ID   NAGS_PICGU              Reviewed;         568 AA.
AC   A5DA88;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 64.
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=PGUG_00193;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408155; EDK36095.2; -; Genomic_DNA.
DR   RefSeq; XP_001486816.1; XM_001486766.1.
DR   AlphaFoldDB; A5DA88; -.
DR   SMR; A5DA88; -.
DR   STRING; 4929.XP_001486816.1; -.
DR   EnsemblFungi; EDK36095; EDK36095; PGUG_00193.
DR   GeneID; 5129553; -.
DR   KEGG; pgu:PGUG_00193; -.
DR   VEuPathDB; FungiDB:PGUG_00193; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; A5DA88; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001997; 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;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..568
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372573"
FT   DOMAIN          393..552
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   568 AA;  64627 MW;  036B18F38B4B519A CRC64;
     MSKLRNLNRQ LISNIKNHEL TTSTKRNLIL SILKSTTTKR EAKNYLQKYQ NQFDFNNSEP
     STGKTISDSQ RELLVDRFLS GRSLHRSLYD ESNQKLEKIP LRLAIFNFKQ LSISPRSWKG
     IRETFMRLLN LGISPVIVLD FDHVRNESFK YNEMYMMNSL NRVMNALEKH EDGNVQTMPL
     WSIFTTKDNS KTFEVGSLEQ ILVPLYQGII PIVMPIAYDT KTTKQTFASA QEITYFLSGA
     LSDLSPGTLS IEKIVFIDPI GGIPSIERNQ TSHVFINLSQ EYSDIVSELF IGYIEPEQRD
     LHLQNLNYMN KLLTLTRDKS GSDDATGIIT TPHIMSINDD QLNPIIYNVL TDRPIISSSL
     PSSRDATPQL STSVLKKGVD VKVLDTSNFS GTFTFDNLVR EDCLDKDRMV HLLNDSFGKK
     LDEEAYFRRI NNSLATVVIA GDYDGAAIIT WENVAGSDKK VAYLDKFAIA KRNQGLPGLA
     DVIFKVILQS HSGELIWRSQ KKNPVNKWYF ERSRGSISSL KSPWRVFYTG TIFDKRINKS
     KHGSSGLDIK RKIHEYIEIG ESIPASFT