AC   MF_01669;
DC   Protein; auto
TR   HAMAP; MF_01669; -; 1; level=0
XX
Names: IolD
XX
ID   IOLD
DE   RecName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase;
DE            Short=THcHDO hydrolase;
DE            EC=3.7.1.22;
GN   Name=iolD;
XX
CC   -!- FUNCTION: Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)-
CC       trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate
CC       (5DG).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3D-3,5/4-trihydroxycyclohexane-1,2-dione + H2O = 5-deoxy-D-
CC         glucuronate + H(+); Xref=Rhea:RHEA:25836, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28446, ChEBI:CHEBI:58852; EC=3.7.1.22;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC       Note=Binds 1 thiamine pyrophosphate per subunit.;
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC       acetyl-CoA from myo-inositol: step 3/7.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
XX
DR   PROSITE; PS00187; TPP_ENZYMES; 1; trigger=no
DR   Pfam; PF02775; TPP_enzyme_C; 1; trigger=no
DR   Pfam; PF00205; TPP_enzyme_M; 1; trigger=no
DR   Pfam; PF02776; TPP_enzyme_N; 1; trigger=no
XX
KW   Hydrolase
KW   Magnesium
KW   Metal-binding
KW   NAD
KW   Thiamine pyrophosphate
XX
GO   GO:0000287; F:magnesium ion binding
GO   GO:0016787; F:hydrolase activity
GO   GO:0030976; F:thiamine pyrophosphate binding
GO   GO:0019310; P:inositol catabolic process
XX
FT   From: IOLD_BACSU (P42415)
FT   REGION          442..522
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         493
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         520
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: N
FT   BINDING         66
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT   Condition: E
XX
Size: 637-645;
Related: None;
Template: P42415;
Scope:
 Bacteria; Bacillota
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACCZ
Plasmid: in BACCZ
Comments: None
XX
# Revision 1.14 2023/01/13
//