HAMAP rule MF_01656

General rule information [?]

Accession	MF_01656
Dates	30-APR-2008 (Created) 1-JUN-2023 (Last updated, Version 37)

Name

HOA

Scope

Bacteria

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]

Triggered by

HAMAP; MF_01656 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier

HOA

Protein name

RecName:		Full=4-hydroxy-2-oxovalerate aldolase;
		Short=HOA;
		EC 4.1.3.39;
AltName:		Full=4-hydroxy-2-keto-pentanoic acid aldolase;
AltName:		Full=4-hydroxy-2-oxopentanoate aldolase;

case <OC:Enterobacterales>

Gene name

mhpE

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
EC 4.1.3.39

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 [?]

Aromatic hydrocarbons catabolism
Lyase
Manganese
Metal-binding

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.

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