AC   MF_01106;
DC   Protein; auto
c?   <OC:Bacteria> or <OC:Archaea>
TR   HAMAP; MF_01106; -; 1; level=0
XX
Names: ArgJ
XX
case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
ID   ARGJ
DE   RecName: Full=Glutamate N-acetyltransferase;
DE            EC=2.3.1.35;
DE   AltName: Full=Ornithine acetyltransferase;
DE            Short=OATase;
DE   AltName: Full=Ornithine transacetylase;
DE   Contains:
DE     RecName: Full=Glutamate N-acetyltransferase alpha chain;
DE   Contains:
DE     RecName: Full=Glutamate N-acetyltransferase beta chain;
GN   Name=argJ;
else
ID   ARGJ
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ;
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase;
DE              EC=2.3.1.35;
DE     AltName: Full=Ornithine acetyltransferase;
DE              Short=OATase;
DE     AltName: Full=Ornithine transacetylase;
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase;
DE              EC=2.3.1.1;
DE     AltName: Full=N-acetylglutamate synthase;
DE              Short=AGSase;
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain;
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain;
GN   Name=argJ;
end case
XX
case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
CC   -!- FUNCTION: Catalyzes the transfer of the acetyl group from N(2)-
CC       acetylornithine to glutamate, forming N-acetylglutamate and L-
CC       ornithine.
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   -!- 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.
else
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   -!- 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   -!- 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   -!- 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.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4.
end case
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the ArgJ family.
XX
DR   Pfam; PF01960; ArgJ; 1; trigger=no
DR   NCBIfam; TIGR00120; ArgJ; 1; trigger=no
XX
KW   Cytoplasm
KW   Amino-acid biosynthesis
KW   Arginine biosynthesis
KW   Autocatalytic cleavage
case not <OC:Methanobacteria> and not <OC:Methanococci> and not <OC:Methanomicrobia> and not <OC:Methanopyri>
KW   Multifunctional enzyme
end case
KW   Transferase
KW   Acyltransferase
XX
case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
GO   GO:0004358; F:L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
else
GO   GO:0004358; F:L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
GO   GO:0004042; F:L-glutamate N-acetyltransferase activity
end case
GO   GO:0006526; P:L-arginine biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: ARGJ_MYCTU (P9WPZ3)
case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
FT   CHAIN           Nter..199
FT                   /note="Glutamate N-acetyltransferase alpha chain"
FT   CHAIN           200..Cter
FT                   /note="Glutamate N-acetyltransferase beta chain"
else
FT   CHAIN           Nter..199
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT   CHAIN           200..Cter
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
end case
FT   ACT_SITE        200
FT                   /note="Nucleophile"
FT   Condition: [TS]
FT   BINDING         166
FT                   /ligand="substrate"
FT   Condition: T
FT   BINDING         189
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         200
FT                   /ligand="substrate"
FT   Condition: [TS]
FT   BINDING         280
FT                   /ligand="substrate"
FT   Condition: E
FT   BINDING         399
FT                   /ligand="substrate"
FT   Condition: N
FT   BINDING         404
FT                   /ligand="substrate"
FT   Condition: [ST]
FT   SITE            127
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT   Condition: T
FT   SITE            128
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT   Condition: G
FT   SITE            199..200
FT                   /note="Cleavage; by autolysis"
FT   Condition: [AG]-[TS]
XX
Size: 379-432;
Related: None;
Template: Q07908; P9WPZ3; Q9Z4S1; P0DJQ5; Q9K8V3; Q57645;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in NOSS1, CLOAB
Plasmid: None
Comments: Some archaea/bacteria possess a monofunctional ArgJ, i.e., capable of
 catalyzing only the fifth step of the arginine biosynthetic pathway.
XX
# Version: 39
# Last updated date: 2025-06-12
# Created date: 2005-02-28
//