ID   NAGS_MAGO7              Reviewed;         694 AA.
AC   A4RKF7; G4MT12;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   25-MAY-2022, entry version 83.
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; ORFNames=MGG_01507;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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; CM001232; EHA54671.1; -; Genomic_DNA.
DR   RefSeq; XP_003714478.1; XM_003714430.1.
DR   AlphaFoldDB; A4RKF7; -.
DR   STRING; 318829.MGG_01507T0; -.
DR   EnsemblFungi; MGG_01507T0; MGG_01507T0; MGG_01507.
DR   GeneID; 2679271; -.
DR   KEGG; mgr:MGG_01507; -.
DR   VEuPathDB; FungiDB:MGG_01507; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; A4RKF7; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000009058; Chromosome 2.
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..56
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..694
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372567"
FT   DOMAIN          513..687
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          20..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   694 AA;  76536 MW;  F685B3F91A5AE67C CRC64;
     MTLRGSAAWK QVGSIAQLPL GKSTNQHKNN HAVRSLSQQP CSSDRLKSPW LLSVRGVSAE
     AEGMRSLYET IMSERDKKMA ENKELLLSVM ETSPTRRGAK KWLKDFAPAL GRKWQPRGIS
     TAGPLPQADT RALEDNLPQV AIVKLREPQS IDETTLKGVG RTLCQLQMLG LLSIVVVDCD
     QDLVKGDALW PVIMKQTERA LAGATIAPLA RPRVMDYVMG IRPGSEGDQA SSLAAGGVFV
     SREEPLIRAL KDDAIVVVPT YAVSTDTCAA RTVQADEVVV ALTRYYSGLQ FPNKSSGGPA
     DTCQQPTAKP KAGIRKVMII DPLGGPPANN RPEGAHVFLN MIQEYDTAMK YIKEADYPEL
     KIASSAIGST SDTSAHIRKK HADNLELTKR IVTLLPSSAS VVITTPEEAA NLRGEKGEES
     HNFGFLAQTR TRKPKNALIH NLITDRPAFS SSLPTTRFAA SKPQAVKTGT MGNMDWTSKP
     IVTQSRTTLA KRGMPLTILP DPFTSPWTPT APGQPRLRLT DICVDLPRLV HLIDDSFDRK
     LDVQDYLNRV EDSLAGIIIV GEYEGGAILT WEAPNPHNIP AAEAYAEAYR QGRLVPYLDK
     FAVLKRAQGE GGIADIVFNA MIRTCFPKGV CWRSRKDNPV NKWYAERSRG FRKLDDSNWS
     MFWTTEWDDH SNADYEDVCR KIQPSWADNK QIVD