AC   MF_01291;
DC   Protein; auto
TR   HAMAP; MF_01291; -; 1; level=0
XX
Names: KDGluc_aldolase
XX
ID   GARL
DE   RecName: Full=5-keto-4-deoxy-D-glucarate aldolase;
DE            Short=KDGluc aldolase;
DE            Short=KDGlucA;
DE            EC=4.1.2.20;
DE   AltName: Full=2-dehydro-3-deoxy-D-glucarate aldolase;
DE   AltName: Full=2-keto-3-deoxy-D-glucarate aldolase;
DE   AltName: Full=5-dehydro-4-deoxy-D-glucarate aldolase;
DE   AltName: Full=Alpha-keto-beta-deoxy-D-glucarate aldolase;
GN   Name=garL;
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CC   -!- FUNCTION: Catalyzes the reversible retro-aldol cleavage of both 5-keto-
CC       4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and
CC       tartronic semialdehyde.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-dehydro-4-deoxy-D-glucarate = 2-hydroxy-3-oxopropanoate +
CC         pyruvate; Xref=Rhea:RHEA:27726, ChEBI:CHEBI:15361, ChEBI:CHEBI:42819,
CC         ChEBI:CHEBI:57978;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-3-deoxy-D-glucarate = 2-hydroxy-3-oxopropanoate +
CC         pyruvate; Xref=Rhea:RHEA:10268, ChEBI:CHEBI:15361, ChEBI:CHEBI:57978,
CC         ChEBI:CHEBI:58098; EC=4.1.2.20;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
end case
CC   -!- PATHWAY: Carbohydrate acid metabolism; galactarate degradation; D-
CC       glycerate from galactarate: step 2/3.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. KDGluc aldolase
CC       subfamily.
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DR   Pfam; PF03328; HpcH_HpaI; 1; trigger=no
DR   NCBIfam; TIGR03239; GarL; 1; trigger=no
XX
KW   Lyase
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
XX
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0008672; F:2-dehydro-3-deoxyglucarate aldolase activity
GO   GO:0042838; P:D-glucarate catabolic process
GO   GO:0046392; P:galactarate catabolic process
XX
FT   From: GARL_ECOLI (P23522)
FT   ACT_SITE        50
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: E
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         151
FT                   /ligand="substrate"
FT   Condition: Q
FT   BINDING         178
FT                   /ligand="substrate"
FT   Condition: S
FT   BINDING         179
FT                   /ligand="substrate"
FT   Condition: D
FT   SITE            75
FT                   /note="Transition state stabilizer"
FT   Condition: R
FT   SITE            89
FT                   /note="Increases basicity of active site His"
FT   Condition: D
XX
Size: 250-282;
Related: None;
Template: P23522;
Scope:
 Bacteria; Gammaproteobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.17 2023/06/01
//