HAMAP rule MF_01656
General rule information
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| Accession | MF_01656 |
| Dates | 30-APR-2008 (Created)
28-NOV-2023 (Last updated, Version 38) |
| Name | HOA |
| Scope(s) |
Bacteria |
| Template(s) | 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
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Identifier, protein and gene names
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| 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 | Name=mhpE; |
| end case | |
Comments
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| 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 | Reaction=(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate; Xref=Rhea:RHEA:22624, ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:73143; 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
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Gene Ontology
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| 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
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| PROSITE | PS50991; PYR_CT; 1; |
| Pfam | PF07836; DmpG_comm; 1; |
| Pfam | PF00682; HMGL-like; 1; |
| NCBIfam | TIGR03217; 4OH_2_O_val_ald; 1; |
Features
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| From: HOA_PSEUF (P51016) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 17 | 18 | /ligand="substrate" | R-D | ||||||||
| ACT_SITE | 21 | 21 | /note="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 | /note="Transition state stabilizer" | R | ||||||||
Additional information
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| Size range | 333-377 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: 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. |