AC   MF_01288;
DC   Protein; auto
TR   HAMAP; MF_01288; -; 1; level=0
XX
Names: Rhamnon_dehydrat
XX
ID   RHMD
case <OC:Bacteria>
DE   RecName: Full=L-rhamnonate dehydratase;
DE            Short=RhamD;
DE            EC=4.2.1.90;
end case
case <OC:Archaea>
DE   RecName: Full=Putative L-rhamnonate dehydratase;
DE            Short=RhamD;
DE            EC=4.2.1.90;
end case
GN   Name=rhmD;
XX
CC   -!- FUNCTION: Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-
CC       L-rhamnonate (KDR).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O;
CC         Xref=Rhea:RHEA:23080, ChEBI:CHEBI:15377, ChEBI:CHEBI:58118,
CC         ChEBI:CHEBI:58371; EC=4.2.1.90;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
end case
case <OC:Pseudomonadota>
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers.
end case
CC   -!- MISCELLANEOUS: Reaction proceeds via a syn dehydration.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. RhamD subfamily.
XX
DR   PROSITE; PS00908; MR_MLE_1; 1; trigger=no
DR   PROSITE; PS00909; MR_MLE_2; 1; trigger=no
DR   Pfam; PF01188; MR_MLE; 1; trigger=no
DR   Pfam; PF02746; MR_MLE_N; 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:0050032; F:L-rhamnonate dehydratase activity
XX
FT   From: RHMD_SALTY (Q8ZNF9)
FT   ACT_SITE        329
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: E
FT   BINDING         280
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: E
FT   BINDING         33
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         59
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         349
FT                   /ligand="substrate"
FT   Condition: E
FT   SITE            302
FT                   /note="Increases basicity of active site His"
FT   Condition: D
FT   SITE            349
FT                   /note="Transition state stabilizer"
FT   Condition: E
XX
Size: 390-428;
Related: None;
Template: Q8ZNF9; P77215; Q12DF1;
Scope:
 Bacteria; Actinomycetota
 Bacteria; Pseudomonadota
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.14 2023/01/26
//