PROSITE documentation PDOC51441
CpcD-like domain profile


Ferredoxin-NADP(+) oxydoreductase (FNR) (EC= 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]:

  • 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-stranded β-sheet, two α-helices, one of which has only about one turn, and the connecting random coil segments (see <PDB:1B33>) [4].

The profile we developed covers the entire cpcD-like domain.

Last update:

March 2009 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

CPCD_LIKE, PS51441; CpcD-like domain profile  (MATRIX)


1AuthorsSchluchter W.M. Bryant D.A.
TitleMolecular 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.
SourceBiochemistry 31:3092-3102(1992).
PubMed ID1554697

2AuthorsNakajima M. Sakamoto T. Wada K.
TitleThe complete purification and characterization of three forms of ferredoxin-NADP(+) oxidoreductase from a thermophilic cyanobacterium Synechococcus elongatus.
SourcePlant Cell Physiol. 43:484-493(2002).
PubMed ID12040095

3AuthorsGomez-Lojero C. Perez-Gomez B. Shen G. Schluchter W.M. Bryant D.A.
TitleInteraction of ferredoxin:NADP+ oxidoreductase with phycobilisomes and phycobilisome substructures of the cyanobacterium Synechococcus sp. strain PCC 7002.
SourceBiochemistry 42:13800-13811(2003).
PubMed ID14636046

4AuthorsReuter W. Wiegand G. Huber R. Than M.E.
TitleStructural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus.
SourceProc. Natl. Acad. Sci. U.S.A. 96:1363-1368(1999).
PubMed ID9990029

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