence={ECO:0000269|PubMed:25886145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.258;
CC Evidence={ECO:0000269|PubMed:25886145};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA)
CC complex, which is composed of ARD1, NAT1 and NAT5.
CC {ECO:0000269|PubMed:14517307}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2370 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; Z75161; CAA99475.1; -; Genomic_DNA.
DR EMBL; AY557750; AAS56076.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11020.1; -; Genomic_DNA.
DR PIR; S67150; S67150.
DR RefSeq; NP_014896.3; NM_001183672.3.
DR PDB; 4XNH; X-ray; 2.10 A; C=1-176.
DR PDB; 4XPD; X-ray; 2.81 A; C=1-176.
DR PDB; 4Y49; X-ray; 3.95 A; C/I/O=1-176.
DR PDB; 6HD5; EM; 4.80 A; v=1-176.
DR PDB; 6HD7; EM; 3.40 A; v=1-176.
DR PDB; 6O07; X-ray; 2.70 A; C=1-176.
DR PDBsum; 4XNH; -.
DR PDBsum; 4XPD; -.
DR PDBsum; 4Y49; -.
DR PDBsum; 6HD5; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6O07; -.
DR AlphaFoldDB; Q08689; -.
DR SMR; Q08689; -.
DR BioGRID; 34643; 61.
DR ComplexPortal; CPX-783; NatA N-alpha-acetyltransferase complex.
DR IntAct; Q08689; 4.
DR MINT; Q08689; -.
DR STRING; 4932.YOR253W; -.
DR iPTMnet; Q08689; -.
DR MaxQB; Q08689; -.
DR PaxDb; Q08689; -.
DR PRIDE; Q08689; -.
DR EnsemblFungi; YOR253W_mRNA; YOR253W; YOR253W.
DR GeneID; 854427; -.
DR KEGG; sce:YOR253W; -.
DR SGD; S000005779; NAT5.
DR VEuPathDB; FungiDB:YOR253W; -.
DR eggNOG; KOG3138; Eukaryota.
DR HOGENOM; CLU_013985_5_3_1; -.
DR InParanoid; Q08689; -.
DR OMA; DKFYQEC; -.
DR BioCyc; YEAST:G3O-33744-MON; -.
DR BRENDA; 2.3.1.258; 984.
DR PRO; PR:Q08689; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08689; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031415; C:NatA complex; IDA:SGD.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IMP:SGD.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:ComplexPortal.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..176
FT /note="N-alpha-acetyltransferase NAT5"
FT /id="PRO_0000240642"
FT DOMAIN 14..176
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:4XNH"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:4XNH"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:4XNH"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4XNH"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:4XNH"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:4XNH"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:4XNH"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:4XNH"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:4XNH"
SQ SEQUENCE 176 AA; 19727 MW; 4F09DC597A690BA0 CRC64;
MGRDICTLDN VYANNLGMLT KLAHVTVPNL YQDAFFSALF AEDSLVAKNK KPSSKKDVHF
TQMAYYSEIP VGGLVAKLVP KKQNELSLKG IQIEFLGVLP NYRHKSIGSK LLKFAEDKCS
ECHQHNVFVY LPAVDDLTKQ WFIAHGFEQV GETVNNFIKG VNGDEQDAIL LKKHIS
