Putative cytochrome P450


NamePutative cytochrome P450
Synonyms
  • 1.14.21.7
  • CYP158A2
  • Cytochrome P450 158A2
Gene Namecyp158a2
OrganismStreptomyces 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 residuesNone
Molecular Weight44354.085
Theoretical pI5.02
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
Components
General FunctionOxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Specific FunctionCatalyze 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).
Transmembrane Regions
GenBank Protein ID
UniProtKB IDQ9FCA6
UniProtKB Entry Name
Cellular LocationNone
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
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. 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 ]
  2. 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 ]
  3. 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 ]
  4. 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 ]

From www.t3db.ca