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   10-APR-2019, entry version 47.
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
OS   9003) (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Psathyrellaceae;
OC   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.,
RA   Borodovsky M., Burns C., Canbaeck B., Casselton L.A., Cheng C.K.,
RA   Deng J., Dietrich F.S., Fargo D.C., Farman M.L., Gathman A.C.,
RA   Goldberg J., Guigo R., Hoegger P.J., Hooker J.B., Huggins A.,
RA   James T.Y., Kamada T., Kilaru S., Kodira C., Kuees U., Kupfer D.,
RA   Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J., Mackey A.J.,
RA   Manning G., Martin F., Muraguchi H., Natvig D.O., Palmerini H.,
RA   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
CC       biosynthesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-
CC         glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.1.1;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 1/4.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AACS02000001; EAU92698.1; -; Genomic_DNA.
DR   RefSeq; XP_001829063.1; XM_001829011.2.
DR   ProteinModelPortal; A8N2M6; -.
DR   STRING; 5346.XP_001829063.1; -.
DR   EnsemblFungi; EAU92698; EAU92698; CC1G_01743.
DR   GeneID; 6005489; -.
DR   KEGG; cci:CC1G_01743; -.
DR   EuPathDB; FungiDB:CC1G_01743; -.
DR   eggNOG; ENOG410ITSY; Eukaryota.
DR   eggNOG; COG5630; LUCA.
DR   InParanoid; A8N2M6; -.
DR   KO; K00618; -.
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   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; Complete proteome;
KW   Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT       1     77       Mitochondrion. {ECO:0000255}.
FT   CHAIN        78    621       Amino-acid acetyltransferase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000372560.
FT   DOMAIN      424    600       N-acetyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00532}.
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
//