ID   NAGS_SCHPO              Reviewed;         500 AA.
AC   O94330;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Amino-acid acetyltransferase, mitochondrial;
DE            EC=2.3.1.1;
DE   AltName: Full=Arginine-requiring protein 6;
DE   AltName: Full=Glutamate N-acetyltransferase;
DE   AltName: Full=N-acetylglutamate synthase;
DE            Short=AGS;
DE            Short=NAGS;
DE   Flags: Precursor;
GN   Name=arg6; ORFNames=SPBC725.14;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA22186.1; -; Genomic_DNA.
DR   PIR; T40666; T40666.
DR   RefSeq; NP_595494.1; NM_001021405.2.
DR   AlphaFoldDB; O94330; -.
DR   SMR; O94330; -.
DR   BioGRID; 277697; 45.
DR   STRING; 4896.SPBC725.14.1; -.
DR   iPTMnet; O94330; -.
DR   MaxQB; O94330; -.
DR   PaxDb; O94330; -.
DR   PRIDE; O94330; -.
DR   EnsemblFungi; SPBC725.14.1; SPBC725.14.1:pep; SPBC725.14.
DR   GeneID; 2541183; -.
DR   KEGG; spo:SPBC725.14; -.
DR   PomBase; SPBC725.14; arg6.
DR   VEuPathDB; FungiDB:SPBC725.14; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; O94330; -.
DR   OMA; PKELIWR; -.
DR   PhylomeDB; O94330; -.
DR   UniPathway; UPA00068; UER00106.
DR   PRO; PR:O94330; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; ISO:PomBase.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; EXP:PomBase.
DR   GO; GO:0006536; P:glutamate metabolic process; NAS:PomBase.
DR   GO; GO:0006592; P:ornithine biosynthetic process; IBA:GO_Central.
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..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..500
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372579"
FT   DOMAIN          336..496
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   500 AA;  55777 MW;  97FD57788EF4E451 CRC64;
     MQKPSLSQDL IWILKSVQSR RSTKGFLQKH SSLKDGSPNK KSFAQPISSS FLNRISITKI
     DDVDSLSDNT LYGIGRSINS LARLGIQSVI VPTSNPIGMT SPFKYLENGT VVAKKRKLSI
     FEELQQQQNR VIRVSEIFSK AGVLTRPSYS SVCQLGPEGP SVENVQGIFQ ALSSLYTVIV
     PSSILMPNVI EVPIDGNEVL AGLTYSLHKP NFGFWVDRIV ILDKNGGMPC SKRQTGSSHV
     LINLAQEFDE LAKTLPPYHR KNLILVRRCL KMLPDDASAL ITTPEDAMLT NPVLDKNPLI
     HNVLTDRSII SCSLPRDRSP ITKTTVLRSG VPVYTFLGPK CLTDGSVSWE RLWVLINDSF
     KRTLDMDAYL DRLKNSLAAV IIAGDYLGTA IVTYEQPDGT TNEKVPYLDK LAVSQGAQGS
     AAISDVMFNV MTDLFPKELI WRSRLTNPVN KWYFERSVGS LKSSKTPWKL FWTGDSHVRN
     LDRVNQYMSV IDKIQPTWLN