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HAMAP rule MF_01288

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General rule information [?]

Accession MF_01288
Dates 19-SEP-2008 (Created)
26-JAN-2023 (Last updated, Version 14)
Name Rhamnon_dehydrat
Scope
Bacteria; Actinomycetota
Bacteria; Pseudomonadota
Archaea
Templates Q8ZNF9 (RHMD_SALTY); P77215 (RHMD_ECOLI); Q12DF1 (RHMD_POLSJ): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
RHMD
case <OC:Bacteria>
Protein name
RecName: Full=L-rhamnonate dehydratase;
Short=RhamD;
EC 4.2.1.90;
end case
case <OC:Archaea>
Protein name
RecName: Full=Putative L-rhamnonate dehydratase;
Short=RhamD;
EC 4.2.1.90;
end case
Gene name
rhmD

Comments [?]

Function Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-L-rhamnonate (KDR).
Catalytic activity RHEA:23080: L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O
EC 4.2.1.90
case <FTGroup:1>
Cofactor Mg(2+)
Note: Binds 1 Mg(2+) ion per subunit.
end case
case <OC:Pseudomonadota>
Subunit Homooctamer; tetramer of dimers.
end case
Miscellaneous Reaction proceeds via a syn dehydration.
Similarity Belongs to the mandelate racemase/muconate lactonizing enzyme family. RhamD subfamily.

Keywords [?]

Lyase
case <FTGroup:1>
Magnesium
Metal-binding
end case

Gene Ontology [?]

case <FTGroup:1>
GO:0000287; Molecular function: magnesium ion binding.
end case
GO:0050032; Molecular function: L-rhamnonate dehydratase activity.

Cross-references [?]

PROSITE PS00908; MR_MLE_1; 1;
PS00909; MR_MLE_2; 1;
Pfam PF01188; MR_MLE; 1;
PF02746; MR_MLE_N; 1;

Features [?]

From: RHMD_SALTY (Q8ZNF9)
Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     329     329       Proton acceptor     H  
BINDING     226     226       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420     D   1
BINDING     252     252       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420     E   1
BINDING     280     280       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420     E   1
BINDING     33     33       /ligand="substrate     H  
BINDING     59     59       /ligand="substrate     R  
BINDING     349     349       /ligand="substrate     E  
SITE     302     302       Increases basicity of active site His     D  
SITE     349     349       Transition state stabilizer     E  

Additional information [?]

Size range 390-428 amino acids
Related rules None
Fusion None


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