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Annotation rule MF_01291
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General rule information [?]

Accession MF_01291
Dates 3-OCT-2008 (Created)
19-NOV-2019 (Last updated, Version 14)
Name KDGluc_aldolase
Scope
Bacteria; Gammaproteobacteria
Template P23522 (GARL_ECOLI)

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
GARL
Protein name
RecName: Full=5-keto-4-deoxy-D-glucarate aldolase;
Short=KDGluc aldolase;
Short=KDGlucA;
EC 4.1.2.20;
AltName: Full=2-dehydro-3-deoxy-D-glucarate aldolase;
AltName: Full=2-keto-3-deoxy-D-glucarate aldolase;
AltName: Full=5-dehydro-4-deoxy-D-glucarate aldolase;
AltName: Full=Alpha-keto-beta-deoxy-D-glucarate aldolase;
Gene name
garL

Comments [?]

Function Catalyzes the reversible retro-aldol cleavage of both 5-keto-4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde.
Catalytic activity RHEA:27726: 5-dehydro-4-deoxy-D-glucarate = 2-hydroxy-3-oxopropanoate + pyruvate
RHEA:10268: 2-dehydro-3-deoxy-D-glucarate = 2-hydroxy-3-oxopropanoate + pyruvate
EC 4.1.2.20
case <FTGroup:1>
Cofactor Mg(2+)
Note: Binds 1 Mg(2+) ion per subunit.
end case
Pathway Carbohydrate acid metabolism; galactarate degradation; D-glycerate from galactarate: step 2/3.
Subunit Homohexamer; trimer of dimers.
Similarity Belongs to the HpcH/HpaI aldolase family. KDGluc aldolase subfamily.

Keywords [?]

case <FTGroup:1>
end case

Gene Ontology [?]

case <FTGroup:1>
GO:0000287; Molecular function: magnesium ion binding.
end case
GO:0008672; Molecular function: 2-dehydro-3-deoxyglucarate aldolase activity.
GO:0042838; Biological process: D-glucarate catabolic process.
GO:0046392; Biological process: galactarate catabolic process.

Cross-references [?]

Pfam PF03328; HpcH_HpaI; 1;
TIGRFAMs TIGR03239; GarL; 1;

Features [?]

From: GARL_ECOLI (P23522)
Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     50     50       Proton acceptor     H  
METAL     153     153       Magnesium     E   1
METAL     179     179       Magnesium     D   1
BINDING     151     151       Substrate     Q  
BINDING     178     178       Substrate; via amide nitrogen     S  
BINDING     179     179       Substrate     D  
SITE     75     75       Transition state stabilizer     R  
SITE     89     89       Increases basicity of active site His     D  

Additional information [?]

Size range 250-282 amino acids
Related rules None
Fusion None