ID   NAGS_PHANO              Reviewed;         725 AA.
AC   Q0U6Q5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=SNOG_12559;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445347; EAT79857.1; -; Genomic_DNA.
DR   RefSeq; XP_001802780.1; XM_001802728.1.
DR   AlphaFoldDB; Q0U6Q5; -.
DR   STRING; 13684.SNOT_12559; -.
DR   EnsemblFungi; SNOT_12559; SNOT_12559; SNOG_12559.
DR   GeneID; 5979691; -.
DR   KEGG; pno:SNOG_12559; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; Q0U6Q5; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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   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..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           47..725
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372572"
FT   DOMAIN          527..702
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          38..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   725 AA;  79509 MW;  9FB2AFB924740DF6 CRC64;
     MFICCKAPAR GFGKGTKTLS KFDNTSYASI ARISTSTHRS ALHTRKASSS AKERQRADRE
     QLTRLLKESP GKRDARNFLK QFDAPKPKKG EGSTAPKAKQ GTSEVVRKDP GTTRTGVNLG
     NLYQPTVFTR EPLPEKKYEE EDKEEPLHLA LVKLRQPQNL DDRTLGGIAL TLSQMAQLGL
     STAVVLDCAE YDSEDLPQID GAYEKMLREQ AARFVATLEE YNEPGALLIE HALGKTKEQN
     VIPSTVQIRG GVEVKNSFLL YPPIDDGVIP VVLPIAYDSD LKKVAVEADD VVLALIREFA
     GIAAHADRGA FEMSEASSGN KDLDDAERPI LDRIIVLDPL GGIPSVNRAD GAHVFVNLEA
     EYRDIKLELQ RLSAAAGDEA KSKPAVSLGT GNPFSKFVEE EVATTHGGSK HHLANPAPMR
     HLKNLDVVQR ALRILPPTSS GLILTPTEAA RKAIPDDDRS TPSKNPLLHN LLTDKPMISS
     SLPTSPASRF LGSVSPNPPT FLKKGIPVTM VPDPRESGPW RPPSASNPSI ELAEDPRINF
     PKLEDLINDS FRRKLDAKDY LDRIRGRVAG IIIAGDYEGG AICTWETPAS LRGVKIPSQA
     SETPDSPYWV PYLDKFAVLT SSQGSGGVSD IVWAALTRTG FPEGVVWRSR TSNPVNKWYQ
     ERSTGTWNLP GDQWTMFWTT NGVTKRWDGN EWDLGQSNSL TRWEAYVDVC NGIVPSWADG
     IKRAD