CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.70 | Alpha-Beta Plaits |
|
3.30.70.100 |
Domain Context
CATH Clusters
| Superfamily | 3.30.70.100 |
| Functional Family | Antibiotic biosynthesis monooxygenase |
Enzyme Information
| 1.14.99.57 |
Heme oxygenase (mycobilin-producing).
based on mapping to UniProt P9WKH3
(1) Protoheme + 3 reduced acceptor + 3 O(2) = mycobilin a + Fe(2+) + 3 acceptor + 3 H(2)O. (2) Protoheme + 3 reduced acceptor + 3 O(2) = mycobilin b + Fe(2+) + 3 acceptor + 3 H(2)O.
-!- The enzyme, characterized from the bacterium Mycobacterium tuberculosis, is involved in heme degradation and iron utilization. -!- The enzyme binds two stacked protoheme molecules per monomer. -!- Unlike the canonical heme oxygenases, the enzyme does not release carbon monoxide or formaldehyde; instead, it forms unique products, named mycobilins, that retain the alpha-meso-carbon at the ring cleavage site as an aldehyde group. -!- EC 1.6.2.4.
|
UniProtKB Entries (1)
| P9WKH3 |
MHUD_MYCTU
Mycobacterium tuberculosis H37Rv
Heme oxygenase (mycobilin-producing)
|
PDB Structure
| PDB | 4NL5 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystallographic and Spectroscopic Insights into Heme Degradation by Mycobacterium tuberculosis MhuD.
Inorg.Chem.
|