Biflaviolin synthase CYP158A2
Details
- Name
- Biflaviolin synthase CYP158A2
- Synonyms
- 1.14.21.7
- CYP158A2
- Cytochrome P450 158A2
- Gene Name
- cyp158a2
- Organism
- Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
- Amino acid sequence
>lcl|BSEQ0011911|Biflaviolin synthase CYP158A2 MTEETISQAVPPVRDWPAVDLPGSDFDPVLTELMREGPVTRISLPNGEGWAWLVTRHDDV RLVTNDPRFGREAVMDRQVTRLAPHFIPARGAVGFLDPPDHTRLRRSVAAAFTARGVERV RERSRGMLDELVDAMLRAGPPADLTEAVLSPFPIAVICELMGVPATDRHSMHTWTQLILS SSHGAEVSERAKNEMNAYFSDLIGLRSDSAGEDVTSLLGAAVGRDEITLSEAVGLAVLLQ IGGEAVTNNSGQMFHLLLSRPELAERLRSEPEIRPRAIDELLRWIPHRNAVGLSRIALED VEIKGVRIRAGDAVYVSYLAANRDPEVFPDPDRIDFERSPNPHVSFGFGPHYCPGGMLAR LESELLVDAVLDRVPGLKLAVAPEDVPFKKGALIRGPEALPVTW
- Number of residues
- 404
- Molecular Weight
- 44354.085
- Theoretical pI
- 5.02
- GO Classification
- Functionsheme binding / iron ion binding / monooxygenase activity / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygenProcessesoxidation-reduction process / pigment metabolic process
- General Function
- Oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- Specific Function
- Catalyze oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments which protect the soil bacterium from deleterious effects of UV irradiation (three isomers of biflaviolin and one triflaviolin).
- Pfam Domain Function
- p450 (PF00067)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011912|Biflaviolin synthase CYP158A2 (cyp158a2) ATGACTGAAGAAACGATTTCCCAGGCCGTGCCACCCGTCCGGGACTGGCCGGCCGTCGAC CTTCCCGGCAGCGACTTCGACCCGGTGCTGACCGAGCTGATGCGCGAGGGTCCCGTCACC CGGATCTCGCTGCCCAACGGCGAGGGCTGGGCCTGGCTCGTGACCCGCCACGACGACGTC CGCCTGGTCACCAACGACCCCCGGTTCGGGCGCGAGGCCGTCATGGACCGCCAGGTCACC CGGCTGGCCCCGCACTTCATCCCGGCGCGCGGCGCGGTGGGCTTCCTGGACCCGCCCGAC CACACCCGGCTGCGCCGCTCGGTGGCCGCGGCCTTCACCGCGCGGGGCGTGGAGCGGGTG CGCGAGCGGTCCCGGGGCATGCTCGACGAGCTGGTCGACGCCATGCTGAGGGCCGGTCCG CCCGCCGACCTCACCGAGGCGGTGCTGAGCCCGTTCCCCATCGCGGTGATCTGCGAGCTG ATGGGTGTGCCGGCCACCGACCGGCACTCCATGCACACCTGGACCCAGCTGATCCTGTCC TCCTCGCACGGCGCCGAGGTCAGCGAGCGGGCCAAGAACGAGATGAACGCCTACTTCTCG GATCTCATCGGGCTCCGCTCCGACAGCGCGGGCGAGGACGTCACCTCGCTGCTGGGTGCC GCCGTGGGGCGGGACGAGATCACGCTGTCGGAGGCCGTCGGGCTCGCGGTGCTGCTCCAG ATCGGCGGCGAGGCGGTCACCAACAACAGCGGGCAGATGTTCCACCTGCTGCTGAGCCGC CCGGAGCTGGCCGAACGCCTGCGCTCCGAGCCGGAGATCCGCCCCCGGGCCATCGACGAG CTGCTGCGCTGGATCCCGCACCGCAACGCCGTGGGGCTGTCCCGGATCGCCCTGGAGGAC GTGGAGATCAAGGGGGTGCGGATCCGCGCGGGCGACGCCGTCTACGTCTCGTACCTGGCG GCCAACCGCGACCCGGAGGTGTTCCCCGACCCGGACCGCATCGACTTCGAGCGCTCCCCC AACCCGCACGTCTCCTTCGGCTTCGGCCCGCACTACTGTCCCGGCGGCATGCTGGCGCGG CTGGAGTCGGAGCTGCTCGTCGACGCGGTCCTGGACCGCGTGCCGGGGCTGAAGCTCGCG GTGGCGCCGGAGGACGTGCCCTTCAAGAAGGGTGCGCTGATCCGCGGGCCCGAGGCCCTG CCGGTGACGTGGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9FCA6 UniProtKB Entry Name C1582_STRCO GenBank Gene ID AL939108 - General References
- Bentley SD, Chater KF, Cerdeno-Tarraga AM, Challis GL, Thomson NR, James KD, Harris DE, Quail MA, Kieser H, Harper D, Bateman A, Brown S, Chandra G, Chen CW, Collins M, Cronin A, Fraser A, Goble A, Hidalgo J, Hornsby T, Howarth S, Huang CH, Kieser T, Larke L, Murphy L, Oliver K, O'Neil S, Rabbinowitsch E, Rajandream MA, Rutherford K, Rutter S, Seeger K, Saunders D, Sharp S, Squares R, Squares S, Taylor K, Warren T, Wietzorrek A, Woodward J, Barrell BG, Parkhill J, Hopwood DA: Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature. 2002 May 9;417(6885):141-7. [Article]
- Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR: Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2. J Biol Chem. 2005 Mar 25;280(12):11599-607. Epub 2005 Jan 19. [Article]
- Zhao B, Guengerich FP, Voehler M, Waterman MR: Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer. J Biol Chem. 2005 Dec 23;280(51):42188-97. Epub 2005 Oct 20. [Article]
- Zhao B, Bellamine A, Lei L, Waterman MR: The role of Ile87 of CYP158A2 in oxidative coupling reaction. Arch Biochem Biophys. 2012 Feb 15;518(2):127-32. doi: 10.1016/j.abb.2011.12.007. Epub 2011 Dec 19. [Article]