ID   NAGS_SCLS1              Reviewed;         696 AA.
AC   A7F8R0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=SS1G_13991;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
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; CH476648; EDN99131.1; -; Genomic_DNA.
DR   RefSeq; XP_001585131.1; XM_001585081.1.
DR   AlphaFoldDB; A7F8R0; -.
DR   STRING; 665079.A7F8R0; -.
DR   GeneID; 5481096; -.
DR   KEGG; ssl:SS1G_13991; -.
DR   InParanoid; A7F8R0; -.
DR   OMA; WAMFWTT; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001312; 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   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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..696
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372580"
FT   DOMAIN          515..676
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          59..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   696 AA;  76715 MW;  21E799E7411B5797 CRC64;
     MPLSLSSRVR EELAKETCEK LSTQHQAKKK AKAIDRDFFL SVLGSSATKR EARSYIQNFK
     PPNTAPTKSK IQESTQQNST ENGANLGSIY TATRAVAESP KFVQQPVLPK PAPEGPLLHV
     ALVKIRAPQL LDDETLSGIG KTLSRLSRLG LVSTVVVDGD DGSDTFLRIS NCEWRNMVKE
     QAARVVAAID ASGTEARLVD NVIGIAEDGS NFEQRPYLKG RVHVTLRELL MTPLRRGVLP
     IIPSIGHTDI TQTVVSATAN DVVLALTREF AGIWSSESPD EHPNVVKERL QALRSEVSLD
     RLILVDPLGG IPASDRKNGY HVFLNMEQEY ELAKQDLINR GGMHSVAPQK PTLPEASANF
     TVGDPILLSS FTENKPGELD DSPPPQNGSP AKHDPRMKFH LENLELVRST LSLLPPSSSA
     LITTPHEAAN SEKQPEFKAA GVGTRRQRNP LIHNLLTDKP AFSSSLPVGR LGPMDKNEPI
     SSSTKFAPTT FAKHGMPVTI FPDPKTTPWQ PPIAGVPQIS LTDPQIDLPR LVHLIEDSFN
     KKLDVQHYLR RVNNRIAGVI IAGEYEGGAL LTWELPPGVP DGSEESRKRM VPYLDKFAVL
     KKSQGSGGVA DVVFKSMVRD CFPGGDNPVN KWYFERSRAT LKLSDTNWTM FFTTPEENMD
     HQTFKDYEAV CKFFGRENVG GYYQQGKRGI YVLDSE