ID   NAGS_ASHGO              Reviewed;         542 AA.
AC   Q75A07;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
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; OrderedLocusNames=ADR120C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR   EMBL; AE016817; AAS52040.1; -; Genomic_DNA.
DR   RefSeq; NP_984216.1; NM_209569.1.
DR   AlphaFoldDB; Q75A07; -.
DR   SMR; Q75A07; -.
DR   STRING; 33169.AAS52040; -.
DR   EnsemblFungi; AAS52040; AAS52040; AGOS_ADR120C.
DR   GeneID; 4620365; -.
DR   KEGG; ago:AGOS_ADR120C; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; Q75A07; -.
DR   OMA; YFQRSVG; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0106098; C:NAGS/NAGK complex; IEA:EnsemblFungi.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006592; P:ornithine biosynthetic process; IBA:GO_Central.
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;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..14
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..542
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372548"
FT   DOMAIN          368..534
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   542 AA;  61904 MW;  A3AC5467177F35EE CRC64;
     MLFRRLLTTK VGYHTPNYVN RRLILSVLKS TATRREAKDY LTKYGDPAVA YHCVLYLRGT
     KTFSAGLIND FAIMLGRLRL LGIRPLVVLS PSKHVMTESE ILRETFYKHG LQSIPINEPM
     ASGTRETILQ NGASYNSIIP IIMPFVYHQQ RAKRMLAEDE VAFMRELVAY MPCRIDKFFI
     INRYGGIPSS ERHDNSHVFV NLSQEYGSLA EVLKQQITDL RHEMDDGLLA ERRATDGSYK
     EFQYTTLTES LTDLELMSAV LSLLLPSSTG LITSMHSAVT NSRYNPLLYN VLTDRSLVSS
     SLPSFKRDPI SDNAWYELPA CGAKIGTQRA NPIFSTTVLK QGVDIKLYDY STLTKENSVG
     FHELLSTAGS AQLPAHKRVN LTKLKGIIEH SFDRNLDMSH YLKRINGKIA SIIVIGDYEG
     IAILTYEGPE KRPFAYLDKF AVLPHLRGSL CISDVIFNLM FKKFGDELVW RSRRENVVNN
     WYFQRSVGVL DLSIDIGHGP KKDNIFKLFY YGGKKGTQFY DFDRLREYIT YVRDIEPSWS
     RK