CATH Classification

Domain Context

CATH Clusters

Superfamily Jelly Rolls
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 1H2L
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
Elkins, J.M., Hewitson, K.S., McNeill, L.A., Seibel, J.F., Schlemminger, I., Pugh, C., Ratcliffe, P., Schofield, C.J.
J.Biol.Chem.
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