ID   NAGS_COPC7              Reviewed;         621 AA.
AC   A8N2M6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=CC1G_01743;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(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}.
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; AACS02000001; EAU92698.1; -; Genomic_DNA.
DR   RefSeq; XP_001829063.1; XM_001829011.2.
DR   AlphaFoldDB; A8N2M6; -.
DR   SMR; A8N2M6; -.
DR   STRING; 5346.XP_001829063.1; -.
DR   EnsemblFungi; EAU92698; EAU92698; CC1G_01743.
DR   GeneID; 6005489; -.
DR   KEGG; cci:CC1G_01743; -.
DR   VEuPathDB; FungiDB:CC1G_01743; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_013088_0_0_1; -.
DR   InParanoid; A8N2M6; -.
DR   OMA; MFWCDAE; -.
DR   OrthoDB; 769117at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001861; 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; IPR006855; Vertebrate-like_GNAT_dom.
DR   Pfam; PF04768; NAT; 2.
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..77
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           78..621
FT                   /note="Amino-acid acetyltransferase, mitochondrial"
FT                   /id="PRO_0000372560"
FT   DOMAIN          424..600
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          213..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  68262 MW;  488F8893CDAB9F46 CRC64;
     MIPRAPPSTQ LFSAKTAVNQ RSQTFKAFYA TIRSLRQPPP EPPESPQAAD NDFILSILKA
     NPSLRDTRSY LASFGVQPQR PKTLEDKKLP EIVIPPPPAP KLTASSTKVV KEEKHAPSPV
     INSILNPIYR RTALVKIQGP FTDVQLDSIT RGLVYLEKLG MVSVIVVESD GVPKGEQEER
     KLLIDEIMRV VTSLEKQGAH ARPIVGAVVR LGPKPGSEEE SEPGFSPPET HIYPSDLTPI
     RSSLRAGEIP VLAPFALDSR CRSVRVDAND AIAGLACGMV EAASENPSPA AHEDGSSDSD
     AIDLTPLRLM IINQRGGVPS YARSGYPHLL INLQQEYDHI LQTFDPRWKD SHPHALSDLA
     LARTCLRYMP PTSSAIMVSH KSPSSLIGNL ITNKPAVSSS LPHALLQGNL RLTPHTPTLL
     RRGLPIRVVR SVSDIDKEKM TALLEQSFGR VLDQEAFYGR LEKTLDFVII AGDYDGTAIV
     TNEVCPGSSQ PISYLDKFAV LPSHQGDGTV DFLWVALHDE SYGLGHPFSA NPNGGKGGKG
     EGRDLVWRSR SNNPVNKWYF ERSTGHLRMG QWVLFWADAE KRLKVEESLR GSAGLSFIED
     WEHGRLGKWA DTITKIPSSW K