AC MF_01290; DC Protein; auto TR HAMAP; MF_01290; -; 1; level=0 XX Names: KDR_aldolase XX ID RHMA DE RecName: Full=2-keto-3-deoxy-L-rhamnonate aldolase; DE Short=KDR aldolase; DE EC=4.1.2.53; DE AltName: Full=2-dehydro-3-deoxyrhamnonate aldolase; GN Name=rhmA; XX CC -!- FUNCTION: Catalyzes the reversible retro-aldol cleavage of 2-keto-3- CC deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-dehydro-3-deoxy-L-rhamnonate = (S)-lactaldehyde + pyruvate; CC Xref=Rhea:RHEA:25784, ChEBI:CHEBI:15361, ChEBI:CHEBI:18041, CC ChEBI:CHEBI:58371; EC=4.1.2.53; case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; end case CC -!- SUBUNIT: Homohexamer. CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. KDR aldolase CC subfamily. XX DR Pfam; PF03328; HpcH_HpaI; 1; trigger=no XX KW Lyase case KW Magnesium KW Metal-binding end case XX case GO GO:0000287; F:magnesium ion binding end case GO GO:0016832; F:aldehyde-lyase activity XX FT From: RHMA_ECOLI (P76469) FT ACT_SITE 49 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: A FT BINDING 179 FT /ligand="substrate" FT Condition: D FT SITE 74 FT /note="Transition state stabilizer" FT Condition: R FT SITE 88 FT /note="Increases basicity of active site His" FT Condition: D XX Size: 267-267; Related: None; Template: P76469; Scope: Bacteria; Enterobacterales Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.14 2022/11/19 //