| Primary Identifier | IPR008213 | Type | Domain |
| Short Name | CpcD-like_dom |
| description | Ferredoxin-NADP(+) oxydoreductase (FNR) () 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 (see ) 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 [, , ]and is associated with:- CpcD, the phycocyanin (PC)-associated, rod-capping, linker polypeptide of PBS. The similarity spans nearly the entire sequence of this linker class.- CpcC, the PC-associated rod linker polypeptide. The similarity is confined only to the C terminus of this linker class.- ApcC, the allophycocyanin (APC)-associated, core linker polypeptide. The similarity only correspond to about half of the molecule.The CpcD-like domain has an elongated shape and consists of a three-strandedβ-sheet, two α-helices, one of which has only about one turn, and theconnecting random coil segments []. |
