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 family protein |
Enzyme Information
| 1.14.99.3 |
Transferred entry: 1.14.14.18.
based on mapping to UniProt P9WKH3
|
| 1.14.14.18 |
Heme oxygenase (biliverdin-producing).
based on mapping to UniProt P9WKH3
Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H(2)O.
-!- This mammalian enzyme participates in the degradation of heme. -!- The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. -!- The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO. -!- The enzyme requires NAD(P)H and EC 1.6.2.4. -!- Cf. EC 1.14.15.20. -!- Formerly EC 1.14.99.3.
|
UniProtKB Entries (1)
| P9WKH3 |
MHUD_MYCTU
Mycobacterium tuberculosis H37Rv
Heme-degrading monooxygenase HmoB
|
PDB Structure
| PDB | 3HX9 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Unusual Diheme Conformation of the Heme-Degrading Protein from Mycobacterium tuberculosis
J.Mol.Biol.
|
