HAMAP rule MF_01292
General rule information
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Accession | MF_01292 |
Dates | 3-OCT-2008 (Created)
1-JUN-2023 (Last updated, Version 14) |
Name | HKHD_aldolase |
Scope(s) |
Bacteria Enterobacterales |
Template(s) | Q47098 (HPCH_ECOLX); [ Recover all ] |
Triggered by |
HAMAP; MF_01292 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | HPCH |
Protein name | RecName: Full=4-hydroxy-2-oxo-heptane-1,7-dioate aldolase; EC=4.1.2.52; AltName: Full=2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; Short=HHED aldolase; AltName: Full=4-hydroxy-2-ketoheptane-1,7-dioate aldolase; Short=HKHD aldolase; |
Gene name | Name=hpcH; Synonyms=hpaI; |
Comments
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FUNCTION | Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2- ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde. |
CATALYTIC ACTIVITY | Reaction=4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde; Xref=Rhea:RHEA:25788, ChEBI:CHEBI:15361, ChEBI:CHEBI:57706, ChEBI:CHEBI:73036; EC=4.1.2.52; |
COFACTOR | Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Note=Binds 1 divalent metal cation per subunit.; |
PATHWAY | Aromatic compound metabolism; 4-hydroxyphenylacetate degradation; pyruvate and succinate semialdehyde from 4- hydroxyphenylacetate: step 7/7. |
SUBUNIT | Homohexamer; trimer of dimers. |
SIMILARITY | Belongs to the HpcH/HpaI aldolase family. |
Keywords
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Gene Ontology
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GO:0016832; Molecular function:aldehyde-lyase activity |
GO:0046872; Molecular function:metal ion binding |
GO:0019439; Biological process:aromatic compound catabolic process |
Cross-references
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Features
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From: HPCH_ECOLX (Q47098) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 45 | 45 | /note="Proton acceptor" | H | ||||||||
BINDING | 149 | 149 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" |
E | ||||||||
BINDING | 175 | 175 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" |
D | ||||||||
BINDING | 147 | 147 | /ligand="substrate" | Q | ||||||||
BINDING | 174 | 174 | /ligand="substrate" | A | ||||||||
BINDING | 175 | 175 | /ligand="substrate" | D | ||||||||
SITE | 70 | 70 | /note="Transition state stabilizer" | R | ||||||||
SITE | 84 | 84 | /note="Increases basicity of active site His" | D |
Additional information
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Size range | 262-267 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |