ID   NAGS_COCIM              Reviewed;         737 AA.
AC   Q1DNE1; J3K5P6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, 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=CIMG_08172;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
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).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704913; EAS29426.3; -; Genomic_DNA.
DR   RefSeq; XP_001241009.1; XM_001241008.2.
DR   AlphaFoldDB; Q1DNE1; -.
DR   STRING; 246410.Q1DNE1; -.
DR   EnsemblFungi; EAS29426; EAS29426; CIMG_08172.
DR   GeneID; 4560512; -.
DR   KEGG; cim:CIMG_08172; -.
DR   VEuPathDB; FungiDB:CIMG_08172; -.
DR   InParanoid; Q1DNE1; -.
DR   OMA; WAMFWTT; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001261; 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..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..737
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372559"
FT   DOMAIN          558..727
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          43..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   737 AA;  81514 MW;  2B989EFCCB029D92 CRC64;
     MSRSTVLGWC TQSCRLLQKH DHSFSFPTFN GSPPLKKRRF CDSAAPAAPR PSIHRPSEYI
     PHSKSGGEAP QDLGHKAREK EAEKEFYLSL LCSASTKREA KSYLSRFKAQ KTTANDGCQH
     ITPRRGDLIS DLELMKDKPG VNLGSMFSET RTVAETPAPK QEWSSAQSTE LFREKIHVAL
     VKLRKPQLLD DQTLHGVAKT LVQLSRLGMS CCIVIDVGTD KDETHRRIIA REQADRLSAV
     IDANHGPDSR QLDSIITVPS ATDMKLSVLS RGPLLSPLQQ GHVVVVVPVG YANDTQRAVL
     LPANEVVFAL SKELAGLELR SGPDEDATTT ANKVNDMQKQ VSLDRIIILD PAGGIPSLQR
     RPHVFINLEQ EFEDIARELS LGSQTGFLSI NDSGTASHKM PVSSLGKSNP ISIFVEEELV
     SLPKTLGESQ EMPRNGKRFA EHLENLNLLQ RTLSYLPPSS SGIIVTPHEV ALSAKGPLNT
     SAVSAVRTRR QRNPLIHNLL TDKPFQSASL PLGRLGVKSD CMSAGQSPAT HSTFVKRGMP
     LTMLPDPRVE VWAAKKRGEP ALTLDDPRID LPRLIHLIED SFGRKLDARH YVDRINPRLA
     GLIIAGEYEG GAVLTWETPP GLSDDGSEEF RARMVPYLDK FAVLKRSQGA GGVADIVFNA
     MVRTCFPQGV CWRSRANNPV NKWYFERSRG TWKLPGTNWT MFWTTAGVPE NQSRFWDYEG
     VCRAIEPSWA DKTQQAD