ID   NAGS_ASPFC              Reviewed;         716 AA.
AC   B0XSH8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=AFUB_027240;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS499595; EDP54664.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XSH8; -.
DR   SMR; B0XSH8; -.
DR   EnsemblFungi; EDP54664; EDP54664; AFUB_027240.
DR   VEuPathDB; FungiDB:AFUB_027240; -.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   PhylomeDB; B0XSH8; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001699; 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..44
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..716
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372550"
FT   DOMAIN          537..706
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          37..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   716 AA;  78710 MW;  BAA6D761975755A0 CRC64;
     MSLHTGWPRT VNSSFLKKHR SSLCTCQHTS SVLPRSFSTT PDRHVQQSAD FSSTSRSYDR
     LGRRAREKLL DREFFLSLLS SATTKREAKS YLARLKAQHP KSPDANKPEP EKSATAPTLP
     SGVNLGSFYG ASRSVYESPV FRQGPSPSAP PSLEPVERLH LALVRLSTPQ SLDDNIIDGV
     AKTLSQLNRL GLTCCVVVDP GTEGVASALR QVAIEQADRL AVAIQKQPDS KSLRLDSVFS
     IDPSRPGLPQ VFSRKALLNP LRHGHTVILT PIAYTEDVPR AIIVPANDAV IALTKELAGL
     ASIPDPDEDP MVTAERIGRL QKEVSLDRVI LLDPLGGIPA FNRRQPSHVF INMEQEYDDI
     ENELLQAREM VPATETSLLK AGPNSVADNN PISKFVHAEV VPVPSGSTPE LKTAVPQRSA
     IEGHLENLRV AQKALAMLPA ASSGIITSPF EVASSAQTSP TSEFSAVGTR RQRNPLIHNL
     LTDKPLLSSS LPMSRRGPTN NGQGAVYPVT SHTTFVKRGM PLTMLPNPWT EPWTPQSRPR
     LKLDDPSIDL PRLVHLIEDS FDRKLDVQDY LNRVNDRLAG LIIAGEYEGG AILTWELPPG
     VEDDGSEASN ARMVPYLDKF AVLKRSQGAG GVADIVFNAM VRSCFPNGVC WRSRKNNPVN
     KWYFERSLGT WKLSDTNWTM FWTTPGLVED SQKFRDYEAV CRSIQPSWAD DTGVVD