ID   NAGS_YARLI              Reviewed;         608 AA.
AC   Q6CEE1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 101.
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=YALI0B16390g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382128; CAG83224.1; -; Genomic_DNA.
DR   RefSeq; XP_500971.1; XM_500971.1.
DR   AlphaFoldDB; Q6CEE1; -.
DR   STRING; 284591.Q6CEE1; -.
DR   EnsemblFungi; CAG83224; CAG83224; YALI0_B16390g.
DR   GeneID; 2907516; -.
DR   KEGG; yli:YALI0B16390g; -.
DR   VEuPathDB; FungiDB:YALI0_B16390g; -.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; Q6CEE1; -.
DR   OMA; NAMVRDC; -.
DR   OrthoDB; 2787556at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR011190; GlcNAc_Synth_fun.
DR   InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR   PANTHER; PTHR23342:SF4; AMINO-ACID ACETYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1.
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           ?..608
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372583"
FT   DOMAIN          402..604
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   608 AA;  67106 MW;  5609EFE173123BDE CRC64;
     MLRSSRITAG TCVSRGWHSY TTKTPTKTAI PPAAKSSNEA KDLILSVLQS AATKREAKTY
     ISRYAPLTGV ELQKKKEGLV QRLLGVGKEQ DNKEIENLTG HAPEGLLGDS EGTLRVAIIK
     IRDIKSIEDD LIAQMGETIA RLSRLGVSPI VVVDAGKARN DFLKLDNKPF RHYQKLILQK
     VFKISDAIDA ASPDVGARPI EGLFSMNKKG LRLAMPQMLM HPLSHGKVPV LAPLAYDDVT
     SEEKLVMADD VVHFLTQKLA EVPANILSVE KIIFVDPLGG IPSVERSGAH VFVNLKQELS
     DIAAELHMGF IPPAQREVHL ANLKAMHKAL KFLPPTASGL ITTPAVAAIP SVGRNPIIYN
     VLTDRPVISP SLPVELKKTP TLETTLLREG MPVITLKSDK GLNLITEHEK GNIDLDRLWH
     LIEDSFGRRI DKQHYLNRVN GKIAGIIIAG DYEGAAIITW EDIDPVKAQE DRDAADRAAA
     EAAAAYAAGI PLPSPPLYQK LGDAVPLNPN QVAYLDKFAV LKRSQGSSSV ADVVFKGMVM
     SQFPNELLWR SRKNNPVNKW YFDRSKGSFK IPGSEWCMFW TGRKTREQYL ERFVDICTRI
     EPSLREEL
//