NAGS_YEAST
ID NAGS_YEAST Reviewed; 574 AA.
AC P40360; D6VWB2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Amino-acid acetyltransferase, mitochondrial {ECO:0000303|PubMed:391804};
DE EC=2.3.1.1 {ECO:0000269|PubMed:11553611, ECO:0000269|PubMed:391804};
DE AltName: Full=Arginine-requiring protein 2 {ECO:0000303|PubMed:391804};
DE AltName: Full=Glutamate N-acetyltransferase {ECO:0000303|PubMed:391804};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000303|PubMed:391804};
DE Short=AGS {ECO:0000303|PubMed:391804};
DE Short=NAGS {ECO:0000303|PubMed:391804};
DE Flags: Precursor;
GN Name=ARG2 {ECO:0000303|PubMed:391804}; OrderedLocusNames=YJL071W;
GN ORFNames=HRB574, J1091;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RA Sor F.J.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762302; DOI=10.1002/yea.320110108;
RA Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F.;
RT "Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces
RT cerevisiae includes the mitochondrial ribosomal protein L8.";
RL Yeast 11:57-60(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=205532; DOI=10.1128/jb.133.3.1096-1107.1978;
RA Jauniaux J.-C., Urrestarazu L.A., Wiame J.-M.;
RT "Arginine metabolism in Saccharomyces cerevisiae: subcellular localization
RT of the enzymes.";
RL J. Bacteriol. 133:1096-1107(1978).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=391804; DOI=10.1128/jb.140.3.874-880.1979;
RA Wipe B., Leisinger T.;
RT "Regulation of activity and synthesis of N-acetylglutamate synthase from
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 140:874-880(1979).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH ACETYLGLUTAMATE KINASE.
RX PubMed=11553611; DOI=10.1074/jbc.m103732200;
RA Abadjieva A., Pauwels K., Hilven P., Crabeel M.;
RT "A new yeast metabolon involving at least the two first enzymes of arginine
RT biosynthesis: acetylglutamate synthase activity requires complex formation
RT with acetylglutamate kinase.";
RL J. Biol. Chem. 276:42869-42880(2001).
RN [8]
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 [9]
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).
CC -!- FUNCTION: N-acetylglutamate synthase involved in arginine biosynthesis.
CC {ECO:0000269|PubMed:11553611, ECO:0000269|PubMed:205532,
CC ECO:0000269|PubMed:391804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC Evidence={ECO:0000269|PubMed:11553611, ECO:0000269|PubMed:391804};
CC -!- ACTIVITY REGULATION: Feedback inhibition by L-arginine.
CC {ECO:0000269|PubMed:391804}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-9.5.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000269|PubMed:11553611,
CC ECO:0000269|PubMed:391804}.
CC -!- SUBUNIT: Interacts with the acetylglutamate kinase chain of AGR5,6.
CC {ECO:0000269|PubMed:11553611}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:205532}.
CC -!- MISCELLANEOUS: Present with 112 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; X88851; CAA61310.1; -; Genomic_DNA.
DR EMBL; Z34288; CAA84051.1; -; Genomic_DNA.
DR EMBL; Z49346; CAA89363.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08728.1; -; Genomic_DNA.
DR PIR; S50800; S50800.
DR RefSeq; NP_012464.1; NM_001181504.1.
DR AlphaFoldDB; P40360; -.
DR SMR; P40360; -.
DR BioGRID; 33684; 21.
DR ComplexPortal; CPX-1151; N-acetylglutamate synthase NAGS/NAGK complex.
DR DIP; DIP-5679N; -.
DR STRING; 4932.YJL071W; -.
DR CarbonylDB; P40360; -.
DR iPTMnet; P40360; -.
DR MaxQB; P40360; -.
DR PaxDb; P40360; -.
DR PRIDE; P40360; -.
DR EnsemblFungi; YJL071W_mRNA; YJL071W; YJL071W.
DR GeneID; 853374; -.
DR KEGG; sce:YJL071W; -.
DR SGD; S000003607; ARG2.
DR VEuPathDB; FungiDB:YJL071W; -.
DR eggNOG; KOG2436; Eukaryota.
DR GeneTree; ENSGT00390000005602; -.
DR HOGENOM; CLU_013088_0_0_1; -.
DR InParanoid; P40360; -.
DR OMA; YFQRSVG; -.
DR BioCyc; YEAST:YJL071W-MON; -.
DR UniPathway; UPA00068; UER00106.
DR PRO; PR:P40360; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40360; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0106098; C:NAGS/NAGK complex; IPI:ComplexPortal.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IDA:SGD.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006592; P:ornithine biosynthetic process; IMP:SGD.
DR InterPro; IPR011190; GlcNAc_Synth_fun.
DR InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR Pfam; PF04768; NAT; 1.
DR PIRSF; PIRSF007892; NAGS_fungal; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT CHAIN 14..574
FT /note="Amino-acid acetyltransferase, mitochondrial"
FT /id="PRO_0000203054"
FT DOMAIN 392..560
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 574 AA; 65610 MW; 167456A4900B7D59 CRC64;
MWRRIFAHEL KYDQPNASSK NLILSVLNTT ATKREAKDYL SKYTNDSGQH NHCLFFIRDL
HKVAPAILSQ FSSVIKRLGM LGLRPMFVIP PSPTHVNIQA ELLDSIVTEA DLKPLHLKEG
LTKSRTGLYH SVFSQESRFF DIGNSNFIPI VKPYVYNEET ASEFMTKDVV KFMDCLCQGN
IPHIDKFFIL NNAGGIPSGE RNDNAHVFIN LSQELEHLSS SLSHNISTLT KREPRSQNLL
HRMEVYVKKD EISSLECEYH DHLENLLLMD KVLSNLAATA TGLITTVKAA ALSSDRKNPL
VYNLLTDRSL ISSSLPRFKK KDGEIDSPAN MFDDHAWYEL PSQQVNAAPS NSDAVLVTTV
LKKGVHIKTY DYKTLTQFNS IGLPKKFHVP EKGAKPSSNS PKLDINKFKS IIDQSFKRSL
DLHDYIKRIN GKIATIIVIG DYEGIAILTY EGSEENSFVY LDKFAVLPHL KGSLGISDII
FNLMFKKFPN EILWRSRKDN VVNKWYFQRS VAVLDLSIDL DPEHCDEKQS QFKLFYYGNP
QYAKRALRDK KRLREFMRSV RDIKPSWENE KNIS
