ID   ARGJ_METMP              Reviewed;         408 AA.
AC   P62065;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   02-SEP-2026, entry version 122.
DE   RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE            EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_01106};
DE   AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE            Short=OATase {ECO:0000255|HAMAP-Rule:MF_01106};
DE   AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Glutamate N-acetyltransferase alpha chain {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Glutamate N-acetyltransferase beta chain {ECO:0000255|HAMAP-Rule:MF_01106};
GN   Name=argJ {ECO:0000255|HAMAP-Rule:MF_01106};
GN   OrderedLocusNames=MMP0897;
OS   Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2
OS   / LL).
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanococci; Methanococcales; Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
CC   -!- FUNCTION: Catalyzes the transfer of the acetyl group from N(2)-
CC       acetylornithine to glutamate, forming N-acetylglutamate and L-
CC       ornithine. {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(2)-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate +
CC         L-ornithine; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=2.3.1.35;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01106};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC       and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine
CC       (cyclic): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01106}.
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DR   EMBL; BX950229; CAF30453.1; -; Genomic_DNA.
DR   RefSeq; WP_011170841.1; NC_005791.1.
DR   AlphaFoldDB; P62065; -.
DR   SMR; P62065; -.
DR   STRING; 267377.MMP0897; -.
DR   MEROPS; T05.002; -.
DR   EnsemblBacteria; CAF30453; CAF30453; MMP0897.
DR   GeneID; 2761925; -.
DR   KEGG; mmp:MMP0897; -.
DR   PATRIC; fig|267377.15.peg.923; -.
DR   eggNOG; arCOG04413; Archaea.
DR   HOGENOM; CLU_027172_1_0_2; -.
DR   OrthoDB; 52592at2157; -.
DR   UniPathway; UPA00068; UER00111.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:L-glutamate N-acetyltransferase activity, acting on acetyl-CoA as donor; IEA:TreeGrafter.
DR   GO; GO:0004358; F:L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006592; P:L-ornithine biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd02152; OAT; 1.
DR   Gene3D; 3.30.2330.10; arginine biosynthesis bifunctional protein suprefamily; 1.
DR   Gene3D; 3.10.20.340; ArgJ beta chain, C-terminal domain; 1.
DR   Gene3D; 3.60.70.12; L-amino peptidase D-ALA esterase/amidase; 1.
DR   HAMAP; MF_01106; ArgJ; 1.
DR   InterPro; IPR002813; Arg_biosynth_ArgJ.
DR   InterPro; IPR016117; ArgJ-like_dom_sf.
DR   InterPro; IPR042195; ArgJ_beta_C.
DR   NCBIfam; TIGR00120; ArgJ; 1.
DR   NCBIfam; NF003802; PRK05388.1; 1.
DR   PANTHER; PTHR23100; ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ; 1.
DR   PANTHER; PTHR23100:SF0; ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ, MITOCHONDRIAL; 1.
DR   Pfam; PF01960; ArgJ; 1.
DR   SUPFAM; SSF56266; DmpA/ArgJ-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Autocatalytic cleavage; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..188
FT                   /note="Glutamate N-acetyltransferase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT                   /id="PRO_0000002279"
FT   CHAIN           189..408
FT                   /note="Glutamate N-acetyltransferase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT                   /id="PRO_0000002280"
FT   ACT_SITE        189
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         403
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         408
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   SITE            112
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   SITE            113
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   SITE            188..189
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
SQ   SEQUENCE   408 AA;  43749 MW;  90B738A0DCAAE179 CRC64;
     MAENFVVVDG GVVAPKGFKA NGHKDRKYGA ALIYSEADAV AAGVFTTNKV YAHPVALSKD
     TLVNNNVFRA IVANSGNANC FTKGGMEDAE LLVKKAAELL KIPENQVLSA STGVIGRKMP
     MDIISLEVER AFENITMESS NENASKAIMT TDAFPKTVAV EFEVNGKSVR IGGIAKGAGM
     IAPNMLHATM LGFITTDIEI SKEDLTNSLQ KATDESFNNA VVDGDMSTND TVYVLANAQS
     GVKYTDCKEE FDHALTYVSK ELAKMIVSDG EGAKKLIEAT VFGAETKEDA KKASMSIVRS
     LLLKTAVFGA DPNWGRIAAA VGYSGAEMDM NNFDIIISDI SSEKQAILVK AGEQIADCGT
     PELKLAEEIM KEDKIKIIVD LKMGSFENTA FGCDLGYDYV KINSEYTT
//