|PROSITE documentation PDOC51441|
Ferredoxin-NADP(+) oxydoreductase (FNR) (EC=22.214.171.124) 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 <PDOC51384>) and an NADP(+)-binding domain. With the exception of Gloeobacter violaceous 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 [1,2,3]:
The cpcD-like domain has an elongated shape and consists of a three-stranded β-sheet, two α-helices, one of which has only about one turn, and the connecting random coil segments (see <PDB:1B33>) .
The profile we developed covers the entire cpcD-like domain.Last update:
March 2009 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Schluchter W.M. Bryant D.A.|
|Title||Molecular characterization of ferredoxin-NADP+ oxidoreductase in cyanobacteria: cloning and sequence of the petH gene of Synechococcus sp. PCC 7002 and studies on the gene product.|
|2||Authors||Nakajima M. Sakamoto T. Wada K.|
|Title||The complete purification and characterization of three forms of ferredoxin-NADP(+) oxidoreductase from a thermophilic cyanobacterium Synechococcus elongatus.|
|Source||Plant Cell Physiol. 43:484-493(2002).|
|3||Authors||Gomez-Lojero C. Perez-Gomez B. Shen G. Schluchter W.M. Bryant D.A.|
|Title||Interaction of ferredoxin:NADP+ oxidoreductase with phycobilisomes and phycobilisome substructures of the cyanobacterium Synechococcus sp. strain PCC 7002.|
|4||Authors||Reuter W. Wiegand G. Huber R. Than M.E.|
|Title||Structural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 96:1363-1368(1999).|