AC   MF_01374;
DC   Protein; auto
TR   HAMAP; MF_01374; -; 1; level=0
XX
Names: Glyoxalase_2
XX
ID   GLO2
DE   RecName: Full=Hydroxyacylglutathione hydrolase;
DE            EC=3.1.2.6;
DE   AltName: Full=Glyoxalase II;
DE            Short=Glx II;
GN   Name=gloB;
XX
CC   -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC       glutathione to form glutathione and D-lactic acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy
CC         carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit.;
CC   -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC       (R)-lactate from methylglyoxal: step 2/2.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       Glyoxalase II family.
XX
DR   Pfam; PF16123; HAGH_C; 1; trigger=no
DR   Pfam; PF00753; Lactamase_B; 1; trigger=no
DR   PIRSF; PIRSF005457; Glx; 1; trigger=no
DR   NCBIfam; TIGR03413; GSH_gloB; 1; trigger=no
XX
KW   Hydrolase
KW   Metal-binding
KW   Zinc
XX
GO   GO:0004416; F:hydroxyacylglutathione hydrolase activity
XX
FT   From: GLO2_ECOLI (P0AC84)
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: H
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: H
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 2; Condition: D
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 2; Condition: H
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: H
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: D
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 2; Condition: D
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 2; Condition: H
XX
Size: 233-272;
Related: None;
Template: P0AC84; Q8ZRM2;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in VIBVY
Plasmid: None
Comments: None
XX
# Revision 1.14 2023/06/01
//