ID   NAGS_YEAS7              Reviewed;         574 AA.
AC   A6ZPQ2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Amino-acid acetyltransferase, mitochondrial;
DE            EC=2.3.1.1;
DE   AltName: Full=Arginine-requiring protein 2;
DE   AltName: Full=Glutamate N-acetyltransferase;
DE   AltName: Full=N-acetylglutamate synthase;
DE            Short=AGS;
DE            Short=NAGS;
DE   Flags: Precursor;
GN   Name=ARG2; ORFNames=SCY_2862;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: N-acetylglutamate synthase involved in arginine biosynthesis.
CC       {ECO:0000250}.
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   -!- ACTIVITY REGULATION: Feedback inhibition by L-arginine. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4.
CC   -!- SUBUNIT: Interacts with the acetylglutamate kinase chain of AGR5,6.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR   EMBL; AAFW02000038; EDN63505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZPQ2; -.
DR   SMR; A6ZPQ2; -.
DR   PRIDE; A6ZPQ2; -.
DR   EnsemblFungi; EDN63505; EDN63505; SCY_2862.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Mitochondrion; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..13
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..574
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372585"
FT   DOMAIN          392..560
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   574 AA;  65590 MW;  93E6BC3A94082331 CRC64;
     MWRRIFAHGL KYDQPNASSK NLILSVLNTT ATKREAKDYL SKYTNDSGQH NHCLFFIRDL
     HKVAPAILSQ FSSVIKRLGM LGLRPMFVIP PSPTHVNIQA ELLDSIVTEA DLKPLHFKEG
     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 IGLPKEFHVS EKGAKPSNNS PKLDINKFKS IIDQSFKRSL
     DLHDYIKRIN GKIATIIVIG DYEGIAILTY EGSEENSFVY LDKFAVLPHL KGSLGISDII
     FNLMFKKFPN EILWRSRKDN VVNKWYFQRS VAVLDLSIDL DPEHCDEKQS QFKLFYYGNP
     QYAKRALRDK KRLREFMRSV RDIKPSWENE KNIS