ID   NAGS_PYRTR              Reviewed;         717 AA.
AC   B2WME0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=PTRG_11150;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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; DS231630; EDU44200.1; -; Genomic_DNA.
DR   RefSeq; XP_001941481.1; XM_001941446.1.
DR   AlphaFoldDB; B2WME0; -.
DR   SMR; B2WME0; -.
DR   STRING; 45151.EDU44200; -.
DR   PRIDE; B2WME0; -.
DR   EnsemblFungi; EDU44200; EDU44200; PTRG_11150.
DR   GeneID; 6349462; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; B2WME0; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
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   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
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..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..717
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372577"
FT   DOMAIN          518..691
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          35..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   717 AA;  79162 MW;  B5179C86F7313EBB CRC64;
     MFIWTKAPAR GLGKASKILP KRDDTQKVFE TTHHKQFHTA TTSVRRSSSS AKERQRAERQ
     QLTRLLKESP GKRDARNFLK QFDVPKKSKA SITAKAKELV SENIHNDLAS LRTGVNLGDL
     YKPTVFTREP LPEESYDAEK DEPVHLALVK LRQPQKLTDR TLGDIALTLS QMARLGLSTA
     VVLDCDEDTS THSIEVKPEY GNMVREQALR LVAALEDYNE PGSLLVEDVL GYSPLDNDMP
     STNQVRGGVE VQHTYLLFPP IDDGVIPVIA PFAYDENLKK VRVQADDVLL ALVREFAGLG
     HSNGMESPRG SLHKTKRVVE RPLLDRIIIL DPLGGIPSEN RADGAHVFVN LEAEYRDIKK
     ELQQLSSKTS NGAGSPTSLS TGNPLSKFVE QEVVSLPGVQ SENLASSAPV RHLKNLDVLE
     RGLKLLPPSS SGLILTPMEA ATKAIPDDAR TTPSKNPLLH NLLTDKPMTS SSLPTSPTSR
     FLGSAAPNPA TFLKKGIPLT MIPDPRVHGP WQPPSASNPS IELADDPRIN FPKLVDLIDD
     SFQRKLHPKN YLDRIHGRVA GIIIAGDYEG GAICTWETPK SLQGATPPSV LTPDSPYWIP
     YLDKFAVLTS SQGSGGVSDI VWAALTRTCF PDGVVWRSRT SNPVNKWYQE RSMGMWKLPG
     DQWTMFWTTE GIVGGWEQGK WGDVDDAKKR DMKRWDACID VCSGIEPSWA DGIQRDD