ID   NAGS_ASPFN              Reviewed;         688 AA.
AC   B8NG97;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=AFLA_134370;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963478; EED50674.1; -; Genomic_DNA.
DR   RefSeq; XP_002379450.1; XM_002379409.1.
DR   AlphaFoldDB; B8NG97; -.
DR   SMR; B8NG97; -.
DR   STRING; 5059.CADAFLAP00007315; -.
DR   EnsemblFungi; EED50674; EED50674; AFLA_134370.
DR   VEuPathDB; FungiDB:AFLA_134370; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   OMA; WAMFWTT; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001875; 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   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..45
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..688
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372551"
FT   DOMAIN          509..678
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  75680 MW;  C3F08F5B54D4CFFA CRC64;
     MSSRALTWPR TAKSSLLKQQ TSSFVGQPKL GTPNCRSFSS TADRPINQSA EFSSSSKSYD
     RLGRRAKEKL LDREFFLSLL NSASTKREAK SYLARLKAQH PPKAQTEPTT GHSKGTVTQS
     LPSGVNLGSF YGASRSVYDS PVFRHDSTPL PPPSELPEER LHLALIKIRT PQLLDDTIIN
     GVAKTLSQLS RLGMACCVVV DPGTAGNANT LRRVAAEQAE RISIAVDAQP DSKSAHLDSV
     LSLSPMFPEL PTVLSRKALL NPLRDGQIVV VAPIAYTEDV PKAVTISAND AILALTKELA
     GLAMRPDPDE DPWLTAQKIA KLQKEVSLDR VILLDPLGGI PSFRGPQTSH VFINMEQEFD
     DIKNELLHVQ SSEACTATTP KGGNTFVEDP LERHLDNLQL SQNVLAMLPS ASSGIITSPL
     EVSNSARTPQ ANPSDVSAVG TRRQRNPLIH NLLTDKPLLS SSLPMSRREA MNRRRGSINT
     PSSHTTFVKR GMPLTMIPNP RVEVWTAQNR PRLSLDDPSI DLPRLVQLIE DSFNRKLDVQ
     DYLNRVNDRL AGLIIAGEYE GGAILTWELP PGVEDDGSPA SEARMVPYLD KFAVLKRSQG
     AGGVADIVFN AMVRSCFPNG VCWRSRKDNP VNKWYFERST GTWKLSDTNW TMFWTTPGLT
     ENSQRFSDYE QVCRSIQPSW ADDTGVVD