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HAMAP rule MF_01656

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General rule information [?]

Accession MF_01656
Dates 30-APR-2008 (Created)
1-JUN-2023 (Last updated, Version 37)
Name HOA
Templates P51020 (HOA_ECOLI); P51015 (HOA4_PARXL); Q9KWS0 (HOA_PSESP); P51014 (HOA_PSES1); Q51983 (HOA2_PSEP1); P51016 (HOA_PSEUF); P51018 (HOA1_PSEP1); P51019 (HOA2_PSEPU); Q53WI0 (HOA_THET8): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=4-hydroxy-2-oxovalerate aldolase;
AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase;
AltName: Full=4-hydroxy-2-oxopentanoate aldolase;
case <OC:Enterobacterales>
Gene name
end case

Comments [?]

case <OC:Enterobacterales>
Function Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds.
end case
Catalytic activity RHEA:22624: (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
case <OC:Enterobacterales>
Pathway Aromatic compound metabolism; 3-phenylpropanoate degradation.
Subunit Interacts with MhpF.
end case
Similarity Belongs to the 4-hydroxy-2-oxovalerate aldolase family.

Keywords [?]

Gene Ontology [?]

GO:0008701; Molecular function: 4-hydroxy-2-oxovalerate aldolase activity.
GO:0030145; Molecular function: manganese ion binding.
GO:0019439; Biological process: aromatic compound catabolic process.

Cross-references [?]

PROSITE PS50991; PYR_CT; 1; trigger=PRU01151;
Pfam PF07836; DmpG_comm; 1;
PF00682; HMGL-like; 1;
NCBIfam TIGR03217; 4OH_2_O_val_ald; 1;

Features [?]

From: HOA_PSEUF (P51016)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     17     18       /ligand="substrate     R-D  
ACT_SITE     21     21       Proton acceptor     H  
BINDING     18     18       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035     D  
BINDING     200     200       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035     H  
BINDING     202     202       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035     H  
BINDING     171     171       /ligand="substrate     S  
BINDING     200     200       /ligand="substrate     H  
BINDING     291     291       /ligand="substrate     Y  
SITE     17     17       Transition state stabilizer     R  

Additional information [?]

Size range 333-377 amino acids
Related rules None
Fusion None
Comments This protein is present in multiple copies in some organisms, each one being located in a cluster involved in the degragation of a different aromatic compound. The E.coli protein showed no observable dependence on divalent metal ions (and no loss of enzyme activity by treatment with EDTA) unlike the purified Pseudomonas sp. strain CF600 and Burkholderia xenovorans aldolases.