HAMAP logo

HAMAP rule MF_01106

Send feedback

General rule information [?]

Accession MF_01106
Dates 28-MAR-2003 (Created)
1-JUN-2023 (Last updated, Version 38)
Name ArgJ
Scope(s) Bacteria
Archaea
Template(s) Q07908 (ARGJ_GEOSE); P9WPZ3 (ARGJ_MYCTU); Q9Z4S1 (ARGJ_THENN); P0DJQ5 (GNAT2_STRCL); Q9K8V3 (ARGJ_HALH5); [ Recover all ]
Triggered by
case c? <OC:Bacteria> or <OC:Archaea>
HAMAP; MF_01106 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier ARGJ
Protein name RecName: Full=Arginine biosynthesis bifunctional protein ArgJ;
                 Includes:
RecName: Full=Glutamate N-acetyltransferase;
                 EC=2.3.1.35;
AltName: Full=Ornithine acetyltransferase;
                 Short=OATase;
AltName: Full=Ornithine transacetylase;
                 Includes:
RecName: Full=Amino-acid acetyltransferase;
                 EC=2.3.1.1;
AltName: Full=N-acetylglutamate synthase;
                 Short=AGSase;
                 Contains:
RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain;
                 Contains:
RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain;
Gene name Name=argJ;

Comments [?]

FUNCTIONCatalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
CATALYTIC ACTIVITY Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N- acetyl-L-glutamate; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=2.3.1.35;
CATALYTIC ACTIVITY Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
PATHWAYAmino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
PATHWAYAmino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 1/4.
SUBUNITHeterotetramer of two alpha and two beta chains.
SUBCELLULAR LOCATIONCytoplasm.
MISCELLANEOUSSome bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
SIMILARITYBelongs to the ArgJ family.

Keywords [?]

Cytoplasm
Amino-acid biosynthesis
Arginine biosynthesis
Autocatalytic cleavage
Multifunctional enzyme
Transferase
Acyltransferase

Gene Ontology [?]

GO:0004042; Molecular function:acetyl-CoA:L-glutamate N-acetyltransferase activity
GO:0004358; Molecular function:glutamate N-acetyltransferase activity
GO:0006526; Biological process:arginine biosynthetic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF01960; ArgJ; 1;
NCBIfam TIGR00120; ArgJ; 1;

Features [?]

From: ARGJ_MYCTU (P9WPZ3)
Key From To Description Tag Condition FTGroup
CHAIN Nter 199 /note="Arginine biosynthesis bifunctional protein ArgJ alpha chain"
CHAIN 200 Cter /note="Arginine biosynthesis bifunctional protein ArgJ beta chain"
ACT_SITE 200 200 /note="Nucleophile" [TS]
BINDING 166 166 /ligand="substrate" T
BINDING 189 189 /ligand="substrate" K
BINDING 200 200 /ligand="substrate" [TS]
BINDING 280 280 /ligand="substrate" E
BINDING 399 399 /ligand="substrate" N
BINDING 404 404 /ligand="substrate" [ST]
SITE 127 127 /note="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" T
SITE 128 128 /note="Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole" G
SITE 199 200 /note="Cleavage; by autolysis" [AG]-[TS]

Additional information [?]

Size range 379-432 amino acids
Related rules None
Fusion Nter: None Cter: None



View rule in raw text format (no links)