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CDS information : Griseo_00170


close this sectionLocation

Organism
StrainJP95
Entry nameGriseorhodin A
Contig
Start / Stop / Direction16,851 / 18,413 / + [in whole cluster]
16,851 / 18,413 / + [in contig]
Location16851..18413 [in whole cluster]
16851..18413 [in contig]
TypeCDS
Length1,563 bp (520 aa)
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close this sectionAnnotation

Category3.3 modification reduction
Productputative oxidoreductase
Product (GenBank)putative FAD-dependent monooxygenase GrhO6
Gene
Gene (GenBank)grhO6
EC number
Keyword
  • final C-C bond cleavage
Note
Note (GenBank)
Reference
ACC
PmId
[12323376] A gene cluster from a marine Streptomyces encoding the biosynthesis of the aromatic spiroketal polyketide griseorhodin A. (Chem Biol. , 2002)
[19175308] Cleavage of four carbon-carbon bonds during biosynthesis of the griseorhodin a spiroketal pharmacophore. (J Am Chem Soc. , 2009)
Related Reference
ACC
Q58PK7
PmId
[16148009] Ablation of the otcC gene encoding a post-polyketide hydroxylase from the oxytetracyline biosynthetic pathway in Streptomyces rimosus results in novel polyketides with altered chain length. (J Biol Chem. , 2005)
ACC
Q194P4
NITE
Mith_00310
PmId
[9889148] Oxidative cleavage of premithramycin B is one of the last steps in the biosynthesis of the antitumor drug mithramycin. (Chem Biol. , 1999)
[11853433] Ketopremithramycins and ketomithramycins, four new aureolic acid-type compounds obtained upon inactivation of two genes involved in the biosynthesis of the deoxysugar moieties of the antitumor drug mithramycin by Streptomyces argillaceus, reveal novel insights into post-PKS tailoring steps of the mithramycin biosynthetic pathway. (J Am Chem Soc. , 2002)
[12813091] Purification and characterization of a monooxygenase involved in the biosynthetic pathway of the antitumor drug mithramycin. (J Bacteriol. , 2003)
[16351075] Characterization of kinetics and products of the Baeyer-Villiger oxygenase MtmOIV, the key enzyme of the biosynthetic pathway toward the natural product anticancer drug mithramycin from Streptomyces argillaceus. (J Am Chem Soc. , 2005)
[16511225] Crystallization and X-ray diffraction properties of Baeyer-Villiger monooxygenase MtmOIV from the mithramycin biosynthetic pathway in Streptomyces argillaceus. (Acta Crystallogr Sect F Struct Biol Cryst Commun. , 2005)
[19364090] Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway . (Biochemistry. , 2009)

