ID   NAGS_CANGA              Reviewed;         566 AA.
AC   Q6FS75;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=CAGL0H02871g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380954; CAG59852.1; -; Genomic_DNA.
DR   RefSeq; XP_446919.1; XM_446919.1.
DR   AlphaFoldDB; Q6FS75; -.
DR   STRING; 5478.XP_446919.1; -.
DR   PRIDE; Q6FS75; -.
DR   EnsemblFungi; CAG59852; CAG59852; CAGL0H02871g.
DR   GeneID; 2888569; -.
DR   KEGG; cgr:CAGL0H02871g; -.
DR   CGD; CAL0129457; CAGL0H02871g.
DR   VEuPathDB; FungiDB:CAGL0H02871g; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; Q6FS75; -.
DR   OMA; YFQRSVG; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0106098; C:NAGS/NAGK complex; IEA:EnsemblFungi.
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   GO; GO:0006592; P:ornithine biosynthetic process; IEA:EnsemblFungi.
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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..566
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372558"
FT   DOMAIN          391..557
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   566 AA;  64760 MW;  EE42D67B1E168BD1 CRC64;
     MWAHLFKHGF KYEQQNSLSK SLILSVLNST ATKREAKDYL IKYANGSSNY HYLLLIRNIA
     TQSERSLHRL SDSIRRLKFL GISPVCVLLP SGRIQTEVEK MDKLITLSQL KPLVLDYGLS
     RAFDGSYESI MQTALDTEYC TTRGIVPIVK PYIYDQSTAS RGLISDPVLF MDQLSRDSSL
     KFDKFFILNR SGGIPSGERN QNSHIFINLS QEYQKIHRTL TSSIRTIVER QPRSEDLLDR
     LELYVRESDI ISLEAEYKEH MENLQLMNTV LSNLSSSATG VITTINAASS PSDTVNPLVH
     NLLTDRSIIS SSLPRFKNKS GNFLSPSGQD WYEMPVEIET DEETLQGEDS VFVTTVLKKG
     VDIKEFDYSH LTSENTVNLP KQFQIKLHDE STYNNSCSKY KLDLVKFKNI IDKSFGRELD
     LNHYLNRING KIASIIIIGD YEGIAILTYE GPPDNKFVYL DKFAVLPHLK GSLGISDIIF
     NLMFKKFPRE VVWRSRANNV VNKWYFQRSV AVLDLSMELD EGDMQESEFK LFYHGDPESS
     LKSIVAIDRL RDLAKYVRNI KPSWVK