NADPH:ferredoxin reductase
Details
- Name
- NADPH:ferredoxin reductase
- Kind
- protein
- Synonyms
- Not Available
- Gene Name
- fpr
- UniProtKB Entry
- Q9L6V3TrEMBL
- Organism
- Rhodobacter capsulatus
- NCBI Taxonomy ID
- 1061
- Amino acid sequence
>lcl|BSEQ0012877|NADPH:ferredoxin reductase TTVNETTPIAPAKVLPDAQTVTSVRHWTDTLFSFRVTRPQTLRFRSGEFVMIGLLDDNGK PIMRAYSIASPAWDEELEFYSIKVPDGPLTSRLQHIKVGEQIILRPKPVGTLVIDALLPG KRLWFLATGTGIAPFASLMREPEAYEKFDEVIMMHACRTVAELEYGRQLVEALQEDPLIG ELVEGKLKYYPTTTREEFHHMGRITDNLASGKVFEDLGIAPMNPETDRAMVCGSLAFNVD VMKVLESYGLREGANSEPREFVVEKAFVGEGI
- Number of residues
- 272
- Molecular Weight
- 30402.685
- Theoretical pI
- 4.87
- GO Classification
- Functionsnucleotide binding / oxidoreductase activity
- General Function
- Transports electrons between flavodoxin or ferredoxin and NADPH.
- Specific Function
- ferredoxin-NADP+ reductase activity
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
- Not Available
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9L6V3 UniProtKB Entry Name Q9L6V3_RHOCA GenBank Protein ID 7025501 GenBank Gene ID AF232063 PDB ID(s) 2BGI, 2BGJ, 2VNH, 2VNI, 2VNJ, 2VNK, 4K1X - General References
- Nogues I, Perez-Dorado I, Frago S, Bittel C, Mayhew SG, Gomez-Moreno C, Hermoso JA, Medina M, Cortez N, Carrillo N: The ferredoxin-NADP(H) reductase from Rhodobacter capsulatus: molecular structure and catalytic mechanism. Biochemistry. 2005 Sep 6;44(35):11730-40. [Article]
- Bortolotti A, Perez-Dorado I, Goni G, Medina M, Hermoso JA, Carrillo N, Cortez N: Coenzyme binding and hydride transfer in Rhodobacter capsulatus ferredoxin/flavodoxin NADP(H) oxidoreductase. Biochim Biophys Acta. 2009 Feb;1794(2):199-210. doi: 10.1016/j.bbapap.2008.09.013. Epub 2008 Oct 7. [Article]
- Bortolotti A, Sanchez-Azqueta A, Maya CM, Velazquez-Campoy A, Hermoso JA, Medina M, Cortez N: The C-terminal extension of bacterial flavodoxin-reductases: involvement in the hydride transfer mechanism from the coenzyme. Biochim Biophys Acta. 2014 Jan;1837(1):33-43. doi: 10.1016/j.bbabio.2013.08.008. Epub 2013 Sep 6. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Heptyl 1-Thiohexopyranoside experimental unknown target Details