ID   NAGS_CRYNB              Reviewed;         565 AA.
AC   P0CM19; Q55W63; Q5KK32;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 46.
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; OrderedLocusNames=CNBC2740;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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; AAEY01000013; EAL22136.1; -; Genomic_DNA.
DR   RefSeq; XP_776783.1; XM_771690.1.
DR   AlphaFoldDB; P0CM19; -.
DR   SMR; P0CM19; -.
DR   EnsemblFungi; EAL22136; EAL22136; CNBC2740.
DR   GeneID; 4934939; -.
DR   KEGG; cnb:CNBC2740; -.
DR   VEuPathDB; FungiDB:CNBC2740; -.
DR   HOGENOM; CLU_013088_1_0_1; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001435; 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   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR   Pfam; PF04768; NAT; 2.
DR   SUPFAM; SSF55729; SSF55729; 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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..565
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000410010"
FT   DOMAIN          352..540
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          38..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  62669 MW;  F12CE0EF5554E3CB CRC64;
     MLTGSSGKAF ILSILQASPS ARDSRSYLSS FAPPQPVDIA TATPAATPSD GAQPPAQNPL
     VNALLNPILR RPALVKIQGP FTDAQLESIC RGMAHLQKLG LVSVIVVDRD DLPSTESSDR
     YEAQRQRAIV RHEVERVVHF LSRHRAAARP VFSTVARIAD PELEPEEAQK GVFVEEEGLD
     HVRRAVGEGE IPVLLPVALD SGCRSRRIPA NRVLLALASA MSTHTSSPVD LTPRRLLVIN
     REGGIPSYAR QGLPHLYINL ASEFSYINRT FQPQWNDSHP TALSNLFLAN GCLAHMPREA
     SALIVSHRSP AALIANLITN KPAHSASLPH ALLVESEGRI TRDTPTLIRK GLPVRVLRSM
     EEVDQDKLTH LLETSFKRTL DREGFYNRLK NDLDFVIVIG DYAGAAVCTL EGKPVSDSFA
     YPPNHPEPIC YLDKFAVHPS HQGDGTVDFL WVALRDETYG LGQLDASNPS IGSLRGVGRG
     RDLVWRSRSD NPVNKWYYER SSGFLKTRDE KWKVFWCDAE QRLGEIWRER EFGGGRLVRV
     VEKEEKGRVK WWEEVIGAIP SAWSA