CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.287 | Helix Hairpins |
|
1.10.287.1010 | Clavaminate synthase-like |
Domain Context
CATH Clusters
| Superfamily | Clavaminate synthase-like |
| Functional Family | Hypoxia-inducible factor 1-alpha inhibitor |
Enzyme Information
| 1.14.11.n4 |
Ankyrin-repeat-histidine dioxagenase.
based on mapping to UniProt Q9NWT6
(1) [Ankyrin-repeat domain protein]-L-histidine + 2-oxoglutarate + O(2) = [ankyrin-repeat domain protein]-(3S)-3-hydroxy-L-histidine + succinate + CO(2). (2) [Ankyrin-repeat domain protein]-L-asparagine + 2-oxoglutarate + O(2) = [ankyrin-repeat domain protein]-(3S)-3-hydroxy-L-asparagine + succinate + CO(2). (3) [Ankyrin-repeat domain protein]-L-aspartate + 2-oxoglutarate + O(2) = [ankyrin-repeat domain protein]-(3S)-3-hydroxy-L-aspartate + succinate + CO(2).
|
| 1.14.11.30 |
Hypoxia-inducible factor-asparagine dioxygenase.
based on mapping to UniProt Q9NWT6
Hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O(2) = hypoxia- inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO(2).
-!- Contains iron, and requires ascorbate. -!- Catalyzes hydroxylation of an asparagine in the C-terminal transcriptional activation domain of HIF-alpha, the alpha subunit of the transcriptional regulator HIF (hypoxia-inducible factor), which reduces its interaction with the transcriptional coactivator protein p300. -!- The requirement of oxygen for the hydroxylation reaction enables animals to respond to hypoxia.
|
UniProtKB Entries (1)
| Q16665 |
HIF1A_HUMAN
Homo sapiens
Hypoxia-inducible factor 1-alpha
|
PDB Structure
| PDB | 1H2K |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of Factor-Inhibiting Hypoxia-Inducible Factor (Hif) Reveals Mechanism of Oxidative Modification of Hif-1Alpha
J.Biol.Chem.
|