ID   NAGS_KLULA              Reviewed;         552 AA.
AC   Q6CRT7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=KLLA0D06523g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382124; CAH00448.1; -; Genomic_DNA.
DR   RefSeq; XP_453352.1; XM_453352.1.
DR   AlphaFoldDB; Q6CRT7; -.
DR   SMR; Q6CRT7; -.
DR   STRING; 28985.XP_453352.1; -.
DR   PRIDE; Q6CRT7; -.
DR   EnsemblFungi; CAH00448; CAH00448; KLLA0_D06523g.
DR   GeneID; 2893520; -.
DR   KEGG; kla:KLLA0_D06523g; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; Q6CRT7; -.
DR   OMA; YFQRSVG; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000598; Chromosome D.
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..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..552
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372564"
FT   DOMAIN          379..545
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   552 AA;  63063 MW;  62714627385DF594 CRC64;
     MIKTWIRCLT TEVRYHQPNA HGRSLVMSVL NSTVTKREAK DYLNKYTDEN NHHYCLVFLR
     HLSEYSDNVL SGFSKTVSRI QTLGLRPILI VDPLCQDISY QSQRLDNHLH DQSLKSIIVL
     DPITIGERGS IDVKLPILNP HIIPIIEPYQ YHEKEAFKKL AGDPSRFLSS LVSNLPINID
     KVFLISKYGG LPSVERHTNS HVFVNLSQEY RELRNSYQNQ LEKLESIQVD NTEKNLVESL
     QLFLNQDKIL SNSDQLKCHM EDLEIMNKTL SVLPHSSTGL ITTILAGSKL SDNNPLVYNI
     LTDRSLISSS LPRFKRSAAA QSKSWYELPS SNVEEEVTSA NDSVLVTTVF KKGIDIHIFD
     FRTLTDDNSI GLPPSQATQT GKSDPVSKKL DLNKLNGIIN SSFKRSLDLS HYLGRINGNI
     ASIIVIGDYE GIAILTYEGP KDKQFVYLDK FAVAQKLKGS LGISDIIFNL MFRKFPHELI
     WRSREDNVVN KWYFQRSTGV LHLSLDLGND DQKQSIFKLF YYGNPESESF HNVERLRDYA
     KYVRDITPSW HK