ID   NAGS_CANDC              Reviewed;         580 AA.
AC   B9W7S3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=CD36_04750;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(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; FM992688; CAX44734.1; -; Genomic_DNA.
DR   RefSeq; XP_002417144.1; XM_002417099.1.
DR   AlphaFoldDB; B9W7S3; -.
DR   STRING; 42374.XP_002417144.1; -.
DR   EnsemblFungi; CAX44734; CAX44734; CD36_04750.
DR   GeneID; 8044679; -.
DR   KEGG; cdu:CD36_04750; -.
DR   CGD; CAL0000159878; Cd36_04750.
DR   VEuPathDB; FungiDB:CD36_04750; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000002605; Chromosome 1.
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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..580
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372557"
FT   DOMAIN          403..560
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   580 AA;  66829 MW;  1FE91F21DA187540 CRC64;
     MSKLKTLNRQ FISNLETHKV TTDAKRNLIL SILKSTTTKR EAKNYLTKYQ NQFDFNDDLD
     FNKNIKIKNE QLSLTNRDSQ RELFINRFLN QSNPFINIYD REDVKLQKVP LRLAIFKIKF
     TKITIKQWKG IAETFKRLIT LGISPIIMLD YDHLPSNSFK NNELYMINQG NKMLNYLGRP
     EEESDLKVTL LRSLFTSHKG VPTLDSLESI LIPLYQGIIP IIQPIVYNAD ASKQEFLESD
     KLLLGLSSAL IEKRTTDLLS IEKIVMIDPM GGIPSIERRQ TSHVFINLSQ EYSDILSELF
     IGHIEPKYRD THVNNLNTMN NVLSFINEKS GNDETTGIIT TPEIMSINID QLNPIIYNVL
     TDRAIISSSL PSTTNRTPHL STTIIKKGVD VQIFDIDNYD KDLTMQNLFD DKLVNKEKLI
     NLLNDSFGKS LDVDPYLDRI NDNIATVVIV GDYDGAAIIT WEYSKGEKIA YLDKFAIAKK
     NQGLPGLADV IFKIILQSHP FELIWRSRKN NPVNKWYFER CCGCMSAPDS QWKIFYTGEV
     FDKKIDRFKR NPRHKNGVVN IDRKLQQYSE ICEGITPSFK