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 |
Enzyme Information
| 4.1.3.17 |
4-hydroxy-4-methyl-2-oxoglutarate aldolase.
based on mapping to UniProt Q5SIP7
(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.
|
| 4.1.1.112 |
Oxaloacetate decarboxylase.
based on mapping to UniProt Q5SIP7
Oxaloacetate = pyruvate + CO(2).
-!- The enzymes from the fish Gadus morhua (Atlantic cod) and the bacterium Micrococcus luteus prefer Mn(2+), while those from the bacteria Pseudomonas putida and Pseudomonas aeruginosa prefer Mg(2+). -!- Unlike EC 7.2.4.2, there is no evidence of the enzyme's involvement in Na(+) transport. -!- Formerly EC 4.1.1.3.
|
UniProtKB Entries (1)
| Q5SIP7 |
RRAAH_THET8
Thermus thermophilus HB8
4-hydroxy-4-methyl-2-oxoglutarate aldolase
|
PDB Structure
| PDB | 1J3L |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of the RNA-processing inhibitor RraA from Thermus thermophilis.
Acta Crystallogr.,Sect.D
|