close this sectionSequence

selected fasta
>putative oxidoreductase [putative FAD-dependent monooxygenase GrhO6]
MPDTKGTTDTIDTPGFDFDVIIVGGGPVGMLLASELRIGRAKAVVLEKLTERTPHSKAFG
LHARSLESLDRRGLADRFREGARSWNNGHFAGLDVWVDFSLLDSAHNYALLSEQTRTERL
LEERAEEFGCTIRRGHEVTAVRQDEDGAEVDVTGPDGPYTLRARYVVGTDGGRSLVRRSA
GIAFPGTGGRVTARLADVVLADRENAPMGMERTERGLLFCVPLDDTYHRVATFDYEQGKE
AGSELGFEEFKDSVRAIWGDDMGASEPRWLSWFTDSACQAETYRAGRILLAGDAAHTHFP
VGGQGVNLGLQDALNLGWKLCADINGWAGEGLLDTYDAERQEPARQVLANTRAQIALMNP
DPYVTQLRELFQDLMRKDQVNHHIAEMLSGVRVRYDLPGPAHRLLGDFARDLRLETEEGP
RTLPKFLRRGNFVLLDLAGRPEIAEEYAKWAAPLDWAGRVRHLVATCEDEPELAGALIRP
DGYVAWAADRDASPAEIAEGLRTAIETWAGITDPTRAVFS
selected fasta
>putative oxidoreductase [putative FAD-dependent monooxygenase GrhO6]
ATGCCGGACACCAAGGGCACCACCGACACCATCGACACCCCGGGCTTCGACTTCGACGTG
ATCATCGTCGGCGGCGGCCCCGTGGGCATGCTGCTCGCCTCGGAGCTGCGCATCGGCCGC
GCCAAGGCCGTCGTCCTGGAGAAGCTCACCGAGCGCACCCCGCACTCCAAGGCGTTCGGG
CTGCACGCGCGGTCGCTGGAGTCGCTCGACCGCCGCGGACTCGCCGACCGCTTCCGCGAG
GGCGCCCGCTCCTGGAACAACGGCCACTTCGCGGGCCTCGACGTCTGGGTCGACTTCTCC
CTCCTGGACAGCGCCCACAACTACGCCCTGCTGTCCGAGCAGACCCGCACCGAACGACTG
CTGGAGGAGCGCGCGGAGGAGTTCGGCTGCACGATCCGCCGCGGCCACGAGGTCACGGCC
GTCCGCCAGGACGAGGACGGCGCCGAGGTCGACGTGACCGGCCCCGACGGCCCGTACACC
CTGCGCGCCCGGTACGTCGTCGGGACCGACGGCGGCCGCAGCCTGGTCCGCAGGTCGGCC
GGGATCGCCTTCCCCGGCACCGGCGGCCGCGTCACCGCGCGGCTCGCCGACGTCGTCCTC
GCCGACCGCGAGAACGCCCCCATGGGCATGGAGCGCACCGAGCGCGGCCTGCTCTTCTGC
GTACCGCTCGACGACACGTACCACCGCGTCGCCACGTTCGACTACGAGCAGGGCAAGGAG
GCGGGCTCCGAGCTCGGCTTCGAGGAGTTCAAGGACAGCGTCCGCGCGATCTGGGGCGAC
GACATGGGCGCCTCCGAGCCGCGCTGGCTCTCCTGGTTCACCGACTCCGCCTGCCAGGCC
GAGACCTACCGCGCCGGCCGGATCCTGCTCGCCGGCGACGCGGCCCACACGCACTTCCCG
GTCGGCGGCCAGGGGGTGAACCTGGGCCTCCAGGACGCGCTCAACCTGGGTTGGAAGCTC
TGCGCCGACATCAACGGCTGGGCCGGCGAAGGGCTGCTCGACACCTACGACGCCGAGCGC
CAGGAGCCCGCGCGTCAGGTCCTGGCCAACACCCGCGCCCAGATCGCGCTGATGAACCCC
GACCCCTACGTCACCCAGCTGCGCGAGCTCTTCCAGGACCTCATGCGCAAGGACCAGGTG
AACCACCACATCGCCGAGATGCTCAGCGGCGTACGGGTCCGCTACGACCTGCCGGGCCCG
GCCCACCGCCTGCTCGGCGACTTCGCCCGCGACCTGCGACTGGAGACGGAGGAGGGGCCC
AGGACCCTCCCGAAGTTCCTGCGGCGCGGCAACTTCGTCCTGCTCGACCTGGCCGGACGG
CCGGAGATCGCGGAGGAGTACGCGAAGTGGGCCGCGCCGCTCGACTGGGCCGGGCGCGTC
CGGCATCTCGTCGCCACGTGCGAGGACGAGCCGGAGCTGGCCGGCGCCCTCATCCGCCCG
GACGGCTACGTGGCCTGGGCCGCCGACCGCGACGCCTCCCCCGCCGAGATCGCGGAGGGG
CTGCGGACGGCGATCGAGACCTGGGCCGGGATCACCGACCCGACCCGCGCGGTCTTCAGC
TGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [18-350]  3.10000000000005e-82 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [19-41]  8.69997440322062e-40 PR00420 [162-177]  8.69997440322062e-40 PR00420 [285-300]  8.69997440322062e-40 PR00420 [300-316]  8.69997440322062e-40 PR00420 [318-336]  8.69997440322062e-40 PR00420 [336-352]  8.69997440322062e-40 PR00420
PR00420   RNGMNOXGNASE
SignalP No significant hit
TMHMM No significant hit