ID   NAGS_NEOFI              Reviewed;         716 AA.
AC   A1DH62;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=NFIA_086740;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW18719.1; -; Genomic_DNA.
DR   RefSeq; XP_001260616.1; XM_001260615.1.
DR   AlphaFoldDB; A1DH62; -.
DR   SMR; A1DH62; -.
DR   STRING; 36630.CADNFIAP00007356; -.
DR   EnsemblFungi; EAW18719; EAW18719; NFIA_086740.
DR   GeneID; 4587174; -.
DR   KEGG; nfi:NFIA_086740; -.
DR   VEuPathDB; FungiDB:NFIA_086740; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000006702; 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;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..44
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..716
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372568"
FT   DOMAIN          537..706
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          99..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   716 AA;  78727 MW;  DBAD183557966C60 CRC64;
     MSPHTGWPRT VNSSLLKKHR SSLCTCQHTS SFLPRSFSTT ADRHVQQSAD FSSTSRSYDR
     LGRRAKEKLL DREFFLSLLS SASTKREAKS YLARLKAQYP KSPDENKPEP EKLATAPTLP
     SGVNLGSFYG ASRSVYESPV FRQGPSPTAP PSLEPVERLH LALVRLSTPQ SLDDNIIDGV
     AKTLSQLNRL GLTCCVVVDP GTEGVASTLR QVAIEQADRL AVAIQKQPDS KSLRLDSVFS
     IDASRPGLPQ VSSRKALLNP LRHGHTVILT PIAYTEDVPR AIIVPANDAV LALTKELAGL
     ASTPDPDEDP MVTAERIGRL QKEVSLDRVI LLDSLGGIPA FNRRQTSHVF INMEQEYDDI
     ENELLQAREM VPATETSLLK AGPSSIADNN PVSKFVNAEV VPVPSGPTQE LKTAAPQRSA
     IEGHLENLRV AQKALTMLPA ASSGIITSPF EVASSAQPSP TSEFSAVGTR RQRNPLIHNL
     LTDKPLLSSS LPMSRRGPTN NGQGTVYPVT SHTTFVKRGM PLTMLPNPWT EPWTPQSRPR
     LKLDDPSIDL PRLVHLIEDS FDRKLDVQDY LNRVNDRLAG LIIAGEYEGG AILTWELPPG
     VEDDGSEASN ARMVPYLDKF AVLKRSQGAG GVADIVFNAM VRSCFPNGVC WRSRKNNPVN
     KWYFERSLGT WKLSDTNWTM FWTTPSLVED SQKFRDYEAV CRSTQPSWAD DTGVVD