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
IPR004559 is a Heme chaperone HemW-like.
<p>Proteins in this entry include HemW (also known as oxygen-independent coproporphyrinogen-III oxidase-like protein). HemW is a heme chaperone catalyzing the insertion of heme into hemoproteins [[cite:PUB00092698]].</p> <p>Experimentally determined examples of oxygen-independent coproporphyrinogen III oxidase, an enzyme that replaces HemF function under anaerobic conditions, belong to a family of proteins called HemN ([interpro:IPR004558]). This family contains a closely related protein, shorter at the amino end and lacking the region containing the motif PYRT[SC]YP found in members of the hemN family. Several species, including Escherichia coli, Helicobacter pylori, Aquifex aeolicus, and Chlamydia trachomatis, have members of both this family and the Escherichia coli hemN family. The member of this family from Bacillus subtilis was shown to complement a hemF/hemN double mutant of Salmonella typhimurium and to prevent accumulation of coproporphyrinogen III under anaerobic conditions, but the exact role of this protein is still uncertain. It is found in a number of species that do not synthesize haem <i>de novo</i>.</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 | Coproporphyrinogen oxidase activity | Catalysis of the reaction: coproporphyrinogen III + 2 H(+) + O(2) = 2 CO(2) + 2 H(2)O + protoporphyrinogen IX. | ||
Cellular component | Cytoplasm | All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. | ||
Biological process | Porphyrin-containing compound biosynthetic process | The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group. | ||
Molecular function | 4 iron, 4 sulfur cluster binding | Interacting selectively and non-covalently with a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
Transcript | Name | Description | Predicted domains | Domain count |
---|---|---|---|---|
– | PREDICTED: oxygen-independent coproporphyrinogen-III oxidase-like protein sll1917-like [Cicer arietinum] gi|502133605|ref|XP_004501826.1| | 14 | ||
– | Oxygen-independent coproporphyrinogen III oxidase, putative; TAIR: AT5G63290.1 Radical SAM superfamily protein; Swiss-Prot: sp|P73245|Y1917_SYNY3 Oxygen-independent coproporphyrinogen-III oxidase-like protein sll1917; TrEMBL-Plants: tr|V7AWC4|V7AWC4_PHAVU Uncharacterized protein; Found in the gene: LotjaGi1g1v0234800 | 14 |
A list of co-occurring predicted domains within the L. japonicus gene space:
Predicted domain | Source | Observations | Saturation (%) |
---|---|---|---|
TIGR00539 | TIGRFAM | 1 | 50.00 |