Putative FAD-monooxygenase
Details
- Name
- Putative FAD-monooxygenase
- Synonyms
- Putative monooxygenase
- Putative polyketide hydroxylase
- rebC
- Gene Name
- rbmD
- Organism
- Nocardia aerocolonigenes
- Amino acid sequence
>lcl|BSEQ0022084|Putative FAD-monooxygenase MNAPIETDVLILGGGPVGMALALDLAHRQVGHLVVEQTDGTITHPRVGTIGPRSMELFRR WGVAKQIRTAGWPGDHPLDAAWVTRVGGHEVYRIPLGTADTRATPEHTPEPDAICPQHWL APLLAEAVGERLRTRSRLDSFEQRDDHVRATITDLRTGATRAVHARYLVACDGASSPTRK ALGIDAPPRHRTQVFRNILFRAPELRSLLGERAALFFFLMLSSSLRFPLRALDGRGLYRL TVGVDDASKSTMDSFELVRRAVAFDTEIEVLSDSEWHLTHRVADSFSAGRVFLTGDAAHT LSPSGGFGMNTGIGSAADLGWKLAATLRGWAGPGLLATYEEERRPVAITSLEEANVNLRR TMDRELPPGLHDDGPRGERIRAAVAEKLERSGARREFDAPGIHFGHTYRSSIVCGEPETE VATGGWRPSARPGARAPHAWLTPTTSTLDLFGRGFVLLSFGTTDGVEAVTRAFADRHVPL ETVTCHAPEIHALYERAHVLVRPDGHVAWRGDHLPAELGGLVDKVRGAA
- Number of residues
- 529
- Molecular Weight
- 57670.68
- Theoretical pI
- 7.28
- GO Classification
- FunctionsFAD binding / monooxygenase activity
- General Function
- Monooxygenase activity
- Specific Function
- Not Available
- Pfam Domain Function
- FAD_binding_3 (PF01494)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0007289|1422 bp ATGACGGCAGACGAGCGCGACCGCGCCCGGTCGGCGTTGCCATTCCTCGTGATCACCCAG CTGATGATCGTGCTGGATGCCTCGATCGTGAACATCGCTCTACCCTCGATGGGCCGTGAG CTCGGCATGGACCAGACAGGCCTGCAGTGGGTGGTCAACGCCTACACGCTCACCTTCGGC GGCTTCCTCATGCTCGGCGGGCGCATGGCCGACCTGATCGGCCGCCGCCTCGTGTTCGTC TCGGGCATCTGCCTGTTCGGTGCCGCCTCCCTGGCCGCCGCGCTCGCACCGGTGGCCGGT GTGCTGGTCGCGGCCCGCGCCGTGCAGGGTCTCTCGGCGGCCGTCGCCTCCGCCGCCGCG TTGTCGATCATCGTCGCGACGTTTCCGGAGGGTAAGGGGCGCAACCAGGCGCTCGCGATG TGGGGGGCCGTCAGCGGCGTCGGTGGTGCCGTCGGCGTGTTGCTCGGCGGCGTGCTGACC TCGGGGCCCGGCTGGCCGTGGATCTTCTACATCAACGTCCCTATCGTCGTCGTGGTCGTG CTCGGGGTGTTCCGCAGCGTGTCCGGCGCTCGCGGCGACACGCGGGGCAGGCTCGACGTC GCCGGTGCCGTCACGCTCACCGGTGGCTTGACGTTGTTGGTCTACGCCATCGTGAGCGGC CAGTCGGGCGACCCCGTCACGATCCTGCTCGCACTGGGTCTCGCCGTCGTGCTGCTGGTG AGCTTCTTCCTCGTGCAGCGCAAGGTGCGTGAACCTCTCGTCCCGCTGTCGTCGTTCCGC AACCGCAACCTCTCCGTCGCCAGTGTCGTCGGCCTCTTCGCGGGTGCCGCGCCGTACGCG ATGTTCTTCCTGCTCTCGCTGCACCTGCAGAACGTCGTGGGTCTCACCCCGCTGCAGACA GGGCTCGGGTTCCTGCCCGTGTCGTTGATCTCGATGGTGGGCGCCGCCGCGCTGGCGCCG CTGGCGATGGCCAGGATCGGCATGCGGTTCACGTTGCTCCTGAGCCTCGGCGTGCTGGCC GTCGGTCTCGTCCTGCTGTCCCGCCTCACCGAGGAGGACGGCTTCGGCGCCACCGTCGCC GGGCAGCTGGTCGCCGGTCTCGGCCTGGGCACGACCTTCGTCGCCGTGACGACGGCCGCC GTCGCGGGACTCGCGGAGAACGAGTCGGGCCTGGCGTCGGGCCTGATCAACACCGCACAG CAGCTGGGTGGCGCGCTGGGGCTCGGTGCGCTGGCGGCGCTGTCCGGTGCGTACTCGGCG GCCGAGCTCGCGAAGGAGCCGCCGGTCTCCGAGGTGGCCGCGCTGTCCAGCGGATACCAG GTGGCGTTCCTGGGTGCCGCCGTTTTCGCCGTGGCCGGCGCCCTGATCGCGCTGGCGTTG CCCCGGCGCGAGTCAGTGCCGGCGACGACACCACACGAGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q8KI25 UniProtKB Entry Name Q8KI25_NOCAE GenBank Protein ID 22536135 GenBank Gene ID AF534707 - General References
- Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan CL: Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC. Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15311-6. Epub 2007 Sep 14. [Article]
- Ryan KS, Chakraborty S, Howard-Jones AR, Walsh CT, Ballou DP, Drennan CL: The FAD cofactor of RebC shifts to an IN conformation upon flavin reduction. Biochemistry. 2008 Dec 23;47(51):13506-13. doi: 10.1021/bi801229w. [Article]
- Goldman PJ, Ryan KS, Hamill MJ, Howard-Jones AR, Walsh CT, Elliott SJ, Drennan CL: An unusual role for a mobile flavin in StaC-like indolocarbazole biosynthetic enzymes. Chem Biol. 2012 Jul 27;19(7):855-65. doi: 10.1016/j.chembiol.2012.05.016. [Article]