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 | Heme oxygenase (staphylobilin-producing) |
Enzyme Information
| 1.14.99.48 |
Heme oxygenase (staphylobilin-producing).
based on mapping to UniProt Q7A649
(1) Protoheme + 5 reduced acceptor + 4 O(2) = 5-oxo-delta-bilirubin + Fe(2+) + formaldehyde + 5 acceptor + 4 H(2)O. (2) Protoheme + 5 reduced acceptor + 4 O(2) = 15-oxo-beta-bilirubin + Fe(2+) + formaldehyde + 5 acceptor + 4 H(2)O.
-!- This enzyme, which is found in some pathogenic bacteria, is involved in an iron acquisition system that catabolizes the host's hemoglobin. -!- The two enzymes from the bacterium Staphylococcus aureus, encoded by the isdG and isdI genes, produce 67.5 % and 56.2 % 5-oxo-delta- bilirubin, respectively.
|
| 1.14.14.18 |
Heme oxygenase (biliverdin-producing).
based on mapping to UniProt Q7A649
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)
| Q7A649 |
HDOX1_STAAN
Staphylococcus aureus subsp. aureus N315
Heme oxygenase (staphylobilin-producing) 1
|
PDB Structure
| PDB | 2ZDO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Ruffling of Metalloporphyrins Bound to IsdG and IsdI, Two Heme-degrading Enzymes in Staphylococcus aureus
J.Biol.Chem.
|
