AC   MF_01108;
DC   Protein; auto
TR   HAMAP; MF_01108; -; 1; level=0
XX
Names: ArgE
XX
ID   ARGE
DE   RecName: Full=Acetylornithine deacetylase;
DE            Short=AO;
DE            Short=Acetylornithinase;
DE            EC=3.5.1.16;
DE   AltName: Full=N-acetylornithinase;
DE            Short=NAO;
GN   Name=argE;
XX
CC   -!- FUNCTION: Catalyzes the hydrolysis of the amide bond of N(2)-acetylated
CC       L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to
CC       form L-ornithine, an intermediate in L-arginine biosynthesis pathway,
CC       and a branchpoint in the synthesis of polyamines.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine;
CC         Xref=Rhea:RHEA:15941, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=3.5.1.16;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC       Note=Binds 2 Zn(2+) or Co(2+) ions per subunit.;
CC   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC       from N(2)-acetyl-L-ornithine (linear): step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
XX
DR   Pfam; PF01546; Peptidase_M20; 1; trigger=no
DR   NCBIfam; TIGR01892; AcOrn-deacetyl; 1; trigger=no
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1; trigger=no
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1; trigger=no
XX
KW   Cytoplasm
KW   Amino-acid biosynthesis
KW   Arginine biosynthesis
KW   Hydrolase
KW   Metal-binding
KW   Cobalt
KW   Zinc
XX
GO   GO:0008777; F:acetylornithine deacetylase activity
GO   GO:0008270; F:zinc ion binding
GO   GO:0006526; P:arginine biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: ARGE_ECOLI (P23908)
FT   ACT_SITE        82
FT   Condition: D
FT   ACT_SITE        144
FT   Condition: E
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Condition: H
XX
Size: 378-389;
Related: None;
Template: P23908;
Scope:
 Bacteria; Enterobacterales
 Bacteria; Vibrionales
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.39 2023/06/01
//