Source:
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Steven Neuhaus
Date created: 2012-09-26 11:00:00
Date modified: 2015-05-08 01:13:49
Phytochrome FphA - first 753 amino acids (Frieburg)
| Types | DnaRegion |
| Roles | Protein_Domain polypeptide_domain |
| Sequences | BBa_K952000_sequence (Version 1) |
Description
Sensory domain of phytochrome FphA which has been codon optimized for expression in E. coli and conforms to RFC25 (Freiburg Standard) in order to allow for the fusion of other protein domains N- and C- terminally.Note that in order for the sensor to function, FphA must bind a chromophore (biliverdin IXalpha (BV) acts as its natural chromophore). The chromophore can either be externally added to the protein, or can be endogenously created through expression of heme oxygenase.
Illumination with saturated red light (636 nm) results in formation of the Pfr form of the phytochrome (Amax 754nm), which can be converted back into the ground Pr form (Amax 707 nm) through illumination with far-red light (750 nm) (Brandt,S., Frankenberg-Dinkel,N., et. al. (2008) J. Biol. Chem. 283 (50), 34605-34614)
Notes
Cut sites had to be removed from the source gene in order to comply with Biobrick standards.Source
This part comes from the fungus Aspergillus nidulans, although it has been codon optimized for expression in E. coli. See http://www.ncbi.nlm.nih.gov/nuccore/167987798| Sequence Annotation | Location | Component / Role(s) |
| C195, biliverdin IX􏰃 binding residue | 583,585 | conserved_region feature/conserved |