ID   NAGS_DEBHA              Reviewed;         575 AA.
AC   Q6BZ43;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 86.
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=DEHA2A04708g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382133; CAG84481.2; -; Genomic_DNA.
DR   RefSeq; XP_456526.2; XM_456526.1.
DR   AlphaFoldDB; Q6BZ43; -.
DR   SMR; Q6BZ43; -.
DR   STRING; 4959.XP_456526.2; -.
DR   PRIDE; Q6BZ43; -.
DR   EnsemblFungi; CAG84481; CAG84481; DEHA2A04708g.
DR   GeneID; 2899813; -.
DR   KEGG; dha:DEHA2A04708g; -.
DR   VEuPathDB; FungiDB:DEHA2A04708g; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; Q6BZ43; -.
DR   OMA; MFWCDAE; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000599; Chromosome A.
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..575
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372562"
FT   DOMAIN          398..557
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   575 AA;  65563 MW;  0D3DC133EA6F057D CRC64;
     MSKLRNLNRQ FISNLKTHET VTNAKRNLIL SILKSTTTKR EARNYLNKYQ NQFDFSDITF
     NNGVPSNSLE KRDSQRELFI NRFLNKQNPF TNIYDDETKL QKIPLRLALF KIKFQSISLE
     NWKGMAETFK RLIHLGISPI IMLDYDHLPA NTFRNNELYM LNQTNKIMNI LGKPTEENDL
     KTIIMRSLFT KKTINDKDLA IDNLESVLIP LYQGVIPIIQ PIVYNASTCM QEFIDSNDLL
     FSLCSSLLTT KNVLSIEKVV MIDPIGGIPS IERNQTSHVF INLSQEYSDI VSELYIGFIK
     PEYRIFHMNN LKAMNKTLTL VSDKTGNDET TGIITTPDIM SVNNDQLNPI IYNVLTDRSI
     ISSSLPTSHN RTPELSTSIL KKGVDVNILD ALNYPKAFTL NNLVQDGSVN KSKLVDLIDD
     SFGKKLDTEK YFDRINDSLA TVVIVGDYDG AAIITWETCS KTNEKIAYLD KFAIASVNQG
     LPGLADIIFK IILQSHPNEL IWRSRKNNPV NKWYFERCCG TLSNPGSQWK IFYTGDIFNK
     KIDKLKKQGI PGGVNIHGKM HQYSDITENI PPSFL