CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.30 | Glucose Oxidase; domain 1 |
|
3.50.30.40 | Ribonuclease E inhibitor RraA/RraA-like |
Domain Context
CATH Clusters
| Superfamily | Ribonuclease E inhibitor RraA/RraA-like |
| Functional Family | 4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase |
Enzyme Information
| 4.1.3.17 |
4-hydroxy-4-methyl-2-oxoglutarate aldolase.
based on mapping to UniProt A5W059
(1) 4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate. (2) 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate.
-!- This enzyme participates in the degradation of protocatechuate (via the meta-cleavage pathway), phthalate, syringate and gallate. -!- The enzyme from Pseudomonas ochraceae can also cleave 4-hydroxy-2- oxoglutarate to glyoxylate and pyruvate, and also catalyzes the reaction of EC 4.1.1.3.
|
| 4.1.1.3 |
Oxaloacetate decarboxylase.
based on mapping to UniProt A5W059
Oxaloacetate = pyruvate + CO(2).
-!- The enzyme from Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. -!- The process is accompanied by the extrusion of two sodium ions from cells. -!- Some animal enzymes require manganese.
|
UniProtKB Entries (1)
| A5W059 |
HMGA_PSEP1
Pseudomonas putida F1
4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase
|
PDB Structure
| PDB | 3NOJ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural and Kinetic Characterization of 4-Hydroxy-4-methyl-2-oxoglutarate/4-Carboxy-4-hydroxy-2-oxoadipate Aldolase, a Protocatechuate Degradation Enzyme Evolutionarily Convergent with the HpaI and DmpG Pyruvate Aldolases.
J.Biol.Chem.
|