AC   MF_03124;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_01106; -; 1; level=0
XX
Names: ArgJ_euk
XX
ID   ARGJ
case <OC:Viridiplantae>
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, chloroplastic;
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase;
DE              Short=GAT;
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=AGS;
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain;
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain;
DE   Flags: Precursor;
else
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, mitochondrial;
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase;
DE              Short=GAT;
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=AGS;
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain;
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain;
DE   Flags: Precursor;
end case
case <OC:Saccharomyces>
GN   Name=ARG7;
end case
XX
CC   -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC       version of arginine biosynthesis: the synthesis of acetylglutamate from
CC       glutamate and acetyl-CoA, and of ornithine by transacetylation between
CC       acetylornithine and glutamate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-
CC         acetyl-L-glutamate; 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=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; 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.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
case <OC:Viridiplantae>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
else
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
end case
case not <OC:Viridiplantae>
CC   -!- PTM: The alpha and beta chains are autoproteolytically processed from a
CC       single precursor protein within the mitochondrion.
end case
case not <OC:Saccharomyces> and not <AnyFeature:TransitM>
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted.
end case
CC   -!- SIMILARITY: Belongs to the ArgJ family.
XX
DR   Pfam; PF01960; ArgJ; 1; trigger=no
DR   NCBIfam; TIGR00120; ArgJ; 1; trigger=no
case not <OC:Saccharomyces>
DR   General; TransitM; -; 0-1; trigger=yes
end case
XX
KW   Acyltransferase
KW   Amino-acid biosynthesis
KW   Arginine biosynthesis
KW   Autocatalytic cleavage
case <OC:Viridiplantae>
KW   Chloroplast
KW   Plastid
else
KW   Mitochondrion
end case
KW   Multifunctional enzyme
KW   Transferase
case <OC:Saccharomyces>
KW   Transit peptide
end case
XX
GO   GO:0006526; P:arginine biosynthetic process
GO   GO:0004358; F:glutamate N-acetyltransferase activity
GO   GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity
case <OC:Viridiplantae>
GO   GO:0009507; C:chloroplast
else
GO   GO:0005759; C:mitochondrial matrix
end case
XX
FT   From: ARGJ_YEAST (Q04728)
case <OC:Saccharomyces>
FT   TRANSIT         Nter..8
FT                   /note="Mitochondrion"
FT   CHAIN           9..214
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
else
FT   CHAIN           Nter..214
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
end case
FT   CHAIN           215..Cter
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT   SITE            214..215
FT                   /note="Cleavage; by autolysis"
FT   Condition: A-T
FT   From: ARGJ_MYCTU (P9WPZ3)
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
XX
Size: 428-520;
Related: None;
Template: Q04728; Q3C251;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in BOTFB
Plasmid: None
Comments: None
XX
# Revision 1.11 2023/06/01
//