{PDOC51441} {PS51441; CPCD_LIKE} {BEGIN} **************************** * CpcD-like domain profile * **************************** Ferredoxin-NADP(+) oxydoreductase (FNR) (EC=1.18.1.2) 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 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 beta-sheet, two alpha-helices, one of which has only about one turn, and the connecting random coil segments (see ) [4]. The profile we developed covers the entire cpcD-like domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: March 2009 / First entry. [ 1] Schluchter W.M., Bryant D.A. "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." Biochemistry 31:3092-3102(1992). PubMed=1554697 [ 2] Nakajima M., Sakamoto T., Wada K. "The complete purification and characterization of three forms of ferredoxin-NADP(+) oxidoreductase from a thermophilic cyanobacterium Synechococcus elongatus." Plant Cell Physiol. 43:484-493(2002). PubMed=12040095 [ 3] Gomez-Lojero C., Perez-Gomez B., Shen G., Schluchter W.M., Bryant D.A. "Interaction of ferredoxin:NADP+ oxidoreductase with phycobilisomes and phycobilisome substructures of the cyanobacterium Synechococcus sp. strain PCC 7002." Biochemistry 42:13800-13811(2003). PubMed=14636046; DOI=10.1021/bi0346998 [ 4] Reuter W., Wiegand G., Huber R., Than M.E. "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." Proc. Natl. Acad. Sci. U.S.A. 96:1363-1368(1999). PubMed=9990029 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}