ID   C5E1I0_ZYGRC            Unreviewed;       572 AA.
AC   C5E1I0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   01-MAY-2013, entry version 31.
DE   RecName: Full=Amino-acid acetyltransferase, mitochondrial;
DE            EC=2.3.1.1;
DE   AltName: Full=Glutamate N-acetyltransferase;
DE   AltName: Full=N-acetylglutamate synthase;
GN   OrderedLocusNames=ZYRO0G21142g;
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 /
OS   NCYC 568 / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
OC   Zygosaccharomyces.
OX   NCBI_TaxID=559307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229;
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- FUNCTION: N-acetylglutamate synthase involved in arginine
CC       biosynthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-
CC       glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the acetyltransferase family.
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DR   EMBL; CU928179; CAR29964.1; -; Genomic_DNA.
DR   RefSeq; XP_002498897.1; XM_002498852.1.
DR   STRING; 559307.ZYRO0G21142g; -.
DR   GeneID; 8206732; -.
DR   KEGG; zro:ZYRO0G21142g; -.
DR   eggNOG; COG5630; -.
DR   HOGENOM; HOG000113727; -.
DR   KO; K00618; -.
DR   OrthoDB; EOG4X6GJ3; -.
DR   UniPathway; UPA00068; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR006855; DUF619.
DR   InterPro; IPR011190; GlcNAc_Synth_fun.
DR   Pfam; PF04768; DUF619; 1.
DR   PIRSF; PIRSF007892; NAGS_fungal; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Mitochondrion; Transferase.
SQ   SEQUENCE   572 AA;  66059 MW;  642156F65C5363F2 CRC64;
     MMWQRLLGQR LGYQQPNALS KNVILSVLNS TATKREARDY LTKYTDGSDK HNYCLLLIRH
     LQNISQKNLH KLSGTITRLR MLGLKPICVI PPSNHVDKQA ESWDRLLSWA DLRPLHLFDS
     LSVGSDGSVE SVLQSQRSML EQSEHLVPIL RPYMYDKSTA RQSMVPESIQ FFRGLCNGQI
     PHIDKFFILN NIGGIPSNER HENSHVFINL SQEFNHISSL LSNQLAQLRN REPNSEDLLD
     RMAVHMKEEE YSLLELKWKE HIEDLQLMNV VLSNLSNSST GLITTTRAAS LAHNSNNPLL
     HNLLTDRSLI SSSLPRFKKR HESLESNDDH AWYELPGDLD EEVREREIRD TNHVKMAENL
     QDAIFVTTVL KKGIHIKIYN DSTLTAENSV GLPNVPYDCA DYVNDSKLNL TKLKRILDQS
     FGRELDLKHY MNRVNGRIAS VIVIGDYEGI AILTYEGPKE NQFVYLDKFA VMPHLKGSLG
     ISDIIFNLMF KLFPKELLWR SRRDNVVNKW YFQRSVAVMD LSMDLSDHDK QPSQFKLFYY
     GDPEAAFKSF NNKDRLKEYA RYVRDIKPSW AK
//