PROSITE documentation PDOC51441CpcD-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 <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.
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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. | |
| Source | Biochemistry 31:3092-3102(1992). | |
| PubMed ID | 1554697 |
| 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). | |
| PubMed ID | 12040095 |
| 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. | |
| Source | Biochemistry 42:13800-13811(2003). | |
| PubMed ID | 14636046 | |
| DOI | 10.1021/bi0346998 |
| 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). | |
| PubMed ID | 9990029 |
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