ID   ARGJ_NEIGO              Reviewed;         406 AA.
AC   P38434; Q53567;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-SEP-2026, entry version 126.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Includes:
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   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01106};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              Short=AGSase {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_01106};
GN   Name=argJ {ECO:0000255|HAMAP-Rule:MF_01106};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CDC 50;
RX   PubMed=1339419; DOI=10.1128/jb.174.8.2694-2701.1992;
RA   Martin P.R., Mulks M.H.;
RT   "Sequence analysis and complementation studies of the argJ gene encoding
RT   ornithine acetyltransferase from Neisseria gonorrhoeae.";
RL   J. Bacteriol. 174:2694-2701(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRL 30465;
RX   PubMed=1339413; DOI=10.1128/iai.60.3.970-975.1992;
RA   Martin P.R., Mulks M.H.;
RT   "Molecular characterization of the argJ mutation in Neisseria gonorrhoeae
RT   strains with requirements for arginine, hypoxanthine, and uracil.";
RL   Infect. Immun. 60:970-975(1992).
CC   -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC       version of arginine biosynthesis: the synthesis of N-acetylglutamate
CC       from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by
CC       transacetylation between N(2)-acetylornithine and glutamate.
CC       {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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+);
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         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   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4. {ECO:0000255|HAMAP-
CC       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; M65216; AAA25447.1; -; Genomic_DNA.
DR   EMBL; S85363; AAB21605.2; -; Genomic_DNA.
DR   PIR; A43850; A43850.
DR   AlphaFoldDB; P38434; -.
DR   SMR; P38434; -.
DR   MEROPS; T05.001; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00111.
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:UniProtKB-UniRule.
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   FunFam; 3.10.20.340:FF:000001; Arginine biosynthesis bifunctional protein ArgJ, chloroplastic; 1.
DR   FunFam; 3.60.70.12:FF:000001; Arginine biosynthesis bifunctional protein ArgJ, chloroplastic; 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; Multifunctional enzyme; Transferase.
FT   CHAIN           1..189
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT                   /id="PRO_0000002197"
FT   CHAIN           190..406
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT                   /id="PRO_0000002198"
FT   ACT_SITE        190
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         401
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         406
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   SITE            119
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            120
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            189..190
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   CONFLICT        120
FT                   /note="G -> A (in Ref. 2; AAB21605)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   406 AA;  42866 MW;  5515EA4EB7503814 CRC64;
     MAVNLTEKTA EQLPDIDGIA LYTAQAGVKK PGHTDLTLIA VAAGSTVGAV FTTNRFCAAP
     VHIAKSHLFD EDGVRALVIN TGNANAGTGA QGRIDALAVC AAAARQIGCK PNQVMPFSTG
     VILEPLPADK IIAALPKMQP AFWNEAARAI MTTDTVPKAA SREGKVGDQH TVRATGIAKG
     SGMIHPNMAT MLGFIATDAK VSQPVLQLMT QEIADETFNT ITVDGDTSTN DSFVIIATGK
     NSQSEIDNIA DPRYAQLKEL LCSLALELAQ AIVRDGEGAT KFITVRVENA KTCDEARQAA
     YAAARSPLVK TAFFASDPNL GKRLAAIGYA DVADLDTDLV EMYLDDILVA EHGGRAASYT
     EAQGQAVMSK DEITVRIKLH RGQAAATVYT CDLSHGYVSI NADYRS
//