ID   NAGS_BOTFB              Reviewed;         734 AA.
AC   A6SG85;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=BC1G_11576;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476930; EDN32940.1; -; Genomic_DNA.
DR   RefSeq; XP_001549743.1; XM_001549693.1.
DR   AlphaFoldDB; A6SG85; -.
DR   SMR; A6SG85; -.
DR   PRIDE; A6SG85; -.
DR   GeneID; 5430240; -.
DR   KEGG; bfu:BCIN_15g05430; -.
DR   VEuPathDB; FungiDB:Bcin15g05430; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
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; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..734
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372555"
FT   DOMAIN          555..724
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          384..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  81144 MW;  5E38F40DAEAE092D CRC64;
     MLLQNLALKK GKEAAGHNIQ SLTKHGNYFV QSSDRRRAYT SNQSAADKVR EELAKETCEK
     LSSQHQAKKK AKAIDRDFFL SVLGSSATKR EARSYIQNFK PLNTSPAKPI SQEPVHKNTN
     ENGANLGSIY TATRAVAESP KFVQQPAVSQ STLGGSILHV ALVKVRAPQL LDDETLNGIG
     KTLSKLCRLG LISTVVVDCE DGTDTHLKVS ECEWRNRIKE QAARVVTAID ASGTEARLVD
     NVIGIAEDGS DVKQQPYLKG GVHVTFRELL MTPLRRGVLP VLPSIGHTDA TQTAVSITAS
     DVVLALTREF AGFRSPQSPD EHPNVVKEHL QALQNEVSLD RLILIDPLGG IPASDRRNGY
     HVFLNMEQEY EQAKQDLIKT GGLYSETSSR STRAEADSNF NLRDDIPLSS FTEQKSGELE
     YSPRHQNDSP TQQDQRMKFH LDNLELVRSA LAILPPSSSA LVTTPDEAAN SGKQHEFKAA
     GVGTRRQRNP LIHNLLTDKP AFSSSLPAGR LGPLDKNEPI TPSTKLAPAT FAKHGMPVTI
     FPDPKTTPWQ PPIAGVPQIS LTDPQIDLPR LVHLIEDSFN KKLDVQDYLR RVNNRIAGVI
     IAGEYEGGAL LTWELPPGVP DDGSEESRKR MVPYLDKFAV LKRSQGSGGV ADVVFKSMVR
     DCFPGGVCWR SRKDNPVNKW YFERSRATLK LMDTNWTMFF TTPEENMDQQ TFQDYEAVCK
     TIEPSWADKQ GVQD