T3DB: Biflaviolin synthase CYP158A2

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	Functions iron ion binding heme binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Processes oxidation-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
GenBank Protein ID	Not Available
UniProtKB ID	Q9FCA6
UniProtKB Entry Name	C1582_STRCO
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
GenBank Gene ID	AL939108
GeneCard ID	Not Available
GenAtlas ID	Not Available
HGNC ID	Not Available
Chromosome Location	Not Available
Locus	Not Available
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. 12000953 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. 15659395 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. 16239228 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. 22203090