ID   NAGS_ASPOR              Reviewed;         678 AA.
AC   Q2UES9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=AO090026000498;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007159; BAE59936.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UES9; -.
DR   SMR; Q2UES9; -.
DR   STRING; 510516.Q2UES9; -.
DR   EnsemblFungi; BAE59936; BAE59936; AO090026000498.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000006564; Chromosome 3.
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;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..678
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372553"
FT   DOMAIN          499..668
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          86..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   678 AA;  74436 MW;  DC2E426DAC8F0782 CRC64;
     MAAVKSCVEE EKIDCDLDFD KVIDVQLDDN HCAKLKAGYE SLLSRGALTV TEADFTPNET
     AESEFFLSLL 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