CpcDCpcD/allophycocyanin linker domain
|SMART accession number:||SM01094|
|Interpro abstract (IPR008213):|
Ferredoxin-NADP(+) oxydoreductase (FNR) (EC 220.127.116.11) transfers electrons from ferredoxin (or flavodoxin) to NADP(+) to generate NADPH. In eucaryotes, the nuclear-encoded, chloroplast-targeted enzyme contains two domains: an FAD-binding domain and an NADP(+)-binding domain. With the exception of Gloeobacter violaceus PCC 7421, the predicted sequences of all cyanobacterial petH genes, encoding FNR, correspond to a protein containing three domains. Two domains at the C terminus correspond to the FAD- and NADP(+)-binding domains of higher plants FNR protein, which compose the catalytic domains of the enzyme. The N-terminal domain is similar to phycobilisome (PBS)-associated linker proteins from numerous cyanobacteria [(PUBMED:1554697), (PUBMED:2040095), (PUBMED:4636046)] and is associated with:
The CpcD-like domain has an elongated shape and consists of a three-stranded beta-sheet, two alpha-helices, one of which has only about one turn, and the connecting random coil segments [(PUBMED:9990029)].
|GO component:||phycobilisome (GO:0030089)|
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)