Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR016053 is a Haem oxygenase-like.
<p>Haem oxygenase ([ec:1.14.99.3]) (HO) [[cite:PUB00001493]] is the microsomal enzyme that, in animals, carries out the oxidation of haem, it cleaves the haem ring at the alpha-methene bridge to form biliverdin and carbon monoxide [[cite:PUB00002451]]. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. In mammals there are three isozymes of haem oxygenase: HO-1 to HO-3. The first two isozymes differ in their tissue expression and their inducibility: HO-1 is highly inducible by its substrate haem and by various non-haem substances, while HO-2 is non-inducible. It has been suggested [[cite:PUB00005160]] that HO-2 could be implicated in the production of carbon monoxide in the brain where it is said to act as a neurotransmitter. In the genome of the chloroplast of red algae as well as in cyanobacteria, there is a haem oxygenase (gene pbsA) that is the key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae [[cite:PUB00004905]]. A haem oxygenase is also present in the bacteria Corynebacterium diphtheriae (gene hmuO), where it is involved in the acquisition of iron from the host haem [[cite:PUB00002314]]. There is, in the central section of these enzymes, a well-conserved region centred on a histidine residue.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Heme oxygenase (decyclizing) activity | Catalysis of the reaction: heme + 3 donor-H2 + 3 O2 = biliverdin + Fe2+ + CO + 3 acceptor + 3 H2O. | ||
| Biological process | Heme oxidation | The chemical reactions and pathways resulting in the loss of electrons from one or more atoms in heme. | ||
| Biological process | Oxidation-reduction process | A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | Chromoplast heme oxygenase 1 [Medicago sativa] gi|300431417|gb|ADK12637.1| | 10 | ||
| – | Heme oxygenase 1; TAIR: AT2G26670.1 Plant heme oxygenase (decyclizing) family protein; Swiss-Prot: sp|O48782|HMOX1_ARATH Heme oxygenase 1, chloroplastic; TrEMBL-Plants: tr|I3SL57|I3SL57_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0199700 | 10 | ||
| – | Heme oxygenase 1; TAIR: AT2G26670.1 Plant heme oxygenase (decyclizing) family protein; Swiss-Prot: sp|O48782|HMOX1_ARATH Heme oxygenase 1, chloroplastic; TrEMBL-Plants: tr|I3SL57|I3SL57_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0199700 | 10 | ||
| – | Heme oxygenase; TAIR: AT2G26550.2 heme oxygenase 2; Swiss-Prot: sp|O48722|HMOX2_ARATH Probable inactive heme oxygenase 2, chloroplastic; TrEMBL-Plants: tr|A0A0B2SHY8|A0A0B2SHY8_GLYSO Putative inactive heme oxygenase 2, chloroplastic; Found in the gene: LotjaGi5g1v0025400 | 8 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd19165 | CDD | 1 | 25.00 |