AC MF_01292; DC Protein; auto TR HAMAP; MF_01292; -; 1; level=0 XX Names: HKHD_aldolase XX ID HPCH DE RecName: Full=4-hydroxy-2-oxo-heptane-1,7-dioate aldolase; DE EC=4.1.2.52; DE AltName: Full=2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; DE Short=HHED aldolase; DE AltName: Full=4-hydroxy-2-ketoheptane-1,7-dioate aldolase; DE Short=HKHD aldolase; GN Name=hpcH; Synonyms=hpaI; XX CC -!- FUNCTION: Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2- CC ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-hydroxy-2-oxoheptanedioate = pyruvate + succinate CC semialdehyde; Xref=Rhea:RHEA:25788, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:57706, ChEBI:CHEBI:73036; EC=4.1.2.52; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Note=Binds 1 divalent metal cation per subunit.; CC -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate CC degradation; pyruvate and succinate semialdehyde from 4- CC hydroxyphenylacetate: step 7/7. CC -!- SUBUNIT: Homohexamer; trimer of dimers. CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. XX DR Pfam; PF03328; HpcH_HpaI; 1; trigger=no DR NCBIfam; TIGR02311; HpaI; 1; trigger=no XX KW Aromatic hydrocarbons catabolism KW Lyase KW Metal-binding XX GO GO:0016832; F:aldehyde-lyase activity GO GO:0046872; F:metal ion binding GO GO:0019439; P:aromatic compound catabolic process XX FT From: HPCH_ECOLX (Q47098) FT ACT_SITE 45 FT /note="Proton acceptor" FT Condition: H FT BINDING 149 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Condition: E FT BINDING 175 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Condition: D FT BINDING 147 FT /ligand="substrate" FT Condition: Q FT BINDING 174 FT /ligand="substrate" FT Condition: A FT BINDING 175 FT /ligand="substrate" FT Condition: D FT SITE 70 FT /note="Transition state stabilizer" FT Condition: R FT SITE 84 FT /note="Increases basicity of active site His" FT Condition: D XX Size: 262-267; Related: None; Template: Q47098; Scope: Bacteria; Enterobacterales Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.14 2023/06/01 //