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CDS information : R1128_00130


close this sectionLocation

Organism
StrainR1128
Entry nameR1128
Contig
Start / Stop / Direction15,270 / 16,823 / + [in whole cluster]
15,270 / 16,823 / + [in contig]
Location15270..16823 [in whole cluster]
15270..16823 [in contig]
TypeCDS
Length1,554 bp (517 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
Productputative oxidoreductase
Product (GenBank)oxygenase
Gene
Gene (GenBank)zhuM
EC number
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[10931852] Cloning, nucleotide sequence, and heterologous expression of the biosynthetic gene cluster for R1128, a non-steroidal estrogen receptor antagonist. Insights into an unusual priming mechanism. (J Biol Chem. , 2000)
Related Reference
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)
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)

close this sectionSequence

selected fasta
>putative oxidoreductase [oxygenase]
MPESDGIDGTYPVVIAGGGPVGTMLACGLRQAGVDVLVLERRTEPDLLPRAGSMGPLAFE
ALERLGLHDALLAAEQDTLAEYGKMFADWAAKKGIGQPATRSAPKEHFAGLEKIDPARRT
DPERRRVRVEQPVLEEILHRHAVSLGAVILRGHEIVGVFQDEERVIVDVRTVDGTVAQVT
TQYLVGADGADSSVRGFVGFDFPGTDATVTGRMAVVELADEEKLSPGFHYTPVGLYVHGL
GVNRLSTVEFDGPPTDDEDMTAEELQGSIRRVSGTDVTISEMSSGTRWIDTARQASAYRL
GRVLLAGDAAHVYAPVGGQGLNVGLVDAANLVWKLAAQVQRWAPHYLLDTYGSERYPVAA
RLLQNTRAQIALMHPDPQTTALREMFEELLDIDEVHRTIADMMAGMDVRYAVEGEHPLLG
TLVPDAKLTGGKAADLWADGRGVLVDFADRADVRDAVGAWSARVNVVTLPGAREDVDALL
VRPDGCVVWALPTGAALADAPPTEALTTWFGRAPRVS
selected fasta
>putative oxidoreductase [oxygenase]
GTGCCTGAGTCCGACGGCATCGACGGCACCTACCCCGTCGTCATCGCGGGCGGCGGCCCG
GTCGGCACCATGCTGGCGTGCGGGCTGCGGCAGGCCGGCGTCGACGTTCTGGTGCTCGAA
CGCCGCACCGAGCCCGACCTGTTGCCGCGCGCCGGCTCGATGGGCCCGCTGGCGTTCGAG
GCGCTGGAACGGCTCGGCCTGCACGACGCGCTGCTGGCCGCCGAGCAGGACACGCTCGCC
GAGTACGGCAAGATGTTCGCCGACTGGGCGGCCAAGAAGGGCATCGGCCAGCCGGCCACC
CGCTCCGCGCCCAAGGAGCACTTCGCGGGCCTGGAGAAGATCGACCCGGCCCGCCGCACC
GACCCCGAGCGCCGCCGGGTGCGCGTCGAGCAGCCGGTGCTCGAGGAGATCCTGCACCGG
CACGCGGTGTCGCTCGGCGCGGTGATCCTGCGCGGCCACGAGATCGTCGGCGTGTTCCAG
GACGAGGAGCGCGTCATCGTCGACGTGCGCACCGTCGACGGGACCGTCGCCCAGGTGACC
ACGCAGTACCTGGTCGGCGCCGACGGCGCGGACAGCAGCGTGCGCGGCTTCGTCGGCTTC
GACTTCCCCGGCACCGACGCGACCGTCACCGGCCGCATGGCGGTCGTGGAGTTGGCCGAC
GAGGAGAAACTCTCCCCGGGCTTCCACTACACGCCGGTCGGCCTGTACGTGCACGGCCTG
GGCGTCAACCGGCTGTCGACGGTCGAGTTCGACGGTCCGCCGACCGACGACGAGGACATG
ACCGCCGAGGAGCTGCAGGGCAGCATCCGACGGGTCAGCGGCACGGACGTGACGATCAGC
GAGATGTCCTCGGGCACCCGCTGGATCGACACGGCGCGGCAGGCGTCCGCGTACCGGCTC
GGCCGGGTGCTGCTGGCCGGCGACGCGGCGCACGTGTACGCGCCGGTCGGCGGCCAGGGC
CTCAACGTCGGCCTGGTCGACGCGGCCAACCTCGTGTGGAAGCTGGCCGCGCAGGTACAG
CGCTGGGCGCCGCACTATCTCCTCGACACCTACGGTTCGGAGCGCTACCCGGTCGCCGCG
CGGCTGTTGCAGAACACCCGCGCGCAGATCGCGCTCATGCACCCCGACCCGCAGACCACC
GCGCTGCGCGAGATGTTCGAGGAACTGCTCGACATCGACGAGGTGCACCGCACGATCGCC
GACATGATGGCCGGAATGGACGTGCGGTACGCCGTCGAGGGCGAGCATCCGCTCCTCGGC
ACGCTGGTCCCGGACGCCAAGCTCACCGGCGGCAAGGCCGCCGACCTGTGGGCGGACGGG
CGCGGCGTGCTCGTCGACTTCGCCGACCGCGCGGACGTGCGCGACGCGGTCGGCGCGTGG
TCGGCGCGGGTCAACGTCGTCACGTTGCCCGGCGCGCGCGAGGACGTCGACGCGCTGCTG
GTCCGGCCCGACGGCTGCGTGGTGTGGGCGCTGCCCACCGGCGCGGCGCTCGCCGACGCG
CCCCCGACCGAGGCCCTGACCACGTGGTTCGGACGCGCCCCGCGCGTGTCCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002938 Monooxygenase, FAD-binding (Domain)
 [11-365]  6.59999999999996e-64 PF01494
PF01494   FAD_binding_3
IPR003042 Aromatic-ring hydroxylase-like (Domain)
 [12-34]  6.20001486442668e-38 PR00420 [180-195]  6.20001486442668e-38 PR00420 [300-315]  6.20001486442668e-38 PR00420 [315-331]  6.20001486442668e-38 PR00420 [333-351]  6.20001486442668e-38 PR00420 [351-367]  6.20001486442668e-38 PR00420
PR00420   RNGMNOXGNASE
SignalP No significant hit
TMHMM No significant hit