ID   NAGS_AJECN              Reviewed;         684 AA.
AC   A6RBX7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=HCAG_07135;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476662; EDN10674.1; -; Genomic_DNA.
DR   RefSeq; XP_001537713.1; XM_001537663.1.
DR   AlphaFoldDB; A6RBX7; -.
DR   STRING; 339724.A6RBX7; -.
DR   EnsemblFungi; EDN10674; EDN10674; HCAG_07135.
DR   GeneID; 5444096; -.
DR   KEGG; aje:HCAG_07135; -.
DR   VEuPathDB; FungiDB:HCAG_07135; -.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000009297; 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   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           ?..684
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372547"
FT   DOMAIN          505..674
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          414..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  75661 MW;  610A6CF0C42B970A CRC64;
     MYDEPSDIVR LVSTVIVSES EHIPVLAIID FFFSLLSSAS TKREAQSYLS RFKAEKPEPA
     KSPPEQSAMG YPSTNFVQSG VNLGGGMFGM AGVIDNHAMF RQESALGKSL PIETVSEETL
     HIALVKIREP QLLNDQTLGE VGRTLSQLSL LGMSCCVVID PGLPQSDTFW RNRSIKQADR
     MLAAIEKNGV DSRRLDDVIR LAPSPKHALS VVSRELILSP LRRGKIAVIP PIGYTEGTLR
     AVPVLADDVV LALTREFTGL GVKARPEDNP HELARRISKL QKEVSVDRLI ILDPAGGIPS
     LKRASKSHVF VNLEQEFEEI TNELREGMAA GDSLVTGDKN ENGQQILSLE KSNPLSTVVE
     REGAASLPSE LQVTSSDRSS VHIPDFERHL DNLTLLHNAL TYLPPASSGI ISIPQDATNS
     ASEPRDPSQL STVATRRKRN PLIHNLLTDK PSHSASLPAG RLRANNGCSS QNNFQVMHST
     FVKKGMPLTL FPDPRVHIWK PPINGKSRMT LNDPHIDLPR LVQLIEDSFN RKLDVQHYLN
     RVSDRLAGLI IAGEYEGGAV LTWELPPGVP NDGSEESRSR MVPYLDKFTV LKRSQGAGGV
     ADIVFNAMVR TCLPKGVCWR SRRDNPVNKW YFERARGTWK LPGSNWTMFW TTDGVLEGDR
     LFRDYEGVCR GIEPSWLDNK HVVD